|
Name |
Accession |
Description |
Interval |
E-value |
| CH_PLEC-like_rpt1 |
cd21188 |
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
647-751 |
2.23e-74 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 243.85 E-value: 2.23e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 647 DRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMRFHKLQNVQIALDYLKHRQVKLVNI 726
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1835643837 727 RNDDIADGNPKLTLGLIWTIILHFQ 751
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
644-762 |
6.27e-72 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 237.62 E-value: 6.27e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 644 DERDRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMRFHKLQNVQIALDYLKHRQVKL 723
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1835643837 724 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVMGQSE 762
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
642-760 |
4.55e-70 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 232.57 E-value: 4.55e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 642 AEDERDRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMRFHKLQNVQIALDYLKHRQV 721
Cdd:cd21236 10 YKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQV 89
|
90 100 110
....*....|....*....|....*....|....*....
gi 1835643837 722 KLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVMGQ 760
Cdd:cd21236 90 KLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
764-869 |
2.36e-68 |
|
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409087 Cd Length: 106 Bit Score: 226.83 E-value: 2.36e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 764 MTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 843
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1835643837 844 PEDVDVPQPDEKSIITYVSSMYDAMP 869
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
765-869 |
1.21e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.80 E-value: 1.21e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 844
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1835643837 845 EDVDVPQPDEKSIITYVSSMYDAMP 869
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
644-761 |
1.06e-60 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 205.27 E-value: 1.06e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 644 DERDRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMRFHKLQNVQIALDYLKHRQVKL 723
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1835643837 724 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVMGQS 761
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
765-869 |
6.80e-58 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 196.75 E-value: 6.80e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDP 844
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1835643837 845 EDVDVPQPDEKSIITYVSSMYDAMP 869
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
763-869 |
1.76e-50 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 175.62 E-value: 1.76e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 763 DMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLL 842
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1835643837 843 DPEDVDVPQPDEKSIITYVSSMYDAMP 869
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
649-752 |
1.50e-49 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 172.95 E-value: 1.50e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 649 VQKKTFTKWVNKHLIKAQR-HVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMRFHKLQNVQIALDYLKHRQVKLVNIR 727
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1835643837 728 NDDIADGNPKLTLGLIWTIILHFQI 752
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
765-865 |
2.91e-47 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 166.43 E-value: 2.91e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 844
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1835643837 845 EDVDVPQPDEKSIITYVSSMY 865
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
644-748 |
1.00e-46 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 165.23 E-value: 1.00e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 644 DERDRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR-EKGRMRFHKLQNVQIALDYLKHRQVK 722
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
|
90 100
....*....|....*....|....*.
gi 1835643837 723 LVNIRNDDIADGNPKLTLGLIWTIIL 748
Cdd:cd21246 91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
765-865 |
4.72e-46 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 162.95 E-value: 4.72e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 844
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1835643837 845 EDVDVPQPDEKSIITYVSSMY 865
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2342-3186 |
4.31e-45 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 183.03 E-value: 4.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEELAKVraemEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKlravSEEAKRQRQI 2421
Cdd:PTZ00121 1086 DNRADEATEEAFGKAEEAKKT----ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARK----AEDAKRVEIA 1157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2422 AEDEAARQRAEAERILKEKLAainDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEE--KIIL 2499
Cdd:PTZ00121 1158 RKAEDARKAEEARKAEDAKKA---EAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAvkKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2500 LKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAE-QEAEKQRQLA 2578
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKaDEAKKKAEEA 1314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2579 LEEEQRRKEAEEKVRKILADEKEAARQRK---AALEEVERLKAKAEEAKRQKELAEK---EAERQIQLAQEAALKKIDAE 2652
Cdd:PTZ00121 1315 KKADEAKKKAEEAKKKADAAKKKAEEAKKaaeAAKAEAEAAADEAEAAEEKAEAAEKkkeEAKKKADAAKKKAEEKKKAD 1394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2653 EKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFAR-TRAEQEAALSRQQVEEAERLKQRAEE-----E 2726
Cdd:PTZ00121 1395 EAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEeAKKADEAKKKAEEAKKAEEAKKKAEEakkadE 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2727 AQAKAQAQDEAEKLRKEAElEAAKRAHAEQAALKQKQLADE--EMDKHKKFAEKTLRQKSQVEQELTKVklqlEETDHQK 2804
Cdd:PTZ00121 1475 AKKKAEEAKKADEAKKKAE-EAKKKADEAKKAAEAKKKADEakKAEEAKKADEAKKAEEAKKADEAKKA----EEKKKAD 1549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2805 TLLDEELQRLKEEVTDAmrQKAQVEEELFKVKIQMEELIKlklRIEEENKMLIMKDKDSTQKLLVEEAEKmrqvAEEAAR 2884
Cdd:PTZ00121 1550 ELKKAEELKKAEEKKKA--EEAKKAEEDKNMALRKAEEAK---KAEEARIEEVMKLYEEEKKMKAEEAKK----AEEAKI 1620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2885 LSIEAQEAARMRKLAEDdlANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQ-EQARKFQEDKEQIEQQLAKET 2963
Cdd:PTZ00121 1621 KAEELKKAEEEKKKVEQ--LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKaEEAKKAEEDEKKAAEALKKEA 1698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2964 EgfqkslEAERRQQLEITAEAERLKLQvlEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQS 3043
Cdd:PTZ00121 1699 E------EAKKAEELKKKEAEEKKKAE--ELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3044 GKEAEELRRAIAE-LEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVL---QTTFLSE-KQLLLEREKYIEEEKAKl 3118
Cdd:PTZ00121 1771 EEIRKEKEAVIEEeLDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVIndsKEMEDSAiKEVADSKNMQLEEADAF- 1849
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 3119 enlyedevrkaqklkqEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQE 3186
Cdd:PTZ00121 1850 ----------------EKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIERE 1901
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
643-865 |
6.86e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 175.90 E-value: 6.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 643 EDERDRVQKKTFTKWVNKHLIKA-QRHVSDLYEDLRDGHNLISLLEVLSGDNLPR--EKGRMRFHKLQNVQIALDYLKHR 719
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 720 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvmgQSEDMTAKEKLLLWSQRMTEGYQ-GLHCDNFTTSWRDGRL 798
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 799 FNAIIHRHKPVLIDMNKVYRQTNLE--NLDQAFNVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSMY 865
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1953-3179 |
7.17e-45 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 181.56 E-value: 7.17e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1953 AEKLKEEERRRLAEVEAQLAKQTQlAEAHAKAKAQAEKEAEELQRRMQ--EEVSKR---------EVVAVdAEQQKQTIQ 2021
Cdd:NF041483 85 ADQLRADAERELRDARAQTQRILQ-EHAEHQARLQAELHTEAVQRRQQldQELAERrqtveshvnENVAW-AEQLRARTE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2022 QELQQLRQNSDMEI-KSKAKQIEEVEynrrkieeeihivRLQLETMQKHKANAEDelqelrARAEkAEQQKKAAQEEAER 2100
Cdd:NF041483 163 SQARRLLDESRAEAeQALAAARAEAE-------------RLAEEARQRLGSEAES------ARAE-AEAILRRARKDAER 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2101 LRKQVKDETQKKREAEEELKRKVQAEKEAARekQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAqqsaaael 2180
Cdd:NF041483 223 LLNAASTQAQEATDHAEQLRSSTAAESDQAR--RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAA-------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2181 nSKRMSFAEKTAQLELSLKQEHIT--VTHLQEEAERLKKLHDEAEKAREEaekelekwhqkanEALRLRLQAEEVAhkKT 2258
Cdd:NF041483 293 -AKQLASAESANEQRTRTAKEEIArlVGEATKEAEALKAEAEQALADARA-------------EAEKLVAEAAEKA--RT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2259 LAQEEAEKQKEDAEREARK-RAKTEESALRQKELAEDELEKQRKLADATAQqkfsaeqeliRLKAETENSEQQRLLLEee 2337
Cdd:NF041483 357 VAAEDTAAQLAKAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEAD----------RLRGEAADQAEQLKGAA-- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2338 lfrlKNEVNEAIQKRKEMEEELAKVRAEMEiLLQSKSRAEEEsRSNTEKSK---QMLEVEASKLRELAeeaAKLRAVSEE 2414
Cdd:NF041483 425 ----KDDTKEYRAKTVELQEEARRLRGEAE-QLRAEAVAEGE-RIRGEARReavQQIEEAARTAEELL---TKAKADADE 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2415 AkrqRQIAEDEAARQRAEAerilkeklaaINDATRLKTEAEIALKEKEAENERLRRLAEDEA-YQRKLLEEQATQHKQDI 2493
Cdd:NF041483 496 L---RSTATAESERVRTEA----------IERATTLRRQAEETLERTRAEAERLRAEAEEQAeEVRAAAERAARELREET 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2494 EEKIILLKKSSDNELERQKNIVEDTLrqrriiEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRS-KEKAEQEAE 2572
Cdd:NF041483 563 ERAIAARQAEAAEELTRLHTEAEERL------TAAEEALADARAEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAE 636
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2573 KQR-QLALEEEQRRKEAEEKvrkiladekeAARQRKAALEEVERLKAKAEE-AKRQKELAEKEAERQIQLAQE------- 2643
Cdd:NF041483 637 RLRtEAAADASAARAEGENV----------AVRLRSEAAAEAERLKSEAQEsADRVRAEAAAAAERVGTEAAEalaaaqe 706
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2644 -AALKKIDAEEKAHTAiVQQKEQEMLQTRKQEQSIL----DKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEA-E 2717
Cdd:NF041483 707 eAARRRREAEETLGSA-RAEADQERERAREQSEELLasarKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSvA 785
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2718 RLKQRAEEE-AQAKAQAQDEAEKLRKEAELEA--------AKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQvEQ 2788
Cdd:NF041483 786 GLQEQAEEEiAGLRSAAEHAAERTRTEAQEEAdrvrsdayAERERASEDANRLRREAQEETEAAKALAERTVSEAIA-EA 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2789 EltkvKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVK----IQMEELIKLKLRIEEENKMLIMKDKDST 2864
Cdd:NF041483 865 E----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERL 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2865 QKLLVEEAEKMR-QVAEEAARLSIEAQ-EAARMRKLAEDDLANQRALAEKMLKE----KMQAIQEASRLKAEA--EMLQK 2936
Cdd:NF041483 941 RDEARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTEaervKAEAAAEAERLRTEAreEADRT 1020
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2937 QKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERlklQVLEMSRAqakAEEDASKFKKKAEEIG 3016
Cdd:NF041483 1021 LDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEA---QADTMVGA---ARKEAERIVAEATVEG 1094
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3017 NKLhqtelATKERMAVVQTLEIQRQQSG---KEAEELR-RAIAELEHEKEKLKREAELLQKNS----QKMQVAQQEQlRQ 3088
Cdd:NF041483 1095 NSL-----VEKARTDADELLVGARRDATairERAEELRdRITGEIEELHERARRESAEQMKSAgercDALVKAAEEQ-LA 1168
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3089 ETQVLQTTFLSEKQLLLEREKYIEEEKAK-----LENLYEDEVRKAQKLKQEQEHQMKHLEEEKdqlKVSMDDAMKKQKE 3163
Cdd:NF041483 1169 EAEAKAKELVSDANSEASKVRIAAVKKAEgllkeAEQKKAELVREAEKIKAEAEAEAKRTVEEG---KRELDVLVRRRED 1245
|
1290
....*....|....*.
gi 1835643837 3164 AEENVRRKQDELQQLD 3179
Cdd:NF041483 1246 INAEISRVQDVLEALE 1261
|
|
| S10_plectin |
pfam03501 |
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ... |
7-99 |
1.24e-44 |
|
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the cytoskeletal muscle protein plectin as well as the ribosomal S10 protein. This domain may be involved in RNA binding.
Pssm-ID: 427337 Cd Length: 92 Bit Score: 158.07 E-value: 1.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 7 MPLDQLRAIYELLFREGVMIAKKDkRPQSLHPEIkGVSNLQVIRALGSLKSRGYVRETFVWRHFYWYLNNEGIVYLRQYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKD-FNLPKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|...
gi 1835643837 87 HLPPEIVPGSLQR 99
Cdd:pfam03501 79 HLPAEIVPATLKR 91
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
643-748 |
7.64e-43 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 153.99 E-value: 7.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 643 EDERDRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR-EKGRMRFHKLQNVQIALDYLkHRQV 721
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKV 88
|
90 100
....*....|....*....|....*..
gi 1835643837 722 KLVNIRNDDIADGNPKLTLGLIWTIIL 748
Cdd:cd21193 89 RLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
645-752 |
8.78e-43 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar proteins; Synaptic nuclear envelope protein 1 (SYNE-1), also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409090 Cd Length: 113 Bit Score: 153.68 E-value: 8.78e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 645 ERDRVQKKTFTKWVNKHLIKAQR--HVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRM--RFHKLQNVQIALDYLKHRQ 720
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1835643837 721 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 752
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2461-3209 |
1.20e-42 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 174.94 E-value: 1.20e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2461 KEAENERLRRLAEDEAYQ--RKLLEEQATQHKQDIEE---KIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVN 2535
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEeaFGKAEEAKKTETGKAEEarkAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2536 FEKASvgksdlELELNQLKNIAEETQRSKE-KAEQEAEKQRQLALEEEQRRKEAE---EKVRKILADEKEAARQRKAALE 2611
Cdd:PTZ00121 1157 ARKAE------DARKAEEARKAEDAKKAEAaRKAEEVRKAEELRKAEDARKAEAArkaEEERKAEEARKAEDAKKAEAVK 1230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2612 EVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRA 2691
Cdd:PTZ00121 1231 KAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2692 AEDAdfarTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDK 2771
Cdd:PTZ00121 1311 AEEA----KKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK 1386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2772 --HKKFAEKTLRQKSQVEQELTKVKLQLEETDHQktlldEELQRLKEEV--TDAMRQKAQVEEELFKVKIQMEELIK--- 2844
Cdd:PTZ00121 1387 aeEKKKADEAKKKAEEDKKKADELKKAAAAKKKA-----DEAKKKAEEKkkADEAKKKAEEAKKADEAKKKAEEAKKaee 1461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2845 LKLRIEEENKMLIMKDKDSTQKllveEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEA 2924
Cdd:PTZ00121 1462 AKKKAEEAKKADEAKKKAEEAK----KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKAD 1537
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2925 SRLKAE----AEMLQKQKELaqeqarKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEitaEAERLKLQVLEMSRAQAK 3000
Cdd:PTZ00121 1538 EAKKAEekkkADELKKAEEL------KKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE---EARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3001 AEEdaskfKKKAEEIGNKLHQTELATKERMAVVQtLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQV 3080
Cdd:PTZ00121 1609 AEE-----AKKAEEAKIKAEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKK 1682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3081 AQQEQLRQETQvlqttflsekqllLEREkyiEEEKAKLENL---YEDEVRKAQKLKQEQEHQMKHLEE---EKDQLKVSM 3154
Cdd:PTZ00121 1683 AEEDEKKAAEA-------------LKKE---AEEAKKAEELkkkEAEEKKKAEELKKAEEENKIKAEEakkEAEEDKKKA 1746
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 3155 DDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKlEQMEEEHRI 3209
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEK-RRMEVDKKI 1800
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2537-3222 |
2.12e-42 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 174.17 E-value: 2.12e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2537 EKASVGKSDLELELNQLKNIAEETQRSKE-KAEQEAEKQRQLALEEEQRRKE----AEEKVRKILADEKEAARQRKAALE 2611
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEaRKAEDARKAEEARKAEDAKRVEiarkAEDARKAEEARKAEDAKKAEAARK 1183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2612 EVERLKA----KAEEAKRQKELAEKEAERQIQLAQEAA-LKKIDAEEKAHTaiVQQKEQEMLQTRKQEQSILDKLKEEAE 2686
Cdd:PTZ00121 1184 AEEVRKAeelrKAEDARKAEAARKAEEERKAEEARKAEdAKKAEAVKKAEE--AKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2687 RA----KRAAEDADFARTRAEQEAALSRQQVEEAERLKQ-RAEEEAQAKAQAQDEAEKLRKEAElEAAKRAHAEQAALKQ 2761
Cdd:PTZ00121 1262 MAhfarRQAAIKAEEARKADELKKAEEKKKADEAKKAEEkKKADEAKKKAEEAKKADEAKKKAE-EAKKKADAAKKKAEE 1340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2762 KQLADEEMDKHKKFAEKTLrQKSQVEQELTKVKlqlEETDHQKTlldEELQRLKEEVTDAMRQKAQVEEElfkvKIQMEE 2841
Cdd:PTZ00121 1341 AKKAAEAAKAEAEAAADEA-EAAEEKAEAAEKK---KEEAKKKA---DAAKKKAEEKKKADEAKKKAEED----KKKADE 1409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2842 LIKL---KLRIEEENKMLIMKDKDSTQKLLVEEAEKmrqvAEEAARLSIEAQEAARMRKLAED----DLANQRALAEKML 2914
Cdd:PTZ00121 1410 LKKAaaaKKKADEAKKKAEEKKKADEAKKKAEEAKK----ADEAKKKAEEAKKAEEAKKKAEEakkaDEAKKKAEEAKKA 1485
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2915 KEKMQAIQEASRLKAEAEMLQKQKELAQEqARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKlQVLEM 2994
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADE-AKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-KAEEK 1563
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2995 SRAQA--KAEEDASKFKKKAEEignkLHQTELA-TKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELL 3071
Cdd:PTZ00121 1564 KKAEEakKAEEDKNMALRKAEE----AKKAEEArIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLK 1639
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3072 QKNSQKMQVAQQEQLRQETQVLQTTFLSEKQlllerekyiEEEKAKLEnlyedEVRKAQKLKQEQEHQMKHLEEEK---D 3148
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKA---------EEDKKKAE-----EAKKAEEDEKKAAEALKKEAEEAkkaE 1705
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 3149 QLKVSMDDAMKKQKEAEENVRRKQDELQQLdKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTD 3222
Cdd:PTZ00121 1706 ELKKKEAEEKKKAEELKKAEEENKIKAEEA-KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKE 1778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2544-3210 |
1.44e-41 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 171.48 E-value: 1.44e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2544 SDLELELNQLK-NIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAE---EKVRKI-----LADEKEAARQRKAALEEVE 2614
Cdd:PTZ00121 1075 SYKDFDFDAKEdNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKkkaEDARKAeearkAEDARKAEEARKAEDAKRV 1154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2615 RLKAKAEEAKRQKELAEKEAERQIQLAQEA-------ALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSildKLKEEAER 2687
Cdd:PTZ00121 1155 EIARKAEDARKAEEARKAEDAKKAEAARKAeevrkaeELRKAEDARKAEAARKAEEERKAEEARKAEDA---KKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAAEDADFARtRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADE 2767
Cdd:PTZ00121 1232 AEEAKKDAEEAK-KAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2768 EMDKHKkfAEKTLRQKSQVEQELTKVKLQLEEtdhqktlldeelQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKlkl 2847
Cdd:PTZ00121 1311 AEEAKK--ADEAKKKAEEAKKKADAAKKKAEE------------AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKK--- 1373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2848 riEEENKMLIMKDKDSTQKllvEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDdlanqralaekmLKEKMQAIQEASRL 2927
Cdd:PTZ00121 1374 --EEAKKKADAAKKKAEEK---KKADEAKKKAEEDKKKADELKKAAAAKKKADE------------AKKKAEEKKKADEA 1436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2928 KAEAEMLQKQKELAQ--EQARKFQEDKEQIEQQlAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDA 3005
Cdd:PTZ00121 1437 KKKAEEAKKADEAKKkaEEAKKAEEAKKKAEEA-KKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEA 1515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3006 SKF--KKKAEEIgNKLHQTELATKERMAVvqtlEIQRQQSGKEAEELRRAiaELEHEKEKLKREAELLQKNSQKMQVAQQ 3083
Cdd:PTZ00121 1516 KKAeeAKKADEA-KKAEEAKKADEAKKAE----EKKKADELKKAEELKKA--EEKKKAEEAKKAEEDKNMALRKAEEAKK 1588
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3084 EQLRQETQVLQTtFLSEKQLLLEREKYIEEEKAKLENLY--EDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQ 3161
Cdd:PTZ00121 1589 AEEARIEEVMKL-YEEEKKMKAEEAKKAEEAKIKAEELKkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEA 1667
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 3162 KEAEENvRRKQDELQQLD---KKRQEQEKLLADENRKLREKLEQMEEEHRIA 3210
Cdd:PTZ00121 1668 KKAEED-KKKAEEAKKAEedeKKAAEALKKEAEEAKKAEELKKKEAEEKKKA 1718
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
645-752 |
2.83e-41 |
|
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The synaptic nuclear envelope (SYNE) family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409039 Cd Length: 113 Bit Score: 149.64 E-value: 2.83e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 645 ERDRVQKKTFTKWVNKHLIKAQRH--VSDLYEDLRDGHNLISLLEVLSGDNLPREKGRM--RFHKLQNVQIALDYLKHRQ 720
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1835643837 721 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 752
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
752-867 |
7.50e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 148.28 E-value: 7.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 752 ISDIQVmgqsEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNV 831
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1835643837 832 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSMYDA 867
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1940-2739 |
1.44e-40 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 168.01 E-value: 1.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1940 TETLRRLNDEEKAAEKLKEEERRRLAEveaqlakqtqlaeahAKAKAQAEKEAEELQRrmQEEVSKREVVAVDAEQQKQT 2019
Cdd:PTZ00121 1093 TEEAFGKAEEAKKTETGKAEEARKAEE---------------AKKKAEDARKAEEARK--AEDARKAEEARKAEDAKRVE 1155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2020 IQQELQQLRQnsdMEIKSKAKQIEEVEYNRRKIEeeihiVRLQLETmqkHKANAEDELQELRaRAEKAEQQKKAAQEEAE 2099
Cdd:PTZ00121 1156 IARKAEDARK---AEEARKAEDAKKAEAARKAEE-----VRKAEEL---RKAEDARKAEAAR-KAEEERKAEEARKAEDA 1223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2100 RLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEV--AQQSAA 2177
Cdd:PTZ00121 1224 KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkAEEKKK 1303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2178 AELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEAlrlRLQAEEVAHKK 2257
Cdd:PTZ00121 1304 ADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAA---EKKKEEAKKKA 1380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2258 tlaqEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQR-KLADATAQQKFSAEQelIRLKAETENSEQQRLLLEE 2336
Cdd:PTZ00121 1381 ----DAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKaDEAKKKAEEKKKADE--AKKKAEEAKKADEAKKKAE 1454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2337 ELFRLKNEVNEAIQKRKemEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKlravSEEAK 2416
Cdd:PTZ00121 1455 EAKKAEEAKKKAEEAKK--ADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKK----ADEAK 1528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2417 RQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEK 2496
Cdd:PTZ00121 1529 KAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK 1608
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2497 IILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKV-NFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQR 2575
Cdd:PTZ00121 1609 AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK 1688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2576 QlalEEEQRRKEAEEK-----VRKILADEKEAARQRKAALEE----VERLKAKAEEAKRQKELAEKEAERQIQLAQEAAL 2646
Cdd:PTZ00121 1689 K---AAEALKKEAEEAkkaeeLKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKE 1765
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2647 KKIDAEE--KAHTAIVQQ--KEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQR 2722
Cdd:PTZ00121 1766 EEKKAEEirKEKEAVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
810
....*....|....*..
gi 1835643837 2723 AEEEAQAKAQAQDEAEK 2739
Cdd:PTZ00121 1846 ADAFEKHKFNKNNENGE 1862
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
626-748 |
2.65e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 147.86 E-value: 2.65e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 626 ETVPVVGVSEMEEPTPAEDERDRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR-EKGRMRFH 704
Cdd:cd21318 15 EPAATAKLFECSRIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIH 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1835643837 705 KLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 748
Cdd:cd21318 95 SLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
764-869 |
4.03e-40 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 145.92 E-value: 4.03e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 764 MTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 843
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1835643837 844 PEDVDVPQPDEKSIITYVSSMYDAMP 869
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
761-865 |
2.03e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 144.38 E-value: 2.03e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 761 SEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTR 840
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1835643837 841 LLDPEDVDVPQPDEKSIITYVSSMY 865
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
761-865 |
3.22e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 144.04 E-value: 3.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 761 SEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTR 840
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1835643837 841 LLDPEDVDVPQPDEKSIITYVSSMY 865
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2070-3191 |
3.85e-39 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 162.69 E-value: 3.85e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2070 KANAEDELQELRARA-----EKAEQQKKAAQE---EAERLRKQVKDETQKKREA-EEELKRKVQ-AEKEAAREKQRAVED 2139
Cdd:NF041483 89 RADAERELRDARAQTqrilqEHAEHQARLQAElhtEAVQRRQQLDQELAERRQTvESHVNENVAwAEQLRARTESQARRL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2140 LEKFRSQAEEAerrMKQAEVEKERqikVAQEvAQQSAAAELNSKRmsfAEKTAQLELSLKqehitvthlqeEAERLkklh 2219
Cdd:NF041483 169 LDESRAEAEQA---LAAARAEAER---LAEE-ARQRLGSEAESAR---AEAEAILRRARK-----------DAERL---- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2220 deaekareeaekeLEKWHQKANEALRlrlQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQkelAEDELEKQ 2299
Cdd:NF041483 224 -------------LNAASTQAQEATD---HAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALRE---ARAEAEKV 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2300 RKLADATAQQKFSAeqelirlkAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILL-----QSKS 2374
Cdd:NF041483 285 VAEAKEAAAKQLAS--------AESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADARAEAEKLVaeaaeKART 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2375 RAEEESRSNTEKSKQMLEVEASKLRELAEeaAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKE-KLAAIND------- 2446
Cdd:NF041483 357 VAAEDTAAQLAKAARTAEEVLTKASEDAK--ATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDtkeyrak 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2447 -------ATRLKTEAEIALKEKEAENERLRRLAEDEAYQRklLEEQATQhkqdiEEKIILLKKSSDNELERQKNIVEDTL 2519
Cdd:NF041483 435 tvelqeeARRLRGEAEQLRAEAVAEGERIRGEARREAVQQ--IEEAART-----AEELLTKAKADADELRSTATAESERV 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2520 RQRRiieeeirilkvnFEKASVgksdlelelnqLKNIAEETQrskEKAEQEAEKQRQLALEE-EQRRKEAEEKVRKILAD 2598
Cdd:NF041483 508 RTEA------------IERATT-----------LRRQAEETL---ERTRAEAERLRAEAEEQaEEVRAAAERAARELREE 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2599 EKEAARQRKA-ALEEVERLKAKAEE----AKRQKELAEKEAER-QIQLAQEAALKKIDAEEKAHTaIVQQKEQEMlqtrk 2672
Cdd:NF041483 562 TERAIAARQAeAAEELTRLHTEAEErltaAEEALADARAEAERiRREAAEETERLRTEAAERIRT-LQAQAEQEA----- 635
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2673 qeqsilDKLKEEAErakraaedADFARTRAEQEAALSRQQVE---EAERLKQRAEEEA-QAKAQAQDEAEKLRKEAeleA 2748
Cdd:NF041483 636 ------ERLRTEAA--------ADASAARAEGENVAVRLRSEaaaEAERLKSEAQESAdRVRAEAAAAAERVGTEA---A 698
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2749 AKRAHAEQAALKQKQLADEEMDKHKKFAEKTL-RQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQ 2827
Cdd:NF041483 699 EALAAAQEEAARRRREAEETLGSARAEADQEReRAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2828 -VEEELFKVKIQMEELIKlKLRIEEENKmlimkdKDSTQKLLVEEAEKMRqvAEEAARLSIEAQEAARMRKLAEDDLANQ 2906
Cdd:NF041483 779 qVRDSVAGLQEQAEEEIA-GLRSAAEHA------AERTRTEAQEEADRVR--SDAYAERERASEDANRLRREAQEETEAA 849
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2907 RALAEKMLKEkmqAIQEASRLKAEAEmlqkqkELAQEQarkfqedkeqieqqlaketegfqksleaeRRQQLEITAEAER 2986
Cdd:NF041483 850 KALAERTVSE---AIAEAERLRSDAS------EYAQRV-----------------------------RTEASDTLASAEQ 891
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2987 lklqvlEMSRAQAKAEEDASKFKKKAEEIGNKL--HQTELATKERMAVVQTLEIQRQQSGKEAEELR--------RAIAE 3056
Cdd:NF041483 892 ------DAARTRADAREDANRIRSDAAAQADRLigEATSEAERLTAEARAEAERLRDEARAEAERVRadaaaqaeQLIAE 965
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3057 LEHEKEKLKREAellqknSQKMQVAQQ--EQLRQETQVLQTTFLSEKqlllerEKYIEEEKAKLENLYEDEVRKAQKLKQ 3134
Cdd:NF041483 966 ATGEAERLRAEA------AETVGSAQQhaERIRTEAERVKAEAAAEA------ERLRTEAREEADRTLDEARKDANKRRS 1033
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 3135 EQEHQMKHLEEEkdqlkvSMDDAMKKQKEAEENVRRKQDELQ-QLDK----KRQEQEKLLAD 3191
Cdd:NF041483 1034 EAAEQADTLITE------AAAEADQLTAKAQEEALRTTTEAEaQADTmvgaARKEAERIVAE 1089
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
643-748 |
6.06e-39 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 143.66 E-value: 6.06e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 643 EDERDRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR-EKGRMRFHKLQNVQIALDYLKHRQV 721
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKV 104
|
90 100
....*....|....*....|....*..
gi 1835643837 722 KLVNIRNDDIADGNPKLTLGLIWTIIL 748
Cdd:cd21317 105 HLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1944-2745 |
1.14e-38 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 161.85 E-value: 1.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1944 RRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEElQRRMQEEVSKREVVAVDAEQQKQTIQQE 2023
Cdd:PTZ00121 1045 KDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEE-AFGKAEEAKKTETGKAEEARKAEEAKKK 1123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2024 LQQLRQNSDMEIKSKAKQIEEVeynrRKIEEE--IHIVRLQLETMQKHKANAEDELQELRArAEKAEQQKKAAQ-EEAER 2100
Cdd:PTZ00121 1124 AEDARKAEEARKAEDARKAEEA----RKAEDAkrVEIARKAEDARKAEEARKAEDAKKAEA-ARKAEEVRKAEElRKAED 1198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2101 LRKQvkdETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAEL 2180
Cdd:PTZ00121 1199 ARKA---EAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAE 1275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2181 NSKRMSFAEKTAQL----ELSLKQEHITVTHLQEEAERLKKLhDEAEKAReeaekelEKWHQKANEalrlrlqaeevAHK 2256
Cdd:PTZ00121 1276 EARKADELKKAEEKkkadEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKA-------EEAKKKADA-----------AKK 1336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2257 KTlaqEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADAtaqqkfsaeqelIRLKAETENSEQQRLLLEE 2336
Cdd:PTZ00121 1337 KA---EEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA------------AKKKAEEKKKADEAKKKAE 1401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2337 ELFRLKNEVNEAIQKRKEmEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAK 2416
Cdd:PTZ00121 1402 EDKKKADELKKAAAAKKK-ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAE 1480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2417 RQRQiaEDEAARQRAEAerilKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDeayQRKLLEEQATQHKQDIEEk 2496
Cdd:PTZ00121 1481 EAKK--ADEAKKKAEEA----KKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADE- 1550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2497 iilLKKSSDNELERQKNIVEDTLRQRRIIeeeirilKVNFEKASVGKSDLELELNQLKNIAEETQRSK----EKAEQEAE 2572
Cdd:PTZ00121 1551 ---LKKAEELKKAEEKKKAEEAKKAEEDK-------NMALRKAEEAKKAEEARIEEVMKLYEEEKKMKaeeaKKAEEAKI 1620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2573 KQRQLALEEEQRRKeaEEKVRKILADEKEAARQRKAALEEV----ERLKAKAEEAKRQKELAEKEAERQiQLAQEAALKK 2648
Cdd:PTZ00121 1621 KAEELKKAEEEKKK--VEQLKKKEAEEKKKAEELKKAEEENkikaAEEAKKAEEDKKKAEEAKKAEEDE-KKAAEALKKE 1697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2649 idAEEKAHTAIVQQKEQEML----QTRKQEQSILDK---LKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLkq 2721
Cdd:PTZ00121 1698 --AEEAKKAEELKKKEAEEKkkaeELKKAEEENKIKaeeAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEI-- 1773
|
810 820
....*....|....*....|....
gi 1835643837 2722 RAEEEAQAKAQAQDEAEKLRKEAE 2745
Cdd:PTZ00121 1774 RKEKEAVIEEELDEEDEKRRMEVD 1797
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1496-1573 |
3.24e-38 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 139.28 E-value: 3.24e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 1496 LSWQYLIRDIQQIQSWSLIMFRTMKPEDYKQALRNLETHYQEFMRDSQDSENFLPDDRMQIEREYNNCIQKYEQLLRT 1573
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1880-2993 |
3.65e-38 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 159.61 E-value: 3.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1880 AIKDYELQLVTYKAQVEPVASPAKKPKVQSTSDSiiqeyVDLRTRYSELTTLTSQYIKFITETLRRLNDE-EKAAEKLKE 1958
Cdd:NF041483 216 ARKDAERLLNAASTQAQEATDHAEQLRSSTAAES-----DQARRQAAELSRAAEQRMQEAEEALREARAEaEKVVAEAKE 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1959 EERRRLAEVEAQLAKQTQLAEAH-AKAKAQAEKEAE----ELQRRMQEEVSKREVVAVDAEQQKQTIQQElqqlrqNSDM 2033
Cdd:NF041483 291 AAAKQLASAESANEQRTRTAKEEiARLVGEATKEAEalkaEAEQALADARAEAEKLVAEAAEKARTVAAE------DTAA 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2034 EIKSKAKQIEEVeynrrkieeeihivrlqletmqKHKAnAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDE-TQKK 2112
Cdd:NF041483 365 QLAKAARTAEEV----------------------LTKA-SEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQaEQLK 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2113 REAEEELK----RKVQAEKEAAREKQRAvedlEKFRSQA-EEAERRMKQAEVEKERQIKVAqevaqQSAAAELNSKRMSF 2187
Cdd:NF041483 422 GAAKDDTKeyraKTVELQEEARRLRGEA----EQLRAEAvAEGERIRGEARREAVQQIEEA-----ARTAEELLTKAKAD 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2188 AEktaqlELSlkqehitvTHLQEEAERLKKlhdeaekareeaekelekwhQKANEALRLRLQAEEVAHKktlAQEEAEKQ 2267
Cdd:NF041483 493 AD-----ELR--------STATAESERVRT--------------------EAIERATTLRRQAEETLER---TRAEAERL 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2268 KEDAEREARK-RAKTEESALRQKELAEdelekqrklaDATAQQKFSAEQELIRLKAETEnseqqrllleeelfrlknevn 2346
Cdd:NF041483 537 RAEAEEQAEEvRAAAERAARELREETE----------RAIAARQAEAAEELTRLHTEAE--------------------- 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2347 eaiQKRKEMEEELAKVRAEMEILlqSKSRAEEESRSNTEKS------KQMLEVEASKLR-ELAEEAAKLRAVSEE-AKRQ 2418
Cdd:NF041483 586 ---ERLTAAEEALADARAEAERI--RREAAEETERLRTEAAerirtlQAQAEQEAERLRtEAAADASAARAEGENvAVRL 660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2419 RQIAEDEAARQRAE----AERILKEKLAAindATRLKTEAEIALKEKEAENERLRRLAEDE-AYQRKLLEEQATQHKQDI 2493
Cdd:NF041483 661 RSEAAAEAERLKSEaqesADRVRAEAAAA---AERVGTEAAEALAAAQEEAARRRREAEETlGSARAEADQERERAREQS 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2494 EEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSD-LELELNQLKNIAEET-QRSKEKAEQEA 2571
Cdd:NF041483 738 EELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEqAEEEIAGLRSAAEHAaERTRTEAQEEA 817
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2572 EKQRQLALEEEQRRKEAEEKVRKILADEKEAA-----RQRKAALEEVERLKAKAEEAKRQkelAEKEAERQIQLA-QEAA 2645
Cdd:NF041483 818 DRVRSDAYAERERASEDANRLRREAQEETEAAkalaeRTVSEAIAEAERLRSDASEYAQR---VRTEASDTLASAeQDAA 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2646 LKKIDAEEKAH---TAIVQQKEQEMLQTRKQEQSILDKLKEEAERAK-RAAEDADFARTRA-EQEAALSRQQVEEAERLK 2720
Cdd:NF041483 895 RTRADAREDANrirSDAAAQADRLIGEATSEAERLTAEARAEAERLRdEARAEAERVRADAaAQAEQLIAEATGEAERLR 974
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2721 QRAeeeAQAKAQAQDEAEKLRKEAE-LEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKtlRQKSQVEQELTKVKLQLEE 2799
Cdd:NF041483 975 AEA---AETVGSAQQHAERIRTEAErVKAEAAAEAERLRTEAREEADRTLDEARKDANK--RRSEAAEQADTLITEAAAE 1049
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2800 TDHQKTLLDEELQRLK---EEVTDAMRQKAQVEEElfkvKIQMEELIKLKLRIE----EENKMLIMKDKDSTQklLVEEA 2872
Cdd:NF041483 1050 ADQLTAKAQEEALRTTteaEAQADTMVGAARKEAE----RIVAEATVEGNSLVEkartDADELLVGARRDATA--IRERA 1123
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2873 EKMR--------QVAEEAARLSIEAQEAARMR-----KLAEDDLANQRALAEKMLKE--------KMQAIQEASRLKAEA 2931
Cdd:NF041483 1124 EELRdritgeieELHERARRESAEQMKSAGERcdalvKAAEEQLAEAEAKAKELVSDanseaskvRIAAVKKAEGLLKEA 1203
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2932 EmlQKQKELAQEqARKFQEDKEQIEQQLAKETegfQKSLEAERRQQLEITAEAERLKlQVLE 2993
Cdd:NF041483 1204 E--QKKAELVRE-AEKIKAEAEAEAKRTVEEG---KRELDVLVRRREDINAEISRVQ-DVLE 1258
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
764-865 |
3.71e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 140.38 E-value: 3.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 764 MTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 843
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1835643837 844 PEDVDVPQPDEKSIITYVSSMY 865
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
649-750 |
2.92e-37 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 137.92 E-value: 2.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 649 VQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR--EKGRMRFHKLQNVQIALDYLKHRQVKLVNI 726
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1835643837 727 RNDDIADGNPKLTLGLIWTIILHF 750
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
645-752 |
4.62e-37 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 137.27 E-value: 4.62e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 645 ERDRVQKKTFTKWVNKHLIKAQ--RHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMRFHKLQNVQIALDYLKHRQVK 722
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1835643837 723 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 752
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
647-748 |
1.06e-36 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 135.98 E-value: 1.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 647 DRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR-EKGRMRFHKLQNVQIALDYLKHRQVKLVN 725
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1835643837 726 IRNDDIADGNPKLTLGLIWTIIL 748
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
749-865 |
6.30e-36 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 134.80 E-value: 6.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 749 HFQISDIQVMGQSEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQA 828
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1835643837 829 FNVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSMY 865
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
768-869 |
1.06e-35 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 133.32 E-value: 1.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 768 EKLLL-WSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 846
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1835643837 847 VDVPQPDEKSIITYVSSMYDAMP 869
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2350-3220 |
2.45e-35 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 150.21 E-value: 2.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2350 QKRKEMEEELAKVRAEMEILlqsksraeEESRSNTEKSKQMLEVEASKlrelAEEAAKLRAVSEEAKRQRQIAE-DEAAR 2428
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRL--------EDILNELERQLKSLERQAEK----AERYKELKAELRELELALLVLRlEELRE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2429 QRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDeaYQRKLLEeqATQHKQDIEEKIILLKKSSDNeL 2508
Cdd:TIGR02168 240 ELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEE--LQKELYA--LANEISRLEQQKQILRERLAN-L 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2509 ERQKNIVEDTLRQRRIIeeeirilkvnfekasvgKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEA 2588
Cdd:TIGR02168 315 ERQLEELEAQLEELESK-----------------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2589 EEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEekahtaiVQQKEQEML 2668
Cdd:TIGR02168 378 EEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE-------LEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2669 QTRKQeqsiLDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKL-------- 2740
Cdd:TIGR02168 451 ELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvls 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2741 -------RKEAELEAAKRAHAEQAALKQKQLADEEMDkhkkfaektlrqkSQVEQELTKVKLqLEETDHQKTLLDEELQR 2813
Cdd:TIGR02168 527 elisvdeGYEAAIEAALGGRLQAVVVENLNAAKKAIA-------------FLKQNELGRVTF-LPLDSIKGTEIQGNDRE 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2814 LKEEVTDAMRQKAQVEEELFKVKIQMEELIklklrieeeNKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAA 2893
Cdd:TIGR02168 593 ILKNIEGFLGVAKDLVKFDPKLRKALSYLL---------GGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITG 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2894 RMRKLAEDDLANQRALAEkmLKEKMQAIQEASR-LKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAketeGFQKSLEA 2972
Cdd:TIGR02168 664 GSAKTNSSILERRREIEE--LEEKIEELEEKIAeLEKALAELRKELEELEEELEQLRKELEELSRQIS----ALRKDLAR 737
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2973 ERRQQLEITAEAERLKLQVLEmsraqakaeedaskFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRR 3052
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTE--------------LEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3053 AIAELEHEKEKLKREAELLQKNSQKMQvAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLyEDEVRKAQKL 3132
Cdd:TIGR02168 804 ALDELRAELTLLNEEAANLRERLESLE-RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNE 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3133 KQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKlEQMEEEHRIALA 3212
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEE-YSLTLEEAEALE 960
|
....*...
gi 1835643837 3213 QTREMRTQ 3220
Cdd:TIGR02168 961 NKIEDDEE 968
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
644-752 |
3.76e-35 |
|
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. This model corresponds to the first CH domain.
Pssm-ID: 409080 Cd Length: 111 Bit Score: 131.97 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 644 DERDRVQKKTFTKWVNKHLIKAQR-HVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMRFHKLQNVQIALDYLKHRQVK 722
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1835643837 723 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 752
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1916-2495 |
4.34e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 148.93 E-value: 4.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1916 QEYVDLRTRYSEL-TTLTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQlaeahakAKAQAEKEAEE 1994
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRL-------ELEELELELEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1995 LQRRMQEEVSKREvvavDAEQQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAE 2074
Cdd:COG1196 286 AQAEEYELLAELA----RLEQDIARLEERRRELEE----RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2075 DELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERrm 2154
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-- 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2155 KQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELE 2234
Cdd:COG1196 436 EEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALL 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2235 KWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKE-----LAEDELEKQRKLADATAQQ 2309
Cdd:COG1196 516 LAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2310 KFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNE-AIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKsk 2388
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA-- 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2389 qmLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERL 2468
Cdd:COG1196 674 --LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
570 580
....*....|....*....|....*..
gi 1835643837 2469 RRLAEDEAYQRKLLEEQATQHKQDIEE 2495
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEA 778
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2254-3010 |
1.53e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 147.98 E-value: 1.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2254 AHKKTLAQEEAEKQKEDAErEARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQElIRLKAETENSEQQRLL 2333
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAE-EAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEE-ARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2334 LEEELFRLKNEVNEAiqKRKEMEEELAKVRAEMEILLQSKSRAEEESR--SNTEKSKQMLEVEASKLRELAEEAAKLRAV 2411
Cdd:PTZ00121 1161 EDARKAEEARKAEDA--KKAEAARKAEEVRKAEELRKAEDARKAEAARkaEEERKAEEARKAEDAKKAEAVKKAEEAKKD 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2412 SEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAE----DEAYQRKLLEEQAT 2487
Cdd:PTZ00121 1239 AEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEkkkaDEAKKKAEEAKKAD 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2488 QHKQDIEEKiillKKSSD---NELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRS- 2563
Cdd:PTZ00121 1319 EAKKKAEEA----KKKADaakKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKAd 1394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2564 --KEKAEQEAEKQRQLALEEEQRRK------EAEEKVR----KILADEKEAARQRKAALEE---VERLKAKAEEAKRQKE 2628
Cdd:PTZ00121 1395 eaKKKAEEDKKKADELKKAAAAKKKadeakkKAEEKKKadeaKKKAEEAKKADEAKKKAEEakkAEEAKKKAEEAKKADE 1474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2629 LAEK--EAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAK--RAAED---ADFARTR 2701
Cdd:PTZ00121 1475 AKKKaeEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADeaKKAEEkkkADELKKA 1554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2702 AEQEAALSRQQVEEAERLKQ-------RAEEEAQAKAQAQDEAEKLRKEAELEAAKRAH-AEQAALKQKQLADEEMDKhk 2773
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEdknmalrKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKkAEEAKIKAEELKKAEEEK-- 1632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2774 kfaeKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEElfkvKIQMEELIKlklRIEEEN 2853
Cdd:PTZ00121 1633 ----KKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED----EKKAAEALK---KEAEEA 1701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2854 KMLimkdkDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAArmRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEM 2933
Cdd:PTZ00121 1702 KKA-----EELKKKEAEEKKKAEELKKAEEENKIKAEEAK--KEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIR 1774
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2934 LQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKK 3010
Cdd:PTZ00121 1775 KEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEK 1851
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2042-2751 |
1.59e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.01 E-value: 1.59e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2042 IEEV----EYNRRKIEEEihivrLQLETMQKHKANAEDELQELRARAEKAEQQKKAA------QEEAERLRKQVKdeTQK 2111
Cdd:COG1196 161 IEEAagisKYKERKEEAE-----RKLEATEENLERLEDILGELERQLEPLERQAEKAeryrelKEELKELEAELL--LLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2112 KREAEEELKRKVQAEKEAAREKQRAVEDLEKfrSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKt 2191
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAE--LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2192 aqlelslkqehitvthLQEEAERLKKLhdeaekareeaekelekwhqkanEALRLRLQAEEVAHKKTLAQEEAEKQKEDA 2271
Cdd:COG1196 311 ----------------RRELEERLEEL-----------------------EEELAELEEELEELEEELEELEEELEEAEE 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2272 EREArKRAKTEESALRQKELAEDELEKQRKLADAtAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQK 2351
Cdd:COG1196 352 ELEE-AEAELAEAEEALLEAEAELAEAEEELEEL-AEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2352 RKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRA 2431
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEG 509
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2432 EAERILKEKLAAIndatrLKTEAEIALKEKEAENERLRRLAEdeayqrkLLEEQATQHKQDIEEKIILLKkssDNELERQ 2511
Cdd:COG1196 510 VKAALLLAGLRGL-----AGAVAVLIGVEAAYEAALEAALAA-------ALQNIVVEDDEVAAAAIEYLK---AAKAGRA 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2512 KNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEK 2591
Cdd:COG1196 575 TFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGE 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2592 VRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTR 2671
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2672 KQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAkaqAQDEAEKLRKE-AELEAAK 2750
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPVNLLAIEEYEE---LEERYDFLSEQrEDLEEAR 811
|
.
gi 1835643837 2751 R 2751
Cdd:COG1196 812 E 812
|
|
| GAS2 |
smart00243 |
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain |
6953-7025 |
5.07e-34 |
|
Growth-Arrest-Specific Protein 2 Domain; GROWTH-ARREST-SPECIFIC PROTEIN 2 Domain
Pssm-ID: 128539 Cd Length: 73 Bit Score: 127.18 E-value: 5.07e-34
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 6953 DQIQDEVNRQVAQCNCTKRFQVEQISANRYRFGESQQLRMVRILRSTLMVRVGGGWIALDEFLVKNDPCRVKG 7025
Cdd:smart00243 1 DKIDDEVKRIVEDCKCPTKFQVEKISEGKYRFGDSQILRLVRILRSTVMVRVGGGWETLDEYLLKHDPCRAKG 73
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
765-865 |
6.76e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 128.29 E-value: 6.76e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 844
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1835643837 845 EDVDVPQPDEKSIITYVSSMY 865
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2398-3073 |
1.07e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 144.31 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2398 LRELAEEAA---KLRAVSEEAKRQRQIAEDEAARqraeAERILKEKLAAINdatRLKTEAEIALKEKEAENERLRRLAED 2474
Cdd:COG1196 157 RRAIIEEAAgisKYKERKEEAERKLEATEENLER----LEDILGELERQLE---PLERQAEKAERYRELKEELKELEAEL 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2475 EAYQRKLLEEQATQHKQDIEEKIILLKkssdnELERQKNIVEDTLRQRRIIEEeirilkvnfekasvgksDLELELNQLK 2554
Cdd:COG1196 230 LLLKLRELEAELEELEAELEELEAELE-----ELEAELAELEAELEELRLELE-----------------ELELELEEAQ 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2555 NIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEA 2634
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2635 ERQIQLAQEAALKKIDAEEKAHTAivQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVE 2714
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALE 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2715 EAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVK 2794
Cdd:COG1196 446 EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2795 LQLEetdhqktLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRieeenkmlimkdkdstqKLLVEEAEK 2874
Cdd:COG1196 526 VAVL-------IGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG-----------------RATFLPLDK 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2875 MRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEkmlkekMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQ 2954
Cdd:COG1196 582 IRARAALAAALARGAIGAAVDLVASDLREADARYYVL------GDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2955 IEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQ 3034
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
650 660 670
....*....|....*....|....*....|....*....
gi 1835643837 3035 TLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQK 3073
Cdd:COG1196 736 ELLEELLEEEELLEEEALEELPEPPDLEELERELERLER 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2547-3214 |
1.45e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.92 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2547 ELE--LNQLKNIAEETQRSKEKAEQEAEKQRQLALeeeQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAK 2624
Cdd:COG1196 197 ELErqLEPLERQAEKAERYRELKEELKELEAELLL---LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2625 RQKELAEKEAERQiQLAQEAALKKIDAEEKAHtAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQ 2704
Cdd:COG1196 274 LELEELELELEEA-QAEEYELLAELARLEQDI-ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2705 EAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKS 2784
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2785 QVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKML------IM 2858
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYegflegVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2859 KDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKmqaiqeASRLKAEAEMLQKQK 2938
Cdd:COG1196 512 AALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAK------AGRATFLPLDKIRAR 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2939 ELAQEQARKFQEDKEQIEQQLAKEtegfqksLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNK 3018
Cdd:COG1196 586 AALAAALARGAIGAAVDLVASDLR-------EADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3019 LHQTELATKermavvqtleiQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQTTFL 3098
Cdd:COG1196 659 GGSLTGGSR-----------RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3099 SEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQL-KVSMdDAMKKQKEAEEnvrrkqdELQQ 3177
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALgPVNL-LAIEEYEELEE-------RYDF 799
|
650 660 670
....*....|....*....|....*....|....*..
gi 1835643837 3178 LDKKRQEqeklLADENRKLREKLEQMEEEHRIALAQT 3214
Cdd:COG1196 800 LSEQRED----LEEARETLEEAIEEIDRETRERFLET 832
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2399-3217 |
5.05e-33 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 142.42 E-value: 5.05e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2399 RELAEEAAKLravseeakrqRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQ 2478
Cdd:pfam02463 169 RKKKEALKKL----------IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2479 RKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTlRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAE 2558
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEE-KEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2559 ETQRSKEKAEQEAEKQRQlalEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQI 2638
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKE---EIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2639 QLAQEAALKKIDAEEKAHtaiVQQKEQEMLQTRKQEQSILDKLKEEAERAKRaAEDADFARTRAEQEAALSRQQVEEAER 2718
Cdd:pfam02463 395 EELELKSEEEKEAQLLLE---LARQLEDLLKEEKKEELEILEEEEESIELKQ-GKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2719 LKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLE 2798
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVI 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2799 ETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQmeelikLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQV 2878
Cdd:pfam02463 551 VEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLP------LKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2879 AEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQ 2958
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2959 LAKETEGFQKSLE------AERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAV 3032
Cdd:pfam02463 705 EQREKEELKKLKLeaeellADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3033 VQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIE 3112
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEIT 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3113 EEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKL-LAD 3191
Cdd:pfam02463 865 KEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELlLEE 944
|
810 820
....*....|....*....|....*.
gi 1835643837 3192 ENRKLREKLEQMEEEHRIALAQTREM 3217
Cdd:pfam02463 945 ADEKEKEENNKEEEEERNKRLLLAKE 970
|
|
| GAS2 |
pfam02187 |
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members ... |
6955-7023 |
1.05e-32 |
|
Growth-Arrest-Specific Protein 2 Domain; The GAR2 domain is common in plakin family members and Gas2 family members. The GAR domain comprises around 57 amino acids and has been shown to bind to microtubules.
Pssm-ID: 460480 Cd Length: 69 Bit Score: 123.48 E-value: 1.05e-32
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 6955 IQDEVNRQVAQCNCTKRFQVEQISANRYRFGESQQLRMVRILRSTLMVRVGGGWIALDEFLVKNDPCRV 7023
Cdd:pfam02187 1 LDDEVRRIVAQCTCPTKFPVEKVGEGKYRFGDSQKLVFVRILRSHVMVRVGGGWDTLEEYLLKHDPCRA 69
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
752-867 |
2.26e-32 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 124.18 E-value: 2.26e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 752 ISDIQvmgqSEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNV 831
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1835643837 832 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSMYDA 867
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-94 |
3.14e-32 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 123.98 E-value: 3.14e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5 MLMPLDQLRAIYELLFREGVMIAKKDkRPQSLHPEIkGVSNLQVIRALGSLKSRGYVRETFVWRHFYWYLNNEGIVYLRQ 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKD-PKGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90
....*....|
gi 1835643837 85 YLHLPPEIVP 94
Cdd:PTZ00034 80 YLHLPPDVFP 89
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
642-753 |
4.35e-32 |
|
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409160 Cd Length: 124 Bit Score: 123.72 E-value: 4.35e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 642 AED-ERDRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGR--MRFHKLQNVQIALDYLKH 718
Cdd:cd21311 7 AEDaQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEE 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 1835643837 719 RQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 753
Cdd:cd21311 87 DEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2047-2926 |
9.68e-32 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 138.27 E-value: 9.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2047 YNRRKIEEEihivrLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQ---------EEAER--LRKQVKDETQKKREA 2115
Cdd:TIGR02168 170 YKERRKETE-----RKLERTRENLDRLEDILNELERQLKSLERQAEKAErykelkaelRELELalLVLRLEELREELEEL 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2116 EEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRM--KQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ 2193
Cdd:TIGR02168 245 QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeeLQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2194 LELSLKQEhitvTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEV--AHKKTLAQEEAEKQKEDA 2271
Cdd:TIGR02168 325 LEELESKL----DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQleTLRSKVAQLELQIASLNN 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2272 EREaRKRAKTEESALRQKELAEDELEKQRKLADAtaqQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQK 2351
Cdd:TIGR02168 401 EIE-RLEARLERLEDRRERLQQEIEELLKKLEEA---ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2352 RKEMEEELAKVRAEMEILLQSKSRAEEESRS--NTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIA----EDE 2425
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvveNLN 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2426 AARQRAEAeriLKEklaaiNDATRLKTEAEIALKEKEAENERLRRLAEDEAYQR--KLLEEQATQHKQDIEEKI--ILLK 2501
Cdd:TIGR02168 557 AAKKAIAF---LKQ-----NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLggVLVV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2502 KSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELElnqlKNIAEETQRSKEKAEQEAEKQRQLAlEE 2581
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERR----REIEELEEKIEELEEKIAELEKALA-EL 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2582 EQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQ 2661
Cdd:TIGR02168 704 RKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2662 QKEQEMLQTRKQEQ-----SILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDE 2736
Cdd:TIGR02168 784 IEELEAQIEQLKEElkalrEALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2737 AEKLRKEAELEAakrahaeQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKE 2816
Cdd:TIGR02168 864 LEELIEELESEL-------EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEV 936
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2817 EVtdaMRQKAQVEEElfkVKIQMEELIKLKLRIEEEnkmlIMKDKDStQKLLVEEAEKMRQVAEEAarlsIEAQEAARMR 2896
Cdd:TIGR02168 937 RI---DNLQERLSEE---YSLTLEEAEALENKIEDD----EEEARRR-LKRLENKIKELGPVNLAA----IEEYEELKER 1001
|
890 900 910
....*....|....*....|....*....|
gi 1835643837 2897 KlaeDDLANQRALAEKMLKEKMQAIQEASR 2926
Cdd:TIGR02168 1002 Y---DFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2678-3225 |
1.15e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 137.76 E-value: 1.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2678 LDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQdEAEKLRKEAELEAAKRAHAE-- 2755
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEEL-EAELAELEAELEELRLELEEle 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2756 ---QAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEEL 2832
Cdd:COG1196 281 lelEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2833 FKVKIQMEELIKLKLRIEEEnkmlimkdkdsTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEK 2912
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEE-----------LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEA 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2913 MLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEgfQKSLEAERRQQLEITAEAERLKLQVL 2992
Cdd:COG1196 430 LAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE--LLEELAEAAARLLLLLEAEADYEGFL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2993 EMSRAQAKAEEDASKFKKKAEEIGnklhqteLATKERMAVVQTLEIQRQQSGkeAEELRRAIAELEHEKEKLKREAELLQ 3072
Cdd:COG1196 508 EGVKAALLLAGLRGLAGAVAVLIG-------VEAAYEAALEAALAAALQNIV--VEDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3073 KNSQKMQVAQQEQLRQETqvlqttfLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKV 3152
Cdd:COG1196 579 LDKIRARAALAAALARGA-------IGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3153 SMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDLA 3225
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEE 724
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
644-748 |
1.34e-31 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 123.62 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 644 DERDRVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR-EKGRMRFHKLQNVQIALDYLKHRQVK 722
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
|
90 100
....*....|....*....|....*.
gi 1835643837 723 LVNIRNDDIADGNPKLTLGLIWTIIL 748
Cdd:cd21316 128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
768-869 |
2.16e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 120.83 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 768 EKLLL-WSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 846
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1835643837 847 VDVPQPDEKSIITYVSSMYDAMP 869
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2262-2939 |
2.34e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 136.61 E-value: 2.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2262 EEAEKQKEDAEREARKrakteesALRQKELAEDELEKQRKLAdatAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRL 2341
Cdd:COG1196 196 GELERQLEPLERQAEK-------AERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQmlevEASKLRELAEEAAKLRAVSEEAKRQRQi 2421
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELE- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2422 aedEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLK 2501
Cdd:COG1196 341 ---ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2502 KSSDNELERQKNIVEDtlrqrriieeeirilkvnfekasvgksDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEE 2581
Cdd:COG1196 418 RLEEELEELEEALAEL---------------------------EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2582 EQRRKEAEEKVrkiLADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEaalkkIDAEEKAHTAIVQ 2661
Cdd:COG1196 471 EAALLEAALAE---LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL-----IGVEAAYEAALEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2662 QKEQEMLQtrkqeqsildKLKEEAERAKRAAEDAdfartraeQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLR 2741
Cdd:COG1196 543 ALAAALQN----------IVVEDDEVAAAAIEYL--------KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2742 KEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDA 2821
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2822 MRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQvAEEAARLSIEAQEAARMRKLAED 2901
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEE-LLEEEELLEEEALEELPEPPDLE 763
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1835643837 2902 DLANQRALAEKMLKEK----MQAIQEASRLKAEAEMLQKQKE 2939
Cdd:COG1196 764 ELERELERLEREIEALgpvnLLAIEEYEELEERYDFLSEQRE 805
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
649-752 |
3.35e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 120.47 E-value: 3.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 649 VQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR--EKGRMRFHKLQNVQIALDYLKHRQVKLVNI 726
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1835643837 727 RNDDIADGNPKLTLGLIWTIILHFQI 752
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2142-2825 |
5.78e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 135.45 E-value: 5.78e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2142 KFRSQAEEAERRMKQAE----------VEKERQIKvaqEVAQQSAAAELnSKRMSFAEKTAQLELSLKQEHitvtHLQEE 2211
Cdd:COG1196 169 KYKERKEEAERKLEATEenlerledilGELERQLE---PLERQAEKAER-YRELKEELKELEAELLLLKLR----ELEAE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2212 AERLKKLHDeaekareeaekelekwhqkANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKrakteeSALRQKEL 2291
Cdd:COG1196 241 LEELEAELE-------------------ELEAELEELEAELAELEAELEELRLELEELELELEEAQ------AEEYELLA 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2292 AEDELEKQRKLADATAQQkfsAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEmeiLLQ 2371
Cdd:COG1196 296 ELARLEQDIARLEERRRE---LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA---LLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2372 SKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLK 2451
Cdd:COG1196 370 AEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAE 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2452 TEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRI 2531
Cdd:COG1196 450 EEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVL 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2532 LKVNFEKASVgksDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKilADEKEAARQRKAALE 2611
Cdd:COG1196 530 IGVEAAYEAA---LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALA--AALARGAIGAAVDLV 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2612 EVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRA 2691
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2692 AEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDK 2771
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2772 HKKFAEKTLRQKSQ-------VEQELTKVKLQLEETDHQKTLLDEELQRLK---EEVTDAMRQK 2825
Cdd:COG1196 765 LERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREDLEEARETLEeaiEEIDRETRER 828
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
764-862 |
6.34e-31 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 119.84 E-value: 6.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 764 MTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 843
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1835643837 844 PEDVDVPQPDEKSIITYVS 862
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
649-752 |
7.71e-31 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 119.34 E-value: 7.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 649 VQKKTFTKWVNKHLIKAQR-HVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMRFHKLQNVQIALDYLKHRQVKLVNIR 727
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1835643837 728 NDDIADGNPKLTLGLIWTIILHFQI 752
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
768-870 |
1.64e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.88 E-value: 1.64e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 768 EKLLL-WSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTN-LENLDQAFNVAERDLGVTRLLDPE 845
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1835643837 846 DVDVPQPDEKSIITYVSSMYDAMPR 870
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1940-2739 |
1.76e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 134.03 E-value: 1.76e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1940 TETLRRLNDEEKAAEKL-----KEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEevskrevvavdAE 2014
Cdd:TIGR02168 212 AERYKELKAELRELELAllvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2015 QQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAA 2094
Cdd:TIGR02168 281 EEIEELQKELYALAN----EISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2095 QEEAERLRKQVKDETQKKREAEEELKRkvQAEKEAAREKQravedLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQ 2174
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLET--LRSKVAQLELQ-----IASLNNEIERLEARLERLEDRRERLQQEIEELLKK 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2175 SAAAELNSKRMSFAEKTAQLElSLKQEHITVthlQEEAERLKKLHDEAEKAREEAEKELEKWHQKAN--EALRLRLQ--- 2249
Cdd:TIGR02168 430 LEEAELKELQAELEELEEELE-ELQEELERL---EEALEELREELEEAEQALDAAERELAQLQARLDslERLQENLEgfs 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2250 ---AEEVAHKKTLA------------QEEAEKQKEDAEREARKRA--KTEESALRQKE-LAEDELEKQRKLADATAQQKF 2311
Cdd:TIGR02168 506 egvKALLKNQSGLSgilgvlselisvDEGYEAAIEAALGGRLQAVvvENLNAAKKAIAfLKQNELGRVTFLPLDSIKGTE 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2312 SAEQELIRLKAETENSEQQRLLLEEELFRLK------------NEVNEAIQKRKEMEEELAKVRAEMEIL----LQSKSR 2375
Cdd:TIGR02168 586 IQGNDREILKNIEGFLGVAKDLVKFDPKLRKalsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVrpggVITGGS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2376 AEEESrSNTEKSKQMLEVEAsKLRELAEEAAKLRAVSEEAKRQRQIAEDEaarqraeaeriLKEKLAAINDATRLKTEAE 2455
Cdd:TIGR02168 666 AKTNS-SILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEE-----------LEQLRKELEELSRQISALR 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2456 IALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKkssdnELERQKNIVEDTLRQrriieeeiriLKVN 2535
Cdd:TIGR02168 733 KDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----EAEAEIEELEAQIEQ----------LKEE 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2536 FEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKI---LADEKEAARQRKAALEE 2612
Cdd:TIGR02168 798 LKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESELEA 877
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2613 VERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQeMLQTRKQEQSILDKLKEE----AERA 2688
Cdd:TIGR02168 878 LLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELR-LEGLEVRIDNLQERLSEEysltLEEA 956
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 2689 KRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEK 2739
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTA 1007
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
770-865 |
2.04e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 118.22 E-value: 2.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 770 LLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED-VD 848
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1835643837 849 VPQPDEKSIITYVSSMY 865
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1916-2686 |
2.05e-30 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 134.03 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1916 QEYVDLRTRYSELT-TLTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLakqtqlaEAHAKAKAQAEKEAEE 1994
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKL-------EELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1995 LQRRMQEEVSKREvvavDAEQQKQTIQQELQQLRQNsdmeIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAE 2074
Cdd:TIGR02168 286 LQKELYALANEIS----RLEQQKQILRERLANLERQ----LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2075 DELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRM 2154
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2155 KQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHIT---VTHLQEEAERLKKLHDEAEKAREEAEK 2231
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLqarLDSLERLQENLEGFSEGVKALLKNQSG 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2232 EL-------------EKWHQKANEALRLRLQA-----EEVAHKKTLAQEEAEKQK-----EDAEREARKRAKTEESALRQ 2288
Cdd:TIGR02168 518 LSgilgvlselisvdEGYEAAIEAALGGRLQAvvvenLNAAKKAIAFLKQNELGRvtflpLDSIKGTEIQGNDREILKNI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2289 KELAE--DELEKQRK------------------LADATAQQK--------FSAEQELIR------------------LKA 2322
Cdd:TIGR02168 598 EGFLGvaKDLVKFDPklrkalsyllggvlvvddLDNALELAKklrpgyriVTLDGDLVRpggvitggsaktnssileRRR 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2323 ETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELA 2402
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2403 EEAAklravsEEAKRQRQIAEDEAARQRAEAERilkEKLAAinDATRLKTEAEIALKEKEAENERLRRLAEDEAyqrkll 2482
Cdd:TIGR02168 758 ELEA------EIEELEERLEEAEEELAEAEAEI---EELEA--QIEQLKEELKALREALDELRAELTLLNEEAA------ 820
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2483 eeQATQHKQDIEEKIILLKKSsdnelerqkniVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQR 2562
Cdd:TIGR02168 821 --NLRERLESLERRIAATERR-----------LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2563 SKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKiLADEKEAARQRKAALE-EVERLKAK-----------AEEAKRQKELA 2630
Cdd:TIGR02168 888 ALALLRSELEELSEELRELESKRSELRRELEE-LREKLAQLELRLEGLEvRIDNLQERlseeysltleeAEALENKIEDD 966
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2631 EKEAERQIQLAQE----------AALKKIDAEEKAHTAIVQQKEqEMLQTRKQEQSILDKLKEEAE 2686
Cdd:TIGR02168 967 EEEARRRLKRLENkikelgpvnlAAIEEYEELKERYDFLTAQKE-DLTEAKETLEEAIEEIDREAR 1031
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1913-2856 |
2.26e-30 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 133.94 E-value: 2.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1913 SIIQEYVDLRTRYSELTTLTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEA 1992
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1993 EELQRRMQEEVSKrevvavdaEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKAN 2072
Cdd:pfam02463 243 QELLRDEQEEIES--------SKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2073 AEDELQELRARAEKAEQQKKAAQEEAErlrkQVKDETQKKREAEEElkRKVQAEKEAAREKQRAVEDLEKFRSQAEEAER 2152
Cdd:pfam02463 315 KLKESEKEKKKAEKELKKEKEEIEELE----KELKELEIKREAEEE--EEEELEKLQEKLEQLEEELLAKKKLESERLSS 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2153 RMKQAEVEKERQIKVAQEVaqqSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKE 2232
Cdd:pfam02463 389 AAKLKEEELELKSEEEKEA---QLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2233 LEKwhQKANEALRLRLQAEEVAHKKtLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFS 2312
Cdd:pfam02463 466 ELK--KSEDLLKETQLVKLQEQLEL-LLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2313 AEQELirlkaetenseqqrllleeelfrlkNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLE 2392
Cdd:pfam02463 543 VAIST-------------------------AVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2393 VEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLA 2472
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE 677
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2473 EDEAYQRKLLEEQATQHKQDIEEKIillKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQ 2552
Cdd:pfam02463 678 IQELQEKAESELAKEEILRRQLEIK---KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2553 LKNIAEETQRSKEKAEQEaEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEK 2632
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLK-EKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEE 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2633 EAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADfARTRAEQEAALSRQQ 2712
Cdd:pfam02463 834 ELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE-EKKELEEESQKLNLL 912
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2713 VEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKrahAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVE----- 2787
Cdd:pfam02463 913 EEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEK---EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEekeer 989
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2788 ---QELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAqveeELFKVKIQMEELIKLKLRIEEENKML 2856
Cdd:pfam02463 990 ynkDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINK----GWNKVFFYLELGGSAELRLEDPDDPF 1057
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
645-754 |
2.63e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 118.07 E-value: 2.63e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 645 ERDRVQKKTFTKWVNKHLIKAQR--HVSDLYEDLRDGHNLISLLEVLSGDNLPRE--KGRMRFHKLQNVQIALDYLKHRQ 720
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1835643837 721 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 754
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
764-862 |
2.94e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.01 E-value: 2.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 764 MTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 843
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1835643837 844 PEDVDVPQPDEKSIITYVS 862
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2262-3078 |
3.43e-29 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 129.79 E-value: 3.43e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2262 EEAEKQKEDAEREARKrakteesALRQKELAEDELEKQRKLAdatAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRL 2341
Cdd:TIGR02168 196 NELERQLKSLERQAEK-------AERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEE------ESRSNTEKSKQMLEVE----ASKLRELAEEAAKLRAV 2411
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQqkqilrERLANLERQLEELEAQleelESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2412 SEEAKRQRQ---IAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQ 2488
Cdd:TIGR02168 346 LEELKEELEsleAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2489 HKQDIEEKiilLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAE 2568
Cdd:TIGR02168 426 LLKKLEEA---ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2569 QEAEKQRQLALEEEQR---------RKEAEEKVRK------------ILADEKEAARQRKAALEEVERLKAKAEEAKRQK 2627
Cdd:TIGR02168 503 GFSEGVKALLKNQSGLsgilgvlseLISVDEGYEAaieaalggrlqaVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2628 ELAEKEAERQIQLAQEAALKKIDAEEKAHTAIvqqkeQEMLQTRKQEQSILDKLKEEAERAKRAAED------------A 2695
Cdd:TIGR02168 583 GTEIQGNDREILKNIEGFLGVAKDLVKFDPKL-----RKALSYLLGGVLVVDDLDNALELAKKLRPGyrivtldgdlvrP 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2696 DFARTRAEQEAALS----RQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDK 2771
Cdd:TIGR02168 658 GGVITGGSAKTNSSilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2772 HKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELiKLKLRIEE 2851
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLN 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2852 ENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEA 2931
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2932 EMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKsLEAERRQQLEITAEAERLKLQVLEmsRAQAKAEEDASKFKKK 3011
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEEAE--ALENKIEDDEEEARRR 973
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 3012 AEEIGNKLhqtelatkERMAVVQTLEIQrqqsgkEAEELRRAIAELEHEKEKLKREAELLQKNSQKM 3078
Cdd:TIGR02168 974 LKRLENKI--------KELGPVNLAAIE------EYEELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
750-867 |
3.90e-29 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 115.18 E-value: 3.90e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 750 FQISDIQVmgqsEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAF 829
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1835643837 830 NVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSMYDA 867
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2423-3225 |
8.73e-29 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 128.55 E-value: 8.73e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2423 EDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQAtqhkqdiEEKIILLKK 2502
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQA-------KKALEYYQL 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2503 SSDNELERQKNIVEDTLrqrriiEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEE 2582
Cdd:pfam02463 216 KEKLELEEEYLLYLDYL------KLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2583 QRRKEAEEKVRkiladEKEAARQRKAALEEverlKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQ 2662
Cdd:pfam02463 290 LLAKEEEELKS-----ELLKLERRKVDDEE----KLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2663 KEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADfartraeqeaalsrQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRK 2742
Cdd:pfam02463 361 LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE--------------EELELKSEEEKEAQLLLELARQLEDLLKEEKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2743 EAELEAAkrahaEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAM 2822
Cdd:pfam02463 427 EELEILE-----EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQK 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2823 RQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLS---IEAQEAARMRKLA 2899
Cdd:pfam02463 502 ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKlvrALTELPLGARKLR 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2900 EDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK--ELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQ 2977
Cdd:pfam02463 582 LLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKraKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEK 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2978 LEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQ-------RQQSGKEAEEL 3050
Cdd:pfam02463 662 SEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLadrvqeaQDKINEELKLL 741
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3051 RRAIAELEHEKEKLKREAELLQknsQKMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQ 3130
Cdd:pfam02463 742 KQKIDEEEEEEEKSRLKKEEKE---EEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3131 KLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIA 3210
Cdd:pfam02463 819 EEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEE 898
|
810
....*....|....*
gi 1835643837 3211 LAQTREMRTQTDDLA 3225
Cdd:pfam02463 899 KKELEEESQKLNLLE 913
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
768-867 |
1.38e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 112.76 E-value: 1.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 768 EKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED- 846
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1835643837 847 VDVPQPDEKSIITYVSSMYDA 867
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
648-750 |
1.90e-28 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 112.57 E-value: 1.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 648 RVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR---EKGRMRFHKLQNVQIALDYLKHRQVKLV 724
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1835643837 725 NIRNDDIADGNPKLTLGLIWTIILHF 750
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1998-3079 |
2.55e-28 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 126.83 E-value: 2.55e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1998 RMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAkQIEEVEYNRRKIEEEIHIVRLQLETmqkHKANAEDEL 2077
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKN-ALQEQLQAETELCAEAEEMRARLAA---RKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2078 QELRARAEKAEQQKKAAQEEAERLRKQVKDeTQKKREAEEELKRKVQAEKEAAREKQRAVEdlEKFRSQAEEAERRMKQA 2157
Cdd:pfam01576 78 HELESRLEEEEERSQQLQNEKKKMQQHIQD-LEEQLDEEEAARQKLQLEKVTTEAKIKKLE--EDILLLEDQNSKLSKER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2158 EVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKT-AQLELSLKQEHITvthlQEEAERLKKLHDEAEKAREEAEKELekw 2236
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEEKG----RQELEKAKRKLEGESTDLQEQIAEL--- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2237 hQKANEALRLRLQAEEVAHKKTLAQ-EEAEKQKEDAEREARkrakteESALRQKELAEDeLEKQRKLADATAQQKFSAEQ 2315
Cdd:pfam01576 228 -QAQIAELRAQLAKKEEELQAALARlEEETAQKNNALKKIR------ELEAQISELQED-LESERAARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2316 ELIRLKAETENSEQQRLLLEEELFRLKNEVNEAiqkRKEMEEELAKVRAEMEILLQSKSRAEEE----------SRSNTE 2385
Cdd:pfam01576 300 ELEALKTELEDTLDTTAAQQELRSKREQEVTEL---KKALEEETRSHEAQLQEMRQKHTQALEElteqleqakrNKANLE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2386 KSKQMLEVEASKLrelaeeAAKLRAVSEeakrqrqiAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAEN 2465
Cdd:pfam01576 377 KAKQALESENAEL------QAELRTLQQ--------AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2466 ERLRR-LAEDEAYQRKLLEEQAT--QHKQDIEEkiiLLKkssdnELERQKNIVEDTLRQrriieeeirilkvnfekasvg 2542
Cdd:pfam01576 443 ESVSSlLNEAEGKNIKLSKDVSSleSQLQDTQE---LLQ-----EETRQKLNLSTRLRQ--------------------- 493
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2543 ksdLELELNQLKNIAEETQRSKEKAEQEAEK-QRQLA-----LEEEQRRKEAEEKVRKILADEKEAARQRkaaLEEVERL 2616
Cdd:pfam01576 494 ---LEDERNSLQEQLEEEEEAKRNVERQLSTlQAQLSdmkkkLEEDAGTLEALEEGKKRLQRELEALTQQ---LEEKAAA 567
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2617 KAKAEEAKR--QKEL----AEKEAERQIQLAQEAALKKID---AEEKAHTA-IVQQKEQEMLQTRKQEQSILdKLKEEAE 2686
Cdd:pfam01576 568 YDKLEKTKNrlQQELddllVDLDHQRQLVSNLEKKQKKFDqmlAEEKAISArYAEERDRAEAEAREKETRAL-SLARALE 646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2687 RAKRAAEDADFART--RAEQEAALSRQ-----QVEEAERLKQRAEEEAQA-KAQAQD--------EAEKLRKEAELEAAK 2750
Cdd:pfam01576 647 EALEAKEELERTNKqlRAEMEDLVSSKddvgkNVHELERSKRALEQQVEEmKTQLEEledelqatEDAKLRLEVNMQALK 726
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2751 RAHAeqaalKQKQLADEEMDKHKKFAEKTLRqksQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEE 2830
Cdd:pfam01576 727 AQFE-----RDLQARDEQGEEKRRQLVKQVR---ELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVK 798
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2831 ELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMrQVAEEAARLSIEAQEAARMRKLAEDDLANQRALA 2910
Cdd:pfam01576 799 QLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGK 877
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2911 EKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAerRQQLEITAEAERLKLQ 2990
Cdd:pfam01576 878 SALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESA--RQQLERQNKELKAKLQ 955
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2991 VLE----------MSRAQAK---AEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAEL 3057
Cdd:pfam01576 956 EMEgtvkskfkssIAALEAKiaqLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQL 1035
|
1130 1140
....*....|....*....|..
gi 1835643837 3058 EHEKEKLKREAELLQKNSQKMQ 3079
Cdd:pfam01576 1036 KRQLEEAEEEASRANAARRKLQ 1057
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
752-867 |
5.95e-28 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 112.10 E-value: 5.95e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 752 ISDIQVmgqsEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNV 831
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1835643837 832 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSMYDA 867
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
752-867 |
6.06e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 109.04 E-value: 6.06e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 752 ISDIQVmgqsEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNV 831
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1835643837 832 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSMYDA 867
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2605-3216 |
9.07e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 122.56 E-value: 9.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2605 QRKAALEEVERLKAKAEE---AKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEmlQTRKQEQSildkl 2681
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDfdfDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE--DARKAEEA----- 1133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2682 kEEAERAKRAAEdadfARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKq 2761
Cdd:PTZ00121 1134 -RKAEDARKAEE----ARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK- 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2762 kqlADEEmdkhKKFAEKTLRQKSQVEQELTKVklqleetdhqktlldEELQRLKEEVTDAMRQKAQVEEELFKvKIQMEE 2841
Cdd:PTZ00121 1208 ---AEEE----RKAEEARKAEDAKKAEAVKKA---------------EEAKKDAEEAKKAEEERNNEEIRKFE-EARMAH 1264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2842 LIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQV--AEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQ 2919
Cdd:PTZ00121 1265 FARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkkADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2920 AIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQqLAKETEGFQKSLEAERRqqleitaeAERLKLQVLEMSRAQA 2999
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKK--------AEEDKKKADELKKAAA 1415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3000 kAEEDASKFKKKAEEIGNKLHQTELATKERMAvvqtleiqrQQSGKEAEELRRAiaELEHEKEKLKREAELLQKNSQKMQ 3079
Cdd:PTZ00121 1416 -AKKKADEAKKKAEEKKKADEAKKKAEEAKKA---------DEAKKKAEEAKKA--EEAKKKAEEAKKADEAKKKAEEAK 1483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3080 VAQQEQLRQEtqvlqttflsEKQLLLEREKYIEEEKAKlenlyEDEVRKAQKLKQEQE---------------------- 3137
Cdd:PTZ00121 1484 KADEAKKKAE----------EAKKKADEAKKAAEAKKK-----ADEAKKAEEAKKADEakkaeeakkadeakkaeekkka 1548
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 3138 HQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTRE 3216
Cdd:PTZ00121 1549 DELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK 1627
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-112 |
3.10e-26 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 106.16 E-value: 3.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5 MLMPLDQLRAIYELLFREGVMIAKKDKRpQSLHPEIkGVSNLQVIRALGSLKSRGYVRETFVWRHFYWYLNNEGIVYLRQ 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|....*...
gi 1835643837 85 YLHLPPEIVPGSLQRVRRPVAMviPARR 112
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQR--PQRR 104
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2116-3223 |
3.32e-26 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 119.89 E-value: 3.32e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2116 EEELKRKvqaekeaAREKQRAVEDLEKFRSQAEEAERrmKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLE 2195
Cdd:pfam01576 4 EEEMQAK-------EEELQKVKERQQKAESELKELEK--KHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQELE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2196 LSLkqeHITVTHLQEEAERLKKLHDEAEKAREEAEKELEkwHQKANEALRLRLQAEEV-AHKKTLAQEEAEKQKEDAERE 2274
Cdd:pfam01576 75 EIL---HELESRLEEEEERSQQLQNEKKKMQQHIQDLEE--QLDEEEAARQKLQLEKVtTEAKIKKLEEDILLLEDQNSK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2275 ARKRAKTEESALRQ--KELAEDElEKQRKLADATAQQKFSAEQELIRLKAEtENSEQQRLLLEEELFRLKNEVNEAIQKR 2352
Cdd:pfam01576 150 LSKERKLLEERISEftSNLAEEE-EKAKSLSKLKNKHEAMISDLEERLKKE-EKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2353 KEMEEELAKVRAEMEILLQS-KSRAEEESRSNTEKSKQMLEVEAsKLRELAEEAAKLRAVSEEAKRQRqiaedeaarqra 2431
Cdd:pfam01576 228 QAQIAELRAQLAKKEEELQAaLARLEEETAQKNNALKKIRELEA-QISELQEDLESERAARNKAEKQR------------ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2432 eaeRILKEKLAAindatrLKTEAEIALKEKEAENErLRRLAEDEAYQ-RKLLEEQATQHKQDIEEkiilLKKSSDNELER 2510
Cdd:pfam01576 295 ---RDLGEELEA------LKTELEDTLDTTAAQQE-LRSKREQEVTElKKALEEETRSHEAQLQE----MRQKHTQALEE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2511 QKNIVEDTLRQrriieeeirilKVNFEKAsvgKSDLELELNQLKNIAEETQRSKekaeqeaekqrqlaLEEEQRRKEAEE 2590
Cdd:pfam01576 361 LTEQLEQAKRN-----------KANLEKA---KQALESENAELQAELRTLQQAK--------------QDSEHKRKKLEG 412
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2591 KVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEA----------ERQIQLAQE----------AALKKID 2650
Cdd:pfam01576 413 QLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNiklskdvsslESQLQDTQEllqeetrqklNLSTRLR 492
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2651 AEEKAHTAIVQQKEQEMLQTRKQEQSI------LDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAE 2724
Cdd:pfam01576 493 QLEDERNSLQEQLEEEEEAKRNVERQLstlqaqLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE 572
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2725 eeaQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKV---KLQLEETD 2801
Cdd:pfam01576 573 ---KTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAlslARALEEAL 649
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2802 HQKTLLDEELQRLKEEVTDAM--------------RQKAQVEEELFKVKIQMEELI-------KLKLRIEEENKMLIMKD 2860
Cdd:pfam01576 650 EAKEELERTNKQLRAEMEDLVsskddvgknvheleRSKRALEQQVEEMKTQLEELEdelqateDAKLRLEVNMQALKAQF 729
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2861 KDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAeddLANQRALaEKMLKEKMQAIQEASRLKAEAemlQKQKEL 2940
Cdd:pfam01576 730 ERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQA---VAAKKKL-ELDLKELEAQIDAANKGREEA---VKQLKK 802
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2941 AQEQARKFQEDKEQIEQQ------LAKETEGFQKSLEAERRQQLEITAEAERLklqvlemsRAQAKAEEDaskfkkkaee 3014
Cdd:pfam01576 803 LQAQMKDLQRELEEARASrdeilaQSKESEKKLKNLEAELLQLQEDLAASERA--------RRQAQQERD---------- 864
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3015 ignklhqtELATkermavvqtlEIQRQQSGKEA--EELRR---AIAELEHEKEKLKREAELLQKNSQKMQVaQQEQLRQE 3089
Cdd:pfam01576 865 --------ELAD----------EIASGASGKSAlqDEKRRleaRIAQLEEELEEEQSNTELLNDRLRKSTL-QVEQLTTE 925
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3090 TQVLQTTFLSEKQLLLEREKYIEEEKAKLENLyEDEVRKAQKLkqeqehQMKHLEEEKDQLKVSMDDAMKKQKEAEENVR 3169
Cdd:pfam01576 926 LAAERSTSQKSESARQQLERQNKELKAKLQEM-EGTVKSKFKS------SIAALEAKIAQLEEQLEQESRERQAANKLVR 998
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 3170 RKQDELQQL-----DKKRQ-EQEKLLADEN----RKLREKLEQMEEEHRIALAQTREMRTQTDD 3223
Cdd:pfam01576 999 RTEKKLKEVllqveDERRHaDQYKDQAEKGnsrmKQLKRQLEEAEEEASRANAARRKLQRELDD 1062
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
648-750 |
6.16e-26 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 105.65 E-value: 6.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 648 RVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR---EKGRMRFHKLQNVQIALDYLKHRQVKLV 724
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1835643837 725 NIRNDDIADGNPKLTLGLIWTIILHF 750
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
1396-1461 |
1.70e-25 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 102.73 E-value: 1.70e-25
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 1396 LKPRStaHPVRGKLPLQAVCDYKQMEITVHKGDECLLLNNSQPYKWKVLNASGSESIVPSVCFLIP 1461
Cdd:pfam17902 2 LKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
752-867 |
1.80e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 104.77 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 752 ISDIQVmgqsEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNV 831
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1835643837 832 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSMYDA 867
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
770-865 |
1.88e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 104.16 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 770 LLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED-VD 848
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1835643837 849 VPQPDEKSIITYVSSMY 865
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
648-753 |
2.56e-25 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 104.34 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 648 RVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPRE---KGRMRFHKLQNVQIALDYLKHRQVKLV 724
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1835643837 725 NIRNDDIADGNPKLTLGLIWTIILHFQIS 753
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2242-3167 |
6.78e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 115.84 E-value: 6.78e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2242 EALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLK 2321
Cdd:pfam02463 161 EAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERID 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2322 AETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEElAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLREL 2401
Cdd:pfam02463 241 LLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEE-EKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKES 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2402 AEEAAKLravsEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKL 2481
Cdd:pfam02463 320 EKEKKKA----EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEE 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2482 LEEQATQHKQDIEEKIILLKKSSDNELERQK---NIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAE 2558
Cdd:pfam02463 396 ELELKSEEEKEAQLLLELARQLEDLLKEEKKeelEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2559 ETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQI 2638
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2639 QLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEA---ERAKRAAEDADFARTRAE--QEAALSRQQV 2713
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPIlnlAQLDKATLEADEDDKRAKvvEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2714 EEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKV 2793
Cdd:pfam02463 636 KLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2794 KLQLEETDHQKTLLDEELQRLKEEVTDaMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAE 2873
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLK-QKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEE 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2874 KMRQVAEEaarlsieaqEAARMRKLAEDDLANQRALAEKMLKEKMQaIQEASRLKAEAEMLQKQKELAQEQARkFQEDKE 2953
Cdd:pfam02463 795 KLKAQEEE---------LRALEEELKEEAELLEEEQLLIEQEEKIK-EEELEELALELKEEQKLEKLAEEELE-RLEEEI 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2954 QIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEmsraqakaeedaskfkkKAEEIGNKLHQTELATKERMAvv 3033
Cdd:pfam02463 864 TKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELE-----------------EESQKLNLLEEKENEIEERIK-- 924
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3034 qtleiqrqQSGKEAEELRRAIAELEHEKEKLKREAELLQKnsqkmqvaQQEQLRQ--ETQVLQTTFLSEKQLLLEREKYI 3111
Cdd:pfam02463 925 --------EEAEILLKYEEEPEELLLEEADEKEKEENNKE--------EEEERNKrlLLAKEELGKVNLMAIEEFEEKEE 988
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 3112 EEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEEN 3167
Cdd:pfam02463 989 RYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGG 1044
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2342-3225 |
1.00e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 115.31 E-value: 1.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEELAKVRAEMEILLQSksRAEEESRSNTEkskqmLEVEA-SKLRELAEEAAKLRA-VSEEAKRQR 2419
Cdd:NF041483 79 RNAQIQADQLRADAERELRDARAQTQRILQE--HAEHQARLQAE-----LHTEAvQRRQQLDQELAERRQtVESHVNENV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2420 QIAEDEAARQRAEAERILKEKlaaindatrlKTEAEIALKEKEAENERLrrlaEDEAYQRKLLEEQATQHkqdiEEKIIL 2499
Cdd:NF041483 152 AWAEQLRARTESQARRLLDES----------RAEAEQALAAARAEAERL----AEEARQRLGSEAESARA----EAEAIL 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2500 LKkssdnelerqknivedtlrqrriieeeirilkvnfekasvGKSDLELELNQLKNIAEETQ------RSKEKAEQEAEK 2573
Cdd:NF041483 214 RR----------------------------------------ARKDAERLLNAASTQAQEATdhaeqlRSSTAAESDQAR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2574 QR--QLALEEEQRRKEAEEKVRKILAdekEAARQRKAALEEVERLKAKAEEAKRQKELAEKEaerqiQLAQeaalkkida 2651
Cdd:NF041483 254 RQaaELSRAAEQRMQEAEEALREARA---EAEKVVAEAKEAAAKQLASAESANEQRTRTAKE-----EIAR--------- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2652 eekahtaIVQQKEQEMLQTRKQEQSILDKLKEEAEraKRAAEDADFARTR-AEQEAALSRQQVEEAERLKQRAEEEAQAK 2730
Cdd:NF041483 317 -------LVGEATKEAEALKAEAEQALADARAEAE--KLVAEAAEKARTVaAEDTAAQLAKAARTAEEVLTKASEDAKAT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2731 AQ-AQDEAEKLRKEAELEAAK-RAHAEQAAlkqKQLADEEMDKHKKFAEKTlrqksqveqeltkVKLQleetdhqktlld 2808
Cdd:NF041483 388 TRaAAEEAERIRREAEAEADRlRGEAADQA---EQLKGAAKDDTKEYRAKT-------------VELQ------------ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2809 EELQRLKEEvTDAMRQKAQVEEElfkvKIQMEELIKLKLRIEEENKmlimkdkdSTQKLLVE---EAEKMRQVAE-EAAR 2884
Cdd:NF041483 440 EEARRLRGE-AEQLRAEAVAEGE----RIRGEARREAVQQIEEAAR--------TAEELLTKakaDADELRSTATaESER 506
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2885 LSIEAQE-AARMRKLAEDDLANQRALAEKMLKE--------KMQAIQEASRLKAEAE--MLQKQKELAQEQARKFQEdke 2953
Cdd:NF041483 507 VRTEAIErATTLRRQAEETLERTRAEAERLRAEaeeqaeevRAAAERAARELREETEraIAARQAEAAEELTRLHTE--- 583
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2954 qIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRA-QAKAEE-----------DASKFKKKAEEIGNKLHQ 3021
Cdd:NF041483 584 -AEERLTAAEEALADARAEAERIRREAAEETERLRTEAAERIRTlQAQAEQeaerlrteaaaDASAARAEGENVAVRLRS 662
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3022 TELATKERMA--VVQTLEIQRQQSGKEAE----ELRRAIAELEHEKEKLKREAELLQKNSQkmQVAQQEQLRQETQvlqt 3095
Cdd:NF041483 663 EAAAEAERLKseAQESADRVRAEAAAAAErvgtEAAEALAAAQEEAARRRREAEETLGSAR--AEADQERERAREQ---- 736
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3096 tflSEkQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENV--RRKQD 3173
Cdd:NF041483 737 ---SE-ELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAaeRTRTE 812
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3174 ELQQLDKKR----QEQEKLLADENRKLREKLEQMEEEHRI-------ALAQTREMRTQTDDLA 3225
Cdd:NF041483 813 AQEEADRVRsdayAERERASEDANRLRREAQEETEAAKALaertvseAIAEAERLRSDASEYA 875
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
766-865 |
1.54e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 101.48 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 766 AKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPE 845
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1835643837 846 D-VDVPQPDEKSIITYVSSMY 865
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
643-752 |
1.95e-24 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 101.76 E-value: 1.95e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 643 EDERDRVQKKTFTKWVNKHLIKAQRHV--SDLYEDLRDGHNLISLLEVLSGDNLPR-EKGRMRFHKLQNVQIALDYLKHR 719
Cdd:cd21247 14 QEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTK 93
|
90 100 110
....*....|....*....|....*....|....
gi 1835643837 720 -QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 752
Cdd:cd21247 94 vPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
768-868 |
3.18e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 100.62 E-value: 3.18e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 768 EKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPEDV 847
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1835643837 848 DVPQPDEKSIITYVSSMYDAM 868
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2141-3025 |
3.58e-24 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 113.53 E-value: 3.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2141 EKFRSQAEEAERRMKQAEVEKERQIKVAQEvaqqsaAAELNSKRMSFAEKTAQLELSLKQEHITvthlQEEAERLKKLHD 2220
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEE------TENLAELIIDLEELKLQELKLKEQAKKA----LEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2221 EAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALrQKELAEDELEKQR 2300
Cdd:pfam02463 222 EEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEE-LKLLAKEEEELKS 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2301 KLADATaQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEES 2380
Cdd:pfam02463 301 ELLKLE-RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2381 RsnteKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKE 2460
Cdd:pfam02463 380 K----LESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2461 KEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKN-------IVEDTLRQRRIIEEEIRILK 2533
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGlkvllalIKDGVGGRIISAHGRLGDLG 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2534 VNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEK-----QRQLALEEEQRRKEAEEKVRKILADEKEAARQRKA 2608
Cdd:pfam02463 536 VAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgarklRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2609 ALEEV-ERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQtrKQEQSILDKLKEEAER 2687
Cdd:pfam02463 616 DEDDKrAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLE--IQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAAEDADFARTRAEQEaalSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADE 2767
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEE---LKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELS 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2768 EMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKA-------QVEEELFKVKIQME 2840
Cdd:pfam02463 771 LKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKikeeeleELALELKEEQKLEK 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2841 ELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKmqA 2920
Cdd:pfam02463 851 LAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEA--E 928
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2921 IQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRA--- 2997
Cdd:pfam02463 929 ILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKkli 1008
|
890 900 910
....*....|....*....|....*....|.
gi 1835643837 2998 QAKAEEDASKFKK---KAEEIGNKLHQTELA 3025
Cdd:pfam02463 1009 RAIIEETCQRLKEfleLFVSINKGWNKVFFY 1039
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
765-865 |
4.05e-24 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 100.19 E-value: 4.05e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDP 844
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1835643837 845 EDVDVPQ-PDEKSIITYVSSMY 865
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2543-3188 |
7.67e-24 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 112.37 E-value: 7.67e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2543 KSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQlALEEEQRRKEAEEKVRKILADEKEAARQRkaalEEVERLKAKAEE 2622
Cdd:TIGR00618 221 KQVLEKELKHLREALQQTQQSHAYLTQKREAQEE-QLKKQQLLKQLRARIEELRAQEAVLEETQ----ERINRARKAAPL 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2623 AKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSIL---DKLKEEAERAK-------RAA 2692
Cdd:TIGR00618 296 AAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHsqeIHIRDAHEVATsireiscQQH 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2693 EDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDE----AEKLRKEAELEAAKRAHAEQAALKQKQLADEE 2768
Cdd:TIGR00618 376 TLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFrdlqGQLAHAKKQQELQQRYAELCAAAITCTAQCEK 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2769 MDK-HKKFAEKTLRQKSQVEQELTKVKLQLEETdhqKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIqMEELIKLKL 2847
Cdd:TIGR00618 456 LEKiHLQESAQSLKEREQQLQTKEQIHLQETRK---KAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN-PGPLTRRMQ 531
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2848 RIEEENKMLIMKDKDsTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEkMQAIQEASRL 2927
Cdd:TIGR00618 532 RGEQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-TEKLSEAEDM 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2928 KAEA---EMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSL--EAERRQQLEITAEAERLKLQVLEMSRAQAKAE 3002
Cdd:TIGR00618 610 LACEqhaLLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLtqERVREHALSIRVLPKELLASRQLALQKMQSEK 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3003 EDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEI----QRQQSGKEAEELRRAIAELEHE-KEKLKREAELLQKNSQK 3077
Cdd:TIGR00618 690 EQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENasssLGSDLAAREDALNQSLKELMHQaRTVLKARTEAHFNNNEE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3078 MQVAQQ-----EQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKlenlYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKV 3152
Cdd:TIGR00618 770 VTAALQtgaelSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPS----DEDILNLQCETLVQEEEQFLSRLEEKSATLG 845
|
650 660 670
....*....|....*....|....*....|....*.
gi 1835643837 3153 SMDdamKKQKEAEENVRRKQDELQQLDKKRQEQEKL 3188
Cdd:TIGR00618 846 EIT---HQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1950-2748 |
1.05e-23 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 112.08 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1950 EKAAEKLkEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKeAEELQRRMQE-EVSKREVVAVDAEQQKQTIQQELQQLR 2028
Cdd:TIGR02169 173 EKALEEL-EEVEENIERLDLIIDEKRQQLERLRREREKAER-YQALLKEKREyEGYELLKEKEALERQKEAIERQLASLE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2029 Q---NSDMEIKSKAKQIEEVEYNRRKIEEEIHivRLQLETMQKHKANAEdELQELRARAEKAEQQKKAAQEEAERLRKQV 2105
Cdd:TIGR02169 251 EeleKLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIG-ELEAEIASLERSIAEKERELEDAEERLAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2106 KDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEkfrsqAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRM 2185
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK-----EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2186 SFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAE 2265
Cdd:TIGR02169 403 ELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2266 KQKEDAERE---ARKRAKTEESALRQKELAEDELEKQRKLADATAQQkfsaeqeLIRLKAETENSEQQRLLLEEELFRLK 2342
Cdd:TIGR02169 483 KELSKLQRElaeAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQ-------LGSVGERYATAIEVAAGNRLNNVVVE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2343 NEV--NEAIQKRKEMEE------ELAKVRAEMEIL--------------------------------------LQSKSRA 2376
Cdd:TIGR02169 556 DDAvaKEAIELLKRRKAgratflPLNKMRDERRDLsilsedgvigfavdlvefdpkyepafkyvfgdtlvvedIEAARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2377 EEESRSNT------EKSKQM------LEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEaarqRAEAERILKEKLAAI 2444
Cdd:TIGR02169 636 MGKYRMVTlegelfEKSGAMtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSE----LRRIENRLDELSQEL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2445 NDATR----LKTEAEIALKEKEAENERLRRLAED-EAYQRKLLEEQAtqhKQDIEEKIILLKKSSDNELERQKNIVEDTL 2519
Cdd:TIGR02169 712 SDASRkigeIEKEIEQLEQEEEKLKERLEELEEDlSSLEQEIENVKS---ELKELEARIEELEEDLHKLEEALNDLEARL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2520 RQRRIIEEEIRILKVNFEKasvgkSDLELELNQLKNIAEETQRSKEKAEQE-AEKQRQLALEEEQR--RKEAEEKVRKIL 2596
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEEV-----SRIEARLREIEQKLNRLTLEKEYLEKEiQELQEQRIDLKEQIksIEKEIENLNGKK 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2597 ADEKEAARQRKAALEEVE--RLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQE 2674
Cdd:TIGR02169 864 EELEEELEELEAALRDLEsrLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2675 QSI------LDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEA 2748
Cdd:TIGR02169 944 EEIpeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
765-869 |
2.31e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.94 E-value: 2.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYqGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 844
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1835643837 845 EDVDVPQPDEKSIITYVSSMYDAMP 869
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
652-749 |
3.35e-23 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 97.39 E-value: 3.35e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 652 KTFTKWVNKHLIKA-QRHVSDLYEDLRDGHNLISLLEVLSGDNLPREK---GRMRFHKLQNVQIALDYLKHRQVKLVNIR 727
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1835643837 728 NDDIADGnPKLTLGLIWTIILH 749
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
764-870 |
6.55e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 96.97 E-value: 6.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 764 MTAKEKLLLWSQRMTEGY-QGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVY--RQTNLENLDQAFNVAERDLGVTR 840
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1835643837 841 -LLDPEDVDvpQPDEKSIITYVSSMYDAMPR 870
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
649-752 |
2.21e-22 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 95.43 E-value: 2.21e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 649 VQKKTFTKWVNKHLIKAQRH--VSDLYEDLRDGHNLISLLEVLSGDNLP-REKGRMRFHKLQNVQIALDYLKHRQ-VKLV 724
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1835643837 725 NIRNDDIADGNPKLTLGLIWTIILHFQI 752
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2473-3223 |
7.65e-22 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 105.64 E-value: 7.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2473 EDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKAsvgKSDLELELNQ 2552
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAAR---KQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2553 LKN-IAEETQRSKEKAEQEAEKQRQLALEEEQRrkEAEEKVRKILADEKEAARQRKAALEEvERLKAKAEEAKRQKE--- 2628
Cdd:pfam01576 80 LESrLEEEEERSQQLQNEKKKMQQHIQDLEEQL--DEEEAARQKLQLEKVTTEAKIKKLEE-DILLLEDQNSKLSKErkl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2629 LAEKEAERQIQLAQEaalkkidaEEKAHTAIVQQKEQEMLQTRKQEQ-SILDKLKEEAERAKRAAeDADFARTRaEQEAA 2707
Cdd:pfam01576 157 LEERISEFTSNLAEE--------EEKAKSLSKLKNKHEAMISDLEERlKKEEKGRQELEKAKRKL-EGESTDLQ-EQIAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2708 LsRQQVEEAERLKQRAEEEAQAkAQAQDEAEKLRKEAELEAAKRAHAEQAALKqkqladEEMDKHKKFAEKTLRQKSQVE 2787
Cdd:pfam01576 227 L-QAQIAELRAQLAKKEEELQA-ALARLEEETAQKNNALKKIRELEAQISELQ------EDLESERAARNKAEKQRRDLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2788 QELTKVKLQLEETdHQKTLLDEELqRLKEEVTDAMRQKAqVEEELFKVKIQMEEL-IKLKLRIEEENKML--IMKDKDST 2864
Cdd:pfam01576 299 EELEALKTELEDT-LDTTAAQQEL-RSKREQEVTELKKA-LEEETRSHEAQLQEMrQKHTQALEELTEQLeqAKRNKANL 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2865 QKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQ 2944
Cdd:pfam01576 376 EKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGK 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2945 ARKFQEDKEQIEQQLaketEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTEL 3024
Cdd:pfam01576 456 NIKLSKDVSSLESQL----QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKK 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3025 ATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQlRQETQVLQTTFLSEKQLL 3104
Cdd:pfam01576 532 KLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ-RQLVSNLEKKQKKFDQML 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3105 LErEKYIEEEKAKLENLYEDEVRK--------------AQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRR 3170
Cdd:pfam01576 611 AE-EKAISARYAEERDRAEAEAREketralslaraleeALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRA 689
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 3171 KQDELQQLDKKRQEQE-KLLADENRKLR-----------------EKLEQMEEEHRIALAQTREMRTQTDD 3223
Cdd:pfam01576 690 LEQQVEEMKTQLEELEdELQATEDAKLRlevnmqalkaqferdlqARDEQGEEKRRQLVKQVRELEAELED 760
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1771-2652 |
1.80e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 104.75 E-value: 1.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1771 ERDVDLDRYREKVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQSVpitdsktmkehL 1850
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKE-----------L 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1851 LQEKKLLDEIESNRDKVDECQKYAKQyidaikdyelQLVTYKAQVEpvaspakkpKVQSTSDSIIQEYVDLRTRYSELtt 1930
Cdd:TIGR02168 291 YALANEISRLEQQKQILRERLANLER----------QLEELEAQLE---------ELESKLDELAEELAELEEKLEEL-- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1931 ltsqyikfiTETLRRLNDEEKAAEKLKEEERRRLAEVEAQLakqTQLAEAHAKAKAQAEKEAEELQRrmqeevskrevva 2010
Cdd:TIGR02168 350 ---------KEELESLEAELEELEAELEELESRLEELEEQL---ETLRSKVAQLELQIASLNNEIER------------- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2011 vdAEQQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEynRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQ 2090
Cdd:TIGR02168 405 --LEARLERLEDRRERLQQ----EIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2091 KKAAQEEAERLRKQVkDETQKKREAEEELKRKVQAEKEAAREK---QRAVEDLEKFRSQAEEA-----ERRMKQAEVEKE 2162
Cdd:TIGR02168 477 LDAAERELAQLQARL-DSLERLQENLEGFSEGVKALLKNQSGLsgiLGVLSELISVDEGYEAAieaalGGRLQAVVVENL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2163 RQIKVAQEvaqqsAAAELNSKRMSFAEKTaqlelSLKQEHITVTHLQEEAErlkklhdeaEKAREEAEKELEKWHQKANE 2242
Cdd:TIGR02168 556 NAAKKAIA-----FLKQNELGRVTFLPLD-----SIKGTEIQGNDREILKN---------IEGFLGVAKDLVKFDPKLRK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2243 ALRLRLQAEEVAHKKTLAQEEAEKQKEDAE-------------REARKRAKTEESAL-RQKELAedELEKQRKLADATAQ 2308
Cdd:TIGR02168 617 ALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggVITGGSAKTNSSILeRRREIE--ELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2309 QkfsAEQELIRLKAETENseqqrllleeelfrLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSK 2388
Cdd:TIGR02168 695 E---LEKALAELRKELEE--------------LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2389 QMLEVEASKLRELAEEAAKLRAVSEE-AKRQRQIAEDEaaRQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENER 2467
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEEELAEAEAEiEELEAQIEQLK--EELKALREALDELRAELTLLNEEAANLRERLESLERRIAA 835
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2468 LRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDnELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLE 2547
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-ELEALLNERASLEEALALLRSELEELSEELRELESKRSELR 914
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2548 LELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKE-AEEKVRKILADEKEAARQRK--------------AALEE 2612
Cdd:TIGR02168 915 RELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKrlenkikelgpvnlAAIEE 994
|
890 900 910 920
....*....|....*....|....*....|....*....|
gi 1835643837 2613 VERLKAKAEEAKRQKELAEkEAERQIqlaqEAALKKIDAE 2652
Cdd:TIGR02168 995 YEELKERYDFLTAQKEDLT-EAKETL----EEAIEEIDRE 1029
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2350-3214 |
2.46e-21 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 103.99 E-value: 2.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2350 QKRKEMEEELAKVrAEMEILLQsKSRAE-EESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAAR 2428
Cdd:TIGR02169 153 VERRKIIDEIAGV-AEFDRKKE-KALEElEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLK 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2429 QRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQ-RKLLEEQATQHKQDIEEKIIllkkssdnE 2507
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEA--------E 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2508 LERQKNIVEDTLRQRRIIEEEIRILKVnfekasvgksdlelelnQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKE 2587
Cdd:TIGR02169 303 IASLERSIAEKERELEDAEERLAKLEA-----------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2588 AEEKVRKILADEKEAARQR---KAALEEVERLKAKAEEAKR-QKELAEKEAERQIQLAQ--------EAALKKIDAEEKA 2655
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRdelKDYREKLEKLKREINELKReLDRLQEELQRLSEELADlnaaiagiEAKINELEEEKED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2656 HTAIVQQKEQEMLQTRKQ---EQSILDKLKEEAERAKRAAEDAdfARTRAEQEAalSRQQVEEAERLKQRAEEEAQAKAQ 2732
Cdd:TIGR02169 446 KALEIKKQEWKLEQLAADlskYEQELYDLKEEYDRVEKELSKL--QRELAEAEA--QARASEERVRGGRAVEEVLKASIQ 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2733 ------AQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADE--EMDKHKKFAEKT---LRQKSQVEQELTKVK------- 2794
Cdd:TIGR02169 522 gvhgtvAQLGSVGERYATAIEVAAGNRLNNVVVEDDAVAKEaiELLKRRKAGRATflpLNKMRDERRDLSILSedgvigf 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2795 -LQLEETDHQ----------KTLLDEELQRLKE---------------EVTDAMR--QKAQVEEELFKVKiQMEELIKLK 2846
Cdd:TIGR02169 602 aVDLVEFDPKyepafkyvfgDTLVVEDIEAARRlmgkyrmvtlegelfEKSGAMTggSRAPRGGILFSRS-EPAELQRLR 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2847 LRIEEENKML--IMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEaarmrkLAEDDLANQRALAEkmLKEKMQAIQEA 2924
Cdd:TIGR02169 681 ERLEGLKRELssLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ------LEQEEEKLKERLEE--LEEDLSSLEQE 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2925 -SRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLA----KETEGFQKSLEAERRQQLEITAEAERlKLQVLEMSRAQA 2999
Cdd:TIGR02169 753 iENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARLREIEQ-KLNRLTLEKEYL 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3000 KaeedaskfkKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQ 3079
Cdd:TIGR02169 832 E---------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3080 VAQQEQ--LRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDE--VRKAQKLKQEQEHQMKHLEEEKdqlkvsmd 3155
Cdd:TIGR02169 903 RKIEELeaQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElsLEDVQAELQRVEEEIRALEPVN-------- 974
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 3156 daMKKQKEAEENVRRkQDELqqldkkrQEQEKLLADENRKLREKLEQMEEEHRIALAQT 3214
Cdd:TIGR02169 975 --MLAIQEYEEVLKR-LDEL-------KEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
769-866 |
2.51e-21 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 92.41 E-value: 2.51e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 769 KLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD-PEDV 847
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1835643837 848 DVPQPDEKSIITYVSSMYD 866
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
765-863 |
2.79e-21 |
|
second calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409033 Cd Length: 103 Bit Score: 91.91 E-value: 2.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYqglHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVY-RQTNLENLDQAFNVAERDLGVTRLLD 843
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1835643837 844 PEDVDVPQPDEKSIITYVSS 863
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
648-753 |
4.17e-21 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 92.45 E-value: 4.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 648 RVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR---EKGRMRFHKLQNVQIALDYLKHRQVKLV 724
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1835643837 725 NIRNDDIADGNPKLTLGLIWTIILHFQIS 753
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1936-2964 |
4.25e-21 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 103.33 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1936 IKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavDAEQ 2015
Cdd:pfam01576 133 IKKLEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGRQ----ELEK 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2016 QKQTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQEL--------------R 2081
Cdd:pfam01576 209 AKRKLEGESTDLQE----QIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELeaqiselqedleseR 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2082 ARAEKAEQQKKAAQEEAERLRKQVKDeTQKKREAEEELKRKVQAEKEaarEKQRAVEDLEK-FRSQAEEAERRMKQAEVE 2160
Cdd:pfam01576 285 AARNKAEKQRRDLGEELEALKTELED-TLDTTAAQQELRSKREQEVT---ELKKALEEETRsHEAQLQEMRQKHTQALEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2161 KERQIKVAQEVAqqsaaAELNSKRMSFAEKTAQLELSLKqehiTVTHLQEEAERLKKlhdeaekareEAEKELEKWHQKA 2240
Cdd:pfam01576 361 LTEQLEQAKRNK-----ANLEKAKQALESENAELQAELR----TLQQAKQDSEHKRK----------KLEGQLQELQARL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2241 NEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESAlrqkelaEDELEKQRKLADATAQQKFSAEQELIRL 2320
Cdd:pfam01576 422 SESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSL-------ESQLQDTQELLQEETRQKLNLSTRLRQL 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2321 KAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNT----EKSKQMLEVEAS 2396
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTqqleEKAAAYDKLEKT 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2397 KLReLAEEaakLRAVSEEAKRQRQIAEDEAARQRaEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEA 2476
Cdd:pfam01576 575 KNR-LQQE---LDDLLVDLDHQRQLVSNLEKKQK-KFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEAL 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2477 YQRKLLEEQATQHKQDIEEkiilLKKSSDN------ELERQKNIVEdtlRQRRIIEEEIRILKVNFEKASVGKSDLELEL 2550
Cdd:pfam01576 650 EAKEELERTNKQLRAEMED----LVSSKDDvgknvhELERSKRALE---QQVEEMKTQLEELEDELQATEDAKLRLEVNM 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2551 NQLKniaeetqrskekaeqeAEKQRQLALEEEQrrkeAEEKVRKILadekEAARQRKAALEEVERLKAKAEEAKRQKELA 2630
Cdd:pfam01576 723 QALK----------------AQFERDLQARDEQ----GEEKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELD 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2631 EKEAERQIQLAQEAalkkidaeekahtaivqqKEQEMLQTRKQeQSILDKLKEEAERAkRAAEDADFARTRaeqeaalsr 2710
Cdd:pfam01576 779 LKELEAQIDAANKG------------------REEAVKQLKKL-QAQMKDLQRELEEA-RASRDEILAQSK--------- 829
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2711 qqveeaerlkqraEEEAQAKAQaqdEAEKLRKEAELEAAKRAHaEQAALKQKQLADEEMDKHKKFAeKTLRQKSQVEQEL 2790
Cdd:pfam01576 830 -------------ESEKKLKNL---EAELLQLQEDLAASERAR-RQAQQERDELADEIASGASGKS-ALQDEKRRLEARI 891
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2791 TKVKLQLEETDHQKTLLDEELQRLKEEVTD------AMRQKAQVEEelfKVKIQMEELIK-LKLRIEEENKMLIMKDKDS 2863
Cdd:pfam01576 892 AQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelaAERSTSQKSE---SARQQLERQNKeLKAKLQEMEGTVKSKFKSS 968
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2864 TQKLlveEAeKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQE 2943
Cdd:pfam01576 969 IAAL---EA-KIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEE 1044
|
1050 1060
....*....|....*....|.
gi 1835643837 2944 QARKFQEDKEQIEQQLAKETE 2964
Cdd:pfam01576 1045 EASRANAARRKLQRELDDATE 1065
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
648-753 |
5.34e-21 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 92.07 E-value: 5.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 648 RVQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR---EKGRMRFHKLQNVQIALDYLKHRQVKLV 724
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1835643837 725 NIRNDDIADGNPKLTLGLIWTIILHFQIS 753
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1955-2645 |
8.36e-21 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 102.35 E-value: 8.36e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1955 KLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLR--QNSD 2032
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLReaLQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2033 MEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQ---KHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDET 2109
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRaqeAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2110 QKKREAEEELKRKVQAEKEAAREKQRAVEDL-----EKFRSQAEEAERRMKQAEVEKE--------RQIKVAQEVAQQSA 2176
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTlhsqeIHIRDAHEVATSIREISCQQHTltqhihtlQQQKTTLTQKLQSL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2177 AAELNSKRMSFAEKTAQ-LELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKaNEALRLRLQAEEVAH 2255
Cdd:TIGR00618 399 CKELDILQREQATIDTRtSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQ-ESAQSLKEREQQLQT 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2256 KKTLAQEEAEKQKEDAERearkrakTEESALRQKELAEDELEKQRKLAD-----ATAQQKFSAEQELIRLKAETENSEQQ 2330
Cdd:TIGR00618 478 KEQIHLQETRKKAVVLAR-------LLELQEEPCPLCGSCIHPNPARQDidnpgPLTRRMQRGEQTYAQLETSEEDVYHQ 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2331 RLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRA 2410
Cdd:TIGR00618 551 LTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDV 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2411 VSEEAKRQRQIAEDEAARQRAEA----ERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQA 2486
Cdd:TIGR00618 631 RLHLQQCSQELALKLTALHALQLtltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2487 TQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEK 2566
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFF 790
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2567 AEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAA 2645
Cdd:TIGR00618 791 NRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQA 869
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2561-2787 |
2.40e-20 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 97.18 E-value: 2.40e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2561 QRSKEKAEQEAEKQRQLalEEEQRRKEAEEKVRKILADEKEAARQRKAALEEverlKAKAEEAKRQKELAEKEAERQIQL 2640
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKK--KEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ----KKQAEEAAKQAALKQKQAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2641 AQEAALKKIDAEEKAHTAIVQQKEQEMlqtrkqeqsildKLKEEAERAKRAAEDAdfartRAEQEAALSRQQVEEAerlK 2720
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAAAKKAAAEA------------KKKAEAEAAKKAAAEA-----KKKAEAEAAAKAAAEA---K 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2721 QRAEEEAQAKAQAQDEaeklrKEAELEAAKRahAEQAALKQKQLADEEmdKHKKFAEKTLRQKSQVE 2787
Cdd:PRK09510 201 KKAEAEAKKKAAAEAK-----KKAAAEAKAA--AAKAAAEAKAAAEKA--AAAKAAEKAAAAKAAAE 258
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2175-2991 |
3.36e-20 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 100.53 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2175 SAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDeaekareeaekelekwhqKANEALRLRLQAEEVA 2254
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRERE------------------KAERYQALLKEKREYE 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2255 HKKTLAQ-EEAEKQKEDAERE-ARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRL 2332
Cdd:TIGR02169 225 GYELLKEkEALERQKEAIERQlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2333 LLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVS 2412
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2413 EEAKRQRQIAED----------------EAARQRAEAERILKEKLAAINDA-TRLKTEAEIALKEKEAENERLRRLAED- 2474
Cdd:TIGR02169 385 DELKDYREKLEKlkreinelkreldrlqEELQRLSEELADLNAAIAGIEAKiNELEEEKEDKALEIKKQEWKLEQLAADl 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2475 EAYQRKLLEEQATQhkQDIEEKIILLKKSSDnELERQKNIVEDTLRqrrIIEEEIRILKVNFEK-----ASVGKSDLELE 2549
Cdd:TIGR02169 465 SKYEQELYDLKEEY--DRVEKELSKLQRELA-EAEAQARASEERVR---GGRAVEEVLKASIQGvhgtvAQLGSVGERYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2550 L-------NQLKNIAEETQRSKEKAEQEAeKQRQLA---------LEEEQR--RKEAEEKVRKILADEKEAARQRKAA-- 2609
Cdd:TIGR02169 539 TaievaagNRLNNVVVEDDAVAKEAIELL-KRRKAGratflplnkMRDERRdlSILSEDGVIGFAVDLVEFDPKYEPAfk 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2610 -----------LEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSIL 2678
Cdd:TIGR02169 618 yvfgdtlvvedIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSEL 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2679 DKLKEEAERAKRAAEDAdfarTRAEQEAALSRQQV-EEAERLKQRAEEEAQAKAQAQDEAEKLRKE-AELEAAKRAHAEQ 2756
Cdd:TIGR02169 698 RRIENRLDELSQELSDA----SRKIGEIEKEIEQLeQEEEKLKERLEELEEDLSSLEQEIENVKSElKELEARIEELEED 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2757 AALKQKQLAD-EEMDKHKKFAEKTlRQKSQVEQELTKVKLQLEETD-------HQKTLLDEELQRLKEEVTDAMRQKAQV 2828
Cdd:TIGR02169 774 LHKLEEALNDlEARLSHSRIPEIQ-AELSKLEEEVSRIEARLREIEqklnrltLEKEYLEKEIQELQEQRIDLKEQIKSI 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2829 EEELFKVKIQMEELIKlklriEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRA 2908
Cdd:TIGR02169 853 EKEIENLNGKKEELEE-----ELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLE 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2909 LAEKMLKE---KMQAIQEASRLKAEAEMLQKQKELAQEQARKFQ-------EDKEQIEQQLaKETEGFQKSLEAERRQQL 2978
Cdd:TIGR02169 928 ALEEELSEiedPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRL-DELKEKRAKLEEERKAIL 1006
|
890
....*....|...
gi 1835643837 2979 EITAEAERLKLQV 2991
Cdd:TIGR02169 1007 ERIEEYEKKKREV 1019
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1631-2378 |
5.38e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 99.75 E-value: 5.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1631 IHFELEGIKKNLNKVSEKTLKVLAQKEQSSSSP--LLRTEHEITHQKMDQVYSLSSIYLEKLKTINLVIRSTQGA----- 1703
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAELRELElaLLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKleelr 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1704 ---EEVVRTYEDQLKEVHAVPSDSKELEATKAELKKLRSQVEGHQPLFNT-----------LEADLNKAKDVNEQMLRSH 1769
Cdd:TIGR02168 274 levSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqleeleskldeLAEELAELEEKLEELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1770 SERDVDLDRYREKVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQSVPITDSKTMKEH 1849
Cdd:TIGR02168 354 ESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1850 LLQE--------KKLLDEIESNRDKVDECQKYAKQYIDAIkdyELQLVTYKAQVEPVASPAKKPKVQSTSDSIIQEYV-- 1919
Cdd:TIGR02168 434 ELKElqaeleelEEELEELQEELERLEEALEELREELEEA---EQALDAAERELAQLQARLDSLERLQENLEGFSEGVka 510
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1920 ---------DLRTRYSELTTLTSQYIKFITETL---------RRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAH 1981
Cdd:TIGR02168 511 llknqsglsGILGVLSELISVDEGYEAAIEAALggrlqavvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGND 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1982 AKAKAQAEKEAEELQRRMQEEVSKREVVA--------VDAEQQKQTIQQELQQL--------------------RQNSDM 2033
Cdd:TIGR02168 591 REILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvVDDLDNALELAKKLRPGyrivtldgdlvrpggvitggSAKTNS 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2034 EIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKR 2113
Cdd:TIGR02168 671 SILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2114 EAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVaqQSAAAELNSKRMSFAEKTAQ 2193
Cdd:TIGR02168 751 QLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL--RAELTLLNEEAANLRERLES 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2194 LELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAER 2273
Cdd:TIGR02168 829 LERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2274 EARKraKTEESALRQKELAEDELEKQR-KLADATAQQKFSAE-----QELIRLKAETENSEQQRLLLEEELFRLKNE--- 2344
Cdd:TIGR02168 909 KRSE--LRRELEELREKLAQLELRLEGlEVRIDNLQERLSEEysltlEEAEALENKIEDDEEEARRRLKRLENKIKElgp 986
|
810 820 830
....*....|....*....|....*....|....*
gi 1835643837 2345 VN-EAIQKRKEMEEELAKVRAEMEILLQSKSRAEE 2378
Cdd:TIGR02168 987 VNlAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
761-866 |
7.79e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-3 seems to act as a Rab effector protein and plays a role in vesicle trafficking. It is involved in exocytic vesicle tethering and fusion. MICAL3 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409100 [Multi-domain] Cd Length: 111 Bit Score: 88.08 E-value: 7.79e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 761 SEDMTAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTR 840
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1835643837 841 LLDPEDV-DVPQPDEKSIITYVSSMYD 866
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
765-865 |
9.55e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 87.78 E-value: 9.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 844
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1835643837 845 EDVDV--PQPDEKSIITYVSSMY 865
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6385-6602 |
1.24e-19 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 90.97 E-value: 1.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6385 RAKQFSESQRLLLDWMEEVELTLEKQvDSSQSQDDIKQQLADHKEFQKVLRTKRPVYEATLRNGRSLREkaQLPEDVQKL 6464
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIE--EGHPDAEEI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6465 DELLGELKEKWDLVCWKSTERQHKLEESLLFSGKFTDALQaLMDWLYWAEPQLSEDvPIRGDKDLVSDLMDKHKIFQKEL 6544
Cdd:cd00176 78 QERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEEL 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 6545 GKRASCVKTLKRSMRDLTRGSISTDSQWLQKQMEELNHRWEVVCKLSVGKQARLEASL 6602
Cdd:cd00176 156 EAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
765-862 |
1.58e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 87.15 E-value: 1.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDP 844
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90
....*....|....*....
gi 1835643837 845 ED-VDVPQPDEKSIITYVS 862
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLC 98
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1705-2301 |
2.44e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.90 E-value: 2.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1705 EVVRTYEDQLK--EVHAVP-SDSKELEATKAE----LKKLRSQVEGHQPLFNTLEADLN-KAKDVNEQMLRSHSERDVDL 1776
Cdd:PTZ00121 1215 EEARKAEDAKKaeAVKKAEeAKKDAEEAKKAEeernNEEIRKFEEARMAHFARRQAAIKaEEARKADELKKAEEKKKADE 1294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1777 DRYREKVQQLLErwqaiLVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQSVPITDSKTMKEHllQEKKL 1856
Cdd:PTZ00121 1295 AKKAEEKKKADE-----AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA--EEKAE 1367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1857 LDEI--ESNRDKVDECQKYA---KQYIDAIKDYE-----LQLVTYKAQVEPVASPAKKPKVQSTSDSIIQEYVDLRTRYS 1926
Cdd:PTZ00121 1368 AAEKkkEEAKKKADAAKKKAeekKKADEAKKKAEedkkkADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAD 1447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1927 ELTTLTSQYIKfiTETLRRLNDEEKAAEKLKE--EERRRLAEVEAQLAKQTQLAEaHAKAKAQAEKEAEELQR----RMQ 2000
Cdd:PTZ00121 1448 EAKKKAEEAKK--AEEAKKKAEEAKKADEAKKkaEEAKKADEAKKKAEEAKKKAD-EAKKAAEAKKKADEAKKaeeaKKA 1524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2001 EEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEiksKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQEL 2080
Cdd:PTZ00121 1525 DEAKKAEEAKKADEAKKAEEKKKADELKKAEELK---KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2081 RA-RAEKAEQQKKAAQE--EAERLRKQ---VKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRM 2154
Cdd:PTZ00121 1602 EEeKKMKAEEAKKAEEAkiKAEELKKAeeeKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAK 1681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2155 KQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKlhdeaekareeaekele 2234
Cdd:PTZ00121 1682 KAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKK----------------- 1744
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2235 kwhqKANEAlrlRLQAEEvahKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRK 2301
Cdd:PTZ00121 1745 ----KAEEA---KKDEEE---KKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIK 1801
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1949-2521 |
2.70e-19 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 97.03 E-value: 2.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1949 EEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKRE---VVAVDAEQQKQTIQqELQ 2025
Cdd:PRK02224 193 KAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREeleTLEAEIEDLRETIA-ETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2026 QLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQV 2105
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2106 KD---ETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEkfrSQAEEAERRMKQAEVEKERqikvaqevaQQSAAAELNS 2182
Cdd:PRK02224 352 DDleeRAEELREEAAELESELEEAREAVEDRREEIEELE---EEIEELRERFGDAPVDLGN---------AEDFLEELRE 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2183 KRMSFAEKTAQLELSLKQEHITVthlqEEAERLkklhdeaekareeaekelekwhQKANEALRLRLQAEEVAHKKTLAQE 2262
Cdd:PRK02224 420 ERDELREREAELEATLRTARERV----EEAEAL----------------------LEAGKCPECGQPVEGSPHVETIEED 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2263 EAEKQKEDAEREARK--RAKTEESALRQKELAEDELEKQRKladataQQKFSAEQELIRLKAETenseqqrllleeelfr 2340
Cdd:PRK02224 474 RERVEELEAELEDLEeeVEEVEERLERAEDLVEAEDRIERL------EERREDLEELIAERRET---------------- 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2341 lknevneaIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEeakrqrQ 2420
Cdd:PRK02224 532 --------IEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRT------L 597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2421 IAEDEAARQRAEAERILKEKLAAINDATRLKteaeiaLKEKeaeNERLRRLAE-------DEAYQRKlleEQATQHKQDI 2493
Cdd:PRK02224 598 LAAIADAEDEIERLREKREALAELNDERRER------LAEK---RERKRELEAefdeariEEAREDK---ERAEEYLEQV 665
|
570 580
....*....|....*....|....*...
gi 1835643837 2494 EEKIILLKKSSDnELERQKNIVEDTLRQ 2521
Cdd:PRK02224 666 EEKLDELREERD-DLQAEIGAVENELEE 692
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2546-3138 |
4.70e-19 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 96.83 E-value: 4.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2546 LELELNQLKNIAEETQRsKEKAEQEAEKQRQLALEEEQRRKEAE--EKVRKILADEKEAARQRKAALEEVERLKAKA--- 2620
Cdd:pfam12128 256 AELRLSHLHFGYKSDET-LIASRQEERQETSAELNQLLRTLDDQwkEKRDELNGELSAADAAVAKDRSELEALEDQHgaf 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2621 EEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAiVQQKEQEMLQTRKQE--------QSILDKLKEEAERAKRAA 2692
Cdd:pfam12128 335 LDADIETAAADQEQLPSWQSELENLEERLKALTGKHQD-VTAKYNRRRSKIKEQnnrdiagiKDKLAKIREARDRQLAVA 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2693 ED---ADFARTRAEQEAALSRQQvEEAERLKQRAEEEAQAKAQAQDEAE-KLRKEAELEAAKRAHAEQAALKQKQL-ADE 2767
Cdd:pfam12128 414 EDdlqALESELREQLEAGKLEFN-EEEYRLKSRLGELKLRLNQATATPElLLQLENFDERIERAREEQEAANAEVErLQS 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2768 EMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQ------------------------KTLLDEELQR--LKEEVTDA 2821
Cdd:pfam12128 493 ELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflrkeapdweqsigKVISPELLHRtdLDPEVWDG 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2822 MRQKaqvEEELFKVKI-----------QMEELIKLKLRIEEEnkmlimkDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQ 2890
Cdd:pfam12128 573 SVGG---ELNLYGVKLdlkridvpewaASEEELRERLDKAEE-------ALQSAREKQAAAEEQLVQANGELEKASREET 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2891 EAARMRKLAEDDL--------ANQRALAEKMLKEKMQAIQEASRLKAEAEML-QKQKELAQEQARKFQEDKEQiEQQLAK 2961
Cdd:pfam12128 643 FARTALKNARLDLrrlfdekqSEKDKKNKALAERKDSANERLNSLEAQLKQLdKKHQAWLEEQKEQKREARTE-KQAYWQ 721
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2962 ETEGFQKSLEAERRQQLEI--TAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQ----- 3034
Cdd:pfam12128 722 VVEGALDAQLALLKAAIAArrSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwy 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3035 --TLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKN-------SQKMQVAQQEQLRQETQVLQ-TTFLSEKQLL 3104
Cdd:pfam12128 802 qeTWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKlemerkaSEKQQVRLSENLRGLRCEMSkLATLKEDANS 881
|
650 660 670
....*....|....*....|....*....|....
gi 1835643837 3105 LEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEH 3138
Cdd:pfam12128 882 EQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEH 915
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1825-2659 |
4.99e-19 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 96.68 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1825 IKDAKQRQEQIQSVpITDSKTMKEHLLQEKKLLDEIESNRDKVDECQKYAKqyIDAIKDYELQLVTYKAQVEpvASPAKK 1904
Cdd:TIGR02169 179 LEEVEENIERLDLI-IDEKRQQLERLRREREKAERYQALLKEKREYEGYEL--LKEKEALERQKEAIERQLA--SLEEEL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1905 PKVQSTSDSIIQEYVDLRTRYSELTT----LTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEA 1980
Cdd:TIGR02169 254 EKLTEEISELEKRLEEIEQLLEELNKkikdLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1981 HAKAKAQAEKEAEELQRR---MQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAK---QIEEVEYNRRKIEE 2054
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRrdkLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKlkrEINELKRELDRLQE 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2055 EIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELkRKVQAEKeaaREKQ 2134
Cdd:TIGR02169 414 ELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEY-DRVEKEL---SKLQ 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2135 RAVEDLEKFRSQAEEAERRMKQAEVEKERQIK-----VAQ--EVAQQSAAA--ELNSKRMSFA----EKTAQLELSLKQE 2201
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtVAQlgSVGERYATAieVAAGNRLNNVvvedDAVAKEAIELLKR 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2202 H-------ITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKA--------------NEALRLRLQAEEVahkkTLA 2260
Cdd:TIGR02169 570 RkagratfLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvvediEAARRLMGKYRMV----TLE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2261 QEEAEKQK-----EDAEREARKRAKTEESALRQKELAEDELEKQRKladataqqkfSAEQELIRLKaetenseqqrllle 2335
Cdd:TIGR02169 646 GELFEKSGamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELS----------SLQSELRRIE-------------- 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2336 eelfrlkNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEE---ESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVS 2412
Cdd:TIGR02169 702 -------NRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELKELEARIEELEEDL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2413 EEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKT-EAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQ 2491
Cdd:TIGR02169 775 HKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2492 DIEEkIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKE-KAEQE 2570
Cdd:TIGR02169 855 EIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaLEEEL 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2571 AEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQR-----KAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAA 2645
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAlepvnMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
890
....*....|....
gi 1835643837 2646 LKKIDAEEKAHTAI 2659
Cdd:TIGR02169 1014 KKKREVFMEAFEAI 1027
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2021-2903 |
1.07e-18 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 95.50 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2021 QQELQQLRQNSDMEIKSKAKQIEEVEYNRRK---IEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEe 2097
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQYKEKaceIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMK- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2098 aerLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFR-SQAEEAERRMKQAEVEKERQIKVAQEVAQQSA 2176
Cdd:TIGR00606 267 ---LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHqRTVREKERELVDCQRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2177 AAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLrlqAEEVAHK 2256
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL---CADLQSK 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2257 KTLAQEEAEKQkEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETE--NSEQQRLLL 2334
Cdd:TIGR00606 421 ERLKQEQADEI-RDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSkaEKNSLTETL 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2335 EEELFRLKNEVNEAIQKRKEMEEELAKV------RAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKL 2408
Cdd:TIGR00606 500 KKEVKSLQNEKADLDRKLRKLDQEMEQLnhhtttRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2409 RAVSEEAKrqrqIAEDEAARQRAEAERiLKEKLAAINDATRLKTEAEIALKEK----------EAENERLRRLAEDEAYQ 2478
Cdd:TIGR00606 580 HSKSKEIN----QTRDRLAKLNKELAS-LEQNKNHINNELESKEEQLSSYEDKlfdvcgsqdeESDLERLKEEIEKSSKQ 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2479 RKLLEEQATQHKQDIEEkiiLLKKSS------DNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQ 2552
Cdd:TIGR00606 655 RAMLAGATAVYSQFITQ---LTDENQsccpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGL 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2553 LKNIAEETQRSKEKAEQEAEKQRQLA--LEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQ-KEL 2629
Cdd:TIGR00606 732 APGRQSIIDLKEKEIPELRNKLQKVNrdIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKiAQQ 811
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2630 AEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKE--QEMLQTR-KQEQSILDKLKEEAERAKRAAEDADFARTRAEQEA 2706
Cdd:TIGR00606 812 AAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIElnRKLIQDQqEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLV 891
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2707 ALSRQQVEEAERLKQRAEEE---AQAKAQAQDEAEKLRKEAElEAAKRAHAEQAALKQK--QLADEEMDKHKKFAEKTLR 2781
Cdd:TIGR00606 892 ELSTEVQSLIREIKDAKEQDsplETFLEKDQQEKEELISSKE-TSNKKAQDKVNDIKEKvkNIHGYMKDIENKIQDGKDD 970
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2782 QKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKI--QMEELIK-LKLRIEEENKMLIM 2858
Cdd:TIGR00606 971 YLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRenELKEVEEeLKQHLKEMGQMQVL 1050
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1835643837 2859 KDKDSTQKLlveeAEKMRQVAEEAARLSIEAQEAARMRKLAEDDL 2903
Cdd:TIGR00606 1051 QMKQEHQKL----EENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6279-6493 |
1.29e-18 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 88.27 E-value: 1.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6279 EFHSSAQDLLKWISRTEDTLLTLPAASLvLETVTNQIQEHKVLLTEVNARGEKLAGLERSACRLKDySSKQDCAVIQNLV 6358
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLIE-EGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6359 LTAQERLSKVQQCTVAKGRELEDSRKRAKQFSESqRLLLDWMEEVELTLEKQvDSSQSQDDIKQQLADHKEFQKVLRTKR 6438
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDA-DDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 6439 PVYEATLRNGRSLREKAQlPEDVQKLDELLGELKEKWDLVCWKSTERQHKLEESL 6493
Cdd:cd00176 160 PRLKSLNELAEELLEEGH-PDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2256-3073 |
1.31e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 95.13 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2256 KKTLAQEEAEKQKEDAER------EARKRAKTEEsalRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQ 2329
Cdd:TIGR02169 171 KKEKALEELEEVEENIERldliidEKRQQLERLR---REREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2330 qrllleeelfrlknEVNEAIQKRKEMEEELAKVRAEMEILLqsksrAEEESRSNTEKSKQMLEVEaSKLRELAEEAAKLR 2409
Cdd:TIGR02169 248 --------------SLEEELEKLTEEISELEKRLEEIEQLL-----EELNKKIKDLGEEEQLRVK-EKIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2410 AVSEEAKRQRQIAEDEAARQRAEAERILKEKLA---AINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQA 2486
Cdd:TIGR02169 308 RSIAEKERELEDAEERLAKLEAEIDKLLAEIEElerEIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDEL 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2487 TQHKQDIEEKiillkKSSDNELERQKNIVEDTLRQRRIIEEEIRIlKVNFEKASVGKSDLELELNQLKNIAEETQRSKEK 2566
Cdd:TIGR02169 388 KDYREKLEKL-----KREINELKRELDRLQEELQRLSEELADLNA-AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2567 AEQEAEKQRQLALEEEQRR--KEAEEKVRKIlaDEKEAarQRKAALEEVERLKAKAEEAKRQKE-----LAE-KEAERQI 2638
Cdd:TIGR02169 462 ADLSKYEQELYDLKEEYDRveKELSKLQREL--AEAEA--QARASEERVRGGRAVEEVLKASIQgvhgtVAQlGSVGERY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2639 QLAQEAALKK------IDAEEKAHTAIvqqkeqEMLQTRKQEQSI---LDKLKEEAERAKRAAEDA------DFARTRAE 2703
Cdd:TIGR02169 538 ATAIEVAAGNrlnnvvVEDDAVAKEAI------ELLKRRKAGRATflpLNKMRDERRDLSILSEDGvigfavDLVEFDPK 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2704 QEAALSR--------QQVEEAERLKQRA---------------------EEEAQAKAQAQDEAEKLRKEAELEAAKRaha 2754
Cdd:TIGR02169 612 YEPAFKYvfgdtlvvEDIEAARRLMGKYrmvtlegelfeksgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKR--- 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2755 EQAALKQKQladeemdkhkKFAEKTLRQKSQVEQELTKvklQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFK 2834
Cdd:TIGR02169 689 ELSSLQSEL----------RRIENRLDELSQELSDASR---KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN 755
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2835 VKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAE--EAARLSIEAQEAARMRKLAEDDLanQRALAEK 2912
Cdd:TIGR02169 756 VKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSklEEEVSRIEARLREIEQKLNRLTL--EKEYLEK 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2913 MLKEKMQAIQEA----SRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQ---LAKETEGFQKSLEAERRQQLEITAEAE 2985
Cdd:TIGR02169 834 EIQELQEQRIDLkeqiKSIEKEIENLNGKKEELEEELEELEAALRDLESRlgdLKKERDELEAQLRELERKIEELEAQIE 913
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2986 RLKLQVLEM-SRAQAKAEEDASKFKKKAEEIG--------NKLHQTELATKERMavvQTLEIQRQQSGKEAEELRRAIAE 3056
Cdd:TIGR02169 914 KKRKRLSELkAKLEALEEELSEIEDPKGEDEEipeeelslEDVQAELQRVEEEI---RALEPVNMLAIQEYEEVLKRLDE 990
|
890
....*....|....*..
gi 1835643837 3057 LEHEKEKLKREAELLQK 3073
Cdd:TIGR02169 991 LKEKRAKLEEERKAILE 1007
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
768-864 |
2.54e-18 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 83.52 E-value: 2.54e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 768 EKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTN----LENLDQAFNVAERDLGVTRLLD 843
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1835643837 844 PEDVDVPQPDEKSIITYVSSM 864
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2049-2885 |
2.77e-18 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 93.98 E-value: 2.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2049 RRKIEEEIHIVrlqlETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKqvkdETQKKREAEEELKRKVQAE-K 2127
Cdd:TIGR02169 155 RRKIIDEIAGV----AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRR----EREKAERYQALLKEKREYEgY 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2128 EAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEkerqikvAQEVAQQSAAAELNskrmsfaektaqlelslkqehitvth 2207
Cdd:TIGR02169 227 ELLKEKEALERQKEAIERQLASLEEELEKLTEE-------ISELEKRLEEIEQL-------------------------- 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2208 LQEEAERLKKLHDeaekareeaekelekwhqkaNEALRLRLQAEEVAHKKTLAQ---EEAEKQKEDAEREARKRAKTEES 2284
Cdd:TIGR02169 274 LEELNKKIKDLGE--------------------EEQLRVKEKIGELEAEIASLErsiAEKERELEDAEERLAKLEAEIDK 333
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2285 ALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETEnseqqrllleeelfRLKNEVNEAIQKRKEMEEELAKVRA 2364
Cdd:TIGR02169 334 LLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELE--------------EVDKEFAETRDELKDYREKLEKLKR 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2365 EMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERI--LKEKLA 2442
Cdd:TIGR02169 400 EINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELydLKEEYD 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2443 AINDATRlKTEAEIALKEKEA----ENERLRRLAE--------------------DEAYQrKLLEEQATQHKQDI----- 2493
Cdd:TIGR02169 480 RVEKELS-KLQRELAEAEAQAraseERVRGGRAVEevlkasiqgvhgtvaqlgsvGERYA-TAIEVAAGNRLNNVvvedd 557
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2494 ---EEKIILLK---------------KSSDNELERQK---------NIVE--------------DTLRQRRIIEEEIRIL 2532
Cdd:TIGR02169 558 avaKEAIELLKrrkagratflplnkmRDERRDLSILSedgvigfavDLVEfdpkyepafkyvfgDTLVVEDIEAARRLMG 637
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2533 KVN--------FEK--------------ASVGKSDLElELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEE 2590
Cdd:TIGR02169 638 KYRmvtlegelFEKsgamtggsraprggILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASR 716
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2591 KVRKILADEKEAARQRKAALEEVERLKAKAEEAKR--------QKELAEKEAERQIQLAQ-EAALKKIDAEEKAHtaIVQ 2661
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQeienvkseLKELEARIEELEEDLHKlEEALNDLEARLSHS--RIP 794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2662 QKEQEMlqtrkqeqsilDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERlkQRAEEEAQAKAQAQdeaeklr 2741
Cdd:TIGR02169 795 EIQAEL-----------SKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE--QRIDLKEQIKSIEK------- 854
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2742 KEAELEAAKRAHAEQAALKQKQLADEEmDKHKKFAEKTLR---QKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEV 2818
Cdd:TIGR02169 855 EIENLNGKKEELEEELEELEAALRDLE-SRLGDLKKERDEleaQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL 933
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2819 TDAMRQKAQVEEELFKVKIqMEELIKLKLRIEEENK------MLIMKDKDSTQKLLVEEAEKMRQVAEEAARL 2885
Cdd:TIGR02169 934 SEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRalepvnMLAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2545-3107 |
2.98e-18 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 93.59 E-value: 2.98e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2545 DLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKI---------LADEKEAARQRKaalEEVER 2615
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIneisselpeLREELEKLEKEV---KELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2616 LKAKAEEAKRQKELAEKEAERQIQLAQEaaLKKIDAEEKAHTAIVQQKEQEM--LQTRKQEQSILDKLKEEAERAKRAAE 2693
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRE--LEERIEELKKEIEELEEKVKELkeLKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2694 DAdfaRTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAEL-EAAKRAHAEQAALKqKQLADEEMDKH 2772
Cdd:PRK03918 314 KR---LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELyEEAKAKKEELERLK-KRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2773 KKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKE----------EVTDAMRQ--KAQVEEELFKVKIQME 2840
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKelLEEYTAELKRIEKELK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2841 ELIKLKLRIEEENKMLIMK-DKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAArmrklAEDdlanQRALAEKMLKEKMQ 2919
Cdd:PRK03918 470 EIEEKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKK-----AEE----YEKLKEKLIKLKGE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2920 AIQEASRLKAEAEmLQKQKELAQEQARKFQEDKEQIEQQLakETEGFQKSLEAERR-QQLE---------------ITAE 2983
Cdd:PRK03918 541 IKSLKKELEKLEE-LKKKLAELEKKLDELEEELAELLKEL--EELGFESVEELEERlKELEpfyneylelkdaekeLERE 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2984 AERLKLQVLEMSRAQ---AKAEEDASKFKKKAEEIGNKLHQTELATKERmavvQTLEIQRQQSGKEA--EELRRAIAELE 3058
Cdd:PRK03918 618 EKELKKLEEELDKAFeelAETEKRLEELRKELEELEKKYSEEEYEELRE----EYLELSRELAGLRAelEELEKRREEIK 693
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1835643837 3059 HEKEKLKREAELLQKnsQKMQVAQQEQLRQETQVLQTTFLSEKQLLLER 3107
Cdd:PRK03918 694 KTLEKLKEELEEREK--AKKELEKLEKALERVEELREKVKKYKALLKER 740
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
765-861 |
3.37e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 83.36 E-value: 3.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDP 844
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90
....*....|....*...
gi 1835643837 845 ED-VDVPQPDEKSIITYV 861
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYL 97
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6498-6707 |
4.30e-18 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 86.73 E-value: 4.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6498 KFTDALQALMDWLYWAEPQLSEDVPIRgDKDLVSDLMDKHKIFQKELGKRASCVKTLKRSMRDLTRGSiSTDSQWLQKQM 6577
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEG-HPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6578 EELNHRWEVVCKLSVGKQARLEASLQQAEEFHTLVHyFLERLSEAERTLKYGVIPEEEKALQECQKQQQELMSVLQCQKL 6657
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEP 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6658 ALDCILSLGEEILNCCHPESIITIKSWLNVTKSRYQEVLNWAEQQGERIQ 6707
Cdd:cd00176 161 RLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLE 210
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
650-750 |
4.37e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 83.01 E-value: 4.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 650 QKKTFTKWVNKHLIKA--QRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGR--MRFHKLQNVQIALDYLKHRQVKLVN 725
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1835643837 726 IRNDDIADGNPKLTLGLIWTIILHF 750
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2551-2783 |
5.87e-18 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 89.52 E-value: 5.87e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2551 NQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILAdEKEAARQRKAALE---EVERLKAKAEEAKRQK 2627
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKA-AKQAEQAAKQAEEkqkQAEEAKAKQAAEAKAK 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2628 elAEKEAERQiqlAQEAALKKIDAEEKAH-TAIVQQKEQEMLQTRKQEqsilDKLKEEAErAKRAAEDAdfartRAEQEA 2706
Cdd:TIGR02794 136 --AEAEAERK---AKEEAAKQAEEEAKAKaAAEAKKKAEEAKKKAEAE----AKAKAEAE-AKAKAEEA-----KAKAEA 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2707 ALSRQQVEEAErlKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQK 2783
Cdd:TIGR02794 201 AKAKAAAEAAA--KAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1708-2308 |
8.88e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.31 E-value: 8.88e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1708 RTYEDQLKEVHAVpSDSKELEATKAELKKLrsqveghqplfntlEADLNKAKDVNEQMLRSHSERDVDLDRYREKVQQLL 1787
Cdd:COG1196 216 RELKEELKELEAE-LLLLKLRELEAELEEL--------------EAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1788 ERWQAILVQIDLRQRELDQLGRQLRYYRETyewlikwIKDAKQRQEQIQsvpitdsKTMKEHLLQEKKLLDEIESNRDKV 1867
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEER-------RRELEERLEELE-------EELAELEEELEELEEELEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1868 DECQKYAKQYIDAIKDYELQLVTYKAQVEpvaspakkpKVQSTSDSIIQEYVDLRTRYSELTTLTSQYIKFITETLRRLN 1947
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELA---------EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1948 DEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQL 2027
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2028 RQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDEL--QELRARAEKAEQQKK-AAQEEAERLRKQ 2104
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAlqNIVVEDDEVAAAAIEyLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2105 VKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKR 2184
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2185 MSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEA 2264
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1835643837 2265 EKQKEDAEREarkrakTEESALRQKELAEDELEKQRKLADATAQ 2308
Cdd:COG1196 738 LEELLEEEEL------LEEEALEELPEPPDLEELERELERLERE 775
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2283-3112 |
1.34e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 91.95 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2283 ESALRQKELAED--ELEKQRKLADATAQQKFSAEQELIRLKAE----TENSEQQRLLLEEELFRLKNEVNEAIQKRKEME 2356
Cdd:TIGR00618 160 AKSKEKKELLMNlfPLDQYTQLALMEFAKKKSLHGKAELLTLRsqllTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2357 EELAKVRAEMEILLQSKSRAEEESRSNTE-KSKQMLEVEASKLRELAEEAAKLRAVSEEAKR------QRQIAEDEAARQ 2429
Cdd:TIGR00618 240 QSHAYLTQKREAQEEQLKKQQLLKQLRARiEELRAQEAVLEETQERINRARKAAPLAAHIKAvtqieqQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2430 RAEAERILKEKLAAINDATRLKtEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATqhkqdIEEKIillkkssdNELE 2509
Cdd:TIGR00618 320 MRSRAKLLMKRAAHVKQQSSIE-EQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHT-----LTQHI--------HTLQ 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2510 RQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQlaleEEQRRKEAE 2589
Cdd:TIGR00618 386 QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ----CEKLEKIHL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2590 EKVRKILADEKEAARQRKAALEEVERLKAkaEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQ 2669
Cdd:TIGR00618 462 QESAQSLKEREQQLQTKEQIHLQETRKKA--VVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQ 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2670 TRKQEQSILDKLKEEAERAKRAAEDADFARtRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEaELEAA 2749
Cdd:TIGR00618 540 LETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC-EQHAL 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2750 KRAHAEQAALKQKQLadeemdkhkkfaekTLRQKSQveqeltkvKLQLEETdhqkTLLDEELQRLKEEVTDAMRQKAQVE 2829
Cdd:TIGR00618 618 LRKLQPEQDLQDVRL--------------HLQQCSQ--------ELALKLT----ALHALQLTLTQERVREHALSIRVLP 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2830 EELFkvkiqmeELIKLKLRIEEENKMLIMKDKDStqklLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRAL 2909
Cdd:TIGR00618 672 KELL-------ASRQLALQKMQSEKEQLTYWKEM----LAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2910 AEKMLKEkmqaiqeasrlkAEAEMLQKQKELAQEQARKFQEdkEQIEQQLAKETEGFQKSLEAERRQqleitaeaerlkl 2989
Cdd:TIGR00618 741 LNQSLKE------------LMHQARTVLKARTEAHFNNNEE--VTAALQTGAELSHLAAEIQFFNRL------------- 793
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2990 qvlemsraqakAEEDASKFKKKAEEIGNKLHQTELAtkermavvqtLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAE 3069
Cdd:TIGR00618 794 -----------REEDTHLLKTLEAEIGQEIPSDEDI----------LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLL 852
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 1835643837 3070 LLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIE 3112
Cdd:TIGR00618 853 KYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIK 895
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2382-3069 |
1.75e-17 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 90.94 E-value: 1.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2382 SNTEKSKQMLEVeASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAaRQRAEAERILKEKLAAINDATRLKTEAEIAlkek 2461
Cdd:pfam05483 68 SDFENSEGLSRL-YSKLYKEAEKIKKWKVSIEAELKQKENKLQEN-RKIIEAQRKAIQELQFENEKVSLKLEEEIQ---- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2462 eaENERLRRLAEDEAYQRKLLEEQATQHKQdieekiillkKSSDNELERqknivEDTLRQRRIIEEEIRILKVNFEKASV 2541
Cdd:pfam05483 142 --ENKDLIKENNATRHLCNLLKETCARSAE----------KTKKYEYER-----EETRQVYMDLNNNIEKMILAFEELRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2542 GKSDLELELN-QLKNIAEETQRSKEKAEQEA-EKQRQLAL------EEEQRRK-------EAEEKVRKILADEKEAARQR 2606
Cdd:pfam05483 205 QAENARLEMHfKLKEDHEKIQHLEEEYKKEInDKEKQVSLlliqitEKENKMKdltflleESRDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2607 KAALEEVERLKAKAEEAK---RQKELAEKEAERQIQLA----------QEAALKKIDAEEKAHTAIVQQKE------QEM 2667
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKmslQRSMSTQKALEEDLQIAtkticqlteeKEAQMEELNKAKAAHSFVVTEFEattcslEEL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2668 LQTRKQE-QSILDKLKE-EAERAKRAAEDADFARTRAEQEAALsrqqvEEAERLKQRAEEEAQAKAQAQDEAEKLR-KEA 2744
Cdd:pfam05483 365 LRTEQQRlEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVEL-----EELKKILAEDEKLLDEKKQFEKIAEELKgKEQ 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2745 ELEAAKRAhaeqaalKQKQLADEEMD--KHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAM 2822
Cdd:pfam05483 440 ELIFLLQA-------REKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMT 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2823 RQKAQVEEELFKVKIQMEELIKlKLRIEEENKMLIMKDKDSTQKLLVEEAE----KMRQVAEEAARLSIEAQEAARMRKL 2898
Cdd:pfam05483 513 LELKKHQEDIINCKKQEERMLK-QIENLEEKEMNLRDELESVREEFIQKGDevkcKLDKSEENARSIEYEVLKKEKQMKI 591
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2899 AEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQL 2978
Cdd:pfam05483 592 LENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEE 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2979 EITAEAERLKLQVLEMSRAQ---------------AKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQS 3043
Cdd:pfam05483 672 KLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNI 751
|
730 740
....*....|....*....|....*.
gi 1835643837 3044 GKEAEELRRAIAELEHEKEKLKREAE 3069
Cdd:pfam05483 752 KAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
769-866 |
1.92e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 81.47 E-value: 1.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 769 KLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD-PEDV 847
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1835643837 848 DVPQPDEKSIITYVSSMYD 866
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1777-2654 |
1.99e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.28 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1777 DRYREKVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKW--IKDAKQRQEQiqsvpitdsktmKEHLLQEK 1854
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYqaLLKEKREYEG------------YELLKEKE 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1855 KLLDEIESNRDKVDECQKYAKQYIDAIKDYELQLVTYKAQVEPVASPAKKpkvqSTSDsiiqEYVDLRTRYSELTTLTSQ 1934
Cdd:TIGR02169 234 ALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKD----LGEE----EQLRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1935 YIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEaQLAKQTqlaEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAe 2014
Cdd:TIGR02169 306 LERSIAEKERELEDAEERLAKLEAEIDKLLAEIE-ELEREI---EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2015 qqkQTIQQELQQLRQNSDM---EIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQK 2091
Cdd:TIGR02169 381 ---AETRDELKDYREKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2092 KAAQEEAERLRKQVKDETQKKREAEEELkrkvqaekeaaREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIK----- 2166
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKEL-----------SKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgt 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2167 VAQ--EVAQQSAAA--ELNSKRMSFA----EKTAQLELSLKQEH-------ITVTHLQEEAERLKKLHDEAEKAREEAEK 2231
Cdd:TIGR02169 527 VAQlgSVGERYATAieVAAGNRLNNVvvedDAVAKEAIELLKRRkagratfLPLNKMRDERRDLSILSEDGVIGFAVDLV 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2232 ELEKWHQKA--------------NEALRLRLQAEEVahkkTLAQEEAEKQ-----KEDAEREARKRAKTEESALRQKELA 2292
Cdd:TIGR02169 607 EFDPKYEPAfkyvfgdtlvvediEAARRLMGKYRMV----TLEGELFEKSgamtgGSRAPRGGILFSRSEPAELQRLRER 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2293 EDELEKQRKladataqqkfSAEQELIRLkaetenseqqrllleeelfrlKNEVNEAIQKRKEMEEELAKVRAEMEILLQS 2372
Cdd:TIGR02169 683 LEGLKRELS----------SLQSELRRI---------------------ENRLDELSQELSDASRKIGEIEKEIEQLEQE 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2373 KSRAEE---ESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATR 2449
Cdd:TIGR02169 732 EEKLKErleELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIE 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2450 LKT-EAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEkIILLKKSSDNELERQKNIVEDTLRQRRIIEEE 2528
Cdd:TIGR02169 812 ARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN-LNGKKEELEEELEELEAALRDLESRLGDLKKE 890
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2529 IRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEaEKQRQLALEEEQRRKEAEEKVRKILAdEKEAARQRKA 2608
Cdd:TIGR02169 891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEE-LSEIEDPKGEDEEIPEEELSLEDVQA-ELQRVEEEIR 968
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1835643837 2609 ALEEVERLKAK--AEEAKRQKELAEKEAerQIQLAQEAALKKIDAEEK 2654
Cdd:TIGR02169 969 ALEPVNMLAIQeyEEVLKRLDELKEKRA--KLEEERKAILERIEEYEK 1014
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2385-3228 |
2.46e-17 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 91.00 E-value: 2.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2385 EKSKQMLEVEASKLRELAEEAAklRAVSEEAKRQRQIAEDEAARQ---RAEAERILKEKLAAINDATRlKTEAEIALKEK 2461
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAE--SELKELEKKHQQLCEEKNALQeqlQAETELCAEAEEMRARLAAR-KQELEEILHEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2462 EAenerlrRLAEDEAYQRKLLEEQA--TQHKQDIEEKIillkksSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFE-- 2537
Cdd:pfam01576 81 ES------RLEEEEERSQQLQNEKKkmQQHIQDLEEQL------DEEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQns 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2538 KASVGKSDLELELNQLK-NIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEaeEKVRKILADEKEAARQRKAAL-EEVER 2615
Cdd:pfam01576 149 KLSKERKLLEERISEFTsNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKE--EKGRQELEKAKRKLEGESTDLqEQIAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2616 LKAKAEEAKRQkeLAEKEAERQIQLA-------QEAALKKIDAEEKAHTAIVQQK-EQEMLQTRKQEQSILDkLKEEAER 2687
Cdd:pfam01576 227 LQAQIAELRAQ--LAKKEEELQAALArleeetaQKNNALKKIRELEAQISELQEDlESERAARNKAEKQRRD-LGEELEA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAAEDAdFARTRAEQEAALSRQQveEAERLKQRAEEEAQA-KAQAQDEAEKLRKEAE-----LEAAKRAhaeQAALKQ 2761
Cdd:pfam01576 304 LKTELEDT-LDTTAAQQELRSKREQ--EVTELKKALEEETRShEAQLQEMRQKHTQALEelteqLEQAKRN---KANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2762 KQLADEEMDKHKKFAEKTLRQKSQveqeltkvklqleETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEE 2841
Cdd:pfam01576 378 AKQALESENAELQAELRTLQQAKQ-------------DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELES 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2842 LIKLKLRIEEENKMLiMKDKDS-------TQKLLVEEAekmRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKML 2914
Cdd:pfam01576 445 VSSLLNEAEGKNIKL-SKDVSSlesqlqdTQELLQEET---RQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLS 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2915 KEKMQAIQEASRLKAEAEMLqkqkELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEI---TAEAERLKLQV 2991
Cdd:pfam01576 521 TLQAQLSDMKKKLEEDAGTL----EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELddlLVDLDHQRQLV 596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2992 LEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLeiqrqqsGKEAEELRRAIAELEHEKEKLKREAELL 3071
Cdd:pfam01576 597 SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSL-------ARALEEALEAKEELERTNKQLRAEMEDL 669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3072 qknsqkmqVAQQEQLRQETQVLQTTflseKQLLlerEKYIEEEKAKLENLyEDEVRKAqklkqeqehqmkhlEEEKDQLK 3151
Cdd:pfam01576 670 --------VSSKDDVGKNVHELERS----KRAL---EQQVEEMKTQLEEL-EDELQAT--------------EDAKLRLE 719
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 3152 VSMDdAMKKQKEAEenvrrkqdeLQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDLAGNL 3228
Cdd:pfam01576 720 VNMQ-ALKAQFERD---------LQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQI 786
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1525-2368 |
3.41e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 90.42 E-value: 3.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1525 KQALRNLETHYQEFMRDsqdsENFLPDDRMQIEREYNNCIQKYEQLLRTQEKGEQDEVTCKNYISQLKDIRLQLEGCESR 1604
Cdd:pfam02463 207 KKALEYYQLKEKLELEE----EYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1605 TIHKIRTPMEKDPIKECSQRISEQQQIHFELEGIKKNLNKVSEKTLKVLAQKEQSSSSPLLRTEHEITHQKMDQVYSLSS 1684
Cdd:pfam02463 283 LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1685 IYLEKLKTINLVIRSTQGAEEVVRTYEDQLKEVHAVPSDSKELEATkaELKKLRSQVEghqplfntleaDLNKAKDVNEQ 1764
Cdd:pfam02463 363 KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQ--LLLELARQLE-----------DLLKEEKKEEL 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1765 MLRSHSERDVDLDRYREKVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQSVPITDSK 1844
Cdd:pfam02463 430 EILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1845 TMKEHLLQEKKLLDEIESNRDKVDEcQKYAKQYIDAIKDYELQLVTYKAQVEPVASPAKKPKVQSTSDSIIQEYVDLrtr 1924
Cdd:pfam02463 510 KVLLALIKDGVGGRIISAHGRLGDL-GVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIP--- 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1925 ySELTTLTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAkaqaEKEAEELQRRMQEEVS 2004
Cdd:pfam02463 586 -KLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK----ESGLRKGVSLEEGLAE 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2005 KREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQkhkaNAEDELQELRARA 2084
Cdd:pfam02463 661 KSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELL----ADRVQEAQDKINE 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2085 EKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMK-----QAEV 2159
Cdd:pfam02463 737 ELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEeelkeEAEL 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2160 EKERQIKVAQEVAQQSAAAELNSKRMSFA---EKTAQLELSLKQEHITVTHL-QEEAERLKKLHDEAEKAREEAEKELEK 2235
Cdd:pfam02463 817 LEEEQLLIEQEEKIKEEELEELALELKEEqklEKLAEEELERLEEEITKEELlQELLLKEEELEEQKLKDELESKEEKEK 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2236 WHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKladaTAQQKFSAEQ 2315
Cdd:pfam02463 897 EEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERN----KRLLLAKEEL 972
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2316 ELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEI 2368
Cdd:pfam02463 973 GKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLEL 1025
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2580-2988 |
3.56e-17 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 89.80 E-value: 3.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2580 EEEQRRKEAEEKVRKILADEKE-AARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKiDAEEKAhta 2658
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTMTPEyTVRYNGQTMTENEFLNQLLHIVQHQKAVSERQQQEKFEKMEQERLRQ-EKEEKA--- 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2659 ivqqkeQEMLQTRKQEqsildklkeEAERAKRAAEDADfARTRAEQEAaLSRQQVEEAERLKQRAEEEAQAKAQAQDEAE 2738
Cdd:pfam17380 310 ------REVERRRKLE---------EAEKARQAEMDRQ-AAIYAEQER-MAMERERELERIRQEERKRELERIRQEEIAM 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2739 KLRKEAELEAAKRAHAEQAALKQKQLadEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDhqktllDEELQRLKEEv 2818
Cdd:pfam17380 373 EISRMRELERLQMERQQKNERVRQEL--EAARKVKILEEERQRKIQQQKVEMEQIRAEQEEAR------QREVRRLEEE- 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2819 tdAMRQKAQVEEELFKVKIQMEeliklKLRIEEENKmlimkdkdSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKL 2898
Cdd:pfam17380 444 --RAREMERVRLEEQERQQQVE-----RLRQQEEER--------KRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAM 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2899 AEDDlaNQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELA-----QEQARKFQEDKEQIEqQLAKETEGFQKSLEAE 2973
Cdd:pfam17380 509 IEEE--RKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEerrriQEQMRKATEERSRLE-AMEREREMMRQIVESE 585
|
410
....*....|....*.
gi 1835643837 2974 R-RQQLEITAEAERLK 2988
Cdd:pfam17380 586 KaRAEYEATTPITTIK 601
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2542-3236 |
4.52e-17 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 90.18 E-value: 4.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2542 GKSDLELELNQLKNIAEETQRSKEKAEQEAEKQR----------QLALEEEQRRKEAEEKVRKILADEKEAAR-QRKAAL 2610
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKfylrqsvidlQTKLQEMQMERDAMADIRRRESQSQEDLRnQLQNTV 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2611 EEVERLKAKAEEAKRQKElAEKEAERQIQLAQEAALKKI-----DAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEea 2685
Cdd:pfam15921 152 HELEAAKCLKEDMLEDSN-TQIEQLRKMMLSHEGVLQEIrsilvDFEEASGKKIYEHDSMSTMHFRSLGSAISKILRE-- 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2686 erakrAAEDADFARTR----AEQEAALSRQQVEEAERLKQraeeeaqakaQAQDEAEKLRKEAELEAAKRAHAEQAALKQ 2761
Cdd:pfam15921 229 -----LDTEISYLKGRifpvEDQLEALKSESQNKIELLLQ----------QHQDRIEQLISEHEVEITGLTEKASSARSQ 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2762 KQLADEEMDKHKKFAEKT----LRQKSQVEQELTKVKLQLEETDHQKTLLDEELQR----LKEEVTDAMRQKAQVEEELF 2833
Cdd:pfam15921 294 ANSIQSQLEIIQEQARNQnsmyMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlvlANSELTEARTERDQFSQESG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2834 KVKIQMEELI------KLKLRIE-EENKMLImkDKDSTQKLLVEEAEKmrqvaeeaaRLSIEAQEAARMRKLaeddLANQ 2906
Cdd:pfam15921 374 NLDDQLQKLLadlhkrEKELSLEkEQNKRLW--DRDTGNSITIDHLRR---------ELDDRNMEVQRLEAL----LKAM 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2907 RALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDK-------EQIEQQLAKETEGFQKSLEAERRQQLE 2979
Cdd:pfam15921 439 KSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtakkmtlESSERTVSDLTASLQEKERAIEATNAE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2980 ITAEAERLKLQVLEMSraQAKAEEDaskfkkKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEH 3059
Cdd:pfam15921 519 ITKLRSRVDLKLQELQ--HLKNEGD------HLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQV 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3060 EKEKLKREAellqkNSQKMQVaqqeqlrQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQ 3139
Cdd:pfam15921 591 EKAQLEKEI-----NDRRLEL-------QEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQL 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3140 MKHLEEEKDQLKVSMDDamkkQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQME--EEHRIALA----- 3212
Cdd:pfam15921 659 LNEVKTSRNELNSLSED----YEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEgsDGHAMKVAmgmqk 734
|
730 740
....*....|....*....|....
gi 1835643837 3213 QTREMRTQTDDLAGNLPLTPTVVT 3236
Cdd:pfam15921 735 QITAKRGQIDALQSKIQFLEEAMT 758
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6058-6268 |
4.86e-17 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 83.65 E-value: 4.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6058 LGQFQSQLEELLQWLSHAADQLQGQRMVSvDLQSCEIELAKHKVLRNDVMSHARTVESVNEVGQGLLlqASLGDNTDTLQ 6137
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGD-DLESVEALLKKHEALEAELAAHEERVEALNELGEQLI--EEGHPDAEEIQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6138 SSLQQMNQRWEFVRTQTERKQLELEnDLSQVQDVTLEITHLLQWLENVELRLSFSKPAwGQPETTKEKLSLHLELWKEME 6217
Cdd:cd00176 79 ERLEELNQRWEELRELAEERRQRLE-EALDLQQFFRDADDLEQWLEEKEAALASEDLG-KDLESVEELLKKHKELEEELE 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 6218 CKQHVYNSARDRLQRLLASCPLSRGSVSEHSLHVLEQKWESVYTKVQDRKE 6268
Cdd:cd00176 157 AHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQK 207
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5847-6055 |
6.99e-17 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 83.26 E-value: 6.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5847 RFWHGFSELTITLNDTQQMVLDiEEASSDPDSIRTKLNTMQALREDVDNLQNDLDTLGILGVELMSSCGDmDKPNVTKSL 5926
Cdd:cd00176 4 QFLRDADELEAWLSEKEELLSS-TDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHP-DAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5927 DDLYATWNSLNKVWNEHYNKLEASLQASLSYQEAMQrLFNWLDTAEARLSEEfLVGGDLDMVKRQLLDLKEFKRELYQRK 6006
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASE-DLGKDLESVEELLKKHKELEEELEAHE 159
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 6007 VELESLHHRTLPVKCE-----DKETSTRLNDFRQRWERLEEEVVDRQHQLEAAL 6055
Cdd:cd00176 160 PRLKSLNELAEELLEEghpdaDEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2566-2763 |
7.79e-17 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 86.05 E-value: 7.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2566 KAEQEAEKQRQ----LALEEEQRRKEAEEKVRKiLADEKEAARQRKAALEEverlKAKAEEAKRQKELAEKEAERQIQLA 2641
Cdd:TIGR02794 47 AVAQQANRIQQqkkpAAKKEQERQKKLEQQAEE-AEKQRAAEQARQKELEQ----RAAAEKAAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2642 QEAALKKIDAEEKAHTAIVQQKEQEMLQtRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVE---EAER 2718
Cdd:TIGR02794 122 EEAKAKQAAEAKAKAEAEAERKAKEEAA-KQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakaKAEA 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1835643837 2719 LKQRAEEEAQAKAQA----QDEAEKLRKEAELEAAKRAHAEQAALKQKQ 2763
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAeaaaAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5957-6163 |
8.71e-17 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 82.88 E-value: 8.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5957 YQEAMQRLFNWLDTAEARLSEEfLVGGDLDMVKRQLLDLKEFKRELYQRKVELESLHHR----TLPVKCEDKETSTRLND 6032
Cdd:cd00176 5 FLRDADELEAWLSEKEELLSST-DYGDDLESVEALLKKHEALEAELAAHEERVEALNELgeqlIEEGHPDAEEIQERLEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6033 FRQRWERLEEEVVDRQHQLEAAlLGLGQFQSQLEELLQWLSHAADQLQGQRMVSvDLQSCEIELAKHKVLRNDVMSHART 6112
Cdd:cd00176 84 LNQRWEELRELAEERRQRLEEA-LDLQQFFRDADDLEQWLEEKEAALASEDLGK-DLESVEELLKKHKELEEELEAHEPR 161
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 6113 VESVNEVGQgLLLQASLGDNTDTLQSSLQQMNQRWEFVRTQTERKQLELEN 6163
Cdd:cd00176 162 LKSLNELAE-ELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEE 211
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2611-3211 |
1.03e-16 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 88.63 E-value: 1.03e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2611 EEVERLKAKAEEAKRQKELAEKEaERQIQLAQEAALKKIDAEEKAHTAIVQQKEQE---MLQTRKQEQSILDKLKEEAER 2687
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQE-NRKIIEAQRKAIQELQFENEKVSLKLEEEIQEnkdLIKENNATRHLCNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAAEDADFARTRAEQEAALSRQQVEEA----ERLKQRAEE-EAQAKAQAQDEAEKLRK-EAELEAAKRAHAEQAALKQ 2761
Cdd:pfam05483 167 SAEKTKKYEYEREETRQVYMDLNNNIEKMilafEELRVQAENaRLEMHFKLKEDHEKIQHlEEEYKKEINDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2762 KQLADEEmDKHKKFAEKTLRQKSQVEQELTKVKLQ---LEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQ 2838
Cdd:pfam05483 247 IQITEKE-NKMKDLTFLLEESRDKANQLEEKTKLQdenLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2839 MEELIKLK-LRIEEENKM-----LIMKDKDST----QKLLVEEAEKMRQVAEEAARLSIEAQ----EAARMRKLAEDDLA 2904
Cdd:pfam05483 326 ICQLTEEKeAQMEELNKAkaahsFVVTEFEATtcslEELLRTEQQRLEKNEDQLKIITMELQkkssELEEMTKFKNNKEV 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2905 NQRALaEKMLKEKMQAIQEASRLKAEAEMLQKQKE----LAQEQARKFQEDKEQI------EQQLAKETEGFQKSLEAER 2974
Cdd:pfam05483 406 ELEEL-KKILAEDEKLLDEKKQFEKIAEELKGKEQelifLLQAREKEIHDLEIQLtaiktsEEHYLKEVEDLKTELEKEK 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2975 RQQLEITAEAERLKLQVLEMSRAQA-------KAEEDASKFKKKAEEIGNK---LHQTELATKERMAVVQTLEIQRQQSG 3044
Cdd:pfam05483 485 LKNIELTAHCDKLLLENKELTQEASdmtlelkKHQEDIINCKKQEERMLKQienLEEKEMNLRDELESVREEFIQKGDEV 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3045 K----EAEELRRAIAELEHEKEKLKREAELLQKNSQKmQVAQQ----EQLRQETQVLQTTFLSEKQLLLERE---KYIEE 3113
Cdd:pfam05483 565 KckldKSEENARSIEYEVLKKEKQMKILENKCNNLKK-QIENKnkniEELHQENKALKKKGSAENKQLNAYEikvNKLEL 643
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3114 EKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADEN 3193
Cdd:pfam05483 644 ELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER 723
|
650 660
....*....|....*....|.
gi 1835643837 3194 RK---LREKLEQMEEEHRIAL 3211
Cdd:pfam05483 724 DSelgLYKNKEQEQSSAKAAL 744
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2102-2837 |
1.08e-16 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 89.13 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2102 RKQVKDETQKKRE------AEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEvAQQS 2175
Cdd:pfam12128 209 DGVVPPKSRLNRQqvehwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQE-TSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2176 AAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHdeaekaREEAEKELEKWHQKANEALRLRLQAEEVah 2255
Cdd:pfam12128 288 LNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQH------GAFLDADIETAAADQEQLPSWQSELENL-- 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2256 KKTLAQEEAEKQKEDAEREARKRAKTEESAlRQKELAEDELEKQRklaDATAQQKFSAEQELIRLKAEtenseqqrllLE 2335
Cdd:pfam12128 360 EERLKALTGKHQDVTAKYNRRRSKIKEQNN-RDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESE----------LR 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2336 EELFRLKNEVNEAIQKRKEMEEEL----AKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEAsklreLAEEAAKLRAV 2411
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLKSRLGELklrlNQATATPELLLQLENFDERIERAREEQEAANAEVER-----LQSELRQARKR 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2412 SEEAKRQRQIAEdEAARQRAEAERILKEKLAAindatrlKTEAEIALKEKEAEN--ERLRRLAEDEAYQRKLLEEQAT-- 2487
Cdd:pfam12128 501 RDQASEALRQAS-RRLEERQSALDELELQLFP-------QAGTLLHFLRKEAPDweQSIGKVISPELLHRTDLDPEVWdg 572
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2488 ------------------------QHKQDIEEKIILLKKSSDNELERQKNIvEDTLRQrriieeeiriLKVNFEKASVGk 2543
Cdd:pfam12128 573 svggelnlygvkldlkridvpewaASEEELRERLDKAEEALQSAREKQAAA-EEQLVQ----------ANGELEKASRE- 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2544 sdLELELNQLKNIAEETQRSKEKAEQEAEKQRQlALEEEQRRkeAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEA 2623
Cdd:pfam12128 641 --ETFARTALKNARLDLRRLFDEKQSEKDKKNK-ALAERKDS--ANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTE 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2624 KRQKELaEKEAERQIQLAQ-EAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRA 2702
Cdd:pfam12128 716 KQAYWQ-VVEGALDAQLALlKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEV 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2703 EQ-EAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEK--- 2778
Cdd:pfam12128 795 LRyFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKlat 874
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2779 ----------------TLRQKSQVEQELTKVKLQLEE---------TDHQKTLLDEELQRLKEEVT---------DAMRQ 2824
Cdd:pfam12128 875 lkedanseqaqgsigeRLAQLEDLKLKRDYLSESVKKyvehfknviADHSGSGLAETWESLREEDHyqndkgirlLDYRK 954
|
810
....*....|...
gi 1835643837 2825 KAQVEEELFKVKI 2837
Cdd:pfam12128 955 LVPYLEQWFDVRV 967
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2578-3124 |
1.12e-16 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 88.56 E-value: 1.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2578 ALEE-EQRRKEAEEKVRKILADEKEAARQRKAALEEVE---------RLKAKAEEAKRQKELAEKEAERQIQLAQEAALK 2647
Cdd:PRK02224 163 KLEEyRERASDARLGVERVLSDQRGSLDQLKAQIEEKEekdlherlnGLESELAELDEEIERYEEQREQARETRDEADEV 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2648 KIDAEEKahtaivqqkeQEMLQTRKQEQSILDKLKEEAERakraaEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEA 2727
Cdd:PRK02224 243 LEEHEER----------REELETLEAEIEDLRETIAETER-----EREELAEEVRDLRERLEELEEERDDLLAEAGLDDA 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2728 QAKA--QAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKT 2805
Cdd:PRK02224 308 DAEAveARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIE 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2806 LLDEELQRLKEEVTDAMRQKAQVEEELfkvkiqmEELIKLKLRIEEENKMLimKDKDSTQKLLVEEAEKMR--------- 2876
Cdd:PRK02224 388 ELEEEIEELRERFGDAPVDLGNAEDFL-------EELREERDELREREAEL--EATLRTARERVEEAEALLeagkcpecg 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2877 QVAEEAARLSIEAQEAARMRKLAED--DLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQ 2954
Cdd:PRK02224 459 QPVEGSPHVETIEEDRERVEELEAEleDLEEEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRER 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2955 IEQqLAKETEGFQKSLEAERR--QQLEITAEAERLKLQVLEMSRAQAKAEEDA-SKFKKKAEEIGNKLHQTElATKERMA 3031
Cdd:PRK02224 539 AEE-LRERAAELEAEAEEKREaaAEAEEEAEEAREEVAELNSKLAELKERIESlERIRTLLAAIADAEDEIE-RLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3032 VVQTLEIQRQQSGKEAEELRRAIAE------LEHEKEKLKREAELLQKNSQKMqvaqqEQLRQETQVLQTTF------LS 3099
Cdd:PRK02224 617 ALAELNDERRERLAEKRERKRELEAefdearIEEAREDKERAEEYLEQVEEKL-----DELREERDDLQAEIgaveneLE 691
|
570 580
....*....|....*....|....*
gi 1835643837 3100 EKQLLLEREKYIEEEKAKLENLYED 3124
Cdd:PRK02224 692 ELEELRERREALENRVEALEALYDE 716
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1956-2425 |
1.96e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 87.52 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1956 LKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQELQQLRQnsDMEI 2035
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE----ELEEELEELEAELEELRE--ELEK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2036 KSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREA 2115
Cdd:COG4717 121 LEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2116 EEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLE 2195
Cdd:COG4717 201 LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLF 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2196 LSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKW-HQKANEALRLRLQAEEVAHKKTLAQE--EAEKQKEDAE 2272
Cdd:COG4717 281 LVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELeELLAALGLPPDLSPEELLELLDRIEElqELLREAEELE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2273 REAR-KRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQK 2351
Cdd:COG4717 361 EELQlEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2352 RKEMEEELAKVRAEMEILLQSKSRAEEESRsnTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDE 2425
Cdd:COG4717 441 LEELEEELEELREELAELEAELEQLEEDGE--LAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1935-2616 |
4.14e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 86.66 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1935 YIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRmQEEVSKREVVAVDAE 2014
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEEL-KEEIEELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2015 QQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEeIHIVRLQLETMQKHKANAEDELQELRARAEKAEqqkkaa 2094
Cdd:PRK03918 252 GSKRKLEEKIRELEE----RIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLE------ 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2095 qEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRaVEDLEKFRSQAEEAER-RMKQAEVEKERQIKVAQEVaq 2173
Cdd:PRK03918 321 -EEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEER-HELYEEAKAKKEELERlKKRLTGLTPEKLEKELEEL-- 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2174 QSAAAELNSKRMSFAEKTAQLELSLKQehitvthLQEEAERLKKlhdeAEKAREEAEKELEKWHqkanealRLRLQAEEV 2253
Cdd:PRK03918 397 EKAKEEIEEEISKITARIGELKKEIKE-------LKKAIEELKK----AKGKCPVCGRELTEEH-------RKELLEEYT 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2254 AHKKTLAQEEAEKqkEDAEREARKRAKTEESALRQkelaEDELEKQRKLADataqQKFSAEQELIRLKAEtenseqqrll 2333
Cdd:PRK03918 459 AELKRIEKELKEI--EEKERKLRKELRELEKVLKK----ESELIKLKELAE----QLKELEEKLKKYNLE---------- 518
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2334 leeelfrlknEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEesrsnTEKSKQMLEveaSKLRELAEEAAKLravse 2413
Cdd:PRK03918 519 ----------ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEE-----LKKKLAELE---KKLDELEEELAEL----- 575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2414 eakrqrqiaEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDI 2493
Cdd:PRK03918 576 ---------LKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELR 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2494 EEKIILLKKSSDNELERQKNivedtlrqrriieeeirilkvNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEK 2573
Cdd:PRK03918 647 KELEELEKKYSEEEYEELRE---------------------EYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEE 705
|
650 660 670 680
....*....|....*....|....*....|....*....|....*....
gi 1835643837 2574 QRQLALEEE------QRRKEAEEKVRKILADEKEaarqrkAALEEVERL 2616
Cdd:PRK03918 706 REKAKKELEklekalERVEELREKVKKYKALLKE------RALSKVGEI 748
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
651-748 |
5.32e-16 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 76.99 E-value: 5.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 651 KKTFTKWVNKHL-IKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPRE--KGRMRFHKLQNVQIALDYLKHRQV-KLVNI 726
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1835643837 727 RNDDI-ADGNPKLTLGLIWTIIL 748
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2759-3210 |
5.85e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 86.73 E-value: 5.85e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2759 LKQKQLADEEMDKHKkfaEKTLRQKSQVEQE--LTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVK 2836
Cdd:PTZ00121 1042 LKEKDIIDEDIDGNH---EGKAEAKAHVGQDegLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAE 1118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2837 IQMEELIKLKlRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSiEAQEAARMRKLAEDDLANQRALAEKMLK- 2915
Cdd:PTZ00121 1119 EAKKKAEDAR-KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAE-EARKAEDAKKAEAARKAEEVRKAEELRKa 1196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2916 EKMQAIQEASRLKAEAEMlqkqkelaqEQARKFQEDKEQIEQQLAKET-EGFQKSLEAERRQQLEITAEAERLKLQVLEM 2994
Cdd:PTZ00121 1197 EDARKAEAARKAEEERKA---------EEARKAEDAKKAEAVKKAEEAkKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2995 SRAQAKAEEdaskfKKKAEEIgNKLHQTELATKERMAVvqtlEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKN 3074
Cdd:PTZ00121 1268 RQAAIKAEE-----ARKADEL-KKAEEKKKADEAKKAE----EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKK 1337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3075 SQKMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKyIEEEKAKLENLYE--DEVRKAQKLKQEQEHQMKHLEE--EKDQL 3150
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADElkKAAAA 1416
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3151 KVSMDDAMKKQKEaeenvRRKQDELqqldkKRQEQEKLLADENRKLREKLEQMEEEHRIA 3210
Cdd:PTZ00121 1417 KKKADEAKKKAEE-----KKKADEA-----KKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
767-878 |
5.99e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 77.34 E-value: 5.99e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 767 KEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 846
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 1835643837 847 -VDVPQPDEKSIITYVSSMYDAMprvpdVQDGV 878
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
770-865 |
6.80e-16 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 77.02 E-value: 6.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 770 LLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAErDLGVTRLLDPED-VD 848
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1835643837 849 VPQPDEKSIITYVSSMY 865
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4655-4693 |
9.26e-16 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 73.90 E-value: 9.26e-16
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 4655 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4693
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1796-2404 |
9.82e-16 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 85.50 E-value: 9.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1796 QIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIqsvpitdsKTMKEHLLQEKKLLDEIESNRDKVDECQKYAK 1875
Cdd:PRK03918 156 GLDDYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELI--------KEKEKELEEVLREINEISSELPELREELEKLE 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1876 QYIDAIKDYELQLVTYKAQVEPVASPAKK--PKVQSTSDSI------IQEYVDLRTRYSELTTLTSQYIKfITETLRRLN 1947
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKleEKIRELEERIeelkkeIEELEEKVKELKELKEKAEEYIK-LSEFYEEYL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1948 DEEKAAEKLKEEERRRLAEVEAQLAKqtqlAEAHAKAKAQAEKEAEELQRRMqEEVSKREVVAVDAEQqkqtIQQELQQL 2027
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKELEKRL-EELEERHELYEEAKA----KKEELERL 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2028 RQN-SDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRA--------RAEKAEQQKKAAQEEA 2098
Cdd:PRK03918 378 KKRlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcGRELTEEHRKELLEEY 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2099 ERLRKQVKDETQKKREAEEELkRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEK-ERQIKVAQEVAQQSAA 2177
Cdd:PRK03918 458 TAELKRIEKELKEIEEKERKL-RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIK 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2178 AElnsKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKlhdeaekareEAEKELEKWHQKANEALRLRLQAEEVAHKK 2257
Cdd:PRK03918 537 LK---GEIKSLKKELEKLEELKKKLAELEKKLDELEEELA----------ELLKELEELGFESVEELEERLKELEPFYNE 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2258 TLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADAtAQQKFSAE--QELIRLKAETENSEQQRLLLE 2335
Cdd:PRK03918 604 YLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE-LEKKYSEEeyEELREEYLELSRELAGLRAEL 682
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2336 EELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAeEESRSNTEKSKQMLEVEA-SKLRELAEE 2404
Cdd:PRK03918 683 EELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERV-EELREKVKKYKALLKERAlSKVGEIASE 751
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1984-2730 |
1.05e-15 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 85.66 E-value: 1.05e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1984 AKAQAEKEA--EELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSD-MEIKSKAKQIEEvEYNRRKieeeihivR 2060
Cdd:pfam12128 185 AKAMHSKEGkfRDVKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGiMKIRPEFTKLQQ-EFNTLE--------S 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2061 LQLETMQKHKANAEDELQElraraekaEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDL 2140
Cdd:pfam12128 256 AELRLSHLHFGYKSDETLI--------ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2141 EKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRmSFAEKTAQLELSLKQEhitvthLQEEAERLKKLHD 2220
Cdd:pfam12128 328 EDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQ-DVTAKYNRRRSKIKEQ------NNRDIAGIKDKLA 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2221 EAEKAREEAEKELEKWHQKANEALRLRLQAEevahkKTLAQEEAEKQKEDAErEARKR---AKTEESALRQKELAEDELE 2297
Cdd:pfam12128 401 KIREARDRQLAVAEDDLQALESELREQLEAG-----KLEFNEEEYRLKSRLG-ELKLRlnqATATPELLLQLENFDERIE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2298 KQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQK------------RKEM---EEELAKV 2362
Cdd:pfam12128 475 RAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflRKEApdwEQSIGKV 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2363 rAEMEILLqsksRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERIlKEKLA 2442
Cdd:pfam12128 555 -ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAA-EEQLV 628
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2443 AINDAT-RLKTEAEIALKEKEAENERLRRLA-EDEAYQRKlLEEQATQHKQDIEEKIILLkkssDNELERQKNIVEDTLR 2520
Cdd:pfam12128 629 QANGELeKASREETFARTALKNARLDLRRLFdEKQSEKDK-KNKALAERKDSANERLNSL----EAQLKQLDKKHQAWLE 703
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2521 QRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLA---------LEEEQRRKEAEEK 2591
Cdd:pfam12128 704 EQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAslgvdpdviAKLKREIRTLERK 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2592 VRKILADEKEAAR----QRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAqEAALKKIDAEEKAhtaivqqkeQEM 2667
Cdd:pfam12128 784 IERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADT-KLRRAKLEMERKA---------SEK 853
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2668 LQTRKQEQsiLDKLKEEAERAKRAAEDADFArtRAEQEAALSRQQVEEAERLKQRAEEEAQAK 2730
Cdd:pfam12128 854 QQVRLSEN--LRGLRCEMSKLATLKEDANSE--QAQGSIGERLAQLEDLKLKRDYLSESVKKY 912
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2347-2707 |
1.62e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 84.40 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2347 EAIQKRKEME---EELAKVRAEMEILLQSKSRAEEE-------------SRSNTEKSKQMLEVEASKLRELAEEAAKlra 2410
Cdd:pfam17380 234 EKMERRKESFnlaEDVTTMTPEYTVRYNGQTMTENEflnqllhivqhqkAVSERQQQEKFEKMEQERLRQEKEEKAR--- 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2411 vseEAKRQRQIAEDEAARQrAEAERilkeKLAAINDATRLKTEAE-----IALKEKEAENERLRR--LAEDEAYQRKL-- 2481
Cdd:pfam17380 311 ---EVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAMERErelerIRQEERKRELERIRQeeIAMEISRMRELer 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2482 LEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDlELELNQLKNIAEETQ 2561
Cdd:pfam17380 383 LQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAR-EMERVRLEEQERQQQ 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2562 RSKEKAEQEAEKQRQLALEEEQR-RKEAEEKVRKILADEKEaARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQiql 2640
Cdd:pfam17380 462 VERLRQQEEERKRKKLELEKEKRdRKRAEEQRRKILEKELE-ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE--- 537
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2641 AQEAALKKIDAEEKahtaivqQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDadfARTRAEQEAA 2707
Cdd:pfam17380 538 AEEERRKQQEMEER-------RRIQEQMRKATEERSRLEAMEREREMMRQIVES---EKARAEYEAT 594
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2871-3179 |
1.84e-15 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 84.40 E-value: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2871 EAEKMRQVAEEAARlsieaqEAARMRKLAEDDLANQRAL---------AEKMLKEKMQAIQEASRLKAEAEMLQ-KQKEL 2940
Cdd:pfam17380 297 EQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMdrqaaiyaeQERMAMERERELERIRQEERKRELERiRQEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2941 AQEQARKFQEDKEQIEQQlaKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEigNKLH 3020
Cdd:pfam17380 371 AMEISRMRELERLQMERQ--QKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE--ERAR 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3021 QTELATKERMAVVQTLEIQRQQSgkeaEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQttfLSE 3100
Cdd:pfam17380 447 EMERVRLEEQERQQQVERLRQQE----EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRK---LLE 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3101 KQLLlEREKYIEEEKAKLENlyEDEVRKAQKLKQEQ--EHQMKHLEEEKDQLkvsmdDAMKKQKEAEENVRRKQDELQQL 3178
Cdd:pfam17380 520 KEME-ERQKAIYEEERRREA--EEERRKQQEMEERRriQEQMRKATEERSRL-----EAMEREREMMRQIVESEKARAEY 591
|
.
gi 1835643837 3179 D 3179
Cdd:pfam17380 592 E 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2575-3205 |
2.27e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.35 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2575 RQLALEEEQRRKEAEEKV-RKILADEK---------EAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEA 2644
Cdd:PRK03918 133 RQGEIDAILESDESREKVvRQILGLDDyenayknlgEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEI 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2645 ALKKIDAEEKAHTAivqQKEQEMLQTRKQEQSILDKLKEEAERAKRAAED--ADFARTRAEQEAALS--RQQVEEAERLK 2720
Cdd:PRK03918 213 SSELPELREELEKL---EKEVKELEELKEEIEELEKELESLEGSKRKLEEkiRELEERIEELKKEIEelEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2721 QRAEEEAQAKAQAQDEAEKLRkeaELEAAKRAHAEQAALKQKQLADEEMDKHKKfaEKTLRQKSQVEQELTKVKLQLEET 2800
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELR---EIEKRLSRLEEEINGIEERIKELEEKEERL--EELKKKLKELEKRLEELEERHELY 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2801 DHQKTLLdEELQRLKEEVTDamrqkaqveEELFKVKIQMEELIKLKLRIEEENKMLI-----MKDKDSTQKLLVEEAEKM 2875
Cdd:PRK03918 365 EEAKAKK-EELERLKKRLTG---------LTPEKLEKELEELEKAKEEIEEEISKITarigeLKKEIKELKKAIEELKKA 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2876 RQVAEEAARLSIEAQEAARMRKLAEDdlanqralAEKMLKEKMQAIQEASRLKAEAEMLQKqKELAQEQARKFQEDKEQI 2955
Cdd:PRK03918 435 KGKCPVCGRELTEEHRKELLEEYTAE--------LKRIEKELKEIEEKERKLRKELRELEK-VLKKESELIKLKELAEQL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2956 EQqLAKETEGFQ-KSLEAERRqqleitaEAERLKLQVLEMSRAQAKAEEDASK---FKKKAEEIGNKLHQTELATKErma 3031
Cdd:PRK03918 506 KE-LEEKLKKYNlEELEKKAE-------EYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAELEKKLDELEEELAE--- 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3032 vvqTLEIQRQQSGKEAEELRRAIAELEhekEKLKREAELlqKNSQKMQVAQQEQLRqetqvlqttflSEKQLLLEREKYI 3111
Cdd:PRK03918 575 ---LLKELEELGFESVEELEERLKELE---PFYNEYLEL--KDAEKELEREEKELK-----------KLEEELDKAFEEL 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3112 EEEKAKLENLyEDEVRKAQKLKQEQEHQ-----MKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQE 3186
Cdd:PRK03918 636 AETEKRLEEL-RKELEELEKKYSEEEYEelreeYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELE 714
|
650
....*....|....*....
gi 1835643837 3187 KLladenRKLREKLEQMEE 3205
Cdd:PRK03918 715 KL-----EKALERVEELRE 728
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2552-2770 |
2.39e-15 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 82.16 E-value: 2.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2552 QLKNIAEETQrskEKAEQEAEKQRQLA---LEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVerlKAKAE-EAKRQK 2627
Cdd:PRK09510 84 KEQQQAEELQ---QKQAAEQERLKQLEkerLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA---KAKAEaEAKRAA 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2628 ELAEKEAERQIQLAQEAALKKIDAEEKAhtaivqqkeqemlqtrkqeqsildklKEEAERAKRAAEDadfARTRAEQEAa 2707
Cdd:PRK09510 158 AAAKKAAAEAKKKAEAEAAKKAAAEAKK--------------------------KAEAEAAAKAAAE---AKKKAEAEA- 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2708 lsrqqveeaerlKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMD 2770
Cdd:PRK09510 208 ------------KKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
767-866 |
3.51e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 75.00 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 767 KEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 846
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1835643837 847 VDV--PQPDEKSIITYVSSMYD 866
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2601-3210 |
4.26e-15 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 83.81 E-value: 4.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2601 EAARQRKAALEEVERLKAKAEEAKRQKEL---AEKEAERQIQLAQEAAlkKIDAEEKAHTAIVQQKEQEMLQTRKQE-QS 2676
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlepIRELAERYAAARERLA--ELEYLRAALRLWFAQRRLELLEAELEElRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2677 ILDKLKEEAERAKRAAEDADFARTRAEQE-AALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAK----- 2750
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeef 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2751 RAHAEQAALKQKQLADEEMDKHKKFAEkTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKeevtDAMRQKAQVEE 2830
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAE-AEAALRDLRRELRELEAEIASLERRKSNIPARLLALR----DALAEALGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2831 -------ELFKVKIQMEE---------------LI------KLKLRIEEENKMlimKDKDSTQKLLVEEAEKMRQVAEE- 2881
Cdd:COG4913 458 aelpfvgELIEVRPEEERwrgaiervlggfaltLLvppehyAAALRWVNRLHL---RGRLVYERVRTGLPDPERPRLDPd 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2882 --AARLSIEAQEAarmRKLAEDDLANQRALA----EKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQED-KEQ 2954
Cdd:COG4913 535 slAGKLDFKPHPF---RAWLEAELGRRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDnRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2955 IEQqLAKETEGFQKSLEAERRQQLEITAEAERL--KLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKErmav 3032
Cdd:COG4913 612 LAA-LEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD---- 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3033 VQTLEiqrqqsgKEAEELRRAIAELEHEKEKLKREAELLQknsQKMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIE 3112
Cdd:COG4913 687 LAALE-------EQLEELEAELEELEEELDELKGEIGRLE---KELEQAEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3113 EEKAKlenlyedevRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQK--------------EAEENVRRKQDELQQL 3178
Cdd:COG4913 757 AALGD---------AVERELRENLEERIDALRARLNRAEEELERAMRAFNrewpaetadldadlESLPEYLALLDRLEED 827
|
650 660 670
....*....|....*....|....*....|....*
gi 1835643837 3179 DKKRQEQ---EKLLADENRKLREKLEQMEEEHRIA 3210
Cdd:COG4913 828 GLPEYEErfkELLNENSIEFVADLLSKLRRAIREI 862
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2597-2789 |
6.00e-15 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 81.01 E-value: 6.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2597 ADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQeaalkkidAEEKAHTAIVQQKEQEMLQTRKQEQS 2676
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ--------AEEAAKQAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2677 ildKLKEEAErAKRAAEDADFARTRAEQEAALSRQQVEEAERlKQRAEEEAQAKA--QAQDEAEKLRKE-AELEAAKRAH 2753
Cdd:PRK09510 146 ---KAKAEAE-AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA-KKKAEAEAAAKAaaEAKKKAEAEAKKkAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|....*.
gi 1835643837 2754 AEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQE 2789
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2342-3177 |
6.13e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 83.17 E-value: 6.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQI 2421
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2422 AEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDeayqrklLEEQATQHKQDIEEKIILLK 2501
Cdd:TIGR00606 324 CQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATR-------LELDGFERGPFSERQIKNFH 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2502 KSSDNELERQKNIVEDTLR--QRRIIEEEIRILKVNFEKASVG------KSDLELELNQLKNIAEETQRSkekaeqEAEK 2573
Cdd:TIGR00606 397 TLVIERQEDEAKTAAQLCAdlQSKERLKQEQADEIRDEKKGLGrtielkKEILEKKQEELKFVIKELQQL------EGSS 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2574 QRQLALEEEQRRKEAE-EKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKEL-AEKEAERQIQLAqeaALKKIDA 2651
Cdd:TIGR00606 471 DRILELDQELRKAERElSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnHHTTTRTQMEML---TKDKMDK 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2652 EEKAHTAIVQQKEQEMLQT-----RKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEE 2726
Cdd:TIGR00606 548 DEQIRKIKSRHSDELTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDK 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2727 AQAKAQAQDEA---EKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKK---FAEKTLRQKSQVEQELTKVKLQLEET 2800
Cdd:TIGR00606 628 LFDVCGSQDEEsdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpVCQRVFQTEAELQEFISDLQSKLRLA 707
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2801 DHQKTLLDEELQRLKEEvTDAMRQKAQVEEELFKVKIQ------------MEELIKLKLRIEEENKML-IMKDKDSTQKL 2867
Cdd:TIGR00606 708 PDKLKSTESELKKKEKR-RDEMLGLAPGRQSIIDLKEKeipelrnklqkvNRDIQRLKNDIEEQETLLgTIMPEEESAKV 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2868 LVEEAEKMRQVAEEaarlsIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARK 2947
Cdd:TIGR00606 787 CLTDVTIMERFQME-----LKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH 861
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2948 FQEDKEQIEqqlakeTEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEE--DASKFKKKAEEIGNKLHQTELA 3025
Cdd:TIGR00606 862 LKSKTNELK------SEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDspLETFLEKDQQEKEELISSKETS 935
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3026 TKERMAVVQTLEIQRQQSGKEAEELRRAIAElEHEKEKLKREAELLQKNSQ-----KMQVAQQEQLRQ-----ETQVLQT 3095
Cdd:TIGR00606 936 NKKAQDKVNDIKEKVKNIHGYMKDIENKIQD-GKDDYLKQKETELNTVNAQleeceKHQEKINEDMRLmrqdiDTQKIQE 1014
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3096 TFLSEKQLLLEREKYIEEEKAKLENlYEDEVRKAQKLKQEQEHQmkHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDEL 3175
Cdd:TIGR00606 1015 RWLQDNLTLRKRENELKEVEEELKQ-HLKEMGQMQVLQMKQEHQ--KLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
..
gi 1835643837 3176 QQ 3177
Cdd:TIGR00606 1092 RE 1093
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
767-870 |
6.29e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 74.31 E-value: 6.29e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 767 KEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 846
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1835643837 847 VDV--PQPDEKSIITYVSSMYDAMPR 870
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
643-749 |
8.38e-15 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 73.86 E-value: 8.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 643 EDERDrvqKKTFTKWVNKHLIKAQrhVSDLYEDLRDGhnlISLLEVL----------SGDNLPREKGRMRfhKLQNVQIA 712
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVLdkiqpgcvnwKKVNKPKPLNKFK--KVENCNYA 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1835643837 713 LDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 749
Cdd:cd21219 71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2545-3211 |
8.67e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 82.71 E-value: 8.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2545 DLELELNQLKNIAEETQRSkEKAEQEAEKQRQLALEEEQRR--------KEAEEKVRKILA-DEKEAARQRKAALEEVER 2615
Cdd:TIGR00618 78 ELEFSLGTKIYRVHRTLRC-TRSHRKTEQPEQLYLEQKKGRgrilaakkSETEEVIHDLLKlDYKTFTRVVLLPQGEFAQ 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2616 -LKAKAEEAKRQ-KELAEKEAERQIQLAQEAALKKIDAE---EKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKr 2690
Cdd:TIGR00618 157 fLKAKSKEKKELlMNLFPLDQYTQLALMEFAKKKSLHGKaelLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREAL- 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2691 AAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKaqaQDEAEKLRKEAELeaakRAHAEQAALKQKQLADEEMD 2770
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ---EAVLEETQERINR----ARKAAPLAAHIKAVTQIEQQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2771 KHKKFAE--KTLRQKSQVEQELTKVKLQLEETDHQKTLLdEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLR 2848
Cdd:TIGR00618 309 AQRIHTElqSKMRSRAKLLMKRAAHVKQQSSIEEQRRLL-QTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQ 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2849 IEeenkMLIMKDKDSTQKLLVEEAEKMRQVAEEAAR--LSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASR 2926
Cdd:TIGR00618 388 KT----TLTQKLQSLCKELDILQREQATIDTRTSAFrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQE 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2927 ----LKAEAEMLQKQKELAQEQARKFQEDKEQIE--QQLAKETEGFQKSLEAERRQQLEITAEAERLK---------LQV 2991
Cdd:TIGR00618 464 saqsLKEREQQLQTKEQIHLQETRKKAVVLARLLelQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQrgeqtyaqlETS 543
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2992 LEMSRAQAKAE-EDASKFKKKAEEIGN---KLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEH-EKEKLKR 3066
Cdd:TIGR00618 544 EEDVYHQLTSErKQRASLKEQMQEIQQsfsILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHaLLRKLQP 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3067 EAELLQKNSQKMQVAQQEQLrqetqvlqttflseKQLLLEREkyieeekakLENLYEDEVRKA---------------QK 3131
Cdd:TIGR00618 624 EQDLQDVRLHLQQCSQELAL--------------KLTALHAL---------QLTLTQERVREHalsirvlpkellasrQL 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3132 LKQEQEHQMKHLEEEKDQLKVSmDDAMKKQKEAEENVRRKQDELQQLDKKRQEQeklLADENRKLREKLEQMEEEHRIAL 3211
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQC-QTLLRELETHIEEYDREFNEIENASSSLGSD---LAAREDALNQSLKELMHQARTVL 756
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2708-3216 |
9.30e-15 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 82.58 E-value: 9.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2708 LSRQQVEeaerlkqRAEEEAQAKAQAQDEAEKLRK-EAELEAAKRAHAEQAALKQKQLADE--EMDKHKKFAEKTLRQKS 2784
Cdd:pfam12128 218 LNRQQVE-------HWIRDIQAIAGIMKIRPEFTKlQQEFNTLESAELRLSHLHFGYKSDEtlIASRQEERQETSAELNQ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2785 QVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEE---ELFKVKIQMEELIKLKLR-IEEENKMLIMKD 2860
Cdd:pfam12128 291 LLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDadiETAAADQEQLPSWQSELEnLEERLKALTGKH 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2861 KDSTQKLLVEEAEKMRQVAEEAARLSIEA----QEAARMRKLAEDDLANQralaEKMLKEKMQAiqeasrLKAEAEMLQK 2936
Cdd:pfam12128 371 QDVTAKYNRRRSKIKEQNNRDIAGIKDKLakirEARDRQLAVAEDDLQAL----ESELREQLEA------GKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2937 QKELAQEQArKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLemsraqakaeedasKFKKKAEEIG 3016
Cdd:pfam12128 441 RLKSRLGEL-KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELR--------------QARKRRDQAS 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3017 NKLHQTELATKERMAVVQTLEIQ-RQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAqqEQLRQETQVLQT 3095
Cdd:pfam12128 506 EALRQASRRLEERQSALDELELQlFPQAGTLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWD--GSVGGELNLYGV 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3096 TfLSEKQL----LLEREKYIEEEKAKLENLYEDevrkAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRK 3171
Cdd:pfam12128 584 K-LDLKRIdvpeWAASEEELRERLDKAEEALQS----AREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRL 658
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1835643837 3172 QDELQQLDKKRQEQ---EKLLADEN-RKLREKLEQMEEEHRIALAQTRE 3216
Cdd:pfam12128 659 FDEKQSEKDKKNKAlaeRKDSANERlNSLEAQLKQLDKKHQAWLEEQKE 707
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4078-4116 |
1.28e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.82 E-value: 1.28e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 4078 ILEAQIATGGIIDPVHSHRVPVDIAYKRGYFDEEMNKIL 4116
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3420-3458 |
1.76e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.76e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 3420 LLEAQIATGGIIDPVDSHRLPLEVAYKRNYFDEEMNEVL 3458
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2557-2904 |
1.89e-14 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 80.30 E-value: 1.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2557 AEETQRSKE-KAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLK---AKAEEaKRQKELAEk 2632
Cdd:pfam02029 4 EEEAARERRrRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLdrtAKREE-RRQKRLQE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2633 EAERQIQLAQEA-------ALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEdadfarTRAEQE 2705
Cdd:pfam02029 82 ALERQKEFDPTIadekesvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEV------RQAEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2706 AALSRQQVEEAERL-KQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAAlkqkQLADEEMDKHKKFAEKTLRQKS 2784
Cdd:pfam02029 156 GEEEEDKSEEAEEVpTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKS----QNGEEEVTKLKVTTKRRQGGLS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2785 QVEQELTKVKLQLeETDHQKTLLDEELQRLKEEVTDAMRQKAQ-VEEELFKVKIQMEEliKLKLRIEEENKmlimKDKDS 2863
Cdd:pfam02029 232 QSQEREEEAEVFL-EAEQKLEELRRRRQEKESEEFEKLRQKQQeAELELEELKKKREE--RRKLLEEEEQR----RKQEE 304
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1835643837 2864 TQKLLVEEAEKmRQVAEEAARLSIEAQEaaRMRKLAEDDLA 2904
Cdd:pfam02029 305 AERKLREEEEK-RRMKEEIERRRAEAAE--KRQKLPEDSSS 342
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2233-2851 |
2.33e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.85 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2233 LEKWHQKANEAlrlRLQAEEVAHKKTLAQEEAEKQKEDAE-REARKRAKTEESALRQKELAEDELEKQRKLADATAQQKF 2311
Cdd:PRK02224 164 LEEYRERASDA---RLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGLESELAELDEEIERYEEQREQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2312 S-------AEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEIllqskSRAEEESrsnt 2384
Cdd:PRK02224 241 EvleeheeRREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGL-----DDADAEA---- 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2385 ekskqmleVEAsKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEklaaindATRLKTEAEIAlkEKEAE 2464
Cdd:PRK02224 312 --------VEA-RREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEER-------AEELREEAAEL--ESELE 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2465 NERlrrlaedeayqrklleEQATQHKQDIEEkiillkksSDNELERQKNIVEDTlrqrriieeeirilKVNFEKASVGKS 2544
Cdd:PRK02224 374 EAR----------------EAVEDRREEIEE--------LEEEIEELRERFGDA--------------PVDLGNAEDFLE 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2545 DLELELNQLKNIAEETQRSKEKAEQEAEKQRQLaLEE------EQRRKEAEEkvrkilADEKEAARQRKAALEEvERLKA 2618
Cdd:PRK02224 416 ELREERDELREREAELEATLRTARERVEEAEAL-LEAgkcpecGQPVEGSPH------VETIEEDRERVEELEA-ELEDL 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2619 KAEEAKRQKELAE----KEAERQIQlaqeaalkkiDAEEKAHTAivqqkeQEMLQTRKqeqsilDKLKEEAERAKRAAED 2694
Cdd:PRK02224 488 EEEVEEVEERLERaedlVEAEDRIE----------RLEERREDL------EELIAERR------ETIEEKRERAEELRER 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2695 ADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAA---KRAHAEQAALKQKQLADEEMDK 2771
Cdd:PRK02224 546 AAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAiadAEDEIERLREKREALAELNDER 625
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2772 HKKFAEKTLRqKSQVEQELTKVKlqLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEE 2851
Cdd:PRK02224 626 RERLAEKRER-KRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREA 702
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2045-2433 |
2.33e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 80.94 E-value: 2.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2045 VEYNRRKIEEEIHIVRLqLETMQKHKANAEDELQEL--RARAEKAEQQKKAAQEEAERLRKQvkDETQKKREAEEELKRK 2122
Cdd:pfam17380 258 VRYNGQTMTENEFLNQL-LHIVQHQKAVSERQQQEKfeKMEQERLRQEKEEKAREVERRRKL--EEAEKARQAEMDRQAA 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2123 VQAEKE-AAREKQRAVEdlekfRSQAEEAERrmkqaEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ-LELSLK- 2199
Cdd:pfam17380 335 IYAEQErMAMERERELE-----RIRQEERKR-----ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeLEAARKv 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2200 --QEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKwhQKANEALRLRLQAEEVAHK-KTLAQEEAEKQKEDAEREAR 2276
Cdd:pfam17380 405 kiLEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKE 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2277 KRAKTEESALRQKELAEDELEKQRKLADATAQQKFSaeqelirlkaetenseqqrllleeelfrlknevneaiqkRKEME 2356
Cdd:pfam17380 483 KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLL---------------------------------------EKEME 523
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2357 EELAKVRAEmeillQSKSRAEEESRSN--TEKSKQMLEveasKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEA 2433
Cdd:pfam17380 524 ERQKAIYEE-----ERRREAEEERRKQqeMEERRRIQE----QMRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2097-3150 |
2.34e-14 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 81.25 E-value: 2.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2097 EAERLRKQVKDETQKKR--EAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMkqaeVEKERQIKVAQEVAQq 2174
Cdd:TIGR00606 167 EGKALKQKFDEIFSATRyiKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQI----TSKEAQLESSREIVK- 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2175 saaaelnskrmSFAEKTAQLELSLKQ-EHI--TVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRlrlqae 2251
Cdd:TIGR00606 242 -----------SYENELDPLKNRLKEiEHNlsKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLN------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2252 EVAHKKTLAQEEAEKQKEDAEREARKRAKteESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQR 2331
Cdd:TIGR00606 305 DLYHNHQRTVREKERELVDCQRELEKLNK--ERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGF 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2332 LLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAV 2411
Cdd:TIGR00606 383 ERGPFSERQIKNFHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2412 SEEAK-RQRQIAEDEAARQRAEAERILKEKlaaiNDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQhk 2490
Cdd:TIGR00606 463 LQQLEgSSDRILELDQELRKAERELSKAEK----NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ-- 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2491 qdiEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKasvgksdleleLNQLKNIAEETQRSKEKAEQE 2570
Cdd:TIGR00606 537 ---MEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHS-----------KSKEINQTRDRLAKLNKELAS 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2571 AEKQRQLALEEEQRRKEAEEKVRKILADekeaARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKID 2650
Cdd:TIGR00606 603 LEQNKNHINNELESKEEQLSSYEDKLFD----VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQS 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2651 AEEKAHTAIVQQKEQEMLQTRKQEQSIL--DKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQ 2728
Cdd:TIGR00606 679 CCPVCQRVFQTEAELQEFISDLQSKLRLapDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNR 758
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2729 AKAQAQDEAEKLRKE-----AELEAAKRAHAEQAALKQKQLADEEMDKhkkfaektlrqksQVEQELTKVklqleetdhQ 2803
Cdd:TIGR00606 759 DIQRLKNDIEEQETLlgtimPEEESAKVCLTDVTIMERFQMELKDVER-------------KIAQQAAKL---------Q 816
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2804 KTLLDEELQRLKEEVTDAmrqkaqvEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKD-STQKL-LVEEAEKMRQVAEE 2881
Cdd:TIGR00606 817 GSDLDRTVQQVNQEKQEK-------QHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElKSEKLqIGTNLQRRQQFEEQ 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2882 AARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMlqkqkelaqeqarKFQEDKEQIEQQLAK 2961
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQD-------------KVNDIKEKVKNIHGY 956
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2962 ETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKkkaeeignklhqtelatkermavvQTLEIQRQ 3041
Cdd:TIGR00606 957 MKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMR------------------------QDIDTQKI 1012
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3042 QSGKEAEELRRAIaeLEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLE-N 3120
Cdd:TIGR00606 1013 QERWLQDNLTLRK--RENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKkE 1090
|
1050 1060 1070
....*....|....*....|....*....|
gi 1835643837 3121 LYEDEVRKAQKLKQEQEHQMKHLEEEKDQL 3150
Cdd:TIGR00606 1091 LREPQFRDAEEKYREMMIVMRTTELVNKDL 1120
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2547-3019 |
2.63e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.58 E-value: 2.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2547 ELELNQLKNIAEETQRSKEKAEQEAEKQRQLA-LEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKR 2625
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEeLEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2626 QKELAEKEAERQIQLAQEaalkkIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQE 2705
Cdd:COG4717 147 RLEELEERLEELRELEEE-----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2706 AALSRQQVEEAERLKQRAEEEAQAKAQAQ-------------------DEAEKLRKEAELEAAKRAHAEQAALKQKQLAD 2766
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLllliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2767 EEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEevtdAMRQKAQVEEELfkvkiqmeeliKLK 2846
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE----LLREAEELEEEL-----------QLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2847 LRIEEENKMLIMKDKDSTQKL--LVEEAEKMRQVAEEAARLSieaqeaARMRKLAEDDLANQRALAEKMLKEKMQaiqea 2924
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELraALEQAEEYQELKEELEELE------EQLEELLGELEELLEALDEEELEEELE----- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2925 sRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKaEED 3004
Cdd:COG4717 436 -ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR-EER 513
|
490
....*....|....*
gi 1835643837 3005 ASKFKKKAEEIGNKL 3019
Cdd:COG4717 514 LPPVLERASEYFSRL 528
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
647-746 |
2.89e-14 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 72.18 E-value: 2.89e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 647 DRVQKKTFTKWVNKHLIKAQ-RHVSDLYEDLRDGHNLISLLEVLSGDNLPRE---KGRMRFHKLQNVQIALDYL-KHRQV 721
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1835643837 722 KLVNIRNDDIADGNPKLTLGLIWTI 746
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2466-3222 |
2.93e-14 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 80.93 E-value: 2.93e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2466 ERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDN------ELERQKNIVEDTLRqrriieeeirilkvnfeKA 2539
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDlqtklqEMQMERDAMADIRR-----------------RE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2540 SVGKSDLElelNQLKNIAEETQRSK-------EKAEQEAEKQRQLALEEEQRRKEaeekVRKILADEKEAARQRKAALEE 2612
Cdd:pfam15921 137 SQSQEDLR---NQLQNTVHELEAAKclkedmlEDSNTQIEQLRKMMLSHEGVLQE----IRSILVDFEEASGKKIYEHDS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2613 VERLKAKAEEAKRQKELAEKEAERQIQLAQ----EAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSI-LDKLKEEAER 2687
Cdd:pfam15921 210 MSTMHFRSLGSAISKILRELDTEISYLKGRifpvEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVeITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAA----EDADFARTRAEQEAALSRQQVEEAER-LKQRAEEEAQAKAQAQDEAEKLRKEAELEAAK--RAHAEQAALK 2760
Cdd:pfam15921 290 ARSQAnsiqSQLEIIQEQARNQNSMYMRQLSDLEStVSQLRSELREAKRMYEDKIEELEKQLVLANSEltEARTERDQFS 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2761 QK------QLADEEMDKHKKFAEKTLrQKSQVEQELTKVKLQLEETDHQKTLLDE---ELQRLkEEVTDAMRQKAQVEEE 2831
Cdd:pfam15921 370 QEsgnlddQLQKLLADLHKREKELSL-EKEQNKRLWDRDTGNSITIDHLRRELDDrnmEVQRL-EALLKAMKSECQGQME 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2832 LFKVKIQ-----MEELIKLKLRIEEENKML-IMKDKDSTQKLLVEEAEkmRQVAEEAARLsieaQEAARMRKLAEDDLAN 2905
Cdd:pfam15921 448 RQMAAIQgknesLEKVSSLTAQLESTKEMLrKVVEELTAKKMTLESSE--RTVSDLTASL----QEKERAIEATNAEITK 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2906 QRALAEKMLKEKMQAIQEASRLK---AEAEMLQKQkelAQEQARKFQEDKEQIEQ--QLAKETEGFQKSLEAERrQQLEI 2980
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDHLRnvqTECEALKLQ---MAEKDKVIEILRQQIENmtQLVGQHGRTAGAMQVEK-AQLEK 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2981 TAEAERLKLQVLEMsraqAKAEEDASKFKKKAEEIGNKLHQTEL--ATKERMAVVQTLEIQRQQSGKEAEELRRAIAELE 3058
Cdd:pfam15921 598 EINDRRLELQEFKI----LKDKKDAKIRELEARVSDLELEKVKLvnAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLS 673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3059 HEKEKLKReaellqknsqkmqvaqqeQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLyEDEVRKAQKLKQEQEH 3138
Cdd:pfam15921 674 EDYEVLKR------------------NFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSM-EGSDGHAMKVAMGMQK 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3139 QMKHLEEEKDQLKvsmdDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMR 3218
Cdd:pfam15921 735 QITAKRGQIDALQ----SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME 810
|
....
gi 1835643837 3219 TQTD 3222
Cdd:pfam15921 811 VALD 814
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
765-865 |
3.20e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 72.41 E-value: 3.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAErDLGVTRLLDP 844
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1835643837 845 ED-VDVPQPDEKSIITYVSSMY 865
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3747-3785 |
3.49e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.66 E-value: 3.49e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 3747 LLDAQLATGGIIDPVNSHRVPLDIAYKRGYLDEETNRSL 3785
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
650-750 |
4.02e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.95 E-value: 4.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 650 QKKTFTKWVNKHLIK--AQRHVSDLYEDLRDGHNLISLLEVLSGDNL------PREKGRMRfhklQNVQIALDYLKHRQV 721
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1835643837 722 KLVNIRNDDIADGNPKLTLGLIWTIILHF 750
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
652-753 |
6.63e-14 |
|
third calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409147 Cd Length: 117 Bit Score: 71.50 E-value: 6.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 652 KTFTKWVNKhlIKAQRHVSDLYEDLRDGHNLISLLEVL-------SGDNLPREKGRMRFHKLQNVQIALDYLKHRQVKLV 724
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1835643837 725 NIRNDDIADGNPKLTLGLIWTIILHFQIS 753
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
668-747 |
6.86e-14 |
|
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of the CH domain in the middle region. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409072 Cd Length: 113 Bit Score: 71.47 E-value: 6.86e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 668 HVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRM----RFHKLQNVQIALDYLKHRQV----KLVNIRNDDIADGNPKLT 739
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1835643837 740 LGLIWTII 747
Cdd:cd21223 105 LALLWRII 112
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2607-2790 |
7.80e-14 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 76.81 E-value: 7.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2607 KAALEEVERLKAKAEEAKRQKELAEKEAERQiqlaQEAALKKIDAEEKAHTAIVQQK--EQEMLQTRKQEQSILDKLKEE 2684
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ----AEEAEKQRAAEQARQKELEQRAaaEKAAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2685 AERAKRAAEDAdfartRAEQEAALSRQQVEEAERlkqRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQL 2764
Cdd:TIGR02794 122 EEAKAKQAAEA-----KAKAEAEAERKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEE 193
|
170 180
....*....|....*....|....*.
gi 1835643837 2765 ADEEMDKHKKFAEKTLRQKSQVEQEL 2790
Cdd:TIGR02794 194 AKAKAEAAKAKAAAEAAAKAEAEAAA 219
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
765-862 |
1.07e-13 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.49 E-value: 1.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGyqgLHCDNFTTSWRDGRLFNAIIHRHKPVLI----DMNKVYRqtnLENLDQAFNVAERDLGVTR 840
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 1835643837 841 LLDPEDVDVPQPDEKSIITYVS 862
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
767-868 |
1.11e-13 |
|
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 (SMTNL1), also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL1 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409109 Cd Length: 116 Bit Score: 70.88 E-value: 1.11e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 767 KEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 846
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1835643837 847 -VDVPQPDEKSIITYVSSMYDAM 868
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2437-3218 |
1.15e-13 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 78.94 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2437 LKEKLAAINDATR----LKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQ----ATQHKQDIEEKIILLKKSSDNEL 2508
Cdd:TIGR00606 171 LKQKFDEIFSATRyikaLETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRdqitSKEAQLESSREIVKSYENELDPL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2509 ERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELEL--------NQLKNIAEETQRS-KEKAEQEAEKQRQLAL 2579
Cdd:TIGR00606 251 KNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMekvfqgtdEQLNDLYHNHQRTvREKERELVDCQRELEK 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2580 EEEQRRKEAEEKVrKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELA--EKEAERQIQLAQEAALKKIDAEEKAHT 2657
Cdd:TIGR00606 331 LNKERRLLNQEKT-ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDgfERGPFSERQIKNFHTLVIERQEDEAKT 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2658 AIVQQKEQEMLQTRKQEQsiLDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEA 2737
Cdd:TIGR00606 410 AAQLCADLQSKERLKQEQ--ADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAEREL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2738 EKLRKEAELEAAKrahAEQAALKQKQLadeEMDKHKKFAEKTLRQKSQVEQELTkvklQLEETDHQKTLLDEELQRLKEE 2817
Cdd:TIGR00606 488 SKAEKNSLTETLK---KEVKSLQNEKA---DLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDKMDKDEQIRKIKSR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2818 VTDAMR-------QKAQVEEELFK----VKIQMEELIKLKLRIE--EENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAAR 2884
Cdd:TIGR00606 558 HSDELTsllgyfpNKKQLEDWLHSkskeINQTRDRLAKLNKELAslEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2885 LSIEAQEAARMRKLAED--DLANQRALAEKMLKEKMQAIQEASRL-----KAEAEMLQKQKELaQEQARKFQEDKEQIEQ 2957
Cdd:TIGR00606 638 ESDLERLKEEIEKSSKQraMLAGATAVYSQFITQLTDENQSCCPVcqrvfQTEAELQEFISDL-QSKLRLAPDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2958 QLAKETEGFQKSLEAERRQQLEI---TAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLH-------------- 3020
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIdlkEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEEsakvcltdvtimer 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3021 -QTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQ-------------------KMQV 3080
Cdd:TIGR00606 797 fQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQdqqeqiqhlksktnelkseKLQI 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3081 AQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMD----- 3155
Cdd:TIGR00606 877 GTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKnihgy 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3156 ------------DAMKKQKEAE---------ENVRRKQDELQQLDKKRQE------QEKLLADE--NRKLREKLEQMEEE 3206
Cdd:TIGR00606 957 mkdienkiqdgkDDYLKQKETElntvnaqleECEKHQEKINEDMRLMRQDidtqkiQERWLQDNltLRKRENELKEVEEE 1036
|
890
....*....|..
gi 1835643837 3207 HRIALAQTREMR 3218
Cdd:TIGR00606 1037 LKQHLKEMGQMQ 1048
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1623-2156 |
1.15e-13 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 78.83 E-value: 1.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1623 QRISEQQQIHFELEGIKKNLNKVsEKTLKVLAQKEQSSSSPLLRTEHEITHqkmdqvyslssiylEKLKTINLVIRSTQG 1702
Cdd:COG1196 257 ELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIAR--------------LEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1703 AEEVVRTYEDQLKEVHAVPSDSKELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRSHSERDVDLDRYREK 1782
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1783 VQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQsvpiTDSKTMKEHLLQEKKLLDEIES 1862
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELE----EEEEALLELLAELLEEAALLEA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1863 NRDKVDECQKYAKQYIDAIKDYELQLVTYKAQVEPVASPAKKPKVQSTSDSIIQEYVDLRTRYSELTTLTSQYIkfiteT 1942
Cdd:COG1196 478 ALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNI-----V 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1943 LRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAK---------AKAQAEKEAEELQRRMQEEVSKREVVAVDA 2013
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALArgaigaavdLVASDLREADARYYVLGDTLLGRTLVAARL 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2014 EQ---QKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQ 2090
Cdd:COG1196 633 EAalrRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2091 KKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQ 2156
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2363-3198 |
1.37e-13 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 78.84 E-value: 1.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2363 RAEMEILLQSKSRAEEESRsnteKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAED------EAARQRAEAERi 2436
Cdd:COG3096 277 ANERRELSERALELRRELF----GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnlvqTALRQQEKIER- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2437 LKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEA---------YQRKLLEEQ--ATQHKQDIeekiillkkssd 2505
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslksqladYQQALDVQQtrAIQYQQAV------------ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2506 NELERQKNIVedtlrqrriieeeirilkvnfekasvGKSDLELElnqlkNIAEETQRSKEKAEQEAEKQRQLaleeEQRr 2585
Cdd:COG3096 420 QALEKARALC--------------------------GLPDLTPE-----NAEDYLAAFRAKEQQATEEVLEL----EQK- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2586 keaeekvrkiLADEKEAARQRKAALEEVERLKAKAEEA---KRQKELAEKEAERQIQLAQEAALKK--IDAEEKAHtaiv 2660
Cdd:COG3096 464 ----------LSVADAARRQFEKAYELVCKIAGEVERSqawQTARELLRRYRSQQALAQRLQQLRAqlAELEQRLR---- 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2661 QQKEQEMLQTR-----KQEQSILDKLKEEAERAKRAAEDA-DFARTRAEQEAALsRQQVEEAERLKQRAEEEAQAKAQAQ 2734
Cdd:COG3096 530 QQQNAERLLEEfcqriGQQLDAAEELEELLAELEAQLEELeEQAAEAVEQRSEL-RQQLEQLRARIKELAARAPAWLAAQ 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2735 DEAEKLRKEAElEAAKRAHAEQAALkQKQLADEemdkhkkfaektlRQKSQVEQELTKVKLQLEETDHQktLL------D 2808
Cdd:COG3096 609 DALERLREQSG-EALADSQEVTAAM-QQLLERE-------------REATVERDELAARKQALESQIER--LSqpggaeD 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2809 EELQRLKEE--------------VTDA---------MRQkAQVEEELFKVKIQMEELiklklriEE--ENKMLIMKDKDS 2863
Cdd:COG3096 672 PRLLALAERlggvllseiyddvtLEDApyfsalygpARH-AIVVPDLSAVKEQLAGL-------EDcpEDLYLIEGDPDS 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2864 TQK--LLVEEAEK--MRQVAEEAARLSIEAQE-----AARMRKLAE-----DDLANQRALAEKMLKEKMQAIQEASRLKA 2929
Cdd:COG3096 744 FDDsvFDAEELEDavVVKLSDRQWRYSRFPEVplfgrAAREKRLEElraerDELAEQYAKASFDVQKLQRLHQAFSQFVG 823
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2930 -----------EAEMLQKQKELAQEQARkfQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQ 2998
Cdd:COG3096 824 ghlavafapdpEAELAALRQRRSELERE--LAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2999 AKAEEDASKFKK-------KAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEH-----EKEKLKR 3066
Cdd:COG3096 902 LDAAQEAQAFIQqhgkalaQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfsyedAVGLLGE 981
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3067 EAELLQKNSQKMQVAQQEQLRQETQVlqttflseKQLLLEREKYIEEEKAklenlyedeVRKAQKLKQEqehQMKHLEEE 3146
Cdd:COG3096 982 NSDLNEKLRARLEQAEEARREAREQL--------RQAQAQYSQYNQVLAS---------LKSSRDAKQQ---TLQELEQE 1041
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3147 KDQLKVSMDDamkkqkEAEENVRRKQDELQ-----------QLDKKRQEQEKLLADENRKLRE 3198
Cdd:COG3096 1042 LEELGVQADA------EAEERARIRRDELHeelsqnrsrrsQLEKQLTRCEAEMDSLQKRLRK 1098
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
767-867 |
1.52e-13 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also called NEDD9-interacting protein with calponin homology and LIM domains, acts as a [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-1 acts as a cytoskeletal regulator that connects NEDD9 to intermediate filaments. It also acts as a negative regulator of apoptosis via its interaction with STK38 and STK38L. MICAL-1 is a Rab effector protein that plays a role in vesicle trafficking. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409045 Cd Length: 106 Bit Score: 70.07 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 767 KEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 846
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1835643837 847 VdVPQPDEKSIITYVSSMYDA 867
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2299-3157 |
1.69e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 78.24 E-value: 1.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2299 QRKLADATA---QQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKnevneaiQKRKEMEEELAKVRAEMEILLQSKSR 2375
Cdd:pfam15921 91 QRRLNESNElheKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRES-------QSQEDLRNQLQNTVHELEAAKCLKED 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2376 AEEESRSNTEKSKQMLEVEASKLRELA------EEAAKLRAVSEEAK-----RQRQIAEDEAARQRAEAERILKEKLAAI 2444
Cdd:pfam15921 164 MLEDSNTQIEQLRKMMLSHEGVLQEIRsilvdfEEASGKKIYEHDSMstmhfRSLGSAISKILRELDTEISYLKGRIFPV 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2445 NDATR-LKTEA----EIALKEKEaenERLRRLAEDEAYQRKLLEEQATQhkqdieekiillKKSSDNELERQKNIVEDTL 2519
Cdd:pfam15921 244 EDQLEaLKSESqnkiELLLQQHQ---DRIEQLISEHEVEITGLTEKASS------------ARSQANSIQSQLEIIQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2520 RQRRIIEEEIRilkvnfekasvgkSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLA--------LEEEQRRKEA--- 2588
Cdd:pfam15921 309 RNQNSMYMRQL-------------SDLESTVSQLRSELREAKRMYEDKIEELEKQLVLAnseltearTERDQFSQESgnl 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2589 EEKVRKILADEKEAARQRKAALEEVERL------------KAKAEEAKRQKELAEKEA-------ERQIQLAQE-AALK- 2647
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLwdrdtgnsitidHLRRELDDRNMEVQRLEAllkamksECQGQMERQmAAIQg 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2648 KIDAEEKAHTAIVQ-QKEQEMLQTRKQEQSILDKLKEEAERAKraaedADFARTRAEQEAALSRQQVEeAERLKQRAEEE 2726
Cdd:pfam15921 456 KNESLEKVSSLTAQlESTKEMLRKVVEELTAKKMTLESSERTV-----SDLTASLQEKERAIEATNAE-ITKLRSRVDLK 529
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2727 AQAKAQAQDEAEKLRK-EAELEAAKRAHAEQAAL-----KQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEET 2800
Cdd:pfam15921 530 LQELQHLKNEGDHLRNvQTECEALKLQMAEKDKVieilrQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEF 609
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2801 DHQKTLLDEELQRLKEEVTDAmrqkaqveeelfkvkiqmeELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQvae 2880
Cdd:pfam15921 610 KILKDKKDAKIRELEARVSDL-------------------ELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRN--- 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2881 EAARLSIEAQEAARmrklaeddlaNQRALAEKMlkekmqaiqEASRLKAEAEMLQKQKELaqEQARKFQEDKEQIEQQLA 2960
Cdd:pfam15921 668 ELNSLSEDYEVLKR----------NFRNKSEEM---------ETTTNKLKMQLKSAQSEL--EQTRNTLKSMEGSDGHAM 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2961 KETEGFQKSLEAERRQqleitAEAERLKLQVLEmsraqaKAEEDASKFKKKAEEIGNKLHQtELAT--KERMAVVQTLEI 3038
Cdd:pfam15921 727 KVAMGMQKQITAKRGQ-----IDALQSKIQFLE------EAMTNANKEKHFLKEEKNKLSQ-ELSTvaTEKNKMAGELEV 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3039 QRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKmQVAQQEQLRQETQVLQ----TTFLSEKQLLLE-------- 3106
Cdd:pfam15921 795 LRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE-SVRLKLQHTLDVKELQgpgyTSNSSMKPRLLQpasftrth 873
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 3107 --------REKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKhlEEEKDQLKVSMDDA 3157
Cdd:pfam15921 874 snvpssqsTASFLSHHSRKTNALKEDPTRDLKQLLQELRSVIN--EEPTVQLSKAEDKG 930
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
765-865 |
2.10e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 70.06 E-value: 2.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAErDLGVTRLLDP 844
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1835643837 845 ED-VDVPQPDEKSIITYVSSMY 865
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2722-3226 |
2.32e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 77.91 E-value: 2.32e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2722 RAEEEAQAKAQ----AQDEAEKL--------RKEAELEAAKRAHAEQAALKQKQLAD-EEMdkhkkfAEKTLRQKSQVEQ 2788
Cdd:pfam01576 2 RQEEEMQAKEEelqkVKERQQKAeselkeleKKHQQLCEEKNALQEQLQAETELCAEaEEM------RARLAARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2789 ELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAqvEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDStqKLL 2868
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLD--EEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS--KLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2869 VEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKE-KMQAIQEASRLKAEAEMLQKQKELAQEQARK 2947
Cdd:pfam01576 152 KERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEeKGRQELEKAKRKLEGESTDLQEQIAELQAQI 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2948 fqedkEQIEQQLAKETEGFQKSLE------AERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQ 3021
Cdd:pfam01576 232 -----AELRAQLAKKEEELQAALArleeetAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3022 TELATKERMAVVQTLEIQRQQsgkEAEELRRAIaelehEKEKLKREA---ELLQKNSQKMQvAQQEQLRQETQVlqttfl 3098
Cdd:pfam01576 307 ELEDTLDTTAAQQELRSKREQ---EVTELKKAL-----EEETRSHEAqlqEMRQKHTQALE-ELTEQLEQAKRN------ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3099 seKQLLLEREKYIEEEKAKLENlyedEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQ-- 3176
Cdd:pfam01576 372 --KANLEKAKQALESENAELQA----ELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELEsv 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 3177 -----QLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDLAG 3226
Cdd:pfam01576 446 ssllnEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2561-3225 |
2.63e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 78.08 E-value: 2.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2561 QRSKEKAEQEAEKQRqlaLEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAkrQKELAEKE--AERQI 2638
Cdd:PRK04863 294 ELYTSRRQLAAEQYR---LVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERY--QADLEELEerLEEQN 368
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2639 QLAQEAALKKIDAEEKAhtaivQQKEQEMLQTRKQ---EQSILDKLKEEA---ERAKRAAEdadfartRAEQEAALSRQQ 2712
Cdd:PRK04863 369 EVVEEADEQQEENEARA-----EAAEEEVDELKSQladYQQALDVQQTRAiqyQQAVQALE-------RAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2713 VEEAERLKQRAEEEAQAKAQAQDEAEklRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLR----------Q 2782
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLE--QKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRrlreqrhlaeQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2783 KSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAM---RQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLimk 2859
Cdd:PRK04863 515 LQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDeleQLQEELEARLESLSESVSEARERRMALRQQLEQL--- 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2860 dkdstqKLLVEEAEKMRQVAeeaarlsIEAQEA-ARMRKLAEDDLANQRALaekmlkekMQAIQeasrlkaeaEMLQKQK 2938
Cdd:PRK04863 592 ------QARIQRLAARAPAW-------LAAQDAlARLREQSGEEFEDSQDV--------TEYMQ---------QLLERER 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2939 ELAQE----QARKFQEDkEQIEQQLAKETEgfqkslEAERRQQLeitaeAERL--------------------------- 2987
Cdd:PRK04863 642 ELTVErdelAARKQALD-EEIERLSQPGGS------EDPRLNAL-----AERFggvllseiyddvsledapyfsalygpa 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2988 --KLQVLEMSRAQAKAEE------------------DASKFkkKAEEIGNKLhqtelatkermaVVQTLEIQRQQS---- 3043
Cdd:PRK04863 710 rhAIVVPDLSDAAEQLAGledcpedlyliegdpdsfDDSVF--SVEELEKAV------------VVKIADRQWRYSrfpe 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3044 ----GKEAEELRraIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQTTFLS--EKQLLLEREKYIEEEkAK 3117
Cdd:PRK04863 776 vplfGRAAREKR--IEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAdpEAELRQLNRRRVELE-RA 852
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3118 LENLYEDEVRKAQKLKQEQEhQMKHLEEEKDQLKVSMDDA-----------MKKQKEAEENVRRKQDELQQLDkkrQEQE 3186
Cdd:PRK04863 853 LADHESQEQQQRSQLEQAKE-GLSALNRLLPRLNLLADETladrveeireqLDEAEEAKRFVQQHGNALAQLE---PIVS 928
|
730 740 750
....*....|....*....|....*....|....*....
gi 1835643837 3187 KLLADEnrklrEKLEQMEEEHRIALAQTREMRTQTDDLA 3225
Cdd:PRK04863 929 VLQSDP-----EQFEQLKQDYQQAQQTQRDAKQQAFALT 962
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2664-3216 |
2.84e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.65 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2664 EQEMLQTRKQEQsILDKLKEEAERAKRAAEDADFART--------RAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQD 2735
Cdd:COG4913 241 HEALEDAREQIE-LLEPIRELAERYAAARERLAELEYlraalrlwFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2736 EAeklrkEAELEAAKRAHAeQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQktlLDEELQRLK 2815
Cdd:COG4913 320 AL-----REELDELEAQIR-GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2816 EEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLimkdkDSTQKLLVEEAEKMRQVAEEAARLSIEA------ 2889
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL-----ERRKSNIPARLLALRDALAEALGLDEAElpfvge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2890 -----QEAARMRKLAEDDLANQR---ALAEKMLKEKMQAIqEASRLKAEAEMLQKQKELAQEQARKFQEDkeQIEQQLAK 2961
Cdd:COG4913 466 lievrPEEERWRGAIERVLGGFAltlLVPPEHYAAALRWV-NRLHLRGRLVYERVRTGLPDPERPRLDPD--SLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2962 ETEGFQKSLEAE--RRQQLEITAEAERLKLQVLEMSRA-QAKAEEDAskFKKKAEEIGNKLHQTELATKERMAVVQtlei 3038
Cdd:COG4913 543 KPHPFRAWLEAElgRRFDYVCVDSPEELRRHPRAITRAgQVKGNGTR--HEKDDRRRIRSRYVLGFDNRAKLAALE---- 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3039 qrqqsgKEAEELRRAIAELEHEKEKLKREAELLqknsqkmqvaqQEQLRQETQVLQTTFLSEKQLLLEREkyIEEEKAKL 3118
Cdd:COG4913 617 ------AELAELEEELAEAEERLEALEAELDAL-----------QERREALQRLAEYSWDEIDVASAERE--IAELEAEL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3119 ENLYE--DEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADEnRKL 3196
Cdd:COG4913 678 ERLDAssDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-RFA 756
|
570 580
....*....|....*....|
gi 1835643837 3197 REKLEQMEEEHRIALAQTRE 3216
Cdd:COG4913 757 AALGDAVERELRENLEERID 776
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1934-2194 |
2.99e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 77.09 E-value: 2.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1934 QYIKFITETLRRLNDEEKaaEKLKEEERRRLAEvEAQLAKQTQLaEAHAKAKAQAEKEAEELQR---RMQEEVSKREV-- 2008
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKE--EKAREVERRRKLE-EAEKARQAEM-DRQAAIYAEQERMAMEREReleRIRQEERKRELer 364
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2009 -----VAVDAEQQKQ--TIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEihivRLQLETMQKHKANAEDE----L 2077
Cdd:pfam17380 365 irqeeIAMEISRMREleRLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQ----KVEMEQIRAEQEEARQRevrrL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2078 QELRARA---------EKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFR---- 2144
Cdd:pfam17380 441 EEERAREmervrleeqERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKllek 520
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2145 -------SQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQL 2194
Cdd:pfam17380 521 emeerqkAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM 577
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1758-2434 |
4.31e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.93 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1758 AKDVNEQMLRSHSERDVDLDRYREKVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIK--DAKQRQEQI 1835
Cdd:TIGR00618 182 ALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREaqEEQLKKQQL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1836 QSVPITDSKTMKEHLLQEKKLLDEIESNRDK---------VDECQKYAKQYIDAIKDYELQLVTYKAQVEPVASPAKKPK 1906
Cdd:TIGR00618 262 LKQLRARIEELRAQEAVLEETQERINRARKAaplaahikaVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1907 VQSTSDSIIQEYVDLRTRYSELTTL----------TSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQ 1976
Cdd:TIGR00618 342 EQRRLLQTLHSQEIHIRDAHEVATSireiscqqhtLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRD 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1977 LAE--AHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQ-KQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIE 2053
Cdd:TIGR00618 422 LQGqlAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQEsAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2054 EEIHIVRLQLETMQkhKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREK 2133
Cdd:TIGR00618 502 EPCPLCGSCIHPNP--ARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2134 QRAVEDLEKFRsQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHL---QE 2210
Cdd:TIGR00618 580 NRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLtltQE 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2211 EAERLKKLHDEAEKAREEAEKELEKWHQkaNEALRLRLQAEEVAHKKTLAQEEAEKQKE---------DAEREARKRAKT 2281
Cdd:TIGR00618 659 RVREHALSIRVLPKELLASRQLALQKMQ--SEKEQLTYWKEMLAQCQTLLRELETHIEEydrefneieNASSSLGSDLAA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2282 EESALRQ--KELAE--DELEKQRKLADATAQQKFSAE----QELIRLKAETENSEQQRLLLEEELFRLKNEVNeaiQKRK 2353
Cdd:TIGR00618 737 REDALNQslKELMHqaRTVLKARTEAHFNNNEEVTAAlqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG---QEIP 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2354 EMEEEL-AKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASK--LRELAEEAAKLRAVSEEA--KRQRQIAEDEAAR 2428
Cdd:TIGR00618 814 SDEDILnLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSkqLAQLTQEQAKIIQLSDKLngINQIKIQFDGDAL 893
|
....*.
gi 1835643837 2429 QRAEAE 2434
Cdd:TIGR00618 894 IKFLHE 899
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2928-3209 |
5.38e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 76.32 E-value: 5.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2928 KAEAEMLQKQKELAQEQARKFQEDKEQI-EQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQV-LEMSRAQakaEEDa 3005
Cdd:pfam17380 282 KAVSERQQQEKFEKMEQERLRQEKEEKArEVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMEReRELERIR---QEE- 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3006 skfKKKAEEignKLHQTELATK-ERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQE 3084
Cdd:pfam17380 358 ---RKRELE---RIRQEEIAMEiSRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEE 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3085 QLRQETQVLQttflSEKQLLLEREKYIEEEKA-KLENLYEDEV-RKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQK 3162
Cdd:pfam17380 432 ARQREVRRLE----EERAREMERVRLEEQERQqQVERLRQQEEeRKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQA 507
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3163 EAEENVRRKQDELQQLDKKR---QEQEKLLADENRKlreKLEQMEEEHRI 3209
Cdd:pfam17380 508 MIEEERKRKLLEKEMEERQKaiyEEERRREAEEERR---KQQEMEERRRI 554
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1959-2821 |
5.42e-13 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 76.91 E-value: 5.42e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1959 EERRRLAEV-----EAQLAKQTQLAEAHAKAKAQAeKEAEELQRRmqeevskREVVAVDAEQQKQTIQQELQQLRQNSdm 2033
Cdd:COG3096 278 NERRELSERalelrRELFGARRQLAEEQYRLVEMA-RELEELSAR-------ESDLEQDYQAASDHLNLVQTALRQQE-- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2034 EIKSKAKQIEEVEYnrrKIEEEIHIVrlqletmqkhkANAEDELQELRARAEkaeqqkkAAQEEAERLRKQVKD-----E 2108
Cdd:COG3096 348 KIERYQEDLEELTE---RLEEQEEVV-----------EEAAEQLAEAEARLE-------AAEEEVDSLKSQLADyqqalD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2109 TQKKR--------EAEEELKR----------KVQAEKEAAREKQ----RAVEDLEKFRSQAEEAERRMKQA--------- 2157
Cdd:COG3096 407 VQQTRaiqyqqavQALEKARAlcglpdltpeNAEDYLAAFRAKEqqatEEVLELEQKLSVADAARRQFEKAyelvckiag 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2158 EVEKERQIKVAQEV-----AQQSAAAELNSKRMSFAEktaqLELSLKQehitvthlQEEAERLkklhdeaekareeaeke 2232
Cdd:COG3096 487 EVERSQAWQTARELlrryrSQQALAQRLQQLRAQLAE----LEQRLRQ--------QQNAERL----------------- 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2233 LEKWHQKANEALRLRLQAEEVahkktlaQEEAEKQKEDAEREARkRAKTEESALRQKElaeDELEKQRKLADATAQQKFS 2312
Cdd:COG3096 538 LEEFCQRIGQQLDAAEELEEL-------LAELEAQLEELEEQAA-EAVEQRSELRQQL---EQLRARIKELAARAPAWLA 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2313 AEQELIRLKAETENSEQQRllleeelfrlkNEVNEAIQKRKEMEEELAKVRAEmeiLLQSKSRAEEESRSNTEKSKqmle 2392
Cdd:COG3096 607 AQDALERLREQSGEALADS-----------QEVTAAMQQLLEREREATVERDE---LAARKQALESQIERLSQPGG---- 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2393 VEASKLRELAE-----------------EAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKL-------AAINDAT 2448
Cdd:COG3096 669 AEDPRLLALAErlggvllseiyddvtleDAPYFSALYGPARHAIVVPDLSAVKEQLAGLEDCPEDLyliegdpDSFDDSV 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2449 RLKTEAEIALKEKEAENE-RLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDN--ELERQKNIVEDTLRQRrii 2525
Cdd:COG3096 749 FDAEELEDAVVVKLSDRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFDvqKLQRLHQAFSQFVGGH--- 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2526 eeeiriLKVNFE--------KASVGKSDLELELNQLkniAEETQRSKEKAEQEAEKQRQLA--------LEEE---QRRK 2586
Cdd:COG3096 826 ------LAVAFApdpeaelaALRQRRSELERELAQH---RAQEQQLRQQLDQLKEQLQLLNkllpqanlLADEtlaDRLE 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2587 EAEEKVRKILADEKEAARQRKAaLEEVERLKA-----KAEEAKRQKELAEKEAERQIQLAQEAALKKIdAEEKAHTAivQ 2661
Cdd:COG3096 897 ELREELDAAQEAQAFIQQHGKA-LAQLEPLVAvlqsdPEQFEQLQADYLQAKEQQRRLKQQIFALSEV-VQRRPHFS--Y 972
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2662 QKEQEMLQtrkQEQSILDKLKEEAERAKRAAEDAdfaRTRAEQeaalSRQQVEEAERLKQRAEEEAQAKAQAQDEAEklR 2741
Cdd:COG3096 973 EDAVGLLG---ENSDLNEKLRARLEQAEEARREA---REQLRQ----AQAQYSQYNQVLASLKSSRDAKQQTLQELE--Q 1040
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2742 KEAELEAAKRAHAEQAALKQKQLADEEMDKHKKfaektlrQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDA 2821
Cdd:COG3096 1041 ELEELGVQADAEAEERARIRRDELHEELSQNRS-------RRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2273-2954 |
5.82e-13 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 76.30 E-value: 5.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2273 REARKRAK---TEESALRQKElaeDELEKQRKLADAT--AQQKFSAEQELIRLKAEtenseqqrllleeelfrlknevnE 2347
Cdd:pfam05483 85 KEAEKIKKwkvSIEAELKQKE---NKLQENRKIIEAQrkAIQELQFENEKVSLKLE-----------------------E 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2348 AIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRS---NTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQR--QIA 2422
Cdd:pfam05483 139 EIQENKDLIKENNATRHLCNLLKETCARSAEKTKKyeyEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhfKLK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2423 EDEAARQRAEaerilKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEE----QATQHKQDIEEKII 2498
Cdd:pfam05483 219 EDHEKIQHLE-----EEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEktklQDENLKELIEKKDH 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2499 L------LKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIA---EETQRSKEKAEQ 2569
Cdd:pfam05483 294 LtkeledIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTcslEELLRTEQQRLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2570 EAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLkakAEEAKRQKELAE--KEAERQIQLAQEAALK 2647
Cdd:pfam05483 374 KNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKL---LDEKKQFEKIAEelKGKEQELIFLLQAREK 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2648 KIDAEEKAHTAIVQQKEQEMLQTRKQ----EQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVE------EAE 2717
Cdd:pfam05483 451 EIHDLEIQLTAIKTSEEHYLKEVEDLktelEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDiinckkQEE 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2718 RLKQRAEEEAQAKAQAQDEAEKLRKEAeleaakRAHAEQAALKQKQlADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQL 2797
Cdd:pfam05483 531 RMLKQIENLEEKEMNLRDELESVREEF------IQKGDEVKCKLDK-SEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2798 EETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEElIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQ 2877
Cdd:pfam05483 604 ENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELAS-AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKA 682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2878 VAEEAARLSIE-----AQEAARMRKLAE------DDLANQRALAEKMLKEKMQAIQ--------EASRLKAEAEMLQKQK 2938
Cdd:pfam05483 683 IADEAVKLQKEidkrcQHKIAEMVALMEkhkhqyDKIIEERDSELGLYKNKEQEQSsakaaleiELSNIKAELLSLKKQL 762
|
730
....*....|....*.
gi 1835643837 2939 ELAQEQARKFQEDKEQ 2954
Cdd:pfam05483 763 EIEKEEKEKLKMEAKE 778
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2353-2976 |
5.96e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 5.96e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2353 KEMEEELAKVRAEMEILLQsksraeeesrsntekskqmleveaskLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAE 2432
Cdd:COG4913 238 ERAHEALEDAREQIELLEP--------------------------IRELAERYAAARERLAELEYLRAALRLWFAQRRLE 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2433 AERILKEKLAAinDATRLKTEAEIALKEKEAENERLRRLaedeayqRKLLEEQATQHKQDIEEKIillkkssdNELERQK 2512
Cdd:COG4913 292 LLEAELEELRA--ELARLEAELERLEARLDALREELDEL-------EAQIRGNGGDRLEQLEREI--------ERLEREL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2513 NIVEDTLRQRRiieeeirilkvnfEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKV 2592
Cdd:COG4913 355 EERERRRARLE-------------ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2593 RKiLADEKEAARQRKAAL-EEVERLKAKAEEAKRQKE-----LAE----KEAERQIQLAQE------------------A 2644
Cdd:COG4913 422 RE-LEAEIASLERRKSNIpARLLALRDALAEALGLDEaelpfVGElievRPEEERWRGAIErvlggfaltllvppehyaA 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2645 ALKKIDA---EEKAHTAIVQQKEQEMLQTRKQEQSILDKL--KE-------EAERAKRAA----------EDADFARTRA 2702
Cdd:COG4913 501 ALRWVNRlhlRGRLVYERVRTGLPDPERPRLDPDSLAGKLdfKPhpfrawlEAELGRRFDyvcvdspeelRRHPRAITRA 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2703 EQ------------EAALSRQQV--EEAERLKQRAEEEAQAKAQAQDEAEKLRkeAELEAAKRAHAEQAALKQKQLADEE 2768
Cdd:COG4913 581 GQvkgngtrhekddRRRIRSRYVlgFDNRAKLAALEAELAELEEELAEAEERL--EALEAELDALQERREALQRLAEYSW 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2769 MDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELfkvkIQMEELIKLKLR 2848
Cdd:COG4913 659 DEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2849 IEEENKMLImkdkdstQKLLVEEAEKMRqvaeeaARLSIEAQEAARMRKLAE--DDLANQRALAEKMLKEKMQAIQEASR 2926
Cdd:COG4913 735 RLEAAEDLA-------RLELRALLEERF------AAALGDAVERELRENLEEriDALRARLNRAEEELERAMRAFNREWP 801
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2927 ---------LKAEAEMLQKQKELAQEQARKFQED-KEQIEQQLAKETEGFQKSLEAERRQ 2976
Cdd:COG4913 802 aetadldadLESLPEYLALLDRLEEDGLPEYEERfKELLNENSIEFVADLLSKLRRAIRE 861
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2604-2832 |
6.16e-13 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 76.14 E-value: 6.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2604 RQRKAALEEVERLKAKAEEAK-----RQKELAEKEAERQIQLAQEAA---LKKIDAEEKAHTAIVQQKEQEMLQTRKQEQ 2675
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKarfeaRQARLEREKAAREARHKKAAEaraAKDKDAVAAALARVKAKKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2676 SILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAK-RAHA 2754
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIaRAKA 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2755 EQAALKQKQLADEEMDkhkkfaEKTLRQKSQVEQELTKV---KLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEE 2831
Cdd:PRK05035 592 KKAAQQAASAEPEEQV------AEVDPKKAAVAAAIARAkakKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQA 665
|
.
gi 1835643837 2832 L 2832
Cdd:PRK05035 666 N 666
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2644-3224 |
6.59e-13 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 76.23 E-value: 6.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2644 AALKKIDAEEKAHTAIVQQKEQEML--QTRKQEQSILD------KLKEEAERAKraaeDADFA--RTRAEQEAALS--RQ 2711
Cdd:PRK02224 119 TELLRMDAEAFVNCAYVRQGEVNKLinATPSDRQDMIDdllqlgKLEEYRERAS----DARLGveRVLSDQRGSLDqlKA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2712 QVEEAER--LKQRAEEEAQAKAQAQDEAEklRKEAELEAAKRahaeqaalkQKQLADEEMDKHkkfaEKTLRQKSQVEQE 2789
Cdd:PRK02224 195 QIEEKEEkdLHERLNGLESELAELDEEIE--RYEEQREQARE---------TRDEADEVLEEH----EERREELETLEAE 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2790 LTKVKLQLEETDHQKTLLDEELQRLKEEVT------DAMRQKAQVEE-ELFKVKIQMEELIKLKLRIEEEnkmliMKDKD 2862
Cdd:PRK02224 260 IEDLRETIAETEREREELAEEVRDLRERLEeleeerDDLLAEAGLDDaDAEAVEARREELEDRDEELRDR-----LEECR 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2863 STQKLLVEEAEKMRqvaEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMlKEKMQAIQEasrlkaEAEMLQKQKELAQ 2942
Cdd:PRK02224 335 VAAQAHNEEAESLR---EDADDLEERAEELREEAAELESELEEAREAVEDR-REEIEELEE------EIEELRERFGDAP 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2943 EQARKFQEDKEQIEQQLAkETEGFQKSLEAERRQQLEITAEAERL-----------------KLQVLEMSRAQ-AKAEED 3004
Cdd:PRK02224 405 VDLGNAEDFLEELREERD-ELREREAELEATLRTARERVEEAEALleagkcpecgqpvegspHVETIEEDRERvEELEAE 483
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3005 ASKFKKKAEEIGNKLHQTElATKERMAVVQTLEIQRQQSGK-------EAEELRRAIAELEHEKEKLKREAELLQKNSQK 3077
Cdd:PRK02224 484 LEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEEliaerreTIEEKRERAEELRERAAELEAEAEEKREAAAE 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3078 MQVAQQEQlRQETQVLQTTfLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQmkhlEEEKDQLKvsmdda 3157
Cdd:PRK02224 563 AEEEAEEA-REEVAELNSK-LAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELN----DERRERLA------ 630
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 3158 mkkqkeaeenvrrkqdelQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDL 3224
Cdd:PRK02224 631 ------------------EKRERKRELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDL 679
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2547-2831 |
7.01e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.93 E-value: 7.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2547 ELELNQLKNIAEETQRSKEKAEQ--EAEKQRQLAL--------EEEQRRKEAEEKVRKILADEK----EAARQRKAALE- 2611
Cdd:pfam17380 295 KMEQERLRQEKEEKAREVERRRKleEAEKARQAEMdrqaaiyaEQERMAMERERELERIRQEERkrelERIRQEEIAMEi 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2612 ----EVERLKAKAEEaKRQKELAEKEAERQIQLAQEAALKKIdaeekahtaivQQKEQEMLQTRKQE----QSILDKLKE 2683
Cdd:pfam17380 375 srmrELERLQMERQQ-KNERVRQELEAARKVKILEEERQRKI-----------QQQKVEMEQIRAEQeearQREVRRLEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2684 EAERAKRAAEDADFARtraEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRkEAELEAAKRAHAEQAAlKQKQ 2763
Cdd:pfam17380 443 ERAREMERVRLEEQER---QQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKIL-EKELEERKQAMIEEER-KRKL 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2764 LADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLK--EEVTDAMRQKAQVEEE 2831
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEamEREREMMRQIVESEKA 587
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1220-1409 |
9.75e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 70.94 E-value: 9.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1220 LHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMAAKKENYSGLMRELELKEKKIKEIQISGDRLQREDHPGKQTVEAFQ 1299
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1300 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVKDTEEYLNKTQETMRKKYQCDrsiTVTRLEDLLQDSIDEKDQLTEY 1379
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1835643837 1380 KGQLSALAKRAKTIVHLKPRSTAHPVRGKL 1409
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4336-4374 |
1.03e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 1.03e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 4336 LLDAQAATGFIIDPVKNEMLTVDEAVRKGVVGPELHDRL 4374
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1847-2497 |
1.17e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 75.72 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1847 KEHLLQEKKLLDEIESnrdkvdecqkyAKQYIDAIKDYELQLVTYKAQVEpVASPAKKpkvqstsdsIIQEYVDLRTRYS 1926
Cdd:COG4913 214 REYMLEEPDTFEAADA-----------LVEHFDDLERAHEALEDAREQIE-LLEPIRE---------LAERYAAARERLA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1927 ELttltsQYIKfitETLRRLNDEEKAAEKlkeeeRRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKR 2006
Cdd:COG4913 273 EL-----EYLR---AALRLWFAQRRLELL-----EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2007 EVvavDAEQQKQTIQQELQQLRQNSDmEIKSKAKQIE-EVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAE 2085
Cdd:COG4913 340 LE---QLEREIERLERELEERERRRA-RLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2086 KAEQQKKAAQEEAERLRKQVKD---ETQKKREA--------EEELKrkVQAE----KEAAREKQRAVEDL---------- 2140
Cdd:COG4913 416 DLRRELRELEAEIASLERRKSNipaRLLALRDAlaealgldEAELP--FVGElievRPEEERWRGAIERVlggfaltllv 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2141 -EKFRSQAEEAERRMKQA------EVEKERQIKVAQEVAQQSAAAELNSKRMSFAEkTAQLELSLKQEHITVTHLQEeae 2213
Cdd:COG4913 494 pPEHYAAALRWVNRLHLRgrlvyeRVRTGLPDPERPRLDPDSLAGKLDFKPHPFRA-WLEAELGRRFDYVCVDSPEE--- 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2214 rlkkLHDEAEK-----AREEAEKELEKWHQKA----------NEALRLRLQAEEVAHKKTLAqeEAEKQKEDAEREARKR 2278
Cdd:COG4913 570 ----LRRHPRAitragQVKGNGTRHEKDDRRRirsryvlgfdNRAKLAALEAELAELEEELA--EAEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2279 AKTEESALRQKELAEDEL---EKQRKLADATAQQK--FSAEQELIRLKAEtenseqqrllleeelfrlkneVNEAIQKRK 2353
Cdd:COG4913 644 QERREALQRLAEYSWDEIdvaSAEREIAELEAELErlDASSDDLAALEEQ---------------------LEELEAELE 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2354 EMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEE-------AAKLRAVSEEAKRQRQIAEDEA 2426
Cdd:COG4913 703 ELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEErfaaalgDAVERELRENLEERIDALRARL 782
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2427 ARQRAEAERILKE-KLAAINDATRLKTEAEiALKEKEAENERLR--RLAEDEAYQRKLLEEQATQHKQDIEEKI 2497
Cdd:COG4913 783 NRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVADLLSKL 855
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2661-3225 |
1.30e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 75.65 E-value: 1.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2661 QQKEQEMLQTRKQEQ--SILDKLKEEAERA--KRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKaQAQDE 2736
Cdd:pfam12128 277 RQEERQETSAELNQLlrTLDDQWKEKRDELngELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLP-SWQSE 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2737 AEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDkhkkfaektlRQKSQVEQELTKVKlqlEETDHQKTLLDEELQRLKE 2816
Cdd:pfam12128 356 LENLEERLKALTGKHQDVTAKYNRRRSKIKEQNN----------RDIAGIKDKLAKIR---EARDRQLAVAEDDLQALES 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2817 EVTDAMRQ-KAQVEEELFKVKIQMEELiklKLRIeeeNKMLIMKDKDSTQKLLVEEAEKMRQvAEEAARLSIEAQEAARM 2895
Cdd:pfam12128 423 ELREQLEAgKLEFNEEEYRLKSRLGEL---KLRL---NQATATPELLLQLENFDERIERARE-EQEAANAEVERLQSELR 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2896 RKLAEDDLANQR-ALAEKMLKEKMQAIQEA-SRLKAEA----EMLQKQ---------KELAQEQARKFQEDKEQIEQQLA 2960
Cdd:pfam12128 496 QARKRRDQASEAlRQASRRLEERQSALDELeLQLFPQAgtllHFLRKEapdweqsigKVISPELLHRTDLDPEVWDGSVG 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2961 KETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRA-------QAKAEEDASKFKKKAEEIGNKLHQTELATKE-RMAV 3032
Cdd:pfam12128 576 GELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDL 655
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3033 VQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQET--------QVLQTTFLSEKQLL 3104
Cdd:pfam12128 656 RRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARtekqaywqVVEGALDAQLALLK 735
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3105 LEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKhLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQE 3184
Cdd:pfam12128 736 AAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAK-LKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLAT 814
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1835643837 3185 QEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDLA 3225
Cdd:pfam12128 815 QLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQ 855
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2767-3213 |
1.31e-12 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 75.39 E-value: 1.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2767 EEMDKHKKFAEKTLRQKSQVEQELTKVKLQLE----ETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKiQMEEL 2842
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQlltlCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLT-QKREA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2843 IKLKLRIEEENKMLIMKDKD-STQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANqraLAEKMLKEKMQAI 2921
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEElRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTE---LQSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2922 QEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAE-RRQQLEITAEAERLKLQVLEMSRAQAK 3000
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQRE 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3001 AEEDASKFKKKAEEIGNKLHqtelATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQknsQKMQV 3080
Cdd:TIGR00618 409 QATIDTRTSAFRDLQGQLAH----AKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQ---TKEQI 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3081 AQQEQlrqETQVLQTTFLSEKQ----LLLEREKYIEEEKAKLENL---------YEDEVRKAQKLKQEQEHQM----KHL 3143
Cdd:TIGR00618 482 HLQET---RKKAVVLARLLELQeepcPLCGSCIHPNPARQDIDNPgpltrrmqrGEQTYAQLETSEEDVYHQLtserKQR 558
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 3144 EEEKDQLKVSMDDAMK------KQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQ 3213
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSIltqcdnRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHL 634
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2704-3002 |
1.33e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.16 E-value: 1.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2704 QEAALSRQQVEEAERLKQraEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAE-QAAL--KQKQLADE---EMDKHKKfaE 2777
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQ--ERLRQEKEEKAREVERRRKLEEAEKARQAEMDrQAAIyaEQERMAMErerELERIRQ--E 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2778 KTLRQKSQVEQEltKVKLQLEETdhqktlldEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEE---------LIKLKLR 2848
Cdd:pfam17380 357 ERKRELERIRQE--EIAMEISRM--------RELERLQMERQQKNERVRQELEAARKVKILEEErqrkiqqqkVEMEQIR 426
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2849 IEEEN------KMLIMKDKDSTQKLLVEEAEK------MRQVAEEAARLSIEAQEAARMRKLAEDDlanQRALAEKMLKE 2916
Cdd:pfam17380 427 AEQEEarqrevRRLEEERAREMERVRLEEQERqqqverLRQQEEERKRKKLELEKEKRDRKRAEEQ---RRKILEKELEE 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2917 KMQAIQEASRLKA--EAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEA-ERRQQLEITAEAERLKLQVLE 2993
Cdd:pfam17380 504 RKQAMIEEERKRKllEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAtEERSRLEAMEREREMMRQIVE 583
|
....*....
gi 1835643837 2994 MSRAQAKAE 3002
Cdd:pfam17380 584 SEKARAEYE 592
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3344-3381 |
1.75e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.66 E-value: 1.75e-12
10 20 30
....*....|....*....|....*....|....*...
gi 1835643837 3344 LLEAQAASGFIIDPVKNKRLSVNEAVKENVIGPELHNK 3381
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1934-2673 |
1.78e-12 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 75.15 E-value: 1.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1934 QYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDA 2013
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2014 EQQKQTIQQELQQLR------QNSDMEIKSKAKQIEEVeyNRRKIEEEIHIVRLQLETM----QKHKANAEDELQELRAR 2083
Cdd:pfam15921 162 EDMLEDSNTQIEQLRkmmlshEGVLQEIRSILVDFEEA--SGKKIYEHDSMSTMHFRSLgsaiSKILRELDTEISYLKGR 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2084 AEKAEQQ----KKAAQEEAERLRKQVKDE---------------TQKKREAEEE---LKRKVQAEKEAAREKQ----RAV 2137
Cdd:pfam15921 240 IFPVEDQlealKSESQNKIELLLQQHQDRieqliseheveitglTEKASSARSQansIQSQLEIIQEQARNQNsmymRQL 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2138 EDLE----KFRSQAEEAERRMKQAEVEKERQIKVAqevaqQSAAAELNSKRMSFAEKTA----QLELSLKQEHITVTHLQ 2209
Cdd:pfam15921 320 SDLEstvsQLRSELREAKRMYEDKIEELEKQLVLA-----NSELTEARTERDQFSQESGnlddQLQKLLADLHKREKELS 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2210 EEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRlqaeevAHKKTLAQE-EAEKQKEDAEREARKRAKTEESALRQ 2288
Cdd:pfam15921 395 LEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLE------ALLKAMKSEcQGQMERQMAAIQGKNESLEKVSSLTA 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2289 KelAEDELEKQRKLADATAQQKF---SAEQELIRLKAETENSEQQRLLLEEELFRLKNEVN---EAIQKRKEMEEELAKV 2362
Cdd:pfam15921 469 Q--LESTKEMLRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNV 546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2363 RAEMEIL---LQSKSRAEEESRSNTEKSKQM----------LEVEASKL-RELAEEAAKLRAVS-EEAKRQRQIAEDEAA 2427
Cdd:pfam15921 547 QTECEALklqMAEKDKVIEILRQQIENMTQLvgqhgrtagaMQVEKAQLeKEINDRRLELQEFKiLKDKKDAKIRELEAR 626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2428 RQRAEAERIL-----KEKLAAINDatrLKTEAEIALKEKEAENERLRRLAED-EAYQRKLleEQATQHKQDIEEKIILLK 2501
Cdd:pfam15921 627 VSDLELEKVKlvnagSERLRAVKD---IKQERDQLLNEVKTSRNELNSLSEDyEVLKRNF--RNKSEEMETTTNKLKMQL 701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2502 KSSDNELERQKNivedTLRQRRIIEEEIRILKVNFEKASVGKSdlelelNQLKNIAEETQrSKEKAEQEAEKQRQLALEE 2581
Cdd:pfam15921 702 KSAQSELEQTRN----TLKSMEGSDGHAMKVAMGMQKQITAKR------GQIDALQSKIQ-FLEEAMTNANKEKHFLKEE 770
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2582 EQRRKEAEEKVrkiladekeaARQRKAALEEVERLKAKaeeakrQKELAEKEAERQIQLaQEAALKKIDAEEkahtaIVQ 2661
Cdd:pfam15921 771 KNKLSQELSTV----------ATEKNKMAGELEVLRSQ------ERRLKEKVANMEVAL-DKASLQFAECQD-----IIQ 828
|
810
....*....|..
gi 1835643837 2662 QKEQEMLQTRKQ 2673
Cdd:pfam15921 829 RQEQESVRLKLQ 840
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5271-5472 |
2.38e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 69.78 E-value: 2.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5271 LEMILSWVSDMEDLISNQKPPSSeVKVVKAQLQEQKLLQRLLEERRPRLERV------LQDMQTSESGEENAKHGSLQAR 5344
Cdd:cd00176 9 ADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALnelgeqLIEEGHPDAEEIQERLEELNQR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5345 WEALIQQADTRNRRLEQILPAAQAFQESLSaFQDWLCATEKHLAELWQVDScLSQIQEAHQQIQVLCKDVRLKSGELDRV 5424
Cdd:cd00176 88 WEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1835643837 5425 LENGQKVLELASGEEELLTQEKLDSLRVRYLITAQSSAAILQRLEQTL 5472
Cdd:cd00176 166 NELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1978-2201 |
3.47e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.10 E-value: 3.47e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1978 AEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIH 2057
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2058 IVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAA-------QEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAA 2130
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2131 REKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKV--AQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQE 2201
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4412-4450 |
3.78e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.89 E-value: 3.78e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 4412 LLDAQLATGGIIDPRFGFHLPVEIAYQRGYFNRETNDRL 4450
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2240-2757 |
4.78e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.41 E-value: 4.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2240 ANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEEsalRQKELAEDELEKQRKLADATAQQKFSAEQELIR 2319
Cdd:COG4913 273 ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA---RLDALREELDELEAQIRGNGGDRLEQLEREIER 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2320 LKAEtenseqqrllleeelfrlkneVNEAIQKRKEMEEELAKVRAEMEillqsksRAEEESRSNTEKSKQMLEVEASKLR 2399
Cdd:COG4913 350 LERE---------------------LEERERRRARLEALLAALGLPLP-------ASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2400 ELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERI---LKEKLAAINDATRLKTE-----AE-IALKEKEAE------ 2464
Cdd:COG4913 402 ALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDALAEALGLDEAelpfvGElIEVRPEEERwrgaie 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2465 ----NERLRRLAEDEAYQR-----------------KLLEEQATQHKQDIEEKIILLK---KSS------DNELERQKNI 2514
Cdd:COG4913 482 rvlgGFALTLLVPPEHYAAalrwvnrlhlrgrlvyeRVRTGLPDPERPRLDPDSLAGKldfKPHpfrawlEAELGRRFDY 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2515 V----EDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQL--KNiaeetqrskekAEQEAEKQRQLAlEEEQRRKEA 2588
Cdd:COG4913 562 VcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLgfDN-----------RAKLAALEAELA-ELEEELAEA 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2589 EEKVRKiLADEKEAARQRKAALEEVERLKAKAEEAKR-QKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEM 2667
Cdd:COG4913 630 EERLEA-LEAELDALQERREALQRLAEYSWDEIDVASaEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEEL 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2668 LQTRKQEQsildKLKEEAERAKRAAEDAdfartRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQdEAEKLRKEAELE 2747
Cdd:COG4913 709 DELKGEIG----RLEKELEQAEEELDEL-----QDRLEAAEDLARLELRALLEERFAAALGDAVERE-LRENLEERIDAL 778
|
570
....*....|
gi 1835643837 2748 AAKRAHAEQA 2757
Cdd:COG4913 779 RARLNRAEEE 788
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1627-2454 |
6.51e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.18 E-value: 6.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1627 EQQQIHFELEGIKKNLNKvsektLKVLAQKEQSSSSPLLRTEHEITHQKMDQVYSLSSIYLEKLKTINLVIRSTQGAEEV 1706
Cdd:TIGR02169 238 QKEAIERQLASLEEELEK-----LTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1707 vrtYEDQLKEVHA-VPSDSKELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRSHSERDVDLDRYREKVQQ 1785
Cdd:TIGR02169 313 ---KERELEDAEErLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1786 LLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQeqiqsvpitdsktmkehllqeKKLLDEIESNRD 1865
Cdd:TIGR02169 390 YREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKI---------------------NELEEEKEDKAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1866 KVDECQKYAKQYIDAIKDYElqlvtykaqvepvaspakkpkvqstsdsiiQEYVDLRTRYS----ELTTLTSQYIKFITE 1941
Cdd:TIGR02169 449 EIKKQEWKLEQLAADLSKYE------------------------------QELYDLKEEYDrvekELSKLQRELAEAEAQ 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1942 --TLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKqtqLAEAHAKAKAQAekeaeeLQRRMQEEVSKREVVAVDAEQQKQT 2019
Cdd:TIGR02169 499 arASEERVRGGRAVEEVLKASIQGVHGTVAQLGS---VGERYATAIEVA------AGNRLNNVVVEDDAVAKEAIELLKR 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2020 IQQ------ELQQLRQN-SDMEIKSKAKQIEE----VEYNR----------------------RKIEEEIHIVRLQLETM 2066
Cdd:TIGR02169 570 RKAgratflPLNKMRDErRDLSILSEDGVIGFavdlVEFDPkyepafkyvfgdtlvvedieaaRRLMGKYRMVTLEGELF 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2067 QK----------------HKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELkrkvqaeKEAA 2130
Cdd:TIGR02169 650 EKsgamtggsraprggilFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKI-------GEIE 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2131 REKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELnsKRMSFAEKTAQLELSLKQEHItvTHLQE 2210
Cdd:TIGR02169 723 KEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE--DLHKLEEALNDLEARLSHSRI--PEIQA 798
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2211 EAERLKKLHdeaekareeaeKELEKWHQKANEALRLRLQAEEVAHKKTlaQEEAEKQKEDAEREARKRAKTEESALRQKE 2290
Cdd:TIGR02169 799 ELSKLEEEV-----------SRIEARLREIEQKLNRLTLEKEYLEKEI--QELQEQRIDLKEQIKSIEKEIENLNGKKEE 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2291 LAEDELEKQRKLADataqqkfsAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILL 2370
Cdd:TIGR02169 866 LEEELEELEAALRD--------LESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIE 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2371 QSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERilKEKLAAINDATRL 2450
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEER--KAILERIEEYEKK 1015
|
....
gi 1835643837 2451 KTEA 2454
Cdd:TIGR02169 1016 KREV 1019
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2585-3223 |
6.58e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.45 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2585 RKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKrQKELAEKEAERQIQLAQEaalkkidaeekaHTAIVQQ-- 2662
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELE-ELSARESDLEQDYQAASD------------HLNLVQTal 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2663 KEQEMLQTRKQEqsiLDKLKEEAERAKRAAEDADFARTRAEQEAALSRqqvEEAERLK------QRAEEEAQAKA----- 2731
Cdd:COG3096 344 RQQEKIERYQED---LEELTERLEEQEEVVEEAAEQLAEAEARLEAAE---EEVDSLKsqladyQQALDVQQTRAiqyqq 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2732 --QAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMdkhkkfaeKTLRQK--------SQVEQELTKVKLQLEETD 2801
Cdd:COG3096 418 avQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEV--------LELEQKlsvadaarRQFEKAYELVCKIAGEVE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2802 HQktlldEELQRLKEEVTDAMRQKAQVEEElfkVKIQMEeLIKLKLRIEEENKmlimkdkdsTQKLLVEEAEKMRQVAEE 2881
Cdd:COG3096 490 RS-----QAWQTARELLRRYRSQQALAQRL---QQLRAQ-LAELEQRLRQQQN---------AERLLEEFCQRIGQQLDA 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2882 AARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEA-------EMLQKQKELAQEQARKFQEDKEQ 2954
Cdd:COG3096 552 AEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqDALERLREQSGEALADSQEVTAA 631
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2955 IEQQLAKETE-GFQKSLEAERRQQLEITAE----------------AERL-----------------------------K 2988
Cdd:COG3096 632 MQQLLEREREaTVERDELAARKQALESQIErlsqpggaedprllalAERLggvllseiyddvtledapyfsalygparhA 711
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2989 LQVLEMSRAQAK-------------AEEDASKFKkkaeeiGNKLHQTELatkERMAVVQTLEIQRQQS--------GK-- 3045
Cdd:COG3096 712 IVVPDLSAVKEQlagledcpedlylIEGDPDSFD------DSVFDAEEL---EDAVVVKLSDRQWRYSrfpevplfGRaa 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3046 ----------EAEELRRAIAELEHEKEKLKR---------------------EAELLQKNSQKMQV-AQQEQLRQETQVL 3093
Cdd:COG3096 783 rekrleelraERDELAEQYAKASFDVQKLQRlhqafsqfvgghlavafapdpEAELAALRQRRSELeRELAQHRAQEQQL 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3094 QTTF--LSEKQLLLER-------------EKYIEEEKAKLENLYEDE--VRKAQKLKQEQEHQMKHLE---EEKDQLKVS 3153
Cdd:COG3096 863 RQQLdqLKEQLQLLNKllpqanlladetlADRLEELREELDAAQEAQafIQQHGKALAQLEPLVAVLQsdpEQFEQLQAD 942
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 3154 MDDAMKKQKEaeenVRRKQDELQQLDKKR-----QEQEKLLA---DENRKLREKLEQMEEEHRIALAQTREMRTQTDD 3223
Cdd:COG3096 943 YLQAKEQQRR----LKQQIFALSEVVQRRphfsyEDAVGLLGensDLNEKLRARLEQAEEARREAREQLRQAQAQYSQ 1016
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2128-2782 |
6.64e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.03 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2128 EAAREKQRAVEDLEKFRSQAEEAERRMKqaevekerqikvaqevaqqsaaaelnskrmsfaektaQLElslkqehitvtH 2207
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIE-------------------------------------LLE-----------P 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2208 LQEEAERLKKLHDEAEkareeaekelekwhqkANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEEsalR 2287
Cdd:COG4913 257 IRELAERYAAARERLA----------------ELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA---R 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2288 QKELAEDELEKQRKLADATAQQKFSAEQELIRLKAetenseqqrllleeelfrlknEVNEAIQKRKEMEEELAKVRAEME 2367
Cdd:COG4913 318 LDALREELDELEAQIRGNGGDRLEQLEREIERLER---------------------ELEERERRRARLEALLAALGLPLP 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2368 illqsksRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERI---LKEKLAAI 2444
Cdd:COG4913 377 -------ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDAL 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2445 NDATRLKTE-----AE-IALKEKEAE----------NERLRRLAEDEAYQrklleeQATQH--KQDIEEKIILLKKSSDN 2506
Cdd:COG4913 450 AEALGLDEAelpfvGElIEVRPEEERwrgaiervlgGFALTLLVPPEHYA------AALRWvnRLHLRGRLVYERVRTGL 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2507 ELERQKNIVEDTLrqrriieeeirILKVNFeKASVGKSDLELELNQLKNIAE-ETQRSKEKAEQEAEKQRQLALEEEQRR 2585
Cdd:COG4913 524 PDPERPRLDPDSL-----------AGKLDF-KPHPFRAWLEAELGRRFDYVCvDSPEELRRHPRAITRAGQVKGNGTRHE 591
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2586 KEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQ-KELAEKEAERQIQLAQEAALKKIDAEE---KAHTAIVQ 2661
Cdd:COG4913 592 KDDRRRIRSRYVLGFDNRAKLAALEAELAELEEELAEAEERlEALEAELDALQERREALQRLAEYSWDEidvASAEREIA 671
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2662 QKEQEMLQTRKqEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLR 2741
Cdd:COG4913 672 ELEAELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1835643837 2742 KEAELEAAKRAHAEQAALK----QKQLADEEMDKHKKFAEKTLRQ 2782
Cdd:COG4913 751 LEERFAAALGDAVERELREnleeRIDALRARLNRAEEELERAMRA 795
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2073-2623 |
6.86e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 72.77 E-value: 6.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2073 AEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELkrkvqaekEAAREKQRAVEDLEkfrsqAEEAER 2152
Cdd:PRK02224 197 EEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVL--------EEHEERREELETLE-----AEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2153 RMKQAEVEKERQiKVAQEVA-QQSAAAELNSKRmsfAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEk 2231
Cdd:PRK02224 264 RETIAETERERE-ELAEEVRdLRERLEELEEER---DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2232 elekwhQKANEALRLRLQAEEVAHKKTLAQEEA---EKQKEDAEREARKRaKTEESALRQK--------ELAEDELEKQR 2300
Cdd:PRK02224 339 ------AHNEEAESLREDADDLEERAEELREEAaelESELEEAREAVEDR-REEIEELEEEieelrerfGDAPVDLGNAE 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2301 KLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLK--------------NEVNEAIQKRKEMEEELAKVRAEM 2366
Cdd:PRK02224 412 DFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsphvETIEEDRERVEELEAELEDLEEEV 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2367 EILLQSKSRAE---------EESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERIL 2437
Cdd:PRK02224 492 EEVEERLERAEdlveaedriERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAR 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2438 kEKLAAINDatrlkteaeiALKEKEAENERLRRLAEdeayqrkLLEEQAtqhkqDIEEKIILL--KKSSDNELERQKniv 2515
Cdd:PRK02224 572 -EEVAELNS----------KLAELKERIESLERIRT-------LLAAIA-----DAEDEIERLreKREALAELNDER--- 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2516 EDTLRQRRIIeeeirilkvnfekasvgKSDLELEL--NQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVR 2593
Cdd:PRK02224 626 RERLAEKRER-----------------KRELEAEFdeARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVEN 688
|
570 580 590
....*....|....*....|....*....|.
gi 1835643837 2594 KIlaDEKEAARQRKAALEE-VERLKAKAEEA 2623
Cdd:PRK02224 689 EL--EELEELRERREALENrVEALEALYDEA 717
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1725-2149 |
9.97e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.11 E-value: 9.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1725 KELEATKAELKKLRSQVEGHQPLFNTLEAdLNKAKDVNEQmLRSHSERDVDLDRYREKVQQLLERWQAILVQIDLRQREL 1804
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEA-ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1805 DQLGRQLRYYRETYEWLIKWIKDAKQRQEQI----QSVPITDSKTMKEHLLQEKKLLDEIESNRDKVDECQKYAKQYIDA 1880
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELeellEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1881 IKDYELQLVTYKAQvEPVASPAKKPKVQSTSDSIIQEYVDLRTRYSELTTLTSQYIKFITETLRRLNDEEKAAEKLKEEE 1960
Cdd:COG4717 229 LEQLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1961 RRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQ-QKQTIQQELQQLRQNSDMEIKSKA 2039
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEEL 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2040 KQIEEVEYNRRKIEEEIHIVRLQLETM---------QKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVK---- 2106
Cdd:COG4717 388 RAALEQAEEYQELKEELEELEEQLEELlgeleelleALDEEELEEELEELEEELEELEEELEELREELAELEAELEqlee 467
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1835643837 2107 -DETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEE 2149
Cdd:COG4717 468 dGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1958-2821 |
1.07e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 72.68 E-value: 1.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1958 EEERRRLAEveaqlakqtqLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQELQQL--RQNSDMEI 2035
Cdd:PRK04863 278 ANERRVHLE----------EALELRRELYTSRRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAAsdHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2036 KSKAKQIEEVEYNRRKIEEeihivrlQLETMQKHKANAEDELQELRARAEkaeqqkkAAQEEAERLRKQVKD-----ETQ 2110
Cdd:PRK04863 344 LRQQEKIERYQADLEELEE-------RLEEQNEVVEEADEQQEENEARAE-------AAEEEVDELKSQLADyqqalDVQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2111 KKR-----EAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEA-------ERRMKQAEVEKERQIKVAQEVaqQSAAA 2178
Cdd:PRK04863 410 QTRaiqyqQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEAteellslEQKLSVAQAAHSQFEQAYQLV--RKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2179 ELNSKRmsfAEKTAQlelSLKQEHITVTHLQEEAERLK-KLHDeaekareeaekeLEKWHQKANEALRLRLQAEEVAHKK 2257
Cdd:PRK04863 488 EVSRSE---AWDVAR---ELLRRLREQRHLAEQLQQLRmRLSE------------LEQRLRQQQRAERLLAEFCKRLGKN 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2258 TLAQEEAEKQKEDAErEARKRAKTEESALRQKELAE----DELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLL 2333
Cdd:PRK04863 550 LDDEDELEQLQEELE-ARLESLSESVSEARERRMALrqqlEQLQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQD 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2334 LEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKsrAEEESRSNTEKSKqmleVEASKLREL-----AEEAAKL 2408
Cdd:PRK04863 629 VTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPG--GSEDPRLNALAER----FGGVLLSEIyddvsLEDAPYF 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2409 RAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAIN-DATRLKT------EAEIALKEKEAENE-RLRRLAEDEAYQRK 2480
Cdd:PRK04863 703 SALYGPARHAIVVPDLSDAAEQLAGLEDCPEDLYLIEgDPDSFDDsvfsveELEKAVVVKIADRQwRYSRFPEVPLFGRA 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2481 LLEEQATQHKQDIEEKIillKKSSDNELERQKniVEDTLRQRRIIEEEIriLKVNFE--------KASVGKSDLELELNQ 2552
Cdd:PRK04863 783 AREKRIEQLRAEREELA---ERYATLSFDVQK--LQRLHQAFSRFIGSH--LAVAFEadpeaelrQLNRRRVELERALAD 855
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2553 LkniAEETQRSKEKAEQEAEKQRQLA--------LEEEQRRKEAEEkVRKILADEKEAAR---QRKAALEEVERLKAKAE 2621
Cdd:PRK04863 856 H---ESQEQQQRSQLEQAKEGLSALNrllprlnlLADETLADRVEE-IREQLDEAEEAKRfvqQHGNALAQLEPIVSVLQ 931
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2622 E-----AKRQKELAEKEAERQIQLAQEAALKKIDAEeKAHTAIvqQKEQEMLQtrkQEQSILDKLKEEAERAKRAaedad 2696
Cdd:PRK04863 932 SdpeqfEQLKQDYQQAQQTQRDAKQQAFALTEVVQR-RAHFSY--EDAAEMLA---KNSDLNEKLRQRLEQAEQE----- 1000
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2697 faRTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAhAEQAALKQKQLadeemdkHKKFA 2776
Cdd:PRK04863 1001 --RTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPADSGA-EERARARRDEL-------HARLS 1070
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1835643837 2777 EKTLRqKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDA 2821
Cdd:PRK04863 1071 ANRSR-RNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVNA 1114
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2533-3070 |
1.25e-11 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 71.60 E-value: 1.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2533 KVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEE----KVRKILADEKEAARQR-K 2607
Cdd:pfam05701 55 KKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQDSELAKLRVEEMEQgiadEASVAAKAQLEVAKARhA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2608 AALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQqkeqemlqtrkqeqsiLDKLKEEAER 2687
Cdd:pfam05701 135 AAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIE----------------LIATKESLES 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAAEDADFARTRaeqeAALSRQQveeaERLKQRAEEEaqakaQAQDEAEKLRK--------EAELEAAKRA----HAE 2755
Cdd:pfam05701 199 AHAAHLEAEEHRIG----AALAREQ----DKLNWEKELK-----QAEEELQRLNQqllsakdlKSKLETASALlldlKAE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2756 QAALKQKQLADE--EMDKHKKFAEKTLRQKSQVEQELTKVKLQLEE-TDHQKTL------LDEELQRLKEEVtDAMRQK- 2825
Cdd:pfam05701 266 LAAYMESKLKEEadGEGNEKKTSTSIQAALASAKKELEEVKANIEKaKDEVNCLrvaaasLRSELEKEKAEL-ASLRQRe 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2826 -------AQVEEELFKVKIQMEeliklklrieeenkMLIMKDKDSTQKlLVEEAEKMRQVAEEAArlsiEAQEAARMrkl 2898
Cdd:pfam05701 345 gmasiavSSLEAELNRTKSEIA--------------LVQAKEKEAREK-MVELPKQLQQAAQEAE----EAKSLAQA--- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2899 AEDDLANQRALAEKMlKEKMQAIQeaSRLKA---EAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGfqksleaerr 2975
Cdd:pfam05701 403 AREELRKAKEEAEQA-KAAASTVE--SRLEAvlkEIEAAKASEKLALAAIKALQESESSAESTNQEDSPR---------- 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2976 qqlEITAEAErlklQVLEMSRAQAKAEEDAskfKKKAEEIgnkLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIA 3055
Cdd:pfam05701 470 ---GVTLSLE----EYYELSKRAHEAEELA---NKRVAEA---VSQIEEAKESELRSLEKLEEVNREMEERKEALKIALE 536
|
570
....*....|....*.
gi 1835643837 3056 ELEHEKE-KLKREAEL 3070
Cdd:pfam05701 537 KAEKAKEgKLAAEQEL 552
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3671-3709 |
1.56e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.56e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 3671 LLEAQAGTGYIIDPVKNEKFPVEEAVKASVVGPEFNEKL 3709
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
767-862 |
1.62e-11 |
|
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409078 Cd Length: 105 Bit Score: 64.33 E-value: 1.62e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 767 KEKLLLWSQRMTEGyqgLHCDNFTTSWRDGRLFNAIIHRHKPVLI-DMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPE 845
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1835643837 846 DVDVPQPDEKSIITYVS 862
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2553-3208 |
1.67e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 71.59 E-value: 1.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2553 LKNIAEetqrSKEKAEQEAEKQ-RQLALEEEQRrkeaEEKVRKILADEKEAARQRKAALEEVERLKakaeeaKRQKELAE 2631
Cdd:TIGR04523 24 YKNIAN----KQDTEEKQLEKKlKTIKNELKNK----EKELKNLDKNLNKDEEKINNSNNKIKILE------QQIKDLND 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2632 KEAERQIQLAQ-EAALKKIDAEEKAHTAIVQQKEQEmlqtrkqeqsiLDKLKEEAERAKRAAEDADFARTRAEQEAALSR 2710
Cdd:TIGR04523 90 KLKKNKDKINKlNSDLSKINSEIKNDKEQKNKLEVE-----------LNKLEKQKKENKKNIDKFLTEIKKKEKELEKLN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2711 QQVEEAERLKQRAEEEaqakaQAQDEAEKLRKEAELEAAKRAHAEQAAL---------KQKQLADE--EMDKHKKFAEKT 2779
Cdd:TIGR04523 159 NKYNDLKKQKEELENE-----LNLLEKEKLNIQKNIDKIKNKLLKLELLlsnlkkkiqKNKSLESQisELKKQNNQLKDN 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2780 LRQK----SQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKlrieEENKM 2855
Cdd:TIGR04523 234 IEKKqqeiNEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQK----EQDWN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2856 LIMKDKDSTQKLLVEEAEKmrQVAEEAARLSIEAQEAARMRKlAEDDLANQRALAEKMLKEKMQAIQ----EASRLKAEA 2931
Cdd:TIGR04523 310 KELKSELKNQEKKLEEIQN--QISQNNKIISQLNEQISQLKK-ELTNSESENSEKQRELEEKQNEIEklkkENQSYKQEI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2932 EMLQKQKelaQEQARKFQEdKEQIEQQLAKETEGFQKSLEaerrqqlEITAEAERLKlqvlemsraqakaeEDASKFKKK 3011
Cdd:TIGR04523 387 KNLESQI---NDLESKIQN-QEKLNQQKDEQIKKLQQEKE-------LLEKEIERLK--------------ETIIKNNSE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3012 AEEIGNKLHQTELATKErmavvqtLEIQRQQSGKEAEELRRAIAELEHEKEKLKREaeLLQKNSQ-KMQVAQQEQLRQET 3090
Cdd:TIGR04523 442 IKDLTNQDSVKELIIKN-------LDNTRESLETQLKVLSRSINKIKQNLEQKQKE--LKSKEKElKKLNEEKKELEEKV 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3091 QVLQttflSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQ-----EHQMKHLEEEKDQLKVSMDDAMKKQKEAE 3165
Cdd:TIGR04523 513 KDLT----KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELkkenlEKEIDEKNKEIEELKQTQKSLKKKQEEKQ 588
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1835643837 3166 ENVRRKQDELQQLDKKRQEQEKLLAdenrKLREKLEQMEEEHR 3208
Cdd:TIGR04523 589 ELIDQKEKEKKDLIKEIEEKEKKIS----SLEKELEKAKKENE 627
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
642-744 |
1.71e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 64.75 E-value: 1.71e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 642 AEDERD-RVqkktFTKWVNKhlIKAQRHVSDLYEDLRDGHNLISLLEVLSGD--------NLPREKGRMRFHKLQNVQIA 712
Cdd:cd21300 3 AEGEREaRV----FTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGsvnwkkvnKAPASAEISRFKAVENTNYA 76
|
90 100 110
....*....|....*....|....*....|..
gi 1835643837 713 LDYLKHRQVKLVNIRNDDIADGNPKLTLGLIW 744
Cdd:cd21300 77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1702-2220 |
1.75e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 71.61 E-value: 1.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1702 GAEEVVRTYEDQLKEVHAvpsdskelEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRSHSERDVDLDRYRE 1781
Cdd:PRK02224 177 GVERVLSDQRGSLDQLKA--------QIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1782 KVQQLLERWQAILvqiDLR------QRELDQLGRQLRYYRETYEWLIKWIKDA--------------KQRQEQIQSVPIT 1841
Cdd:PRK02224 249 RREELETLEAEIE---DLRetiaetEREREELAEEVRDLRERLEELEEERDDLlaeaglddadaeavEARREELEDRDEE 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1842 DSKTMKEHLLQEKKLLDEIESNRDKVDECQKYAKQYIDAIKDYELQLVTYKAQVEpvaspakkpKVQSTSDSIIQEYVDL 1921
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVE---------DRREEIEELEEEIEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1922 RTRYSELTTL---TSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAK-------QTQLAEAHAKAKAQAEKE 1991
Cdd:PRK02224 397 RERFGDAPVDlgnAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1992 AEELQRRMQeevskrevvavDAEQQKQTIQQELQQLRqnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKA 2071
Cdd:PRK02224 477 VEELEAELE-----------DLEEEVEEVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2072 NAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKR--KVQAEKEAAREKQRAVEDL-EKFRSQAE 2148
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLrEKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2149 -EAERRMKQAEvEKERQIKVAQEVaQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQ-------EEAERLKKLHD 2220
Cdd:PRK02224 621 lNDERRERLAE-KRERKRELEAEF-DEARIEEAREDKERAEEYLEQVEEKLDELREERDDLQaeigaveNELEELEELRE 698
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1947-2157 |
1.77e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 70.18 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1947 NDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQE---EVSKREVVAVDAEQQKQTIQQE 2023
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2024 LQQLR--------------QNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKAnaedELQELRARAEKAEQ 2089
Cdd:COG4942 99 LEAQKeelaellralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2090 QKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQA 2157
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2947-3228 |
1.79e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 71.63 E-value: 1.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2947 KFQEDKEQIEQQLAKETEGFQK--SLEAERRQQLEitaeaeRLKLQVlemsraqakaeEDASKFKKKAEEignkLHQTEL 3024
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRleDILNELERQLK------SLERQA-----------EKAERYKELKAE----LRELEL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3025 AtkermavVQTLEIQRQQsgKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEqLRQETQVLQTTFLSEKQLL 3104
Cdd:TIGR02168 228 A-------LLVLRLEELR--EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-LEEEIEELQKELYALANEI 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3105 LEREKYIEEEKAKLENLYEDEVRKAQKLkQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQE 3184
Cdd:TIGR02168 298 SRLEQQKQILRERLANLERQLEELEAQL-EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1835643837 3185 QEKLLADENRKLREKLEQMEEehriALAQTREMRTQTDDLAGNL 3228
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIAS----LNNEIERLEARLERLEDRR 416
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2781-3229 |
1.91e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.64 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2781 RQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEvtdamRQKAQVEEELFKVKIQMEELIKLK-LRIEEENKMLIMK 2859
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-----REKAERYQALLKEKREYEGYELLKeKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2860 DKDSTQKLLVEEAEKMRQVAEEAARLSIE-AQEAARMRKLAEDDlanQRALAEKMLKekmqaiqeasrLKAEAEMLQKQK 2938
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLlEELNKKIKDLGEEE---QLRVKEKIGE-----------LEAEIASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2939 ELAQEQARKFQEDKEQIEQQLAK---ETEGFQKSLEAERRQQLEITAEAERLKlQVLEMSRAQAKAEEdaskfkkkaeei 3015
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAEIDKllaEIEELEREIEEERKRRDKLTEEYAELK-EELEDLRAELEEVD------------ 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3016 gnklhqtelatkermavvqtleiqrqqsgKEAEELRRAIAELEHEKEKLKREAELLQKNSQKmqvaqqeqlrqetqvlqt 3095
Cdd:TIGR02169 378 -----------------------------KEFAETRDELKDYREKLEKLKREINELKRELDR------------------ 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3096 tflsekqlLLEREKYIEEEKAKLENlyedevrkaqklkqeqehQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDEL 3175
Cdd:TIGR02169 411 --------LQEELQRLSEELADLNA------------------AIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADL 464
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 3176 ----QQLDKKRQEQEKlLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDLAGNLP 3229
Cdd:TIGR02169 465 skyeQELYDLKEEYDR-VEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQ 521
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2389-2937 |
1.94e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.48 E-value: 1.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2389 QMLE-----VEASKLRELAEEAAKLRAVSEEAKRQR----QIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALK 2459
Cdd:COG4913 216 YMLEepdtfEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2460 EKEAENERLRRLAEdeayQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKvnfEKA 2539
Cdd:COG4913 296 ELEELRAELARLEA----ELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2540 SVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKiLADEKEAARQRKAAL-EEVERLKA 2618
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-LEAEIASLERRKSNIpARLLALRD 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2619 KAEEAKRQKE-----LAE----KEAERQIQLAQE------------------AALKKIDA---EEKAHTAIVQQKEQEML 2668
Cdd:COG4913 448 ALAEALGLDEaelpfVGElievRPEEERWRGAIErvlggfaltllvppehyaAALRWVNRlhlRGRLVYERVRTGLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2669 QTRKQEQSILDKLK--------------------------EEAERAKRAA----------------------------ED 2694
Cdd:COG4913 528 RPRLDPDSLAGKLDfkphpfrawleaelgrrfdyvcvdspEELRRHPRAItragqvkgngtrhekddrrrirsryvlgFD 607
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2695 ADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADeemdkhkk 2774
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELER-------- 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2775 fAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEEL--FKVKIQMEELIKLKLRIEEE 2852
Cdd:COG4913 680 -LDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLeaAEDLARLELRALLEERFAAA 758
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2853 NKMLIMKD-KDSTQKLLVEEAEKMRQVAEEAARL-----------------SIEAQE--AARMRKLAEDDLANQRALAEK 2912
Cdd:COG4913 759 LGDAVERElRENLEERIDALRARLNRAEEELERAmrafnrewpaetadldaDLESLPeyLALLDRLEEDGLPEYEERFKE 838
|
650 660
....*....|....*....|....*..
gi 1835643837 2913 MLKEKMQAIQE--ASRLKAEAEMLQKQ 2937
Cdd:COG4913 839 LLNENSIEFVAdlLSKLRRAIREIKER 865
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2294-2747 |
2.02e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.95 E-value: 2.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2294 DELEKQRKLADATAQQKFSAEQELIRLKAETEnseqqrllleeelfrlknevnEAIQKRKEMEEELAKVRAEMEI--LLQ 2371
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELE---------------------ELEAELEELREELEKLEKLLQLlpLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2372 SKSRAEEESRSNTEKSKQMLEveasKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLK 2451
Cdd:COG4717 133 ELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2452 TEAEIALKEKEAENERLRRlaEDEAYQRKLLEEQATQHKQDIEEKIIL-------------LKKSSDNELERQKNIVEDT 2518
Cdd:COG4717 209 AELEEELEEAQEELEELEE--ELEQLENELEAAALEERLKEARLLLLIaaallallglggsLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2519 LRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILAD 2598
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2599 EKEAARQR---KAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAlkkiDAEEKAHTAIVQQKEQEMLQTRKQEQ 2675
Cdd:COG4717 367 ELEQEIAAllaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLG----ELEELLEALDEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2676 SILDKLKEeaERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELE 2747
Cdd:COG4717 443 ELEEELEE--LREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2777-3144 |
2.49e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.92 E-value: 2.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2777 EKTLRQKSQVEQELTKVKLQLEETDHQKTLLD------------EELQRLKEEVTDAMRQKAQVEEelfKVKIQMEELIK 2844
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAVSErqqqekfekmeqERLRQEKEEKAREVERRRKLEE---AEKARQAEMDR 331
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2845 LKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAArlsieAQEAARMRKLAeddlanqralaekmlKEKMQAIQEA 2924
Cdd:pfam17380 332 QAAIYAEQERMAMERERELERIRQEERKRELERIRQEEI-----AMEISRMRELE---------------RLQMERQQKN 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2925 SRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLeaeRRQQLEITAEAERLKLQVLEMSRAQAKAEED 3004
Cdd:pfam17380 392 ERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREV---RRLEEERAREMERVRLEEQERQQQVERLRQQ 468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3005 ASKFKKKAEEIGNKLHQTELATKERMAVVQtleiqrqqsgKEAEELRRAIAELEHEKEKLKREAELLQK---NSQKMQVA 3081
Cdd:pfam17380 469 EEERKRKKLELEKEKRDRKRAEEQRRKILE----------KELEERKQAMIEEERKRKLLEKEMEERQKaiyEEERRREA 538
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3082 QQEQLRQETqvlqttfLSEKQLLLEREKYIEEEKAKLENLYEDevRKAQKLKQEQEHQMKHLE 3144
Cdd:pfam17380 539 EEERRKQQE-------MEERRRIQEQMRKATEERSRLEAMERE--REMMRQIVESEKARAEYE 592
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2395-3206 |
2.72e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.14 E-value: 2.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2395 ASKLRELAEEAAKLRAVSEEAKRQRqiaedEAARQRAEAeriLKEKLAAINDAtRLKTEAEIalkekEAENERLRRLAED 2474
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQL-----AAEQYRLVE---MARELAELNEA-ESDLEQDY-----QAASDHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2475 EAYQrklleEQATQHKQDIEEKIIllkkssdnELERQKNIVEDtlrqrriieeeirilkvnfekasvgksdlelelnqLK 2554
Cdd:PRK04863 344 LRQQ-----EKIERYQADLEELEE--------RLEEQNEVVEE-----------------------------------AD 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2555 NIAEETQRSKEKAEQEA-EKQRQLA-----LEEEQRR-------KEAEEKVRKILADEKEAARQRKAALEEverLKAKAE 2621
Cdd:PRK04863 376 EQQEENEARAEAAEEEVdELKSQLAdyqqaLDVQQTRaiqyqqaVQALERAKQLCGLPDLTADNAEDWLEE---FQAKEQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2622 EAkrqkELAEKEAERQIQLAQEA---------ALKKI-------DAEEKAHTAIVQQKEQEMLQTrkQEQSILDKLKEeA 2685
Cdd:PRK04863 453 EA----TEELLSLEQKLSVAQAAhsqfeqayqLVRKIagevsrsEAWDVARELLRRLREQRHLAE--QLQQLRMRLSE-L 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2686 ERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEE----AQAKAQAQDEAEKLRKEAE-LEA-----AKRA--- 2752
Cdd:PRK04863 526 EQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARleslSESVSEARERRMALRQQLEqLQAriqrlAARApaw 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2753 HAEQAALKQ-----------KQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKE----- 2816
Cdd:PRK04863 606 LAAQDALARlreqsgeefedSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPRLNALAErfggv 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2817 ---------EVTDA---------MRQkAQVEEELFKVKIQMEELIKLKlrieeENKMLIMKDKDS--TQKLLVEEAEK-- 2874
Cdd:PRK04863 686 llseiyddvSLEDApyfsalygpARH-AIVVPDLSDAAEQLAGLEDCP-----EDLYLIEGDPDSfdDSVFSVEELEKav 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2875 MRQVAEEAARLSIEAQE-----AARMRKLAedDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLqkqkeLAQEQARKFQ 2949
Cdd:PRK04863 760 VVKIADRQWRYSRFPEVplfgrAAREKRIE--QLRAEREELAERYATLSFDVQKLQRLHQAFSRF-----IGSHLAVAFE 832
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2950 EDKEQIEQQLAKETEGFQKSLEA--ERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASkFKKKAEEIGNKLHQTELAtk 3027
Cdd:PRK04863 833 ADPEAELRQLNRRRVELERALADheSQEQQQRSQLEQAKEGLSALNRLLPRLNLLADET-LADRVEEIREQLDEAEEA-- 909
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3028 ermavvqtlEIQRQQSGKEAEELRRAIAELEHEKEKLkreaELLQKNSQKMQvAQQEQLRQE----TQVLQ--TTF-LSE 3100
Cdd:PRK04863 910 ---------KRFVQQHGNALAQLEPIVSVLQSDPEQF----EQLKQDYQQAQ-QTQRDAKQQafalTEVVQrrAHFsYED 975
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3101 KQLLLEREKYIEEE-KAKLENLYEDEVRKAQKLKQEQ--------------------EHQMKHLEEEKDQLKVSMDDamk 3159
Cdd:PRK04863 976 AAEMLAKNSDLNEKlRQRLEQAEQERTRAREQLRQAQaqlaqynqvlaslkssydakRQMLQELKQELQDLGVPADS--- 1052
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 3160 kqkEAEENVRRKQDELQ-----------QLDKKRQEQEKLLADENRKLR---EKLEQMEEE 3206
Cdd:PRK04863 1053 ---GAEERARARRDELHarlsanrsrrnQLEKQLTFCEAEMDNLTKKLRkleRDYHEMREQ 1110
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2662-3091 |
3.05e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 70.57 E-value: 3.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2662 QKEQEMLQTRKQEQSILDKLK-EEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKL 2740
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2741 RKEAELEA-------------AKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLL 2807
Cdd:COG4717 132 QELEALEAelaelperleeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2808 DEELQRLKEEVTDAMRQKAQVEEELFKVKIQmEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEE----AA 2883
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllalLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2884 RLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAI-----QEASRLKAEAEMLQKQKELAQEQARKFQE-DKEQIEQ 2957
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdLSPEELLELLDRIEELQELLREAEELEEElQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2958 QLAKETEGFQKSLEAERRQQLEITAEAERLK--LQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQT 3035
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKeeLEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3036 L--EIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQ--EQLRQETQ 3091
Cdd:COG4717 451 LreELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALEllEEAREEYR 510
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1782-2440 |
3.41e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 70.52 E-value: 3.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1782 KVQQLLERWQaILVQIDLRQREldqlgRQLRYYRETYEWLIKWIKDAKQRQEQIqsvpitdSKTMKEHLLQEKKLLDEIE 1861
Cdd:pfam05483 85 KEAEKIKKWK-VSIEAELKQKE-----NKLQENRKIIEAQRKAIQELQFENEKV-------SLKLEEEIQENKDLIKENN 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1862 SNRDKVDECQKYAKQYIDAIKDYELQ-------LVTYKAQVEPVASPAKKPKVQStSDSIIQEYVDLRTRYSELTTLTSQ 1934
Cdd:pfam05483 152 ATRHLCNLLKETCARSAEKTKKYEYEreetrqvYMDLNNNIEKMILAFEELRVQA-ENARLEMHFKLKEDHEKIQHLEEE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1935 YIKFITETLRRLN----------DEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVS 2004
Cdd:pfam05483 231 YKKEINDKEKQVSllliqitekeNKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMS 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2005 KREVVAVDAEQQKQTIQQELQQlrQNSDMEIKSKAKQ-----IEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQE 2079
Cdd:pfam05483 311 TQKALEEDLQIATKTICQLTEE--KEAQMEELNKAKAahsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2080 LRARAEKAEQQKKAAQEEAERLRK------QVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLE----KFRSQAEE 2149
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKilaedeKLLDEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEiqltAIKTSEEH 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2150 AERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEA--ERLKKLHDEAEKARE 2227
Cdd:pfam05483 469 YLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERmlKQIENLEEKEMNLRD 548
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2228 EAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATA 2307
Cdd:pfam05483 549 ELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAEN 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2308 QQKFSAEQELIRLKAETENSEQQ------------------RLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEIL 2369
Cdd:pfam05483 629 KQLNAYEIKVNKLELELASAKQKfeeiidnyqkeiedkkisEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVAL 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2370 LQS------KSRAEEESRSNTEKSKqmlEVEASKLR-ELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAER---ILKE 2439
Cdd:pfam05483 709 MEKhkhqydKIIEERDSELGLYKNK---EQEQSSAKaALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEntaILKD 785
|
.
gi 1835643837 2440 K 2440
Cdd:pfam05483 786 K 786
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1949-2151 |
4.10e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 69.06 E-value: 4.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1949 EEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavdAEQQKQTiqqELQQLR 2028
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQKQA---EEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2029 QNSDMEIKSKAKQiEEVEYNRRKIEEEIHiVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAerlrKQVKDE 2108
Cdd:PRK09510 141 AAAAAKAKAEAEA-KRAAAAAKKAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAK----KKAAAE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1835643837 2109 TQKKREAE-EELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAE 2151
Cdd:PRK09510 215 AKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2711-3147 |
4.95e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.80 E-value: 4.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2711 QQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKE-AELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQE 2789
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEElEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2790 LTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQK-AQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLL 2868
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2869 VEEAEKMRQVAEE------------AARLSIEAQEAARMRKLAEDD--LANQRALAEKMLKEKMQAIQEASRLKAEAEML 2934
Cdd:COG4717 231 QLENELEAAALEErlkearlllliaAALLALLGLGGSLLSLILTIAgvLFLVLGLLALLFLLLAREKASLGKEAEELQAL 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2935 QKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASkfkkKAEE 3014
Cdd:COG4717 311 PALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVE----DEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3015 IGNKLHQTELATKERmAVVQTLEIQRQQSGKEAEELRRAI--AELEHEKEKLKREAELLQKnsqKMQVAQQEQLRQETQV 3092
Cdd:COG4717 387 LRAALEQAEEYQELK-EELEELEEQLEELLGELEELLEALdeEELEEELEELEEELEELEE---ELEELREELAELEAEL 462
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 3093 LQttfLSEKQLLLEREKYIEEEKAKLENLyEDEVRKAQKLKQEQEHQMKHLEEEK 3147
Cdd:COG4717 463 EQ---LEEDGELAELLQELEELKAELREL-AEEWAALKLALELLEEAREEYREER 513
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
767-866 |
5.00e-11 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 62.74 E-value: 5.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 767 KEKLLLWSQRMTEGYQGLHCDNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTN---LENLDQAFNVAER-DLGVTRLL 842
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1835643837 843 DPEDVdVPQPDEKSIITYVSSMYD 866
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2569-3216 |
5.15e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 69.78 E-value: 5.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2569 QEAEKQRQLALEEEQRRKEAEEKVRKIladeKEAARQRKAALE----EVERLkAKAEEAKRqkelAEKEAERQIQLAQEA 2644
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLL----RETSLQQKMRLEaqamELDAL-AVAEKAGQ----AEAEGLRAALAGAEM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2645 ALKKIDAEEKAHTAIVQQKEQEMLQTRKQ-EQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRA 2723
Cdd:pfam07111 130 VRKNLEEGSQRELEEIQRLHQEQLSSLTQaHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2724 EEEAQAKAQAqdeAEKLRKEAELEAAKRAHAEQAALKQKQLadeeMDKHKKFAEKtlRQKSQVEQELTKVKLQleETDHQ 2803
Cdd:pfam07111 210 QEELEAQVTL---VESLRKYVGEQVPPEVHSQTWELERQEL----LDTMQHLQED--RADLQATVELLQVRVQ--SLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2804 KTLLDEELQR-------LKEEVTDAMRQK-AQVEEELFKVKIQMeeliklklrieeenKMLIMKDKDSTQKLLVeeaekm 2875
Cdd:pfam07111 279 LALQEEELTRkiqpsdsLEPEFPKKCRSLlNRWREKVFALMVQL--------------KAQDLEHRDSVKQLRG------ 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2876 rQVAEEAARLSIEAQEAARMrklaeddlanQRALAEKmlkekmQAIQEASRLKAEAemLQKQKELAQEQARkfqedkeqi 2955
Cdd:pfam07111 339 -QVAELQEQVTSQSQEQAIL----------QRALQDK------AAEVEVERMSAKG--LQMELSRAQEARR--------- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2956 eqqlaketegfqksleaerRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKE------R 3029
Cdd:pfam07111 391 -------------------RQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhtikgL 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3030 MAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQ-KMQVAQQE--------------------QLRQ 3088
Cdd:pfam07111 452 MARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQlSAHLIQQEvgrareqgeaerqqlsevaqQLEQ 531
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3089 ETQVLQTTFLSEKQLL---LEREKYIEEEKAKL-ENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEA 3164
Cdd:pfam07111 532 ELQRAQESLASVGQQLevaRQGQQESTEEAASLrQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKA 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 3165 EENVRRKQDELQQLDKKRQE----QEKLLADENRKLREKLEQMEEEHRIALAQTRE 3216
Cdd:pfam07111 612 VVSLRQIQHRATQEKERNQElrrlQDEARKEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2088-2316 |
5.49e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 68.68 E-value: 5.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2088 EQQKKAAQEEAERLRKqvKDETQKkreaEEELKRKVQAEKE--AAREKQRAVEDLEKfrSQAEEAERRMKQAEVEKERQI 2165
Cdd:PRK09510 67 QQQQQKSAKRAEEQRK--KKEQQQ----AEELQQKQAAEQErlKQLEKERLAAQEQK--KQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2166 KVAQEVAQQSAAAElnSKRMSFAEKTAqlelslkqehitvthlqeEAERLKKlhdeaekareeaekelEKWHQKANEALR 2245
Cdd:PRK09510 139 AKAAAAAKAKAEAE--AKRAAAAAKKA------------------AAEAKKK----------------AEAEAAKKAAAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2246 LRLQAEEVAHKKtlAQEEAEKQ-----KEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQE 2316
Cdd:PRK09510 183 AKKKAEAEAAAK--AAAEAKKKaeaeaKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2553-2745 |
5.75e-11 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 68.75 E-value: 5.75e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2553 LKNIAEETQRS-KEKAEQEAEKQRQLAlEEEQRRKEAEEKVRKILADEKEAARQRkaaleevERLKAKAEEaKRQKELAE 2631
Cdd:COG2268 191 RRKIAEIIRDArIAEAEAERETEIAIA-QANREAEEAELEQEREIETARIAEAEA-------ELAKKKAEE-RREAETAR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2632 KEAERQIQLAQEAALKKIDAEekahTAIVQQKEQEMLQTRKQEQSIldklkEEAERAKRAAEDADfaRTRAEQEAalsrq 2711
Cdd:COG2268 262 AEAEAAYEIAEANAEREVQRQ----LEIAEREREIELQEKEAEREE-----AELEADVRKPAEAE--KQAAEAEA----- 325
|
170 180 190
....*....|....*....|....*....|....*
gi 1835643837 2712 qveeaerlkqraEEEAQA-KAQAQDEAEKLRKEAE 2745
Cdd:COG2268 326 ------------EAEAEAiRAKGLAEAEGKRALAE 348
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2036-2496 |
8.34e-11 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 69.27 E-value: 8.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2036 KSKAKQIEEVEYNRRKIEEEIhivRLQLETmQKHKANAE----------DELQELRARAEKAEQQK-KAAQEEAERLRKQ 2104
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEI---QKSLDK-RKHTQNVAlnkklsdiktEYLYELNVLKEKSEAELtSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2105 VKDETQKKREAEEELKRKV-QAEKEAAREKQravEDLEKFRSQAEEA-ERRMKQAEVE-KERQIKVAQEVAQQSaaaeln 2181
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVeEAEKKAKDQKE---EDRRNYPTNTYKTlELEIAESDVEvKKAELELVKEEAKEP------ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2182 skrmsfaektaQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREeaekelekwhqkanEALRLRLQAEEVAHKKTLAQ 2261
Cdd:NF033838 201 -----------RDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEE--------------EAKRRADAKLKEAVEKNVAT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2262 EEAEKQKEDAEREA----------RKRAKTEESALRQKELAEDELEKQRKLADAtaqQKFSAEQElirLKAETENSEQQR 2331
Cdd:NF033838 256 SEQDKPKRRAKRGVlgepatpdkkENDAKSSDSSVGEETLPSPSLKPEKKVAEA---EKKVEEAK---KKAKDQKEEDRR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2332 LLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAemeillqsksraeEESRsNTEKSKQMLEVEASKLrelaEEAAKLrav 2411
Cdd:NF033838 330 NYPTNTYKTLELEIAESDVKVKEAELELVKEEA-------------KEPR-NEEKIKQAKAKVESKK----AEATRL--- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2412 sEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEA---YQRKLLEE--QA 2486
Cdd:NF033838 389 -EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQAeedYARRSEEEynRL 467
|
490
....*....|
gi 1835643837 2487 TQHKQDIEEK 2496
Cdd:NF033838 468 TQQQPPKTEK 477
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2582-2758 |
9.21e-11 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 68.65 E-value: 9.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2582 EQRRKEAEEKVRKILAD-EKEAARQRKAAL----EEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKah 2656
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEaKKEAEAIKKEALleakEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEK-- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2657 taivqqKEQEMLQTRK---QEQSILDKLKEEAERAKRAAEDadfartRAEQEAALSRqqvEEA-ERLKQRAEEEAQAKA- 2731
Cdd:PRK12704 108 ------REEELEKKEKeleQKQQELEKKEEELEELIEEQLQ------ELERISGLTA---EEAkEILLEKVEEEARHEAa 172
|
170 180 190
....*....|....*....|....*....|....*
gi 1835643837 2732 --------QAQDEAEKLRKEAELEAAKRAHAEQAA 2758
Cdd:PRK12704 173 vlikeieeEAKEEADKKAKEILAQAIQRCAADHVA 207
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4924-4962 |
9.87e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.65 E-value: 9.87e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 4924 LLEAQACTGGIIDINTGQKFSVTDAVNKGLVDKIMVDRI 4962
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2557-2855 |
1.00e-10 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 67.25 E-value: 1.00e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2557 AEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKaaLEEVERLKAKAEEAKRQKELAEKEAER 2636
Cdd:pfam13868 39 KEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKR--QEEYEEKLQEREQMDEIVERIQEEDQA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2637 QIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAER---------AKRAAEDADFARTRAEQEAA 2707
Cdd:pfam13868 117 EAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEReeereaereEIEEEKEREIARLRAQQEKA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2708 LSRQqvEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAA-KRAHAEQAALKQKQLAdEEMDKHKKFAEKTLRQKSQV 2786
Cdd:pfam13868 197 QDEK--AERDELRAKLYQEEQERKERQKEREEAEKKARQRQElQQAREEQIELKERRLA-EEAEREEEEFERMLRKQAED 273
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2787 EQeltKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKM 2855
Cdd:pfam13868 274 EE---IEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1939-2178 |
1.38e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 67.18 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1939 ITETLRRLNDEEKAAEKlKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRmqeevskrevvavdAEQQKQ 2018
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAK-KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ--------------AEQAAK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2019 tiqqelqqlrqnsdmEIKSKAKQIEEveyNRRKIEEEihivrlqletmQKHKANAEDELQELRARAEKAEQQKKA----- 2093
Cdd:TIGR02794 113 ---------------QAEEKQKQAEE---AKAKQAAE-----------AKAKAEAEAERKAKEEAAKQAEEEAKAkaaae 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2094 AQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAE-----EAERRMKQAEVEKERQIKVA 2168
Cdd:TIGR02794 164 AKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAaaaaaEAERKADEAELGDIFGLASG 243
|
250
....*....|
gi 1835643837 2169 QEVAQQSAAA 2178
Cdd:TIGR02794 244 SNAEKQGGAR 253
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2014-2193 |
1.45e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 67.14 E-value: 1.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2014 EQQKQTIQQELQQLRQnsdmeiKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELR--------ARAE 2085
Cdd:PRK09510 67 QQQQQKSAKRAEEQRK------KKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAAlkqkqaeeAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2086 KAEQQKKAAQEEAERLR---KQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKE 2162
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190
....*....|....*....|....*....|.
gi 1835643837 2163 RQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ 2193
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAA 251
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2762-3216 |
1.47e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2762 KQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLdEELQRLKEEVTDAMRQKAQVEEELFKVK--IQM 2839
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQ-EELEELEEELEELEAELEELREELEKLEklLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2840 EELIKLKLRIEEEnkmliMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAarmrklaeddlanQRALAEKMLKEKMQ 2919
Cdd:COG4717 128 LPLYQELEALEAE-----LAELPERLEELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2920 AIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQA 2999
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3000 KAEE----------------------DASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAEL 3057
Cdd:COG4717 270 SLILtiagvlflvlgllallflllarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3058 EhekeklkreaELLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKqlllerekyiEEEKAKLENLYEDEVRKAQKLKQEQE 3137
Cdd:COG4717 350 Q----------ELLREAEELEEELQLEELEQEIAALLAEAGVED----------EEELRAALEQAEEYQELKEELEELEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3138 HQMKHLEEEKDQLKVSMDDAMKKQ-KEAEENVRRKQDELQQLDKKRQEqeklladenrkLREKLEQMEEEHRIALAQTRE 3216
Cdd:COG4717 410 QLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAE-----------LEAELEQLEEDGELAELLQEL 478
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2538-2964 |
1.48e-10 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 68.00 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2538 KASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVrkilADEKEAARQRKAALEEVERlK 2617
Cdd:pfam07888 28 RAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRV----AELKEELRQSREKHEELEE-K 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2618 AKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEmlqtrkqeqsiLDKLKEEAERAKRAAEDadf 2697
Cdd:pfam07888 103 YKELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETE-----------LERMKERAKKAGAQRKE--- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2698 artraeqeaalsrqqvEEAERlkqraeEEAQAKAQaQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKkfae 2777
Cdd:pfam07888 169 ----------------EEAER------KQLQAKLQ-QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2778 ktLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEEL------IKLKLRiee 2851
Cdd:pfam07888 222 --LTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLtlqladASLALR--- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2852 ENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEasrLKAEA 2931
Cdd:pfam07888 297 EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASL 373
|
410 420 430
....*....|....*....|....*....|...
gi 1835643837 2932 EMLQKQKELAQEQARKFQEDKEQIEQQLAKETE 2964
Cdd:pfam07888 374 RVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2554-2818 |
1.59e-10 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 67.31 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2554 KNIAEETQRSKEKAEQEA--EKQRQLALEEEQRRKEAEEKvrkilADEKEAARQRKAALEEV-------------ERLKA 2618
Cdd:PRK07735 29 KHGAEISKLEEENREKEKalPKNDDMTIEEAKRRAAAAAK-----AKAAALAKQKREGTEEVteeekakakakaaAAAKA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2619 KAEEAKRQKELAEKEAERQiqlAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDklkEEAERAKRAAEDADFA 2698
Cdd:PRK07735 104 KAAALAKQKREGTEEVTEE---EKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETD---KEKAKAKAAAAAKAKA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2699 RTRAEQEAALSRQQVEEAERlkqraEEEAQAKAQAQDEAeklrkeaelEAAKRAHAEQAALKQKQLADEEMDKHKKF--- 2775
Cdd:PRK07735 178 AALAKQKAAEAGEGTEEVTE-----EEKAKAKAKAAAAA---------KAKAAALAKQKASQGNGDSGDEDAKAKAIaaa 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1835643837 2776 ---AEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEV 2818
Cdd:PRK07735 244 kakAAAAARAKTKGAEGKKEEEPKQEEPSVNQPYLNKYVEVIKEKL 289
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2543-2894 |
1.66e-10 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 66.98 E-value: 1.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2543 KSDLELELNQLKNIAEETQRSKEKAEQE-AEKQRQLALEEEQRRKEAEEKVRKILAD--EKEAARQRKAALEEVErlkak 2619
Cdd:pfam15558 19 EEQRMRELQQQAALAWEELRRRDQKRQEtLERERRLLLQQSQEQWQAEKEQRKARLGreERRRADRREKQVIEKE----- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2620 aEEAKRQKELAEKEAERQIQLAQEAAlkkidaeekahtaivqqkeqemlQTRKQEQSILDKLKEEAERAKRaaedadfar 2699
Cdd:pfam15558 94 -SRWREQAEDQENQRQEKLERARQEA-----------------------EQRKQCQEQRLKEKEEELQALR--------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2700 traEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAEL-EAAKRAHAEQA----ALKQK-QLADEEMDKHK 2773
Cdd:pfam15558 141 ---EQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKvLVDCQAKAEELlrrlSLEQSlQRSQENYEQLV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2774 KFAEKTLRQKSQVEQE-LTKVKLQLEETDHQKTLLDEELQRLKEEvtdAMRQKAQVEEELFKVKIQ-MEELIKLKLRIEE 2851
Cdd:pfam15558 218 EERHRELREKAQKEEEqFQRAKWRAEEKEEERQEHKEALAELADR---KIQQARQVAHKTVQDKAQrARELNLEREKNHH 294
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1835643837 2852 ENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAAR 2894
Cdd:pfam15558 295 ILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEAR 337
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2549-3179 |
1.78e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.40 E-value: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2549 ELNQLKNIAEETQRSKEKAEQ-EAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKA---ALEEVERLKAKAEEAK 2624
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEleeLRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2625 RQKELAEKE---AERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTR 2701
Cdd:COG4913 316 ARLDALREEldeLEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2702 AEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRK--EAELEAAKRAHAEQAALKQKQL--ADEEMD---KHKK 2774
Cdd:COG4913 396 LEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSniPARLLALRDALAEALGLDEAELpfVGELIEvrpEEER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2775 F---AEKTLRQKSQ---VEQELTKVKLQLEETDHQKTLLDeeLQRLKEEVTDAMRQKAQveeelfkvkiqmEELIKLKLR 2848
Cdd:COG4913 476 WrgaIERVLGGFALtllVPPEHYAAALRWVNRLHLRGRLV--YERVRTGLPDPERPRLD------------PDSLAGKLD 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2849 IEEEN-----KMLIMKDKDSTQkllVEEAEKMRQvaeEAARLSIEAQ---EAARMRKLAEDDLA--------NQRALAEk 2912
Cdd:COG4913 542 FKPHPfrawlEAELGRRFDYVC---VDSPEELRR---HPRAITRAGQvkgNGTRHEKDDRRRIRsryvlgfdNRAKLAA- 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2913 mLKEKMQAIQEA-SRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLakETEGFQKSLeAERRQQLEiTAEAERLKLQV 2991
Cdd:COG4913 615 -LEAELAELEEElAEAEERLEALEAELDALQERREALQRLAEYSWDEI--DVASAEREI-AELEAELE-RLDASSDDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2992 LEMSRAQAKAEEDAS-----KFKKKAEEIGNKLHQ-TELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLK 3065
Cdd:COG4913 690 LEEQLEELEAELEELeeeldELKGEIGRLEKELEQaEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3066 REAELLQKNSQKMQVAQQEqLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDE-VRKAQKLKQEQEHQMkhlE 3144
Cdd:COG4913 770 NLEERIDALRARLNRAEEE-LERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGlPEYEERFKELLNENS---I 845
|
650 660 670
....*....|....*....|....*....|....*
gi 1835643837 3145 EEKDQLKVSMDDAmkkQKEAEENVRRKQDELQQLD 3179
Cdd:COG4913 846 EFVADLLSKLRRA---IREIKERIDPLNDSLKRIP 877
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2383-2853 |
2.14e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.87 E-value: 2.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2383 NTEKSKQMLEVEASKLRELAEEAAKLRAVSEE-AKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEK 2461
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2462 EAENERLR-RLAEDEAYQRKL--LEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEdtlrqrriieeeirilkvnfek 2538
Cdd:COG4717 145 PERLEELEeRLEELRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELE---------------------- 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2539 asvgksDLELELNQLKNIAEETQRSKEKAEQEAEK-QRQLALEEEQRRKEAEEKVRKILA---------DEKEAARQRKA 2608
Cdd:COG4717 203 ------ELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKEARLLLLIAAallallglgGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2609 ----------ALEEVERLKAKAEEAKRQKELAEKEAERQI-QLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSI 2677
Cdd:COG4717 277 gvlflvlgllALLFLLLAREKASLGKEAEELQALPALEELeEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2678 lDKLKEEAERAKRAAE-DADFARTRAEQEAALsRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQ 2756
Cdd:COG4717 357 -EELEEELQLEELEQEiAALLAEAGVEDEEEL-RAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2757 AALKQKQLADEEmdkhkkfaektlrQKSQVEQELTKVKLQLEETDHqktllDEELQRLKEEVTDAMRQKAQVEEELFKVK 2836
Cdd:COG4717 435 EELEEELEELEE-------------ELEELREELAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALK 496
|
490
....*....|....*..
gi 1835643837 2837 IQMEELIKLKLRIEEEN 2853
Cdd:COG4717 497 LALELLEEAREEYREER 513
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2643-3225 |
2.60e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2643 EAALKKIDAEEKaHTAIVQQKEQEMLQTrkqeqsiLDKLKEEAERAKRAAedaDFARTRAEQEAALSRQQVEEAERLKQR 2722
Cdd:TIGR02169 173 EKALEELEEVEE-NIERLDLIIDEKRQQ-------LERLRREREKAERYQ---ALLKEKREYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2723 AEEEAQAKAQAQDEAEKLRKEAELE-AAKRAHAEQAALKQKQLADEEMdkhkkfaektlrqkSQVEQELTKVKLQLEETD 2801
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRlEEIEQLLEELNKKIKDLGEEEQ--------------LRVKEKIGELEAEIASLE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2802 HQKTLLDEELQRLKEEVtdamrqkAQVEEELFKVKIQMEElikLKLRIEEENKMLImKDKDSTQKLLVEEAEKMRQVAEE 2881
Cdd:TIGR02169 308 RSIAEKERELEDAEERL-------AKLEAEIDKLLAEIEE---LEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2882 AARLSIEAQEAARMRKLAED---DLANQRALAEKMLKEKMQAIQEASRLKAEAE-MLQKQKELAQ--EQARKFQEDKEQI 2955
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAgIEAKINELEEekEDKALEIKKQEWK 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2956 EQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQvLEMSRAQAKAEEDASKFKKKAEEI-------------------- 3015
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-LAEAEAQARASEERVRGGRAVEEVlkasiqgvhgtvaqlgsvge 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3016 ----------GNKLH----QTELATKE-------------------RMA------------------------------- 3031
Cdd:TIGR02169 536 ryataievaaGNRLNnvvvEDDAVAKEaiellkrrkagratflplnKMRderrdlsilsedgvigfavdlvefdpkyepa 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3032 ---------VVQTLEIQRQQSGK------------------------------------EAEELRRAIAELEHEKEKLKR 3066
Cdd:TIGR02169 616 fkyvfgdtlVVEDIEAARRLMGKyrmvtlegelfeksgamtggsraprggilfsrsepaELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3067 EAELLQKN----SQKMQVAQQE--QLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENlYEDEVRKAQKLKQEQEHQM 3140
Cdd:TIGR02169 696 ELRRIENRldelSQELSDASRKigEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIEN-VKSELKELEARIEELEEDL 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3141 KHLEEEKDQLkvsmddamkKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLRE---KLEQMEEEHRIALAQTREM 3217
Cdd:TIGR02169 775 HKLEEALNDL---------EARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRltlEKEYLEKEIQELQEQRIDL 845
|
....*...
gi 1835643837 3218 RTQTDDLA 3225
Cdd:TIGR02169 846 KEQIKSIE 853
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1970-2192 |
2.95e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 66.37 E-value: 2.95e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1970 QLAKQTQLAEAHAKAKAQAEKEAEELQRRmqeevskrevvaVDAEQQKQtiqQELQQLRQNSDMEIKSKAKQIEEVEYNR 2049
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQK------------QAAEQERL---KQLEKERLAAQEQKKQAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2050 RKIEEEihivrlQLETMQKHKANAEDELQELRARAEKAEQQKKaaqeeaerlrKQVKDETQKKREAEEELKRKVQAEKEA 2129
Cdd:PRK09510 132 KQAEEA------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAK----------KKAEAEAAKKAAAEAKKKAEAEAAAKA 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2130 AREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTA 2192
Cdd:PRK09510 196 AAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2688-2894 |
3.31e-10 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 66.90 E-value: 3.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAAEDADFARTRAEQeaalSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAhaEQAALKQKQLADE 2767
Cdd:pfam15709 326 EKREQEKASRDRLRAER----AEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRF--EEIRLRKQRLEEE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2768 EMDKhkkfAEKTLRQKSQVEQELTKVKLQLEEtdHQKTLLDEELQRLKEEVTDAMRQKAQVEEElfkvKIQMEELIKLKL 2847
Cdd:pfam15709 400 RQRQ----EEEERKQRLQLQAAQERARQQQEE--FRRKLQELQRKKQQEEAERAEAEKQRQKEL----EMQLAEEQKRLM 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2848 RIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIE-----AQEAAR 2894
Cdd:pfam15709 470 EMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4002-4040 |
3.52e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 3.52e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 4002 LLEAQAATGFITDAVKNQKLYVNEAVKAGVVGPELHEKL 4040
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2617-2837 |
4.55e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 66.05 E-value: 4.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2617 KAKAEEAKRQKELAEKEAERQIQLAQEAALKkidaeekahtaivQQKEQEMLQtrKQEQSILDKLKEEAERAKRAAE--- 2693
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQANR-------------EAEEAELEQ--EREIETARIAEAEAELAKKKAEerr 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2694 DADFARTRAEQEAALSRQQVE-EAERLKQRAEEEAQAKAQaqdEAEKLRKEAELEAAKRAHAEqaALKQKQLADEEmdkh 2772
Cdd:COG2268 256 EAETARAEAEAAYEIAEANAErEVQRQLEIAEREREIELQ---EKEAEREEAELEADVRKPAE--AEKQAAEAEAE---- 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2773 kkfAE-KTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEevtdAMRQKAQVEEELFKVKI 2837
Cdd:COG2268 327 ---AEaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE----IAEAAAKPLEKIDKITI 385
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
643-750 |
5.65e-10 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 60.29 E-value: 5.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 643 EDERDRVQ--KKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLP----REKGRMRFHKLQNVQIALDYL 716
Cdd:cd21222 8 DEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 1835643837 717 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 750
Cdd:cd21222 88 EDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1724-2154 |
6.37e-10 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 66.62 E-value: 6.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1724 SKELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRSHSERDVDLDRYREKVQQLLERWQailvQIDLRQRE 1803
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIA----QLSKELTE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1804 LDQLGRQLRYYRETYEWLIKWIKDAKQRQEQiqsvpitdsktmkehllQEKKLLDEIESNRDKVDECQKyakqyidaikd 1883
Cdd:TIGR02168 759 LEAEIEELEERLEEAEEELAEAEAEIEELEA-----------------QIEQLKEELKALREALDELRA----------- 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1884 yELQLVTYKAQvepvaspakkpKVQSTSDSIIQEYVDLRTRyselttltsqyIKFITETLRRLNDEEKAAEKLKEEERRR 1963
Cdd:TIGR02168 811 -ELTLLNEEAA-----------NLRERLESLERRIAATERR-----------LEDLEEQIEELSEDIESLAAEIEELEEL 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1964 LAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEevskrevvavdAEQQKQTIQQELQQLRQnsdmeikskakqiE 2043
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRE-----------LESKRSELRRELEELRE-------------K 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2044 EVEYNRRKIEEEIHIVRLQletmQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELkrkv 2123
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQ----ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEY---- 995
|
410 420 430
....*....|....*....|....*....|.
gi 1835643837 2124 QAEKEAAREKQRAVEDLEKFRSQAEEAERRM 2154
Cdd:TIGR02168 996 EELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1954-2483 |
6.82e-10 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 66.30 E-value: 6.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1954 EKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDM 2033
Cdd:pfam05557 64 EAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2034 EiKSKAKQIEEveynrrkieeeihiVRLQLETMQKHKANAEDELQELRARAEKAEQQK---KAAQEEAERLRKQVKdETQ 2110
Cdd:pfam05557 144 L-KAKASEAEQ--------------LRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSeivKNSKSELARIPELEK-ELE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2111 KKREAEE---ELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQE--------VAQQSAAAE 2179
Cdd:pfam05557 208 RLREHNKhlnENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDtglnlrspEDLSRRIEQ 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2180 LNSKRMSFAEKTAQLELSLKQEHITVTHLQEE-AERLKKLHDeaekareeaekelEKWHQKANEALRLRLQaeevaHKKT 2258
Cdd:pfam05557 288 LQQREIVLKEENSSLTSSARQLEKARRELEQElAQYLKKIED-------------LNKKLKRHKALVRRLQ-----RRVL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2259 LAQEEAEKQKEDAEREARKRAKTEESA--LRQKELAEDELEKQRKLADATAQQKFSAEQELIRLK-----AETENSEQQR 2331
Cdd:pfam05557 350 LLTKERDGYRAILESYDKELTMSNYSPqlLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKqqaqtLERELQALRQ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2332 LLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSK--QMLEVEASKLRE-LAEEAAKL 2408
Cdd:pfam05557 430 QESLADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlHLSMNPAAEAYQqRKNQLEKL 509
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2409 RavseeakrqrqiAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIA--LKEKEAENERLRRLaeDEAYQRKLLE 2483
Cdd:pfam05557 510 Q------------AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLdlRKELESAELKNQRL--KEVFQAKIQE 572
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
651-747 |
6.93e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 59.89 E-value: 6.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 651 KKTFTKWVN---------KHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMR-----FHKLQNVQIALDYL 716
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1835643837 717 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 747
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1978-2192 |
7.51e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.85 E-value: 7.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1978 AEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEynrRKIEEEIH 2057
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAE---AEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2058 IVRLQLETMQKHKANA-----------------------------EDELQELRARAEKAEQQKKAAQEEAERLRKQVKDE 2108
Cdd:COG3883 87 ELGERARALYRSGGSVsyldvllgsesfsdfldrlsalskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2109 TQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFA 2188
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
....
gi 1835643837 2189 EKTA 2192
Cdd:COG3883 247 AGAG 250
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2567-3184 |
8.01e-10 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 65.92 E-value: 8.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2567 AEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAAlEEVERLKakaEEAKRQKELAEKEAERQIQLAQEAAL 2646
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLD-RESDRNQ---ELQKRIRLLEKREAEAEEALREQAEL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2647 KKIdaeEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAE-- 2724
Cdd:pfam05557 78 NRL---KKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEql 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2725 -EEAQAKAQAQDEAEKLRKEAELEAAKRAH--AEQAALKQKQLADEEMDKHKKfaektlRQKSQVEQeltkvklqLEETD 2801
Cdd:pfam05557 155 rQNLEKQQSSLAEAEQRIKELEFEIQSQEQdsEIVKNSKSELARIPELEKELE------RLREHNKH--------LNENI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2802 HQKTLLDEELQRLK---EEVTDAMRQKAQVEEELFKVKIQMEELIKLklrieEENKMLIMKDKDSTQKLLVEEAEKMRQV 2878
Cdd:pfam05557 221 ENKLLLKEEVEDLKrklEREEKYREEAATLELEKEKLEQELQSWVKL-----AQDTGLNLRSPEDLSRRIEQLQQREIVL 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2879 AEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKmqaiqeaSRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQ 2958
Cdd:pfam05557 296 KEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKL-------KRHKALVRRLQRRVLLLTKERDGYRAILESYDKE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2959 LAKETEGFQKSLEAERRQQLeitaeAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIgnklhQTELATKERmavvQTLEI 3038
Cdd:pfam05557 369 LTMSNYSPQLLERIEEAEDM-----TQKMQAHNEEMEAQLSVAEEELGGYKQQAQTL-----ERELQALRQ----QESLA 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3039 QRQQSGKEAEELRRAIAELEHEKEKLKReaellQKNSQKMQVAQQEqLRQETQVLQTTFLSEKQ---LLLEREKYIEEEK 3115
Cdd:pfam05557 435 DPSYSKEEVDSLRRKLETLELERQRLRE-----QKNELEMELERRC-LQGDYDPKKTKVLHLSMnpaAEAYQQRKNQLEK 508
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 3116 AKLENlyEDEVRKAQKLKQEQEhQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQldKKRQE 3184
Cdd:pfam05557 509 LQAEI--ERLKRLLKKLEDDLE-QVLRLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQ--AKIQE 572
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2636-3089 |
8.17e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 8.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2636 RQIQLAQEAALKKIDAEEKAHTAIVQQKEQEmLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEE 2715
Cdd:COG4717 66 PELNLKELKELEEELKEAEEKEEEYAELQEE-LEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2716 AERLKQrAEEEAQAKAQAQDEAEKLRKEAEleaAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKL 2795
Cdd:COG4717 145 PERLEE-LEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2796 QLEETDHQKTLLDEELQRLK-EEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLI------MKDKDSTQKLL 2868
Cdd:COG4717 221 ELEELEEELEQLENELEAAAlEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllallFLLLAREKASL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2869 VEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKF 2948
Cdd:COG4717 301 GKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2949 QEDKEQIEQQLAKETEgfQKSLEAERRQ---QLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIgNKLHQTELA 3025
Cdd:COG4717 381 VEDEEELRAALEQAEE--YQELKEELEEleeQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL-EELREELAE 457
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 3026 TKERMAVV---QTLEIQRQqsgkEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQE 3089
Cdd:COG4717 458 LEAELEQLeedGELAELLQ----ELEELKAELRELAEEWAALKLALELLEEAREEYREERLPPVLER 520
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1747-2301 |
1.04e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 65.90 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1747 LFNTLEADLNKAKDVNEQMLRSHSERDVDLDRYREKVQQLLERWQAilvQIDLRQRELDQLGRQLRYYRETYEWLIKWIK 1826
Cdd:pfam05483 188 LNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1827 DAKQRQEQIQSVPITDSKTMKEHLLQEKKLLDEIESNRDKVDECQKYAKQYidaikDYELQLVT---YKAQVEPVASPAK 1903
Cdd:pfam05483 265 ESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKAL-----EEDLQIATktiCQLTEEKEAQMEE 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1904 KPKVQSTSDSIIQEYVD--------LRTRYSELTTLTSQyIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQT 1975
Cdd:pfam05483 340 LNKAKAAHSFVVTEFEAttcsleelLRTEQQRLEKNEDQ-LKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1976 QLAEAhakaKAQAEKEAEELQRRMQEEV---SKREVVAVDAEQQKQTIQ-QELQQLRQNSDMEIKSKAKQIEEVEYN--- 2048
Cdd:pfam05483 419 KLLDE----KKQFEKIAEELKGKEQELIfllQAREKEIHDLEIQLTAIKtSEEHYLKEVEDLKTELEKEKLKNIELTahc 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2049 ------RRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVK---DETQKKREAEEEL 2119
Cdd:pfam05483 495 dkllleNKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgDEVKCKLDKSEEN 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2120 KRKVQAEKEAAREK-----------QRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKvAQEVAQQSAAAELNSKRMSFA 2188
Cdd:pfam05483 575 ARSIEYEVLKKEKQmkilenkcnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLN-AYEIKVNKLELELASAKQKFE 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2189 EKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKeleKWHQKANEALRLrLQAEEVAHKKTLAQEEAE--- 2265
Cdd:pfam05483 654 EIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDK---RCQHKIAEMVAL-MEKHKHQYDKIIEERDSElgl 729
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1835643837 2266 -KQKEDAEREARKRAKTEESALRQKELA---EDELEKQRK 2301
Cdd:pfam05483 730 yKNKEQEQSSAKAALEIELSNIKAELLSlkkQLEIEKEEK 769
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1963-2136 |
1.17e-09 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 62.63 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1963 RLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQELQQLRQNsdmeIKSKAKQI 2042
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEAR----IKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2043 EEVEYNRrkieeEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRK 2122
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....
gi 1835643837 2123 vQAEKEAAREKQRA 2136
Cdd:COG1579 158 -LEELEAEREELAA 170
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
5000-5038 |
1.22e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 56.57 E-value: 1.22e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 5000 FLEVQYLTGGLIEPDLPNRVNLDEALRKGIIDARTAQKL 5038
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1945-2140 |
1.44e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1945 RLNDEEKaaEKLKEEERRRLAEVEAQLA--KQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKrevvavdAEQQKQTIQQ 2022
Cdd:PRK09510 102 RLKQLEK--ERLAAQEQKKQAEEAAKQAalKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-------AAAEAKKKAE 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2023 ELQQLRQnsdmEIKSKAKQIEEVeynRRKIEEEihivrlqletmQKHKANAEDELQELRARAEKAEQQKKAAQEEAerlr 2102
Cdd:PRK09510 173 AEAAKKA----AAEAKKKAEAEA---AAKAAAE-----------AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA---- 230
|
170 180 190
....*....|....*....|....*....|....*...
gi 1835643837 2103 kqvkdETQKKREAEEELKRKvQAEKEAAREKQRAVEDL 2140
Cdd:PRK09510 231 -----AAEAKAAAEKAAAAK-AAEKAAAAKAAAEVDDL 262
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2348-2721 |
1.47e-09 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 65.03 E-value: 1.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2348 AIQKRKEMEEELAKVRAEMEILLQSKSR---AEEESRSNTEKSKQMLEvEASKLRELAEEAAKlrAVSEEAKR------- 2417
Cdd:NF033838 95 DIKTEYLYELNVLKEKSEAELTSKTKKEldaAFEQFKKDTLEPGKKVA-EATKKVEEAEKKAK--DQKEEDRRnyptnty 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2418 ---QRQIAEDEAARQRAEAErILKEKLAAINDATRLKtEAEIALKEKEAENERLRRLAEDeayqRKLLEEQAtQHKQDIE 2494
Cdd:NF033838 172 ktlELEIAESDVEVKKAELE-LVKEEAKEPRDEEKIK-QAKAKVESKKAEATRLEKIKTD----REKAEEEA-KRRADAK 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2495 EKIILLKKSSDNELERQKNIVedtlRQRRIIEEEIRILKVNFEKA---SVGKSDL-ELELNQLKNIAEeTQRSKEKAEQE 2570
Cdd:NF033838 245 LKEAVEKNVATSEQDKPKRRA----KRGVLGEPATPDKKENDAKSsdsSVGEETLpSPSLKPEKKVAE-AEKKVEEAKKK 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2571 AEKQRqlaleEEQRR---------------------KEAEEKVRKILADEKEAARQRKAALEEVERLKAKA---EEAKRQ 2626
Cdd:NF033838 320 AKDQK-----EEDRRnyptntyktleleiaesdvkvKEAELELVKEEAKEPRNEEKIKQAKAKVESKKAEAtrlEKIKTD 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2627 KELAEKEAERQIqlAQEAALKKIDAEEKAhTAIVQQKEQEMLQTRKQEQSildklkEEAERAKRAAEDADFARTRAEQEA 2706
Cdd:NF033838 395 RKKAEEEAKRKA--AEEDKVKEKPAEQPQ-PAPAPQPEKPAPKPEKPAEQ------PKAEKPADQQAEEDYARRSEEEYN 465
|
410
....*....|....*
gi 1835643837 2707 ALSRQQVEEAERLKQ 2721
Cdd:NF033838 466 RLTQQQPPKTEKPAQ 480
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2396-2935 |
1.50e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.45 E-value: 1.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2396 SKLRELAEEAAKLRAVSEEAKRQRQIAED--EAARQRAEAERILKEklaAINDATRLKTEAEialKEKEAENERLRRLAE 2473
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEvlEEHEERREELETLEA---EIEDLRETIAETE---REREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2474 deayQRKLLEEQATQhkqdieekiiLLKKSSDNELERqknivedtlrqrriieeeirilkvnfEKASVGKSDLELELNQL 2553
Cdd:PRK02224 287 ----RLEELEEERDD----------LLAEAGLDDADA--------------------------EAVEARREELEDRDEEL 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2554 KNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKI---LADEKEAARQRKAALEEVERLKAKAEEA------- 2623
Cdd:PRK02224 327 RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELeseLEEAREAVEDRREEIEELEEEIEELRERfgdapvd 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2624 -----KRQKELAEKEAERQIQLAQ-EAALKKI-DAEEKAHTAIVQQKEQEMLQTRKqEQSILDKLKE-EAERAKRAAEDA 2695
Cdd:PRK02224 407 lgnaeDFLEELREERDELREREAElEATLRTArERVEEAEALLEAGKCPECGQPVE-GSPHVETIEEdRERVEELEAELE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2696 DFARTRAEQEAALSR-----QQVEEAERLKQRAE------EEAQAKAQAQDE-AEKLRKEA-ELEAAKRAHAEQAAlKQK 2762
Cdd:PRK02224 486 DLEEEVEEVEERLERaedlvEAEDRIERLEERREdleeliAERRETIEEKRErAEELRERAaELEAEAEEKREAAA-EAE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2763 QLADEEMDKHKKFAEKTLRQKSQVEQeLTKVKLQLEETDHqktlLDEELQRLKEEVTDAMRQKAQVEEELfkvKIQMEEL 2842
Cdd:PRK02224 565 EEAEEAREEVAELNSKLAELKERIES-LERIRTLLAAIAD----AEDEIERLREKREALAELNDERRERL---AEKRERK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2843 IKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLsieaQEAARMrklAEDDLANQRALAEKM--LKEKMQA 2920
Cdd:PRK02224 637 RELEAEFDEARIEEAREDKERAEEYLEQVEEKLDELREERDDL----QAEIGA---VENELEELEELRERReaLENRVEA 709
|
570
....*....|....*
gi 1835643837 2921 IQEasrLKAEAEMLQ 2935
Cdd:PRK02224 710 LEA---LYDEAEELE 721
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
3002-3225 |
1.52e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.46 E-value: 1.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3002 EEDA--SKFKKKAEEIGNKLHQT-------ELATKERMAVVQTLEIQRQQsgkeAEELRraiaELEHEKEKLKREAELLQ 3072
Cdd:TIGR02168 162 EEAAgiSKYKERRKETERKLERTrenldrlEDILNELERQLKSLERQAEK----AERYK----ELKAELRELELALLVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3073 KNSQKmqvAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLyEDEVRKAQKLKQEQEHQMKHLEEEKDQLKV 3152
Cdd:TIGR02168 234 LEELR---EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSEL-EEEIEELQKELYALANEISRLEQQKQILRE 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3153 SMDDAMKKQKEAE---ENVRRKQDELQ----QLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDLA 3225
Cdd:TIGR02168 310 RLANLERQLEELEaqlEELESKLDELAeelaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2402-2775 |
1.54e-09 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 64.50 E-value: 1.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2402 AEEAAKLRAVSEEAKRQRQIAEDEAARQraEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEayQRKL 2481
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQ--VTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERR--QKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2482 LEEQATQHKQD---IEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRilkvnfEKASVGKSDLELELNQLKNIAE 2558
Cdd:pfam02029 80 QEALERQKEFDptiADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE------ETEIREKEYQENKWSTEVRQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2559 ETQRSKEKAEQEAEKQRQLALEEEQ-----RRKEAEEKVR-KILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEK 2632
Cdd:pfam02029 154 EEGEEEEDKSEEAEEVPTENFAKEEvkdekIKKEKKVKYEsKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2633 EAERQIQLAQEAALKKIDAEEKAHtaivQQKEQEMLQTRKQEQsildklkeeaerAKRAAEDADFARTRAEQeaalsRQQ 2712
Cdd:pfam02029 234 QEREEEAEVFLEAEQKLEELRRRR----QEKESEEFEKLRQKQ------------QEAELELEELKKKREER-----RKL 292
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2713 VEEAERlkQRAEEEAQAKAQAQDEAEKLRKEAEleaakRAHAEQAALKQKQLADEEMDKHKKF 2775
Cdd:pfam02029 293 LEEEEQ--RRKQEEAERKLREEEEKRRMKEEIE-----RRRAEAAEKRQKLPEDSSSEGKKPF 348
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1967-2193 |
1.63e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.71 E-value: 1.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1967 VEAQLAKQTQLAEAHAKAKAQAEKEAeelqRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQnsDMEIKSKAKQIEEve 2046
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAA----KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ--RAAAEKAAKQAEQ-- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2047 ynRRKIEEEihivrlqletmqKHKANAEdelqelrARAEKAEQQKKAAQEEAERlrkQVKDETQKKREAEEELKRKVQAE 2126
Cdd:TIGR02794 110 --AAKQAEE------------KQKQAEE-------AKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEAKAKAAAEAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2127 KEAAREKQRAVEDLEKfrsqAEEAERRMKQ--AEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ 2193
Cdd:TIGR02794 166 KKAEEAKKKAEAEAKA----KAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKAD 230
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2536-3186 |
1.65e-09 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 65.21 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2536 FEKASVGKSDLELELNQLKNIA---EETQRSKEKAEQ--EAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAAl 2610
Cdd:PRK10246 190 FEQHKSARTELEKLQAQASGVAlltPEQVQSLTASLQvlTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQ- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2611 eeverlkAKAEEAKRQKELAekeaerQIQLAQEAAlkkidaEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKR 2690
Cdd:PRK10246 269 -------ALAAEEKAQPQLA------ALSLAQPAR------QLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRAR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2691 AAEDAdfARTRAEQEAALSR--QQVEEAER--------------LKQRAEEEAQAKAQAQDEAEKLRKEA---------- 2744
Cdd:PRK10246 330 IRHHA--AKQSAELQAQQQSlnTWLAEHDRfrqwnnelagwraqFSQQTSDREQLRQWQQQLTHAEQKLNalpaitltlt 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2745 --ELEAAKRAHAEQAALKQKQLAdeemdKHKKFAEKTLRQK------SQVEQELTKVKLQLEETDHQKTLLDEELQRLK- 2815
Cdd:PRK10246 408 adEVAAALAQHAEQRPLRQRLVA-----LHGQIVPQQKRLAqlqvaiQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKt 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2816 -----EEVTDAMRQKAQVEE---------------------ELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLV 2869
Cdd:PRK10246 483 iceqeARIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQR 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2870 EEAEKMRQVAEEAArLSIEAQE---AARMRKLAEDDLANQraLAEKMLKEKmQAIQEASRLkaeaeMLQKQKELAQEQAR 2946
Cdd:PRK10246 563 DESEAQSLRQEEQA-LTQQWQAvcaSLNITLQPQDDIQPW--LDAQEEHER-QLRLLSQRH-----ELQGQIAAHNQQII 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2947 KFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAErlklqvlEMSRAQAkaeedaskfkkkaeeignklHQTELAT 3026
Cdd:PRK10246 634 QYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQ-------EAQSWQQ--------------------RQNELTA 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3027 -KERMAVVQTLEIQRQQSGKEAEELRRAIAE--LEHEKEKLKREAE---LLQKNSQKMQVAQQEQLRQETQVLQTTFLSE 3100
Cdd:PRK10246 687 lQNRIQQLTPLLETLPQSDDLPHSEETVALDnwRQVHEQCLSLHSQlqtLQQQDVLEAQRLQKAQAQFDTALQASVFDDQ 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3101 KQL---LLEREKY--IEEEKAKLENLYEDE----VRKAQKLKQEQEHQ---------MKHLEEEKDQLKVSMDDAMKKQ- 3161
Cdd:PRK10246 767 QAFlaaLLDEETLtqLEQLKQNLENQRQQAqtlvTQTAQALAQHQQHRpdgldltvtVEQIQQELAQLAQQLRENTTRQg 846
|
730 740 750
....*....|....*....|....*....|.
gi 1835643837 3162 ------KEAEENVRRKQDELQQLDKKRQEQE 3186
Cdd:PRK10246 847 eirqqlKQDADNRQQQQALMQQIAQATQQVE 877
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4579-4617 |
1.66e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 56.18 E-value: 1.66e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 4579 LLEAQAATGYVIDPIKCLKLAVEDAVRMGIVGSEFKDKL 4617
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2653-2798 |
1.68e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 63.71 E-value: 1.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2653 EKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAK--RAAEDADFARTR-----------AEQEAALSRQQVEEAERL 2719
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEkqRAAEQARQKELEqraaaekaakqAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2720 KQRAEEEAQAKAQAQDE---AEKLRKEAELEAAKRAHAE--QAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVK 2794
Cdd:TIGR02794 125 KAKQAAEAKAKAEAEAErkaKEEAAKQAEEEAKAKAAAEakKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAK 204
|
....
gi 1835643837 2795 LQLE 2798
Cdd:TIGR02794 205 AAAE 208
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2539-2765 |
1.83e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 1.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2539 ASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKA 2618
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2619 KAEEakRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAED--AD 2696
Cdd:COG4942 98 ELEA--QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAerAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2697 FARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLA 2765
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2468-2944 |
2.23e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.40 E-value: 2.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2468 LRRLAEDEAyQRKLLEEQATQHKQDIEEKiillkkssdNELERQKNIVEDTLRQRRIIEEEIRILKVNFEkASVGKSDLE 2547
Cdd:COG4717 70 LKELKELEE-ELKEAEEKEEEYAELQEEL---------EELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2548 LELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQK 2627
Cdd:COG4717 139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2628 ELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAA 2707
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2708 LSRQQVEEAERLKQRAEEEAQakaQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQksQVE 2787
Cdd:COG4717 299 SLGKEAEELQALPALEELEEE---ELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQ--EIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2788 QELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAmrqKAQVEEELFKVKIQMEELIKLKLRIEEENkmlimkdkdsTQKL 2867
Cdd:COG4717 374 ALLAEAGVEDEEELRAALEQAEEYQELKEELEEL---EEQLEELLGELEELLEALDEEELEEELEE----------LEEE 440
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2868 LVEEAEKMRQVAEEAARLSieaqeaARMRKLAEDDLANQRALAEKMLKEKMQ-AIQEASRLKAEAEMLQKQKELAQEQ 2944
Cdd:COG4717 441 LEELEEELEELREELAELE------AELEQLEEDGELAELLQELEELKAELReLAEEWAALKLALELLEEAREEYREE 512
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2752-2989 |
2.37e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 2.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2752 AHAEQAALKQKQLAD--EEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVE 2829
Cdd:COG4942 17 AQADAAAEAEAELEQlqQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2830 EELFKVKIQMEELIKLKLRIEEENK-MLIMKDKDSTQklLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRA 2908
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLD--AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2909 LAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLK 2988
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 1835643837 2989 L 2989
Cdd:COG4942 255 L 255
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2666-3187 |
2.68e-09 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 63.89 E-value: 2.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2666 EMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAE-EEAQAKaqaQD-EAEKLRKE 2743
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQtEEAQAK---QDsELAKLRVE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2744 ---------------AELEAAKRAHAeqAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLD 2808
Cdd:pfam05701 109 emeqgiadeasvaakAQLEVAKARHA--AAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2809 EELQRLKEEVTDAMRQKAQVEEELFKVKIQMEElikLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIE 2888
Cdd:pfam05701 187 IELIATKESLESAHAAHLEAEEHRIGAALAREQ---DKLNWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2889 AQEAARMrklaeDDLANQRALAEKMLKEKMQAIQEA-SRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKEtegfq 2967
Cdd:pfam05701 264 AELAAYM-----ESKLKEEADGEGNEKKTSTSIQAAlASAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKE----- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2968 KSLEAERRQQ-----LEITAEAERLKLQVLEMSRAQAKAEEDaskfKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQ 3042
Cdd:pfam05701 334 KAELASLRQRegmasIAVSSLEAELNRTKSEIALVQAKEKEA----REKMVELPKQLQQAAQEAEEAKSLAQAAREELRK 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3043 SGKEAEELRRAIAELEHEKEKLKREAElLQKNSQKMQVAQQEQLrQETQV---LQTTFLSEKQLLLEREKYIE------- 3112
Cdd:pfam05701 410 AKEEAEQAKAAASTVESRLEAVLKEIE-AAKASEKLALAAIKAL-QESESsaeSTNQEDSPRGVTLSLEEYYElskrahe 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3113 -EEKA---------KLENLYEDEVRKAQKLKQeqehqmkhLEEEKDQLKVSMDDAMKKQKEAEENvrrKQDELQQLDKKR 3182
Cdd:pfam05701 488 aEELAnkrvaeavsQIEEAKESELRSLEKLEE--------VNREMEERKEALKIALEKAEKAKEG---KLAAEQELRKWR 556
|
....*
gi 1835643837 3183 QEQEK 3187
Cdd:pfam05701 557 AEHEQ 561
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1958-2586 |
2.70e-09 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 64.39 E-value: 2.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1958 EEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQnsdmEIKS 2037
Cdd:pfam07111 79 EEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQRELEEIQRLHQ----EQLS 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2038 KAKQIEEveynrrkieeeihivrLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKdETQKKREAEE 2117
Cdd:pfam07111 155 SLTQAHE----------------EALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLS-KTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2118 ELkrkvqaekeaarekqraVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELS 2197
Cdd:pfam07111 218 TL-----------------VESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLA 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2198 LKQEHITvthlqeeaERLKKLHDEAEKAREEAEKELEKWHQKANeALRLRLQAEEVAHKKTLAQEEAEKqkedAEREARK 2277
Cdd:pfam07111 281 LQEEELT--------RKIQPSDSLEPEFPKKCRSLLNRWREKVF-ALMVQLKAQDLEHRDSVKQLRGQV----AELQEQV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2278 RAKTEESALRQKEL----AEDELEK------QRKLADAT------AQQKFSAEQELIRL-------KAETENSEQQRLLL 2334
Cdd:pfam07111 348 TSQSQEQAILQRALqdkaAEVEVERmsakglQMELSRAQearrrqQQQTASAEEQLKFVvnamsstQIWLETTMTRVEQA 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2335 EEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEE 2414
Cdd:pfam07111 428 VARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQQE 507
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2415 AKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAEnerlrrlAEDEAYQRKLLEEQATQHKQDIE 2494
Cdd:pfam07111 508 VGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQES-------TEEAASLRQELTQQQEIYGQALQ 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2495 EKIILLKKSSDNELERQKNIVEDTLRQRRiieeeirilkvnfeKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQ 2574
Cdd:pfam07111 581 EKVAEVETRLREQLSDTKRRLNEARREQA--------------KAVVSLRQIQHRATQEKERNQELRRLQDEARKEEGQR 646
|
650
....*....|..
gi 1835643837 2575 RQLALEEEQRRK 2586
Cdd:pfam07111 647 LARRVQELERDK 658
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1943-2174 |
3.74e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 62.63 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1943 LRRLNDEEKAAEKLKE--EERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTI 2020
Cdd:pfam13868 65 EERKEERKRYRQELEEqiEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2021 QQELQQLRQNSDME--IKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEA 2098
Cdd:pfam13868 145 LEKEEEREEDERILeyLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKER 224
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2099 ERLRK--QVKDETQKKREAEEELKRKVQAEkEAAREKQRAVEDLEKfrsQAEEAERRMKQAEVEKERQIKVAQEVAQQ 2174
Cdd:pfam13868 225 EEAEKkaRQRQELQQAREEQIELKERRLAE-EAEREEEEFERMLRK---QAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1978-2664 |
3.84e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.97 E-value: 3.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1978 AEAHAKAKAQAEKEAEELqrrmqeevsKREVVAVDAEqqkqtIQQELQQLRQNSDMeIKSKAKQIEEVEYNRRKI----E 2053
Cdd:pfam05483 73 SEGLSRLYSKLYKEAEKI---------KKWKVSIEAE-----LKQKENKLQENRKI-IEAQRKAIQELQFENEKVslklE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2054 EEIHIVR--LQLETMQKHKANAedeLQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKrkVQAEKEAAR 2131
Cdd:pfam05483 138 EEIQENKdlIKENNATRHLCNL---LKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELR--VQAENARLE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2132 EKQRAVEDLEKFRSQAEEAERRMKQAE----------VEKERQIKVAQEVAQQSaaaelNSKRMSFAEKTAQLELSLKQE 2201
Cdd:pfam05483 213 MHFKLKEDHEKIQHLEEEYKKEINDKEkqvsllliqiTEKENKMKDLTFLLEES-----RDKANQLEEKTKLQDENLKEL 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2202 HITVTHLQEEAERLKklhdEAEKAREEAEKELEKWHQKANEALRlrlqaeEVAHKKTLAQEEAEKQKEDAE---REARKR 2278
Cdd:pfam05483 288 IEKKDHLTKELEDIK----MSLQRSMSTQKALEEDLQIATKTIC------QLTEEKEAQMEELNKAKAAHSfvvTEFEAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2279 AKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETE---NSEQQRLLLEEELFRLKNEVNEAIQKRKEM 2355
Cdd:pfam05483 358 TCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEvelEELKKILAEDEKLLDEKKQFEKIAEELKGK 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2356 EEELA-------KVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAAR 2428
Cdd:pfam05483 438 EQELIfllqareKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKK 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2429 Q-------RAEAERILKEKLAAINDATRLKTEAEIALKE-KEAENERLRRLAEDEAYQRKLLEEQATQHKQD--IEEKII 2498
Cdd:pfam05483 518 HqediincKKQEERMLKQIENLEEKEMNLRDELESVREEfIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMkiLENKCN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2499 LLKKSSDNeleRQKNIVE-DTLRQRRIIEEEIRILKVNFEKASVGKSDLELE---------LNQLKNIAEETQRSKEKAE 2568
Cdd:pfam05483 598 NLKKQIEN---KNKNIEElHQENKALKKKGSAENKQLNAYEIKVNKLELELAsakqkfeeiIDNYQKEIEDKKISEEKLL 674
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2569 QEAEKQRQLALEEEQRRKEAEEKVRKILAD-----------------------------EKEAARQRKAALEEVERLKAK 2619
Cdd:pfam05483 675 EEVEKAKAIADEAVKLQKEIDKRCQHKIAEmvalmekhkhqydkiieerdselglyknkEQEQSSAKAALEIELSNIKAE 754
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1835643837 2620 AEEAKRQKELAEKEAErqiqlaqeaalkKIDAEEKAHTAIVQQKE 2664
Cdd:pfam05483 755 LLSLKKQLEIEKEEKE------------KLKMEAKENTAILKDKK 787
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2565-2815 |
4.05e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 63.81 E-value: 4.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2565 EKAEQEAEKQRQLALEEEQRRKEAeekvRKiladekeaARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEA 2644
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEAKARFEA----RQ--------ARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2645 ALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAE-QEAALSRQQVEEAERLKQRA 2723
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKkAAQQAANAEAEEEVDPKKAA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2724 EEEAQAKAQA--------------QDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTL-RQKSQVEQ 2788
Cdd:PRK05035 582 VAAAIARAKAkkaaqqaasaepeeQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIaRAKARKAA 661
|
250 260
....*....|....*....|....*..
gi 1835643837 2789 ELTKVKLQLEETDHQKTLLDEELQRLK 2815
Cdd:PRK05035 662 QQQANAEPEEAEDPKKAAVAAAIARAK 688
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1124-1313 |
4.08e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.54 E-value: 4.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1124 LRYLQELLLWVEENQRRINGAEWGVDLPSVESHLGSHRGLHQSIDEFRSKIERARADESQL---SPGSRGSYRDCLGKLD 1200
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1201 LQYAKLLNSSKSRLRHLE---SLHAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMAAKKENYSGLMRELELKEKKIKEI 1277
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1835643837 1278 QISGDRLQREDHPGKQ-TVEAFQAALQTQWSWMLQLC 1313
Cdd:cd00176 166 NELAEELLEEGHPDADeEIEEKLEELNERWEELLELA 202
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
643-749 |
4.54e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 57.51 E-value: 4.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 643 EDERDrvqKKTFTKWVNKhlIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKG-----RMRFHKLQNVQIALDYLK 717
Cdd:cd21299 1 ETSRE---ERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1835643837 718 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 749
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2042-2323 |
4.57e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 62.17 E-value: 4.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2042 IEEVEYNRRKIEEEIHIVRLQLETMqkhKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDEtQKKREAEEELKR 2121
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE-KAAKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2122 KVQAEKEAAREKQRAvedlEKFRSQAEEAERRMKQAEvEKERQikvAQEVAQQSAAAELNSKRmsfAEKTAQLELSLKQE 2201
Cdd:TIGR02794 114 AEEKQKQAEEAKAKQ----AAEAKAKAEAEAERKAKE-EAAKQ---AEEEAKAKAAAEAKKKA---EEAKKKAEAEAKAK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2202 hitvthlqEEAERlkklhdeaekareeaekelekwhqKAnealrlrlQAEEVAHKKtlaqeEAEKQKedAEREARKRAKT 2281
Cdd:TIGR02794 183 --------AEAEA------------------------KA--------KAEEAKAKA-----EAAKAK--AAAEAAAKAEA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1835643837 2282 EESALrqkelaeDELEKQRKLADATAQQKFSAEQELIRLKAE 2323
Cdd:TIGR02794 216 EAAAA-------AAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2608-2778 |
5.70e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.13 E-value: 5.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2608 AALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEaalkKIDAEekahtaivQQKEQEMLQTRKQEQSIldklKEEAER 2687
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAEELQQ----KQAAE--------QERLKQLEKERLAAQEQ----KKQAEE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAAEDAdfartraEQEAALSRQQVEEAERLKQRAEEE--AQAKAQAQDEAEKLRK-EAELEAAKRAHAEQAALKQKQL 2764
Cdd:PRK09510 123 AAKQAALK-------QKQAEEAAAKAAAAAKAKAEAEAKraAAAAKKAAAEAKKKAEaEAAKKAAAEAKKKAEAEAAAKA 195
|
170
....*....|....
gi 1835643837 2765 ADEEMDKHKKFAEK 2778
Cdd:PRK09510 196 AAEAKKKAEAEAKK 209
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2664-2943 |
5.72e-09 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 62.69 E-value: 5.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2664 EQEMLQTRKQEQSilDKLKEEAER---AKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQA----QDE 2736
Cdd:PRK07735 3 PEKDLEDLKKEAA--RRAKEEARKrlvAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAAlakqKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2737 AEKLRKEAELEAAKRAHAEQAALKQKQLADEEmdkhkkfaEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEElqrlKE 2816
Cdd:PRK07735 81 GTEEVTEEEKAKAKAKAAAAAKAKAAALAKQK--------REGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQK----RE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2817 EVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKllVEEAEKMRQVAEEAARLSIEA-QEAARM 2895
Cdd:PRK07735 149 GTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEE--EKAKAKAKAAAAAKAKAAALAkQKASQG 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1835643837 2896 RKLAEDDLANQRALAEKMLKEKmqaiqEASRLKAEAEMLQKQKELAQE 2943
Cdd:PRK07735 227 NGDSGDEDAKAKAIAAAKAKAA-----AAARAKTKGAEGKKEEEPKQE 269
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2077-2297 |
5.85e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.13 E-value: 5.85e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2077 LQELRARAEKAEQQ--KKAAQEEAERLRKQVKD-ETQKKREAEEELKRKVQAEKEAAREKQRAVEDlekfrsQAEEAerR 2153
Cdd:PRK09510 67 QQQQQKSAKRAEEQrkKKEQQQAEELQQKQAAEqERLKQLEKERLAAQEQKKQAEEAAKQAALKQK------QAEEA--A 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2154 MKQAEVEK---ERQIKVAQEVAQQsAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAErlkklhdeaekareeae 2230
Cdd:PRK09510 139 AKAAAAAKakaEAEAKRAAAAAKK-AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK----------------- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2231 kelekwhQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELE 2297
Cdd:PRK09510 201 -------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6178-6383 |
5.89e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.15 E-value: 5.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6178 LLQWLENVELRLSFSKPAwGQPETTKEKLSLHLELWKEMECKQHVYNSARDRLQRLLASCPLSRGSVSEHsLHVLEQKWE 6257
Cdd:cd00176 12 LEAWLSEKEELLSSTDYG-DDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER-LEELNQRWE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6258 SVYTKVQDRKECLTEGLSVTtEFHSSAQDLLKWISRTEDTLLTLPAASLvLETVTNQIQEHKVLLTEVNARGEKLAGLER 6337
Cdd:cd00176 90 ELRELAEERRQRLEEALDLQ-QFFRDADDLEQWLEEKEAALASEDLGKD-LESVEELLKKHKELEEELEAHEPRLKSLNE 167
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1835643837 6338 SACRLKDYSSKQDCAVIQNLVLTAQERLSKVQQCTVAKGRELEDSR 6383
Cdd:cd00176 168 LAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2470-2697 |
6.11e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.13 E-value: 6.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2470 RLAEDEAYQRKLLEEQATQHKQDIEEkiilLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKvnfekasvgksdleLE 2549
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEE----LQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAK--------------QA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2550 LNQLKNIAEETQRSKEKAEQEAEKQrQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRqkel 2629
Cdd:PRK09510 128 ALKQKQAEEAAAKAAAAAKAKAEAE-AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK---- 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2630 AEKEAERQiqlAQEAALKKIDAEEKAHTAIVQQKEQEmlqtrKQEQSILDKLKEEAERAKRAAEDADF 2697
Cdd:PRK09510 203 AEAEAKKK---AAAEAKKKAAAEAKAAAAKAAAEAKA-----AAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2776-3003 |
7.79e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 7.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2776 AEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELfkvKIQMEELIKLKLRIEEENKM 2855
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2856 LImKDKDSTQKLLVEeAEKMRQVAEEAARLSIE-AQEAARMRKLAEDDLANQRALAEKmLKEKMQAIQE-ASRLKAEAEM 2933
Cdd:COG4942 99 LE-AQKEELAELLRA-LYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEE-LRADLAELAAlRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2934 LQKQKELAQEQARKFQEDKEQIEQQLAKetegFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEE 3003
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLAR----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1927-2681 |
1.01e-08 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 62.46 E-value: 1.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1927 ELTTLTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEK-----EAEELQRRMQE 2001
Cdd:pfam07111 56 EGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEGlraalAGAEMVRKNLE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2002 EVSKREVvavdaeQQKQTIQQE-LQQLRQNSDMEIKSKAKQIEEVEYNrrkieeeihivrlqLETMQKHKANAEDELQEl 2080
Cdd:pfam07111 136 EGSQREL------EEIQRLHQEqLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQLAE- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2081 raraekaeqqkkaAQEEAERLRKQVKdETQKKREAEEELkrkvqaekeaarekqraVEDLEKFRSQAEEAERRMKQAEVE 2160
Cdd:pfam07111 195 -------------AQKEAELLRKQLS-KTQEELEAQVTL-----------------VESLRKYVGEQVPPEVHSQTWELE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2161 KERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITvthlqeeaERLKKLHDEAEKAREEAEKELEKWHQKA 2240
Cdd:pfam07111 244 RQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELT--------RKIQPSDSLEPEFPKKCRSLLNRWREKV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2241 NeALRLRLQAEEVAHKKTLAQEEAEKqkedAEREARKRAKTEESALRQKELaedelekqrkladataqQKFSAEQELIRL 2320
Cdd:pfam07111 316 F-ALMVQLKAQDLEHRDSVKQLRGQV----AELQEQVTSQSQEQAILQRAL-----------------QDKAAEVEVERM 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2321 KAETenseqqrllleeelfrLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSraeeesrsnteKSKQMLEVEASKLRE 2400
Cdd:pfam07111 374 SAKG----------------LQMELSRAQEARRRQQQQTASAEEQLKFVVNAMS-----------STQIWLETTMTRVEQ 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2401 LAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAEriLKEKLAAINDATRlKTEAEIALKEKEAENERLRRLAEDEAYQRK 2480
Cdd:pfam07111 427 AVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQ--LRQESCPPPPPAP-PVDADLSLELEQLREERNRLDAELQLSAHL 503
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2481 LLEEQATQHKQDIEEKIILLKKSSDNELERQKniVEDTLrqrriieeeirilkvnfekASVGKsdlelelnQLKNIAEET 2560
Cdd:pfam07111 504 IQQEVGRAREQGEAERQQLSEVAQQLEQELQR--AQESL-------------------ASVGQ--------QLEVARQGQ 554
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2561 QRSKEKAeqeAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQ---KELAEKEAERQ 2637
Cdd:pfam07111 555 QESTEEA---ASLRQELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQiqhRATQEKERNQE 631
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2638 IQLAQEAALK--------KIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKL 2681
Cdd:pfam07111 632 LRRLQDEARKeegqrlarRVQELERDKNLMLATLQQEGLLSRYKQQRLLAVL 683
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1656-2641 |
1.05e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 62.76 E-value: 1.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1656 KEQSSSSPLLRTEHEITHQKMDQVYSLSSIYLEKLKTINLVIRSTQGAEEVVRTYEDQLKEVHAVPSDSKELEATKAELK 1735
Cdd:TIGR00606 203 QEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQME 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1736 KLRSQVE--GHQPLFNTlEADLNKAKDVNEQMLRSHSERDVDLDRYREKV----QQLLERWQAILVQIDLRQRELDQLGR 1809
Cdd:TIGR00606 283 KDNSELElkMEKVFQGT-DEQLNDLYHNHQRTVREKERELVDCQRELEKLnkerRLLNQEKTELLVEQGRLQLQADRHQE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1810 QLRYYRetyewLIKWIKDAKQRQEQIQSVPITDSKTMKEHLLQEKKLLDE---IESNRDKVDECQKYAKQYIDAIKDYEL 1886
Cdd:TIGR00606 362 HIRARD-----SLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQEDEaktAAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1887 QLvtykaqvepvaspakKPKVQSTSDSIIQEYVDLRTRYSELTTLTSQyIKFITETLRRLNDEEKAAEKLKEEerrrlAE 1966
Cdd:TIGR00606 437 GL---------------GRTIELKKEILEKKQEELKFVIKELQQLEGS-SDRILELDQELRKAERELSKAEKN-----SL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1967 VEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVdaEQQKQTIQQELQQLRQNSDMEIKSKAKQIEeve 2046
Cdd:TIGR00606 496 TETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEML--TKDKMDKDEQIRKIKSRHSDELTSLLGYFP--- 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2047 yNRRKIEEEIHivrlqleTMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREA--EEELKRKVQ 2124
Cdd:TIGR00606 571 -NKKQLEDWLH-------SKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVcgSQDEESDLE 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2125 AEKEaarEKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQ-----QSAAAELNSKRMSFAEKTAQLELSLK 2199
Cdd:TIGR00606 643 RLKE---EIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQteaelQEFISDLQSKLRLAPDKLKSTESELK 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2200 QehitvthLQEEAERLkklhdeaekareeaekeLEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAErearKRA 2279
Cdd:TIGR00606 720 K-------KEKRRDEM-----------------LGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIE----EQE 771
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2280 KTEESALRQKELAEDelekqrKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEElfrlkneVNEAIQKRKEMEEEL 2359
Cdd:TIGR00606 772 TLLGTIMPEEESAKV------CLTDVTIMERFQMELKDVERKIAQQAAKLQGSDLDRT-------VQQVNQEKQEKQHEL 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2360 AKVRAEMEillqsksraeeESRSNTEKSKQMLEVEASKLRELAEEAAKLravSEEAKRQRQIAEdeaarQRAEAERILKE 2439
Cdd:TIGR00606 839 DTVVSKIE-----------LNRKLIQDQQEQIQHLKSKTNELKSEKLQI---GTNLQRRQQFEE-----QLVELSTEVQS 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2440 KLAAINDATRLKTEAEIALKEKEAENERL-------RRLAEDEAYQRKLLEEQATQHKQDIEEKII----LLKKSSDNEL 2508
Cdd:TIGR00606 900 LIREIKDAKEQDSPLETFLEKDQQEKEELissketsNKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgkdDYLKQKETEL 979
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2509 ERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEA 2588
Cdd:TIGR00606 980 NTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKL 1059
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2589 EEKVRKILADEKEAARQRKAALEEVERLKAKAEEaKRQKELAEKEAERQIQLA 2641
Cdd:TIGR00606 1060 EENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE-PQFRDAEEKYREMMIVMR 1111
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1551-2401 |
1.08e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 62.76 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1551 DDRMQIEReYNNCIQKYEQLLRTQEKGEQDEVTCKNYISQLKD----IRLQLEGCE-----SRTIHKiRTPMEKDPIKEC 1621
Cdd:TIGR00606 176 DEIFSATR-YIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEkaceIRDQITSKEaqlesSREIVK-SYENELDPLKNR 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1622 SQRISEQQQIHFELEGIKKNLNKVSEKTLKVLAQKEQSSSSPLLRTEHEIT-----HQKMDQVYSLSSIYLEK-LKTINL 1695
Cdd:TIGR00606 254 LKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNdlyhnHQRTVREKERELVDCQReLEKLNK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1696 VIR--STQGAEEVVRTYEDQLK-EVHAVPSDSKELE----ATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRS 1768
Cdd:TIGR00606 334 ERRllNQEKTELLVEQGRLQLQaDRHQEHIRARDSLiqslATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTAAQL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1769 HSERDVDLDRYREKVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQI----QSVPITDSK 1844
Cdd:TIGR00606 414 CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELrkaeRELSKAEKN 493
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1845 TMKEHLLQEKKLLDEIESNRDKVDECQKYAKQYIDAIKDYELQLVTYKAQVEPVASPAKKPKVQSTSDSIIQ-EYVDLRT 1923
Cdd:TIGR00606 494 SLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlGYFPNKK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1924 RYSELTTLTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQaEKEAEELQRRMQEEV 2003
Cdd:TIGR00606 574 QLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-ESDLERLKEEIEKSS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2004 SKREVVAVDAEQQKQTIQQ--------------------ELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQL 2063
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQltdenqsccpvcqrvfqteaELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLA 732
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2064 ETMQKHKANAEDELQELRARAEKAE---QQKKAAQEEAERLRKQVKDE-------------TQKKREAEEELKRKV--QA 2125
Cdd:TIGR00606 733 PGRQSIIDLKEKEIPELRNKLQKVNrdiQRLKNDIEEQETLLGTIMPEeesakvcltdvtiMERFQMELKDVERKIaqQA 812
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2126 EKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQ--QSAAAELNSKRMSFAEKTAQLELSLKQEHI 2203
Cdd:TIGR00606 813 AKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQhlKSKTNELKSEKLQIGTNLQRRQQFEEQLVE 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2204 TVTHLQEEAERLKKLHDEAEKAREEAEKELE--------KWHQKANEALRLRLQAEEV----AHKKTL---AQEEAEKQK 2268
Cdd:TIGR00606 893 LSTEVQSLIREIKDAKEQDSPLETFLEKDQQekeelissKETSNKKAQDKVNDIKEKVknihGYMKDIenkIQDGKDDYL 972
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2269 EDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEA 2348
Cdd:TIGR00606 973 KQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQM 1052
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2349 IQKRKEMEEELAKV-RAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLREL 2401
Cdd:TIGR00606 1053 KQEHQKLEENIDLIkRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYREM 1106
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
6604-6778 |
1.14e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 59.00 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6604 QAEEFHTLVHYFLERLSEAERTLKYGVIPEEEKALQECQKQQQELMSVLQCQKLALDCILSLGEEILNCCHPESIItIKS 6683
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-IQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6684 WLNVTKSRYQEVLNWAEQQGERIQmQSVSLATEREEIARLIDWITAAEESLSlrdQDPLPKEMEALEDLISQHTVFMDEL 6763
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLE-EALDLQQFFRDADDLEQWLEEKEAALA---SEDLGKDLESVEELLKKHKELEEEL 155
|
170
....*....|....*
gi 1835643837 6764 DKKQPEVEKVTKNCK 6778
Cdd:cd00176 156 EAHEPRLKSLNELAE 170
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2567-2790 |
1.29e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.93 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2567 AEQEAEKQRQLALEEEQRRKEAEEKVRkiladeKEAARQRKAALEEVERLKAKAEEAKRQkelaEKEAERQIQLAQEAAL 2646
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKEL------AALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2647 KKIDAEEKAHTAIVQQKEQEMLQTRK-QEQSILDKLK-----EEAERAKRAAED-ADFARTRAEQEAALsRQQVEEAERL 2719
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRAlYRLGRQPPLAlllspEDFLDAVRRLQYlKYLAPARREQAEEL-RADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 2720 KQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQEL 2790
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2080-2960 |
1.56e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 62.28 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2080 LRARAEKAEQQKKAAQEEAERL--RKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRS---QAEEAERRm 2154
Cdd:COG3096 274 MRHANERRELSERALELRRELFgaRRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalrQQEKIERY- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2155 kQAEVEkERQIKVAQevaQQSAAAELNSKRmsfAEKTAQLELSlkqehitvthlQEEAERLK-KLHDEAEKAREEAEKEL 2233
Cdd:COG3096 353 -QEDLE-ELTERLEE---QEEVVEEAAEQL---AEAEARLEAA-----------EEEVDSLKsQLADYQQALDVQQTRAI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2234 EkwHQKANEALRlrlQAEEVAHKKTLAQEEAEkqkedaEREARKRAKteESALRQKELaedELEKQRKLADATAQQKFSA 2313
Cdd:COG3096 414 Q--YQQAVQALE---KARALCGLPDLTPENAE------DYLAAFRAK--EQQATEEVL---ELEQKLSVADAARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2314 EQELIRLKAETENSEQQRLLleeelfrlknevNEAIQKRKEMEEELAKVR------AEMEILLQSKSRAEEESRSNTEKS 2387
Cdd:COG3096 478 YELVCKIAGEVERSQAWQTA------------RELLRRYRSQQALAQRLQqlraqlAELEQRLRQQQNAERLLEEFCQRI 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2388 KQ------MLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEK 2461
Cdd:COG3096 546 GQqldaaeELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADS 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2462 EAENERLRRLAEDEAyQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEdtlrqrriieeeirilKVNFEKASV 2541
Cdd:COG3096 626 QEVTAAMQQLLERER-EATVERDELAARKQALESQIERLSQPGGAEDPRLLALAE----------------RLGGVLLSE 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2542 GKSDLELE--------LNQLKN--IAEETQRSKEKAEQEAEKQRQLALEE------EQRRKEAEEKVRKILAdeKEAARQ 2605
Cdd:COG3096 689 IYDDVTLEdapyfsalYGPARHaiVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfDDSVFDAEELEDAVVV--KLSDRQ 766
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2606 -RKAALEEVERLKAKAeeakRQKELAEKEAERQIQlaqeaalkkidAEEKAHTAIVQQKEQEMLQTRkqEQSILDKLKee 2684
Cdd:COG3096 767 wRYSRFPEVPLFGRAA----REKRLEELRAERDEL-----------AEQYAKASFDVQKLQRLHQAF--SQFVGGHLA-- 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2685 aerakrAAEDADfartrAEQEAALSRQQVEEAER-LKQRAEEEAQAKAQAQDEAE------KLRKEAEL----EAAKRAH 2753
Cdd:COG3096 828 ------VAFAPD-----PEAELAALRQRRSELEReLAQHRAQEQQLRQQLDQLKEqlqllnKLLPQANLladeTLADRLE 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2754 AEQAALKQKQLADEEMDKHKKFAEK------TLR----QKSQVEQELTKVKLQLEETDHQKTLLDEELQRL--------- 2814
Cdd:COG3096 897 ELREELDAAQEAQAFIQQHGKALAQleplvaVLQsdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRphfsyedav 976
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2815 -----KEEVTDAMRQK-AQVEEELFKVKIQMEELIKlklRIEEENKMLIMKD--KDSTQKLLveeAEKMRQVAEEAARLS 2886
Cdd:COG3096 977 gllgeNSDLNEKLRARlEQAEEARREAREQLRQAQA---QYSQYNQVLASLKssRDAKQQTL---QELEQELEELGVQAD 1050
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2887 IEAQEAARMRKlaeDDLaNQRALAEKMLKEKMqaiqEASRLKAEAEMLQKQKELAQEQaRKFQEDKEQIEQQLA 2960
Cdd:COG3096 1051 AEAEERARIRR---DEL-HEELSQNRSRRSQL----EKQLTRCEAEMDSLQKRLRKAE-RDYKQEREQVVQAKA 1115
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2558-2737 |
1.62e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 61.51 E-value: 1.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2558 EETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKilaDEKEAARQRKAALEEVERLKAKAEEAK---RQKELAEKEA 2634
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERKQRLQLQAAQERarqQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2635 ERQIQLAQEAAlKKIDAEEKahtaivQQKEQEMlqtrkqeqsildKLKEEAERAKRAAEDADFARTRAEQEAALSRQQve 2714
Cdd:pfam15709 434 ELQRKKQQEEA-ERAEAEKQ------RQKELEM------------QLAEEQKRLMEMAEEERLEYQRQKQEAEEKARL-- 492
|
170 180
....*....|....*....|....*...
gi 1835643837 2715 EAERLKQRAEEEA-----QAKAQAQDEA 2737
Cdd:pfam15709 493 EAEERRQKEEEAArlaleEAMKQAQEQA 520
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2464-2805 |
1.66e-08 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 61.57 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2464 ENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSD--NELERQKNIVEDTlRQRRIIEEEIRILKVNFEKasv 2541
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDikTEYLYELNVLKEK-SEAELTSKTKKELDAAFEQ--- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2542 gksdLELELNQLKNIAEETQRSKEKAEQEAEKQRqlaleEEQRRKEAEEKVRKILADEKEAARQRKAAleEVERLKAKAE 2621
Cdd:NF033838 130 ----FKKDTLEPGKKVAEATKKVEEAEKKAKDQK-----EEDRRNYPTNTYKTLELEIAESDVEVKKA--ELELVKEEAK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2622 EAKRQKELAEKEAERQIQLAQEAALKKI-----DAEEKA-HTAIVQQKEQEMLQTRKQEQsilDKLKEeaeRAKRAAEDA 2695
Cdd:NF033838 199 EPRDEEKIKQAKAKVESKKAEATRLEKIktdreKAEEEAkRRADAKLKEAVEKNVATSEQ---DKPKR---RAKRGVLGE 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2696 DFARTRAEQEAALSRQQVEEaERL--------KQRAE-----EEAQAKAQAQDEAEKLR--------------------K 2742
Cdd:NF033838 273 PATPDKKENDAKSSDSSVGE-ETLpspslkpeKKVAEaekkvEEAKKKAKDQKEEDRRNyptntyktleleiaesdvkvK 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2743 EAELEAAKRAHAEQAALKQKQLADEEMDKHKKFA---EKTLRQKSQVEQElTKVKLQLEETDHQKT 2805
Cdd:NF033838 352 EAELELVKEEAKEPRNEEKIKQAKAKVESKKAEAtrlEKIKTDRKKAEEE-AKRKAAEEDKVKEKP 416
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6060-6162 |
1.86e-08 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 55.41 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6060 QFQSQLEELLQWLSHAADQLQGQRmVSVDLQSCEIELAKHKVLRNDVMSHARTVESVNEVGQGLLlqASLGDNTDTLQSS 6139
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLI--EEGHPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1835643837 6140 LQQMNQRWEFVRTQTERKQLELE 6162
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| EFh |
cd00051 |
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal ... |
6878-6940 |
1.87e-08 |
|
EF-hand, calcium binding motif; A diverse superfamily of calcium sensors and calcium signal modulators; most examples in this alignment model have 2 active canonical EF hands. Ca2+ binding induces a conformational change in the EF-hand motif, leading to the activation or inactivation of target proteins. EF-hands tend to occur in pairs or higher copy numbers.
Pssm-ID: 238008 [Multi-domain] Cd Length: 63 Bit Score: 54.09 E-value: 1.87e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 6878 RILDIFRSIDRDQDGRISQQEFIESVLSSKFPTNSLEMNAVASIFDYNGDGFIDYYEFVSALH 6940
Cdd:cd00051 1 ELREAFRLFDKDGDGTISADELKAALKSLGEGLSEEEIDEMIREVDKDGDGKIDFEEFLELMA 63
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2342-3028 |
2.03e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 61.57 E-value: 2.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEELAKVRAEME--------ILLQSKSRAEEESRSNTE---------KSKQMLEVEASKLRELAEE 2404
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKnkekelknLDKNLNKDEEKINNSNNKikileqqikDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2405 AAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEaeiaLKEKEAENERLRRLAEDEAYQRKLLEE 2484
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2485 QatqhKQDIEEKIILLKKssdnelerQKNIVEDTLrqrriieeeirilkVNFEKASVGKSDLELELNQLKNIAEETQRSK 2564
Cdd:TIGR04523 181 E----KLNIQKNIDKIKN--------KLLKLELLL--------------SNLKKKIQKNKSLESQISELKKQNNQLKDNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2565 EKAEQEAEKQrqlaleeEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEA 2644
Cdd:TIGR04523 235 EKKQQEINEK-------TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2645 ALKKIDAEEKAhtaivQQKEQEMLQTR-KQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRA 2723
Cdd:TIGR04523 308 WNKELKSELKN-----QEKKLEEIQNQiSQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2724 EEEAQA-KAQAQDEAEKLRKEAELEAAKRAHAEQAAlKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDH 2802
Cdd:TIGR04523 383 KQEIKNlESQINDLESKIQNQEKLNQQKDEQIKKLQ-QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDN 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2803 QKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRqvaeea 2882
Cdd:TIGR04523 462 TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE------ 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2883 arlsIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEasrLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKE 2962
Cdd:TIGR04523 536 ----KESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEK 608
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2963 TegfqKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKE 3028
Cdd:TIGR04523 609 E----KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2557-2767 |
2.29e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 61.12 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2557 AEETQRSKEKAEQEAEKQR---QLALEEEQRRKEAEEKVRKI----LADEKEAARQRKAAleeverlKAKAEEAKRQKEL 2629
Cdd:PRK05035 467 AAREARHKKAAEARAAKDKdavAAALARVKAKKAAATQPIVIkagaRPDNSAVIAAREAR-------KAQARARQAEKQA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2630 AEKEAERQIQLA---QEAALKKIDAEEKAHTAIVQ--------QKEQEMLQTRKQEQSILDKLKEEAERA---KRAAEDA 2695
Cdd:PRK05035 540 AAAADPKKAAVAaaiARAKAKKAAQQAANAEAEEEvdpkkaavAAAIARAKAKKAAQQAASAEPEEQVAEvdpKKAAVAA 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2696 DFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKA----QAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADE 2767
Cdd:PRK05035 620 AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAkarkAAQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2783-3155 |
2.52e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 60.68 E-value: 2.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2783 KSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLK---LRIEEENKMLIMK 2859
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKdalLAQRAAHEARIRE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2860 DKDSTQKLlveeAEKMRQVAEEAARLSIEAQEAARMRKLAEDDlanqralaEKMLKEKMQAIQEasRLKAEAEMLQKQKE 2939
Cdd:pfam07888 134 LEEDIKTL----TQRVLERETELERMKERAKKAGAQRKEEEAE--------RKQLQAKLQQTEE--ELRSLSKEFQELRN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2940 LAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAER-RQQLEITAE--------AERLKLQVLEMSRAQAKAEEDASKFKK 3010
Cdd:pfam07888 200 SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAlLEELRSLQErlnaserkVEGLGEELSSMAAQRDRTQAELHQARL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3011 KAEEIGNKLHQTELATKErmavvqtleiQRQQSGKEAEELRRAiAELEHEK-EKLKREAellqknsQKMQVAQQEQlRQE 3089
Cdd:pfam07888 280 QAAQLTLQLADASLALRE----------GRARWAQERETLQQS-AEADKDRiEKLSAEL-------QRLEERLQEE-RME 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3090 TQVLQTTFLSEKQ----LLLEREKYIEEEKAKLenlyedevRKAQKLKQEQEHQMKHLEEEKDQLKVSMD 3155
Cdd:pfam07888 341 REKLEVELGREKDcnrvQLSESRRELQELKASL--------RVAQKEKEQLQAEKQELLEYIRQLEQRLE 402
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2560-2782 |
2.55e-08 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 60.74 E-value: 2.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2560 TQRSKEKAEQE---AEKQRQLALEEEQRRKEAEEKvRKILADEKEAARQRKAALEEVERlkAKAEEAKRQKELAEKEAER 2636
Cdd:pfam15709 326 EKREQEKASRDrlrAERAEMRRLEVERKRREQEEQ-RRLQQEQLERAEKMREELELEQQ--RRFEEIRLRKQRLEEERQR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2637 QiqlaqeaalkkidAEEKAHTAIVQQKEQEmlQTRKQEQSILDKLKEEaeRAKRAAEDADFARTRAEQEAALSRQQVEEA 2716
Cdd:pfam15709 403 Q-------------EEEERKQRLQLQAAQE--RARQQQEEFRRKLQEL--QRKKQQEEAERAEAEKQRQKELEMQLAEEQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2717 ERLKQRAEEEaqakaqaqdEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQ 2782
Cdd:pfam15709 466 KRLMEMAEEE---------RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2994-3230 |
2.60e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 60.16 E-value: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2994 MSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQK 3073
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3074 NSQKMQVAQQEQLRQETQVLQTTFLSEKQ----LLLERE------------KYIEEEKAKLENLYEDEVRKAQKLKQEqe 3137
Cdd:COG4942 91 EIAELRAELEAQKEELAELLRALYRLGRQpplaLLLSPEdfldavrrlqylKYLAPARREQAEELRADLAELAALRAE-- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3138 hqmkhLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLAD---ENRKLREKLEQMEEEhrIALAQT 3214
Cdd:COG4942 169 -----LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAE--AAAAAE 241
|
250
....*....|....*.
gi 1835643837 3215 REMRTQTDDLAGNLPL 3230
Cdd:COG4942 242 RTPAAGFAALKGKLPW 257
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4922-4959 |
2.73e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 52.87 E-value: 2.73e-08
10 20 30
....*....|....*....|....*....|....*...
gi 1835643837 4922 QRLLEAQACTGGIIDINTGQKFSVTDAVNKGLVDKIMV 4959
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2419-2902 |
2.82e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2419 RQIAEDEAARQRAEA-ERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLleEQATQHKQDIEEKI 2497
Cdd:COG4717 71 KELKELEEELKEAEEkEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL--EALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2498 illkkssdNELERQKNIVEDTLRQRRIIEEEIRILKvnfekasvgkSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQL 2577
Cdd:COG4717 149 --------EELEERLEELRELEEELEELEAELAELQ----------EELEELLEQLSLATEEELQDLAEELEELQQRLAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2578 ALEEEQRRKEaeekvrkiladEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHT 2657
Cdd:COG4717 211 LEEELEEAQE-----------ELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2658 AIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEdadfaRTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEA 2737
Cdd:COG4717 280 FLVLGLLALLFLLLAREKASLGKEAEELQALPALEE-----LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2738 EKLRKEAELEAAKRAHAEQAALKQKQLADEEMdkhkkFAEK--TLRQKSQVEQELTKVKLQLEE--TDHQKTLLDEELQR 2813
Cdd:COG4717 355 EAEELEEELQLEELEQEIAALLAEAGVEDEEE-----LRAAleQAEEYQELKEELEELEEQLEEllGELEELLEALDEEE 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2814 LKEEVTDAMRQKAQVEEELfkvKIQMEELIKLKLRIEEenkmliMKDKDSTQKLLVEEAE---KMRQVAEEAARLSIEAQ 2890
Cdd:COG4717 430 LEEELEELEEELEELEEEL---EELREELAELEAELEQ------LEEDGELAELLQELEElkaELRELAEEWAALKLALE 500
|
490
....*....|..
gi 1835643837 2891 EAARMRKLAEDD 2902
Cdd:COG4717 501 LLEEAREEYREE 512
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1585-2148 |
3.11e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 60.85 E-value: 3.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1585 KNYISQLKDIRLQLEGCESR---TIHKIRTPMEKDP-----IKECSQRISEQQQIHFELEGIKKNLNKVsEKTLKVLAQK 1656
Cdd:PRK03918 182 EKFIKRTENIEELIKEKEKEleeVLREINEISSELPelreeLEKLEKEVKELEELKEEIEELEKELESL-EGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1657 EQSSSSPLLRTEHEITHQKmDQVYSLSSI------YLEKLKTINLVIRSTQGAEEVVRTYEDQLKEVHAVPSDSKELEAT 1730
Cdd:PRK03918 261 IRELEERIEELKKEIEELE-EKVKELKELkekaeeYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEER 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1731 KAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMlRSHSERDVDLDryREKVQQLLERWQAILVQIDLRQRELDQLGRQ 1810
Cdd:PRK03918 340 LEELKKKLKELEKRLEELEERHELYEEAKAKKEEL-ERLKKRLTGLT--PEKLEKELEELEKAKEEIEEEISKITARIGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1811 LRYYRETYEWLIKWIKDAKqRQEQIQSVPITD---SKTMKEHLLQEKKLLDEIESNRDKVDECQKYAKQyIDAIKDYELQ 1887
Cdd:PRK03918 417 LKKEIKELKKAIEELKKAK-GKCPVCGRELTEehrKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-LEKVLKKESE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1888 LVTYKAQVEPVASPAKKPKVQSTSDsIIQEYVDLRTRYSELTTLTSQyIKFITETLRRLNDEEKAAEKLKEEerrrLAEV 1967
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKKYNLEE-LEKKAEEYEKLKEKLIKLKGE-IKSLKKELEKLEELKKKLAELEKK----LDEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1968 EaqlakqTQLAEAHAKAKAQAEKEAEELQRRMQ--EEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEV 2045
Cdd:PRK03918 569 E------EELAELLKELEELGFESVEELEERLKelEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2046 EYNRRKIEEeihivrLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQ---EEAERLRKQVKDETQKKREAEEELKR- 2121
Cdd:PRK03918 643 EELRKELEE------LEKKYSEEEYEELREEYLELSRELAGLRAELEELEkrrEEIKKTLEKLKEELEEREKAKKELEKl 716
|
570 580
....*....|....*....|....*...
gi 1835643837 2122 -KVQAEKEAAREKQRAVEDLEKFRSQAE 2148
Cdd:PRK03918 717 eKALERVEELREKVKKYKALLKERALSK 744
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2543-3073 |
3.12e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 60.80 E-value: 3.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2543 KSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLA------LEEEQRRKEAEEKVRKILADEKE--------AARQRKA 2608
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELeklnnkYNDLKKQKEELENELNLLEKEKLniqknidkIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2609 ALEEVERLKAKAEEAKR-QKELAEKEaERQIQLAQEAALKKIDAEEKahTAIVQQKEQEMLQTRKQEQSILDKLKE---E 2684
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSlESQISELK-KQNNQLKDNIEKKQQEINEK--TTEISNTQTQLNQLKDEQNKIKKQLSEkqkE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2685 AERAKRAAED---------ADFARTRAEQEAALS-------RQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKE-AELE 2747
Cdd:TIGR04523 276 LEQNNKKIKElekqlnqlkSEISDLNNQKEQDWNkelkselKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKElTNSE 355
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2748 AAKRAHAEQAALKQKQLADEEMDKHKKFAEKTlrqksQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEvtdamrqKAQ 2827
Cdd:TIGR04523 356 SENSEKQRELEEKQNEIEKLKKENQSYKQEIK-----NLESQINDLESKIQNQEKLNQQKDEQIKKLQQE-------KEL 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2828 VEEELFKVKiqmEELIKLKLRIEEenkmliMKDKDSTQKLLVEEAEKMRQVAEEAAR-LSIEAQEAARMRKLAEDDLANQ 2906
Cdd:TIGR04523 424 LEKEIERLK---ETIIKNNSEIKD------LTNQDSVKELIIKNLDNTRESLETQLKvLSRSINKIKQNLEQKQKELKSK 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2907 RALAEKMLKEKMQAIQEASRLKAE-AEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEitaEAE 2985
Cdd:TIGR04523 495 EKELKKLNEEKKELEEKVKDLTKKiSSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNK---EIE 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2986 RLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLhqtelatKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLK 3065
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLK 644
|
....*...
gi 1835643837 3066 REAELLQK 3073
Cdd:TIGR04523 645 QEVKQIKE 652
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1961-2178 |
3.75e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.89 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1961 RRRLAEVEAQLAKQTQLAEAHA-KAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQnsdmeiksKA 2039
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETA--------RA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2040 KQIEEVEynrrkIEEEihivrlqletmqkhkaNAEdelQELRARAEKAEQQKKAAQEEAERLRKQvkdetqkkREAEEEL 2119
Cdd:COG2268 263 EAEAAYE-----IAEA----------------NAE---REVQRQLEIAEREREIELQEKEAEREE--------AELEADV 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2120 KRKVQAEKEAAREKQRAveDLEKFRSQAE-EAERRMKQAEVEKE-----RQIKVAQ---EVAQQSAAA 2178
Cdd:COG2268 311 RKPAEAEKQAAEAEAEA--EAEAIRAKGLaEAEGKRALAEAWNKlgdaaILLMLIEklpEIAEAAAKP 376
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2400-2628 |
3.83e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 3.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2400 ELAEEAAKLRAVSEEAKRQRQIAEdEAARQRAEAERILKEKLAAINDATRL--KTEAEIALKEKEAE--NERLRRLAEDE 2475
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2476 AYQRKLLEEQ-ATQHKQDIEEKIILLKKSSD-NELERQKNIVEDTLRQRRiieeeirilkvnfEKASVGKSDLElELNQL 2553
Cdd:COG4942 100 EAQKEELAELlRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARR-------------EQAEELRADLA-ELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2554 KNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKE 2628
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2547-2755 |
3.86e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.82 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2547 ELELNQLKNIAEETQRSKEKAEQEAekqrqlaleEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERlKAKAEEAKRQ 2626
Cdd:PRK09510 110 RLAAQEQKKQAEEAAKQAALKQKQA---------EEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKK-KAEAEAAKKA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2627 KELAEKEAErqiqlaqEAALKKIDAEEKAhtaivqqkeqemlqtrkqeqsildklKEEAERAKRAAEDADfartraeqea 2706
Cdd:PRK09510 180 AAEAKKKAE-------AEAAAKAAAEAKK--------------------------KAEAEAKKKAAAEAK---------- 216
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1835643837 2707 alsrqqvEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAE 2755
Cdd:PRK09510 217 -------KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2271-2473 |
4.33e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2271 AEREARKRAKTEESALRQK-ELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAI 2349
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2350 QKRKEMEEELAKV---------RAEMEILLQSKSRAEEESRSNTEKS-KQMLEVEASKLRELAEEAAKLRAVSEEAKRQR 2419
Cdd:COG4942 97 AELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2420 QIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAE 2473
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4653-4689 |
4.45e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 52.10 E-value: 4.45e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1835643837 4653 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4689
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2981-3195 |
4.52e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.39 E-value: 4.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2981 TAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHE 3060
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3061 KEKLKREAELLQKNSQKMQVAQQEQL---RQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENL------YEDEVRKAQK 3131
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELaalraeLEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 3132 LKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRK 3195
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1949-2164 |
4.68e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 59.16 E-value: 4.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1949 EEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEElqrRMQEEVSKREVVAVDAEQQKQTIQQELQQLR 2028
Cdd:pfam13868 50 EEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEE---KLQEREQMDEIVERIQEEDQAEAEEKLEKQR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2029 QNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKaEQQKKAAQEEAERLRKQVKDE 2108
Cdd:pfam13868 127 QLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKER-EIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2109 TQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQ 2164
Cdd:pfam13868 206 LRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE 261
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2233-3064 |
5.23e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 60.36 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2233 LEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAER--EARKRAKTEESALR-QKELAEDE-LEKQRKLADAT-- 2306
Cdd:PRK04863 326 LEQDYQAASDHLNLVQTALRQQEKIERYQADLEELEERLEEqnEVVEEADEQQEENEaRAEAAEEEvDELKSQLADYQqa 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2307 --AQQKFS-----AEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQS----KSR 2375
Cdd:PRK04863 406 ldVQQTRAiqyqqAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAyqlvRKI 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2376 AEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAkRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAE 2455
Cdd:PRK04863 486 AGEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSEL-EQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2456 IALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIillkkSSDNELERQKNIVEDTLRQRRIIEEEIRILKVN 2535
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWL-----AAQDALARLREQSGEEFEDSQDVTEYMQQLLER 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2536 FEKASVGKSDLELELNQLKniaEETQRSKEKAEQEAEKQRQLA----------------LEEEQRRKEAEEKVRK-ILAD 2598
Cdd:PRK04863 640 ERELTVERDELAARKQALD---EEIERLSQPGGSEDPRLNALAerfggvllseiyddvsLEDAPYFSALYGPARHaIVVP 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2599 EKEAARQRKAALEE-----------VERLKA---KAEEakRQKELAEKEAERQIQL------------AQEAALKKIDAE 2652
Cdd:PRK04863 717 DLSDAAEQLAGLEDcpedlyliegdPDSFDDsvfSVEE--LEKAVVVKIADRQWRYsrfpevplfgraAREKRIEQLRAE 794
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2653 ekahtaivQQKEQEMLQTRKQEQSILDKLKEEAER--AKRAAE--DADfartrAEQEAALSRQQVEEAERlkqraeEEAQ 2728
Cdd:PRK04863 795 --------REELAERYATLSFDVQKLQRLHQAFSRfiGSHLAVafEAD-----PEAELRQLNRRRVELER------ALAD 855
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2729 AKAQAQDEAEKLRKEAELEAAKRAHAEQAALkqkqLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLD 2808
Cdd:PRK04863 856 HESQEQQQRSQLEQAKEGLSALNRLLPRLNL----LADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQ 931
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2809 ---EELQRLKEEVTDAMRQKAQVEEELFKVKiqmeELI--KLKLRIEEENKMLImKDKDSTQKLL--VEEAEKMRQVAEE 2881
Cdd:PRK04863 932 sdpEQFEQLKQDYQQAQQTQRDAKQQAFALT----EVVqrRAHFSYEDAAEMLA-KNSDLNEKLRqrLEQAEQERTRARE 1006
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2882 AARlsiEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEAS-RLKAEAEM-LQKQKELAQEQARKFQEDKEQIEQQL 2959
Cdd:PRK04863 1007 QLR---QAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGvPADSGAEErARARRDELHARLSANRSRRNQLEKQL 1083
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2960 AketegfqkSLEAERRQQLEITAEAERlKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATkermavvQTLEIQ 3039
Cdd:PRK04863 1084 T--------FCEAEMDNLTKKLRKLER-DYHEMREQVVNAKAGWCAVLRLVKDNGVERRLHRRELAY-------LSADEL 1147
|
890 900
....*....|....*....|....*
gi 1835643837 3040 RQQSGKEAEELRRAIAELEHEKEKL 3064
Cdd:PRK04863 1148 RSMSDKALGALRLAVADNEHLRDVL 1172
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
6060-6163 |
5.47e-08 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 54.25 E-value: 5.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6060 QFQSQLEELLQWLSHAADQLQGQRMVSvDLQSCEIELAKHKVLRNDVMSHARTVESVNEVGQGLLlqASLGDNTDTLQSS 6139
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSEDYGK-DLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI--DEGHYASEEIQER 81
|
90 100
....*....|....*....|....
gi 1835643837 6140 LQQMNQRWEFVRTQTERKQLELEN 6163
Cdd:pfam00435 82 LEELNERWEQLLELAAERKQKLEE 105
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2040-2179 |
5.94e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.50 E-value: 5.94e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2040 KQIEEVEYNRRKIEEEIhivrlQLETmQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQ----VKDETQKKR-- 2113
Cdd:COG2268 192 RKIAEIIRDARIAEAEA-----ERET-EIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKaeerREAETARAEae 265
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2114 ----EAEEELKRKVQAEKEAA-REKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQ---EVAQQSAAAE 2179
Cdd:COG2268 266 aayeIAEANAEREVQRQLEIAeREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEaeaEAIRAKGLAE 339
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2695-3114 |
6.57e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.97 E-value: 6.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2695 ADFARTRAEQ----EAALSRQQvEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAE-----QAALKQKQLA 2765
Cdd:COG3096 271 ADYMRHANERrelsERALELRR-ELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnlvQTALRQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2766 DEEMDKHKKFAEKTLRQKSQVEQeltkVKLQLEETDHQKTLLDEELQRLKEEVTDAMR----------QKAQVEEELFKV 2835
Cdd:COG3096 350 ERYQEDLEELTERLEEQEEVVEE----AAEQLAEAEARLEAAEEEVDSLKSQLADYQQaldvqqtraiQYQQAVQALEKA 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2836 KiQMEELIKLKLR-IEEENKMLIMKDKDSTQKLLveEAEKMRQVAEEAARLSIEAQEAarMRKLA---EDDLANQRAlae 2911
Cdd:COG3096 426 R-ALCGLPDLTPEnAEDYLAAFRAKEQQATEEVL--ELEQKLSVADAARRQFEKAYEL--VCKIAgevERSQAWQTA--- 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2912 kmlkekMQAIQEASRLKAEAEMLQkQKELAQEQARKFQEDKEQIEQQLaketEGFQKSLEAERRQQLEITAEAERLKLQV 2991
Cdd:COG3096 498 ------RELLRRYRSQQALAQRLQ-QLRAQLAELEQRLRQQQNAERLL----EEFCQRIGQQLDAAEELEELLAELEAQL 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2992 LEMSRAQAKAEEDASKFKKKAEEignklhqtelatkermavvqtLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAEll 3071
Cdd:COG3096 567 EELEEQAAEAVEQRSELRQQLEQ---------------------LRARIKELAARAPAWLAAQDALERLREQSGEALA-- 623
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1835643837 3072 qkNSQKMQVAQQEQLRQETQVLQttflsEKQLLLEREKYIEEE 3114
Cdd:COG3096 624 --DSQEVTAAMQQLLEREREATV-----ERDELAARKQALESQ 659
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2567-2768 |
6.62e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.07 E-value: 6.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2567 AEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQ-KELAEKEAERQIQLAQEA- 2644
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiAEAEAEIEERREELGERAr 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2645 ALKKIDAEEKAHTAIVQQKE-------QEMLQT-RKQEQSILDKLKEEAERAKRAAEDADfaRTRAEQEAALSRQQVEEA 2716
Cdd:COG3883 94 ALYRSGGSVSYLDVLLGSESfsdfldrLSALSKiADADADLLEELKADKAELEAKKAELE--AKLAELEALKAELEAAKA 171
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2717 ERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEE 2768
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1948-2301 |
6.88e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.50 E-value: 6.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1948 DEEKAA---EKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEE-------VSKREVVAVDAEQQK 2017
Cdd:pfam02029 3 DEEEAArerRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafldrTAKREERRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2018 QTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKH---KANAEDELQELRARAEKAEQQKKAA 2094
Cdd:pfam02029 83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEireKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2095 QEEAERLRKQV-KDETQKKREAEEELKRKvqaekeaarEKQRAVEDLEKFRSqaeeaERRMKQAEVEkerqiKVAQEVAQ 2173
Cdd:pfam02029 163 SEEAEEVPTENfAKEEVKDEKIKKEKKVK---------YESKVFLDQKRGHP-----EVKSQNGEEE-----VTKLKVTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2174 QSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEK--WHQKANEALRLRLQAE 2251
Cdd:pfam02029 224 KRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKreERRKLLEEEEQRRKQE 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2252 EvAHKKTLAQEEAEKQKEDAEreaRKRAkteESALRQKELAEDELEKQRK 2301
Cdd:pfam02029 304 E-AERKLREEEEKRRMKEEIE---RRRA---EAAEKRQKLPEDSSSEGKK 346
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
645-752 |
7.15e-08 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 55.01 E-value: 7.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 645 ERDRVQKKTFTKWVNKhlIKAQRHVSDLYEDLRDGHNLISLLEVL-------SGDNLPREKGRMRFHKLQNVQIALDYLK 717
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 1835643837 718 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 752
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1931-2142 |
7.70e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.12 E-value: 7.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1931 LTSQYIKFITETLRRLNDEEKAAEK---LKEEERRRLAEvEAQLAKQTQLAEAhAKAKAQAE---KEAEELQRRMQEEVS 2004
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAEReteIAIAQANREAE-EAELEQEREIETA-RIAEAEAElakKKAEERREAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2005 KREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEeeihivrlqletmqkhKANAEDELQELRARA 2084
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRK----------------PAEAEKQAAEAEAEA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2085 EKaeqQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEK 2142
Cdd:COG2268 328 EA---EAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDK 382
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1674-2277 |
8.48e-08 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 59.26 E-value: 8.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1674 QKMDQVYSLSSIYLEKLKTINLVIRSTQGAEEVVRTYEDQLKEvhavpsDSKELEATKAELKKLRSQVEGHQPLFNTLEA 1753
Cdd:TIGR04523 51 NKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKK------NKDKINKLNSDLSKINSEIKNDKEQKNKLEV 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1754 DLNKAK-----------DVNEQMLRSHSERDVDLDRYRE--KVQQLLERWQAILV-QIDLRQRELDQLGRQLRYYRETYE 1819
Cdd:TIGR04523 125 ELNKLEkqkkenkknidKFLTEIKKKEKELEKLNNKYNDlkKQKEELENELNLLEkEKLNIQKNIDKIKNKLLKLELLLS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1820 WLIKWIKDAKQRQEQIqsvpiTDSKTmkehllQEKKLLDEIESNRDKVDECQKYAKQYIDAIKDYELQLVTYKAQVEpva 1899
Cdd:TIGR04523 205 NLKKKIQKNKSLESQI-----SELKK------QNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLS--- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1900 spAKKPKVQSTSDSIIQEYVDLRTRYSELTTLTSQYIKfitETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAE 1979
Cdd:TIGR04523 271 --EKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ---DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1980 AHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQ------ELQQLRQNSDMEIKSKAKQIEEVEYNRRKIE 2053
Cdd:TIGR04523 346 QLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2054 EEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREK 2133
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEK 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2134 QRAVEDLEKFRSQAEEAERRMKQAEVEKerqikvaqevaqqsaaAELNSKRMSFAEKTAQLELSLKQEHITvTHLQEEAE 2213
Cdd:TIGR04523 506 KELEEKVKDLTKKISSLKEKIEKLESEK----------------KEKESKISDLEDELNKDDFELKKENLE-KEIDEKNK 568
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2214 RLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEvahkKTLAQEEAEKQKEDAEREARK 2277
Cdd:TIGR04523 569 EIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE----KEKKISSLEKELEKAKKENEK 628
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5766-5951 |
8.53e-08 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 56.69 E-value: 8.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5766 IREQIRDNTLVLGELEKLGVSLHTIQRHVEELLSNTQAVGSEltakgIQDQAELLLGQWQSLRSQAEERECWLKSLLTLA 5845
Cdd:cd00176 35 VEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEE-----IQERLEELNQRWEELRELAEERRQRLEEALDLQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5846 DRFWHgFSELTITLNDTQQMVLDiEEASSDPDSIRTKLNTMQALREDVDNLQNDLDTLGILGVELMSSCGDMDKPNVTKS 5925
Cdd:cd00176 110 QFFRD-ADDLEQWLEEKEAALAS-EDLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEK 187
|
170 180
....*....|....*....|....*.
gi 1835643837 5926 LDDLYATWNSLNKVWNEHYNKLEASL 5951
Cdd:cd00176 188 LEELNERWEELLELAEERQKKLEEAL 213
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2611-2950 |
8.57e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.39 E-value: 8.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2611 EEVERLKAKAEEAK----RQKELAEKEAERQIQLAQEAAL-KKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEA 2685
Cdd:pfam13868 6 DELRELNSKLLAAKcnkeRDAQIAEKKRIKAEEKEEERRLdEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2686 ERaKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQkqlA 2765
Cdd:pfam13868 86 EQ-KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEY---L 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2766 DEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDE-ELQRLKEEVTDAMRQKAQVEEElfkVKIQMEELIK 2844
Cdd:pfam13868 162 KEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDElRAKLYQEEQERKERQKEREEAE---KKARQRQELQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2845 LKLRIEEENKmliMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAE-DDLANQRALAEKM-LKEKMQAIQ 2922
Cdd:pfam13868 239 QAREEQIELK---ERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHrRELEKQIEEREEQrAAEREEELE 315
|
330 340
....*....|....*....|....*...
gi 1835643837 2923 EASRLKAEAEmlQKQKELAQEQARKFQE 2950
Cdd:pfam13868 316 EGERLREEEA--ERRERIEEERQKKLKE 341
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2553-2952 |
8.58e-08 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 58.90 E-value: 8.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2553 LKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEK 2632
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2633 ---EAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQsilDKLKEEAERAKRAAEDADFARTRAEQEAALS 2709
Cdd:COG3064 85 aaaEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAE---EEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2710 RQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKtlRQKSQVEQE 2789
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR--EAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2790 LTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLV 2869
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2870 EEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQ 2949
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
...
gi 1835643837 2950 EDK 2952
Cdd:COG3064 400 LLG 402
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2073-2496 |
8.74e-08 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 59.39 E-value: 8.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2073 AEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKR-EAEEELKRKVQ-AEKEAAREKQRAVEDLEKFRSQAEEA 2150
Cdd:pfam09731 50 ALGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKiPRQSGVSSEVAeEEKEATKDAAEAKAQLPKSEQEKEKA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2151 ERRMKQAEVEK----ERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLElslKQEHITVTHLQEEAERLKKLHDEAEKAR 2226
Cdd:pfam09731 130 LEEVLKEAISKaesaTAVAKEAKDDAIQAVKAHTDSLKEASDTAEISRE---KATDSALQKAEALAEKLKEVINLAKQSE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2227 eeaekelekwHQKANEalrLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKqrKLADAT 2306
Cdd:pfam09731 207 ----------EEAAPP---LLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVS--IFPDII 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2307 AQQK-----FSAEQELIRLKAetenseqqrllleeelfrlKNEVNEAIQKRKEMeeelaKVRAEMEILLQSKSRAEEESR 2381
Cdd:pfam09731 272 PVLKednllSNDDLNSLIAHA-------------------HREIDQLSKKLAEL-----KKREEKHIERALEKQKEELDK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2382 SNTEKSKQMLEVEASKLRELAEEAAklRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAinDATRLKTEAEIALKEK 2461
Cdd:pfam09731 328 LAEELSARLEEVRAADEAQLRLEFE--REREEIRESYEEKLRTELERQAEAHEEHLKDVLVE--QEIELQREFLQDIKEK 403
|
410 420 430
....*....|....*....|....*....|....*.
gi 1835643837 2462 EAENERLRRLAEDEAYQR-KLLEEQATQHKQDIEEK 2496
Cdd:pfam09731 404 VEEERAGRLLKLNELLANlKGLEKATSSHSEVEDEN 439
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
652-746 |
8.83e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 53.88 E-value: 8.83e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 652 KTFTKWVNKHLIKA--QRHVSDLYEDLRDGHNLISLLEVLSGDNL------PREKGRMrfhkLQNVQIALDYLKHRQVKL 723
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1835643837 724 VNIRNDDIADGNPKLTLGLIWTI 746
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2905-3218 |
9.11e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.01 E-value: 9.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2905 NQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQK-ELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEA--ERRQQLEIT 2981
Cdd:pfam13868 12 NSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLdEMMEEERERALEEEEEKEEERKEERKRYRQELEEqiEEREQKRQE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2982 AEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMavvqtlEIQRQQSGKEAEELRRAiaeLEHEK 3061
Cdd:pfam13868 92 EYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQA------EWKELEKEEEREEDERI---LEYLK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3062 EKLKREAELLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQE------ 3135
Cdd:pfam13868 163 EKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQElqqare 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3136 --QEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQ 3213
Cdd:pfam13868 243 eqIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLRE 322
|
....*
gi 1835643837 3214 TREMR 3218
Cdd:pfam13868 323 EEAER 327
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1958-2304 |
9.36e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.01 E-value: 9.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1958 EEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKqtiQQELQQLRQNSDMEIKs 2037
Cdd:pfam13868 4 NSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEK---EEERKEERKRYRQELE- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2038 kaKQIEEVEyNRRKIEEEihivRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQE--EAERLRKQVKdETQKKREA 2115
Cdd:pfam13868 80 --EQIEERE-QKRQEEYE----EKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEidEFNEEQAEWK-ELEKEEER 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2116 EEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAER---RMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTA 2192
Cdd:pfam13868 152 EEDERILEYLKEKAEREEEREAEREEIEEEKEREIARlraQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2193 QLELSLKQEHIT-VTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDA 2271
Cdd:pfam13868 232 RQRQELQQAREEqIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAERE 311
|
330 340 350
....*....|....*....|....*....|...
gi 1835643837 2272 EREARKRAKTEESALRQKELAEdelEKQRKLAD 2304
Cdd:pfam13868 312 EELEEGERLREEEAERRERIEE---ERQKKLKE 341
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1724-2636 |
9.57e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.42 E-value: 9.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1724 SKELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRSHserDVDLDRYREKVQQLLERWQAILVQIDLRQRE 1803
Cdd:pfam01576 298 GEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSH---EAQLQEMRQKHTQALEELTEQLEQAKRNKAN 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1804 LDQLGRQLRyyretyewlikwiKDAKQRQEQIQSVpiTDSKTMKEHllQEKKLLDEIESNRDKVDECQKYAKQYIDAIKD 1883
Cdd:pfam01576 375 LEKAKQALE-------------SENAELQAELRTL--QQAKQDSEH--KRKKLEGQLQELQARLSESERQRAELAEKLSK 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1884 YELQLVTYKAQVEPVASPA-KKPKVQSTSDSIIQEYVDLrtryseLTTLTSQYIKFITEtLRRLNDEEKAAEKLKEEERR 1962
Cdd:pfam01576 438 LQSELESVSSLLNEAEGKNiKLSKDVSSLESQLQDTQEL------LQEETRQKLNLSTR-LRQLEDERNSLQEQLEEEEE 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1963 RLAEVEAQLAK-QTQLAeahakakaqaekeaeELQRRMQEEVSKREVvavdAEQQKQTIQQELQQLRQnsdmEIKSKAKQ 2041
Cdd:pfam01576 511 AKRNVERQLSTlQAQLS---------------DMKKKLEEDAGTLEA----LEEGKKRLQRELEALTQ----QLEEKAAA 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2042 IEEVEYNRRKIEEEIHIVRLQLetmqkhkanaeDELQELRARAEKaeQQKKAAQEEAErlrkqvkDETQKKREAEEelkr 2121
Cdd:pfam01576 568 YDKLEKTKNRLQQELDDLLVDL-----------DHQRQLVSNLEK--KQKKFDQMLAE-------EKAISARYAEE---- 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2122 KVQAEKEAAREKQRAV---EDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAElNSKRmsfaektaqlelSL 2198
Cdd:pfam01576 624 RDRAEAEAREKETRALslaRALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELE-RSKR------------AL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2199 KQEhitvthLQEEAERLKKLHDEAekareeaekelekwhqKANEALRLRLqaeEVAHKKTLAQEEAEKQKEDAEREARKR 2278
Cdd:pfam01576 691 EQQ------VEEMKTQLEELEDEL----------------QATEDAKLRL---EVNMQALKAQFERDLQARDEQGEEKRR 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2279 AkteesALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRllleeelfrlknevNEAIQKRKEMEEE 2358
Cdd:pfam01576 746 Q-----LVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGR--------------EEAVKQLKKLQAQ 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2359 LAKVRAEMEILLQSKSRAEEESRSNTEKSKQMlEVEASKLRELAeeaaklrAVSEEAKRQRQIAEDEAARQRAEAeriLK 2438
Cdd:pfam01576 807 MKDLQRELEEARASRDEILAQSKESEKKLKNL-EAELLQLQEDL-------AASERARRQAQQERDELADEIASG---AS 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2439 EKLAAINDATRLktEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDT 2518
Cdd:pfam01576 876 GKSALQDEKRRL--EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAK 953
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2519 LRQRRIIEEEIRilkvnfeKASVgkSDLELELNQLkniaeetqrsKEKAEQEAeKQRQLALEEEQRRKEAEEKVRKILAD 2598
Cdd:pfam01576 954 LQEMEGTVKSKF-------KSSI--AALEAKIAQL----------EEQLEQES-RERQAANKLVRRTEKKLKEVLLQVED 1013
|
890 900 910
....*....|....*....|....*....|....*...
gi 1835643837 2599 EKEAARQRKaalEEVERLKAKAEEAKRQKELAEKEAER 2636
Cdd:pfam01576 1014 ERRHADQYK---DQAEKGNSRMKQLKRQLEEAEEEASR 1048
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
760-862 |
9.62e-08 |
|
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and similar proteins; Drosophila melanogaster filamin-A (dFLNA or dFLN-A), also called actin-binding protein 280 (ABP-280) or filamin-1, is involved in germline ring canal formation. It may tether actin microfilaments within the ovarian ring canal to the cell membrane and contributes to actin microfilament organization. dFLNA contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409164 Cd Length: 118 Bit Score: 54.02 E-value: 9.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 760 QSEDMTAKEKLLLWSQRMTEGyqgLHCDNFTTSWRDGRLFNAIIHRHKPVLI-DMNKVYRQTNLENLDQAFNVAERDLGV 838
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 1835643837 839 TRLLDPEDVDVPQPDEKSIITYVS 862
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2014-2593 |
9.70e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 58.89 E-value: 9.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2014 EQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEeihiVRLQLETMQKHKANA--EDELQELRARaekaEQQK 2091
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLERAQTEEAQAkqDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2092 KAAQEEAERLRKQVKDETQKKREAEEELK------RKVQAEKEA-AREKQRAVEDLEKFRSQAEEAERRMKQAEVEkerQ 2164
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKsvkeelESLRKEYASlVSERDIAIKRAEEAVSASKEIEKTVEELTIE---L 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2165 IKVAQEV-AQQSAAAELNSKRMSFA----EKTAQLELSLKQehitvthLQEEAERLKKlhdeAEKAREEAEKELEkwhqk 2239
Cdd:pfam05701 190 IATKESLeSAHAAHLEAEEHRIGAAlareQDKLNWEKELKQ-------AEEELQRLNQ----QLLSAKDLKSKLE----- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2240 ANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTeesALRQKELAEDELEKQRKLADATAQQKFSAEqelir 2319
Cdd:pfam05701 254 TASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAAL---ASAKKELEEVKANIEKAKDEVNCLRVAAAS----- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2320 LKAETENSEQQRLlleeelfrlknevneAIQKRKEM--------EEELAKVRAEMEiLLQSKsraEEESRsntEKSKQMl 2391
Cdd:pfam05701 326 LRSELEKEKAELA---------------SLRQREGMasiavsslEAELNRTKSEIA-LVQAK---EKEAR---EKMVEL- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2392 eveASKLRELAEEAaklravsEEAKRQRQIAEDEAARQRAEAErilKEKLAAINDATRLkteaEIALKEKEAENERlRRL 2471
Cdd:pfam05701 383 ---PKQLQQAAQEA-------EEAKSLAQAAREELRKAKEEAE---QAKAAASTVESRL----EAVLKEIEAAKAS-EKL 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2472 AEDEAyqRKLLEEQATQHKQDIE--EKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEirilKVNFEKASVGKSdlele 2549
Cdd:pfam05701 445 ALAAI--KALQESESSAESTNQEdsPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVS----QIEEAKESELRS----- 513
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1835643837 2550 LNQLKNIAEETQRSKEK---AEQEAEKQR--QLALEEEQRRKEAEEKVR 2593
Cdd:pfam05701 514 LEKLEEVNREMEERKEAlkiALEKAEKAKegKLAAEQELRKWRAEHEQR 562
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2727-2978 |
1.18e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 58.24 E-value: 1.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2727 AQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTL 2806
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2807 LDEELQRLKEEVTDAMRqKAQveeelfkvkiQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLS 2886
Cdd:COG4942 95 LRAELEAQKEELAELLR-ALY----------RLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2887 IEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGF 2966
Cdd:COG4942 164 ALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
250
....*....|..
gi 1835643837 2967 QKSLEAERRQQL 2978
Cdd:COG4942 244 PAAGFAALKGKL 255
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1906-2106 |
1.25e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.85 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1906 KVQSTSDSIIQEYVDLRTRYSELTTL---TSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHA 1982
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1983 KAKAQAEKEAEELQRRMQEEVSKRevvAVDAEQQKQTiQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQ 2062
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPAR---REQAEELRAD-LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1835643837 2063 LETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVK 2106
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2269-2632 |
1.32e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.34 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2269 EDAEREARKRAKteESALRQKELaEDELEKQRKLADATAQQKFSAEQELirlkaETENSEQQRLLLEEELFRLKNEvnEA 2348
Cdd:pfam02029 5 EEAARERRRRAR--EERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSEL-----KPSGQGGLDEEEAFLDRTAKRE--ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2349 IQKRKEMEEElakvraemeillqsksRAEEESRSNTEKSKQMleveASKLRELAEEAAKlrAVSEEAKRQRQIAEDEAA- 2427
Cdd:pfam02029 75 RQKRLQEALE----------------RQKEFDPTIADEKESV----AERKENNEEEENS--SWEKEEKRDSRLGRYKEEe 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2428 ---RQRAEAERILKEKLAAINDatrlkTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQatqhKQDIEEKIILLKKSS 2504
Cdd:pfam02029 133 teiREKEYQENKWSTEVRQAEE-----EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEK----KVKYESKVFLDQKRG 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2505 DNELERQkNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELElnqlKNIAEETQRSKEKAEQEAEKQRQ------LA 2578
Cdd:pfam02029 204 HPEVKSQ-NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAE----QKLEELRRRRQEKESEEFEKLRQkqqeaeLE 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2579 LEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEK 2632
Cdd:pfam02029 279 LEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2045-2307 |
1.35e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2045 VEYNR------RKIEEEihivrlqletmqKHKANAEDELQELR-ARAEKAEQQKKA-AQEEAERLRKQVKDETQkkrEAE 2116
Cdd:PRK05035 428 VQYYRqakaeiRAIEQE------------KKKAEEAKARFEARqARLEREKAAREArHKKAAEARAAKDKDAVA---AAL 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2117 EELKRKVQAEKEAAREKQRAVEDlekfRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRmSFAEKTAQLEL 2196
Cdd:PRK05035 493 ARVKAKKAAATQPIVIKAGARPD----NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIAR-AKAKKAAQQAA 567
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2197 SLKQEHITVTHLQEEAERL-----KKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDA 2271
Cdd:PRK05035 568 NAEAEEEVDPKKAAVAAAIarakaKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA 647
|
250 260 270
....*....|....*....|....*....|....*.
gi 1835643837 2272 EREARKRAKTEESALRQKELAEDELEKQRKLADATA 2307
Cdd:PRK05035 648 VAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAA 683
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1711-2366 |
1.36e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.03 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1711 EDQLKEVHAVPSDSKELEATKAE-LKKLRSQVEGHQPLFNTLEADLNK-AKDVNEqmlrshserdvdLDRYREKVQQLL- 1787
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEkLSKLQSELESVSSLLNEAEGKNIKlSKDVSS------------LESQLQDTQELLq 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1788 -ERWQAILVQIDLRQRELDQLGRQLRYYRETyewlikwikDAKQRQE-QIQSVPItdsktmkeHLLQEKKLLDEIESNRD 1865
Cdd:pfam01576 479 eETRQKLNLSTRLRQLEDERNSLQEQLEEEE---------EAKRNVErQLSTLQA--------QLSDMKKKLEEDAGTLE 541
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1866 KVDECQKYAKQYIDAIKdyeLQLVTYKAQVEpvaspakkpKVQSTSDSIIQEY----VDLRTRYSELTTLTSQYIKFite 1941
Cdd:pfam01576 542 ALEEGKKRLQRELEALT---QQLEEKAAAYD---------KLEKTKNRLQQELddllVDLDHQRQLVSNLEKKQKKF--- 606
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1942 tlRRLNDEEKAAEKLKEEERRRlAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRR-----MQEEVSKREVVAVDA--- 2013
Cdd:pfam01576 607 --DQMLAEEKAISARYAEERDR-AEAEAREKETRALSLARALEEALEAKEELERTNKqlraeMEDLVSSKDDVGKNVhel 683
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2014 EQQKQTIQQELQQLRQnsdmeikskakQIEEVEYNRRKIEEeihiVRLQLE-TMQKHKANAEDELQelrARAEKAEQQKK 2092
Cdd:pfam01576 684 ERSKRALEQQVEEMKT-----------QLEELEDELQATED----AKLRLEvNMQALKAQFERDLQ---ARDEQGEEKRR 745
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2093 A-------AQEEAERLRKQVKDETQKKREAEEELK--------------------RKVQAE-KEAAREKQRAVEDLEKFR 2144
Cdd:pfam01576 746 QlvkqvreLEAELEDERKQRAQAVAAKKKLELDLKeleaqidaankgreeavkqlKKLQAQmKDLQRELEEARASRDEIL 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2145 SQAEEAERRMKQAEVE----------KERQIKVAQ--------EVAQQSA--AAELNSKRMSFAeKTAQLELSLKQEHIT 2204
Cdd:pfam01576 826 AQSKESEKKLKNLEAEllqlqedlaaSERARRQAQqerdeladEIASGASgkSALQDEKRRLEA-RIAQLEEELEEEQSN 904
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2205 VTHLQEEAERLKKLHDEAEKAREEAEKELEKWH------QKANEALRLRLQAEEVA----HKKTLAQEEA--EKQKEDAE 2272
Cdd:pfam01576 905 TELLNDRLRKSTLQVEQLTTELAAERSTSQKSEsarqqlERQNKELKAKLQEMEGTvkskFKSSIAALEAkiAQLEEQLE 984
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2273 REARKRAKTEEsALRQKELAEDEL----EKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEA 2348
Cdd:pfam01576 985 QESRERQAANK-LVRRTEKKLKEVllqvEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQRELDDA 1063
|
730
....*....|....*...
gi 1835643837 2349 IQKRKEMEEELAKVRAEM 2366
Cdd:pfam01576 1064 TESNESMNREVSTLKSKL 1081
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2005-2323 |
1.37e-07 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2005 KREVVAVDAEQQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARA 2084
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2085 EKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQ 2164
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2165 IKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEAL 2244
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2245 RLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAE 2323
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6388-6490 |
1.40e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 53.10 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6388 QFSESQRLLLDWMEEVELTLEKQvDSSQSQDDIKQQLADHKEFQKVLRTKRPVYEATLRNGRSLREKAqlPEDVQKLDEL 6467
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEG--HPDAEEIEER 78
|
90 100
....*....|....*....|...
gi 1835643837 6468 LGELKEKWDLVCWKSTERQHKLE 6490
Cdd:smart00150 79 LEELNERWEELKELAEERRQKLE 101
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2081-2274 |
1.44e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 58.42 E-value: 1.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2081 RARAEKAEQQkkaaQEEAERLRKQvkdETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVE 2160
Cdd:pfam15709 337 RLRAERAEMR----RLEVERKRRE---QEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2161 KERQIKVAQEVAQQsaaaelnsKRMSFAEKTAQLELSLKQEHitVTHLQEEAERLKKLH-----DEAEKAREEAEKELEK 2235
Cdd:pfam15709 410 QRLQLQAAQERARQ--------QQEEFRRKLQELQRKKQQEE--AERAEAEKQRQKELEmqlaeEQKRLMEMAEEERLEY 479
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1835643837 2236 WHQKANEALRLRLQAEEVAHKKT----LAQEEAEKQKEDAERE 2274
Cdd:pfam15709 480 QRQKQEAEEKARLEAEERRQKEEeaarLALEEAMKQAQEQARQ 522
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2569-3016 |
1.77e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 58.13 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2569 QEAEKQRQLALEEEQRRKEAEEKvrKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKK 2648
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAE--KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2649 IDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQ 2728
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2729 AKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLD 2808
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2809 EELQRLKEEVTDAMRQKAQVEE--ELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLS 2886
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGaaLAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2887 IEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGF 2966
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2967 QKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIG 3016
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLV 449
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2808-3014 |
1.83e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.53 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2808 DEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLiMKDKDSTQKLLVEEAEKMRQVAEEAARLSI 2887
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2888 EAQEAARMRKLAE--------DDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQL 2959
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2960 AKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEE 3014
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
760-867 |
2.07e-07 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 52.79 E-value: 2.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 760 QSEDMTAKEKLLLWSQRMTEGyqgLHCDNFTTSWRDGRLFNAIIHRHKPVLI-DMNKVYRQTNLENLDQAFNVAERDLGV 838
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1835643837 839 TRLLDPEDVDVPQPDEKSIITYVSSMYDA 867
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2419-2609 |
2.20e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 57.87 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2419 RQIAEDEAARQRAEAERILKEklaAINDATRLKTEAEIALKEkeaENERLRRLAEDEAYQRKL----LEEQATQHKQDIE 2494
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEE---AKKEAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNelqkLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2495 EKIILLKKSsDNELERQKNIVEdtlrqrriieeeirILKVNFEKASVGKSDLELELNQ-LKNIA-----EETQRSKEKAE 2568
Cdd:PRK12704 100 RKLELLEKR-EEELEKKEKELE--------------QKQQELEKKEEELEELIEEQLQeLERISgltaeEAKEILLEKVE 164
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1835643837 2569 QEA--EKQRQLALEEEQRRKEAEEKVRKILADekeaARQRKAA 2609
Cdd:PRK12704 165 EEArhEAAVLIKEIEEEAKEEADKKAKEILAQ----AIQRCAA 203
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4756-4784 |
2.22e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 50.40 E-value: 2.22e-07
10 20
....*....|....*....|....*....
gi 1835643837 4756 IVDPETGKEMSVYEAYRKGLIDQQTYTEL 4784
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
765-862 |
2.36e-07 |
|
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409163 Cd Length: 115 Bit Score: 52.77 E-value: 2.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 765 TAKEKLLLWSQRMTEGyqgLHCDNFTTSWRDGRLFNAIIHRHKPVLI-DMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 843
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90
....*....|....*....
gi 1835643837 844 PEDVDVPQPDEKSIITYVS 862
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLS 106
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2071-2901 |
2.38e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.43 E-value: 2.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2071 ANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAV---EDLEKFRSQA 2147
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTALrqqEKIERYQEDL 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2148 EEAERRMK-QAEVEKERQIKVAQEVAQQSAA-AELNSKRMSFAEKTAQLELSLK---QEHITVTHLqEEAERLKKLHDEA 2222
Cdd:COG3096 357 EELTERLEeQEEVVEEAAEQLAEAEARLEAAeEEVDSLKSQLADYQQALDVQQTraiQYQQAVQAL-EKARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2223 EKAreeaekeLEKWHQ----KANEALRLRLQAEevaHKKTLAqEEAEKQKEDA-----------ERE-ARKRAKteeSAL 2286
Cdd:COG3096 436 PEN-------AEDYLAafraKEQQATEEVLELE---QKLSVA-DAARRQFEKAyelvckiagevERSqAWQTAR---ELL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2287 R----QKELAEDELEKQRKLADAtaQQKFSAEQELIRLKaetenseqqrllleeelfrlkNEVNEAIQKRKEMEEELAKV 2362
Cdd:COG3096 502 RryrsQQALAQRLQQLRAQLAEL--EQRLRQQQNAERLL---------------------EEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2363 RAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKR-QRQIAE--------DEAARQRAEA 2433
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERlREQSGEaladsqevTAAMQQLLER 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2434 ER---ILKEKLAAINDatRLKTEAEIALKEKEAENERLRRLAE-------DEAYQRKLLEE------------------- 2484
Cdd:COG3096 639 EReatVERDELAARKQ--ALESQIERLSQPGGAEDPRLLALAErlggvllSEIYDDVTLEDapyfsalygparhaivvpd 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2485 -----QATQHKQDIEEKIILLKKSSD---------NELERqKNIVEDTLRQRRIIEEEIRILkvnFEKASVGK--SDLEL 2548
Cdd:COG3096 717 lsavkEQLAGLEDCPEDLYLIEGDPDsfddsvfdaEELED-AVVVKLSDRQWRYSRFPEVPL---FGRAAREKrlEELRA 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2549 ELNQL-KNIAE------ETQRSKEKAEQEAEKQRQLALEEE---------QRRKEAE---EKVRKILADEKEAARQRKAA 2609
Cdd:COG3096 793 ERDELaEQYAKasfdvqKLQRLHQAFSQFVGGHLAVAFAPDpeaelaalrQRRSELErelAQHRAQEQQLRQQLDQLKEQ 872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2610 LEEVERL------------KAKAEEAKRQKELAEkEAERQIQLAQEAALK---KIDA--EEKAHTAIVQQKEQEMLQTRK 2672
Cdd:COG3096 873 LQLLNKLlpqanlladetlADRLEELREELDAAQ-EAQAFIQQHGKALAQlepLVAVlqSDPEQFEQLQADYLQAKEQQR 951
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2673 QEQSILDKLKEEAERakRAAEDADFARTRAEQEAALS---RQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRkeAELEAA 2749
Cdd:COG3096 952 RLKQQIFALSEVVQR--RPHFSYEDAVGLLGENSDLNeklRARLEQAEEARREAREQLRQAQAQYSQYNQVL--ASLKSS 1027
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2750 KRAHAEQ-AALKQ--KQL---ADEEMdkhkkfAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMR 2823
Cdd:COG3096 1028 RDAKQQTlQELEQelEELgvqADAEA------EERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAER 1101
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2824 QKAQVEEELFKVKIQMEELIKLklrieeenkmliMKDKD-----STQKLLVEEAEKMRQVAEE---AARLSIEAQEAAR- 2894
Cdd:COG3096 1102 DYKQEREQVVQAKAGWCAVLRL------------ARDNDverrlHRRELAYLSADELRSMSDKalgALRLAVADNEHLRd 1169
|
....*..
gi 1835643837 2895 MRKLAED 2901
Cdd:COG3096 1170 ALRLSED 1176
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2459-2692 |
2.63e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.78 E-value: 2.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2459 KEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILlkkssdnELERQKNIVEDTLRQRRIIEEeirilkvnfEK 2538
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA-------EQARQKELEQRAAAEKAAKQA---------EQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2539 ASVGKSDLELELNQLKNIAEETQrsKEKAEQEAEKQRQLAL----EEEQRRKEAEEKVRKILADEKEAARQRKAAlEEVE 2614
Cdd:TIGR02794 110 AAKQAEEKQKQAEEAKAKQAAEA--KAKAEAEAERKAKEEAakqaEEEAKAKAAAEAKKKAEEAKKKAEAEAKAK-AEAE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2615 RlKAKAEEAKRQKELAEK--EAERQIQLAQEAALK-KIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRA 2691
Cdd:TIGR02794 187 A-KAKAEEAKAKAEAAKAkaAAEAAAKAEAEAAAAaAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYA 265
|
.
gi 1835643837 2692 A 2692
Cdd:TIGR02794 266 A 266
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2582-2799 |
2.96e-07 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 56.91 E-value: 2.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2582 EQRRKEAEEKVrkiladeKEAARQRKAALEEVErlKAKAEEAKRQKElaeKEAERQIQLAQEAALKKIDAEEKAHTAIVQ 2661
Cdd:PRK07735 8 EDLKKEAARRA-------KEEARKRLVAKHGAE--ISKLEEENREKE---KALPKNDDMTIEEAKRRAAAAAKAKAAALA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2662 qkeqemlqtRKQEQSILDKLKEEAERAKRAAEDAdfARTRAeqeAALSRQQVEEAErlkqRAEEEAQAKAQAQDEAEKLR 2741
Cdd:PRK07735 76 ---------KQKREGTEEVTEEEKAKAKAKAAAA--AKAKA---AALAKQKREGTE----EVTEEEKAAAKAKAAAAAKA 137
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2742 KEAELEAAKRAHAEQAAlKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEE 2799
Cdd:PRK07735 138 KAAALAKQKREGTEEVT-EEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEE 194
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2626-2926 |
3.00e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.78 E-value: 3.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2626 QKELAEKEAERQIQLAQEAALKKIDAEEKAhtaivQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEdadfartrAEQE 2705
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKL-----EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ--------AEQA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2706 AALSRQQVEEAERLKQRAEEEAQAKAQAQDE---AEKLRKEAELEAAKRAhAEQAALKQKQLADEEMDKHKKFAEKtlrq 2782
Cdd:TIGR02794 111 AKQAEEKQKQAEEAKAKQAAEAKAKAEAEAErkaKEEAAKQAEEEAKAKA-AAEAKKKAEEAKKKAEAEAKAKAEA---- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2783 ksqveqeltkvklqleetdhqktlldeelqrlkeevtdamRQKAQVEEELFKVKIQMEeliklklrieeenkmlimkdkd 2862
Cdd:TIGR02794 186 ----------------------------------------EAKAKAEEAKAKAEAAKA---------------------- 203
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2863 stqKLLVEEAEKMRQVAEEAARLsiEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASR 2926
Cdd:TIGR02794 204 ---KAAAEAAAKAEAEAAAAAAA--EAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVD 262
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2935-3063 |
3.26e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 57.72 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2935 QKQKELAQEQA-RKFQEDKEQIEQQLAKEtegfQKSLEAERRQQLEitAEAERLKLQVLEMSRAQAKAEEDASKFKKKAE 3013
Cdd:PTZ00491 662 KSQEAAARHQAeLLEQEARGRLERQKMHD----KAKAEEQRTKLLE--LQAESAAVESSGQSRAEALAEAEARLIEAEAE 735
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 3014 eignkLHQTEL-ATKERMAVVQTLEIQRQQsgKEAE-ELRRAIAELEHEKEK 3063
Cdd:PTZ00491 736 -----VEQAELrAKALRIEAEAELEKLRKR--QELElEYEQAQNELEIAKAK 780
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2547-2693 |
3.44e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 56.80 E-value: 3.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2547 ELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQ 2626
Cdd:COG2268 231 EREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADV 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2627 KELAEKEAERQIQLAqEAALKKIDAEEKAHtAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAE 2693
Cdd:COG2268 311 RKPAEAEKQAAEAEA-EAEAEAIRAKGLAE-AEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAK 375
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2031-2217 |
3.65e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2031 SDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKD--- 2107
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2108 ETQKKREAE------------EELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEaerrmKQAEVEKERQIKVAQEVAQQS 2175
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA-----KKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1835643837 2176 AAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKK 2217
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA 210
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2016-2214 |
3.71e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.39 E-value: 3.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2016 QKQTIQQELQQLRQNsdmEIKSKAKQIEeveynrRKIEEEIhivrlQLETMQKHKANAEDELQELRARAEKAEQQKKAAQ 2095
Cdd:TIGR02794 44 DPGAVAQQANRIQQQ---KKPAAKKEQE------RQKKLEQ-----QAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2096 EeaerlRKQVKDetqkKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQS 2175
Cdd:TIGR02794 110 A-----AKQAEE----KQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAK 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 1835643837 2176 AAAElnskrmsFAEKTAQLELSLKQEHITVTHLQEEAER 2214
Cdd:TIGR02794 181 AKAE-------AEAKAKAEEAKAKAEAAKAKAAAEAAAK 212
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1958-2176 |
4.08e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.88 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1958 EEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKeaeelQRRMQEEVSKREvvavdAEQQKQTIQQELQQLRQnsdMEiks 2037
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRAERAE-----MRRLEVERKRRE-----QEEQRRLQQEQLERAEK---MR--- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2038 kakqiEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDElqelRARAEKAEQQKKAAQEEA------ERLRKQVKDETQK 2111
Cdd:pfam15709 376 -----EELELEQQRRFEEIRLRKQRLEEERQRQEEEERK----QRLQLQAAQERARQQQEEfrrklqELQRKKQQEEAER 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2112 kreAEEELKRKVQAEKEAAREKQRAV-----EDLEKFRSQAEEAERRMKQAE---VEKERQIKVAQEVAQQSA 2176
Cdd:pfam15709 447 ---AEAEKQRQKELEMQLAEEQKRLMemaeeERLEYQRQKQEAEEKARLEAEerrQKEEEAARLALEEAMKQA 516
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6498-6599 |
4.16e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 51.56 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6498 KFTDALQALMDWLYWAEPQLSEDvPIRGDKDLVSDLMDKHKIFQKELGKRASCVKTLKRSMRDLTRGSIStDSQWLQKQM 6577
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASE-DLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1835643837 6578 EELNHRWEVVCKLSVGKQARLE 6599
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2062-2463 |
4.17e-07 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 56.97 E-value: 4.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2062 QLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKRE--AEEELKRKVQAEKEAAREKQRAVED 2139
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAelAAEAAKKLAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2140 LEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLH 2219
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2220 DEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQ 2299
Cdd:COG3064 177 GAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2300 RKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEE 2379
Cdd:COG3064 257 VGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAAS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2380 SRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALK 2459
Cdd:COG3064 337 LEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAAS 416
|
....
gi 1835643837 2460 EKEA 2463
Cdd:COG3064 417 AVEL 420
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2865-3088 |
4.67e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.01 E-value: 4.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2865 QKLLVEEAEKMRQVAEEAARLSIEAQEAARMRK--LAEDDLANQRALAEkmLKEKMQAIQEAsrlkAEAEMLQKQKELAQ 2942
Cdd:TIGR02794 45 PGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAeeAEKQRAAEQARQKE--LEQRAAAEKAA----KQAEQAAKQAEEKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2943 EQARKfQEDKEQIEQQLAKETEGFQKSLEAERRQqleitAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQT 3022
Cdd:TIGR02794 119 KQAEE-AKAKQAAEAKAKAEAEAERKAKEEAAKQ-----AEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAE 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 3023 ELATKERMAVvqtlEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQ 3088
Cdd:TIGR02794 193 EAKAKAEAAK----AKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2455-2875 |
5.12e-07 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 56.50 E-value: 5.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2455 EIALKEKEAENERLRRLAEDEAYQR--KLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLrqRRIIEEEIRIL 2532
Cdd:COG5185 130 IVALKDELIKVEKLDEIADIEASYGevETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELK--KAEPSGTVNSI 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2533 KVNFEKASVGKSDLELELNQLKNIaEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAAR----QRKA 2608
Cdd:COG5185 208 KESETGNLGSESTLLEKAKEIINI-EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKrlneNANN 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2609 ALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAEra 2688
Cdd:COG5185 287 LIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE-- 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2689 kraaedadfaRTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAeLEAAKRAHAEQAALKQKQLAD-- 2766
Cdd:COG5185 365 ----------NIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT-LEDTLKAADRQIEELQRQIEQat 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2767 ---EEMDKHKKFAEKTLRQKSQVEQELTKVKLQlEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELI 2843
Cdd:COG5185 434 ssnEEVSKLLNELISELNKVMREADEESQSRLE-EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQL 512
|
410 420 430
....*....|....*....|....*....|..
gi 1835643837 2844 KlKLRIEEENKMLIMKDKDSTQKLLVEEAEKM 2875
Cdd:COG5185 513 E-GVRSKLDQVAESLKDFMRARGYAHILALEN 543
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2991-3247 |
5.26e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 55.99 E-value: 5.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2991 VLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAEL 3070
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3071 LQKNSQKMQVAQQEQLRQET---QVLQTTFLSEkqlLLEREKYIEeekaKLENLYEDEVRKAQKLKQEQEHQMKHLEEEK 3147
Cdd:COG3883 84 RREELGERARALYRSGGSVSyldVLLGSESFSD---FLDRLSALS----KIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3148 DQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDLAGN 3227
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
250 260
....*....|....*....|
gi 1835643837 3228 LPLTPTVVTQTKAMPNGRDA 3247
Cdd:COG3883 237 AAAAAAAASAAGAGAAGAAG 256
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2076-2732 |
5.43e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.67 E-value: 5.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2076 ELQELRARAEKAEQQKKaaQEEAERLRKQVkdETQKKREAeeeLKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAerrmk 2155
Cdd:pfam05557 3 ELIESKARLSQLQNEKK--QMELEHKRARI--ELEKKASA---LKRQLDRESDRNQELQKRIRLLEKREAEAEEA----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2156 qaevekerqikvaqevaqqsaaaelnskrmsfaektaqlelslkqehitvthLQEEAERLKKLhdeaekareeaEKELEK 2235
Cdd:pfam05557 71 ----------------------------------------------------LREQAELNRLK-----------KKYLEA 87
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2236 WHQKANEALRLRLQAEEVAHKKTlaqeeaekqkeDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQkfsAEQ 2315
Cdd:pfam05557 88 LNKKLNEKESQLADAREVISCLK-----------NELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASE---AEQ 153
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2316 ELIRLKAETEnseqqrllleeelfrlknEVNEAIQKRKEMEEELAKVRAEMEILlqSKSRAEEESRSNTEKSKQMLEVEA 2395
Cdd:pfam05557 154 LRQNLEKQQS------------------SLAEAEQRIKELEFEIQSQEQDSEIV--KNSKSELARIPELEKELERLREHN 213
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2396 SKLRELAEEAAKLRAVSEEAKR---QRQIAEDEAARQRAEAERILKE----KLAAINDATRLKTEAEIALKEKEAENERL 2468
Cdd:pfam05557 214 KHLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQElqswVKLAQDTGLNLRSPEDLSRRIEQLQQREI 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2469 RRLAEDEAYQRKLLEEQATQhKQDIEEKIILLKKSSD--NELERQKNIVEDTLRQRRIIEEEIRILKVNFE--------- 2537
Cdd:pfam05557 294 VLKEENSSLTSSARQLEKAR-RELEQELAQYLKKIEDlnKKLKRHKALVRRLQRRVLLLTKERDGYRAILEsydkeltms 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2538 KASVGKSDLELELNQL----KNIAEETQRSKEKAEQEAEKQRQLA----LEEEQRRKEAEEKVRKILADEKEAARQrkaa 2609
Cdd:pfam05557 373 NYSPQLLERIEEAEDMtqkmQAHNEEMEAQLSVAEEELGGYKQQAqtleRELQALRQQESLADPSYSKEEVDSLRR---- 448
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2610 leEVERLKAKAEEAKRQKELAEKEAERQiQLAQEAALKKidaeekahTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAK 2689
Cdd:pfam05557 449 --KLETLELERQRLREQKNELEMELERR-CLQGDYDPKK--------TKVLHLSMNPAAEAYQQRKNQLEKLQAEIERLK 517
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2690 RAAEDADFAR-----------TRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQ 2732
Cdd:pfam05557 518 RLLKKLEDDLeqvlrlpettsTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQ 571
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1953-2495 |
5.68e-07 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 56.58 E-value: 5.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1953 AEKLKEEERRRLAEVE--------AQLAKQTQLAEAhakAKAQAEKEAEELQRRMQE---EVSKREVVAVDAEQQKQTIQ 2021
Cdd:pfam05701 28 AHRIQTVERRKLVELElekvqeeiPEYKKQSEAAEA---AKAQVLEELESTKRLIEElklNLERAQTEEAQAKQDSELAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2022 QELQQLRQNSDMEIKSKAKQIEEVEYNRR-KIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAeqqkKAAQEEAEr 2100
Cdd:pfam05701 105 LRVEEMEQGIADEASVAAKAQLEVAKARHaAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEA----VSASKEIE- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2101 lrKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQaeeAERRMKQAEVEKER---QIKVAQEVAQQSAA 2177
Cdd:pfam05701 180 --KTVEELTIELIATKESLESAHAAHLEAEEHRIGAALAREQDKLN---WEKELKQAEEELQRlnqQLLSAKDLKSKLET 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2178 AELNSKRMSfAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKwhqKANEALRLRLQAEEVahkk 2257
Cdd:pfam05701 255 ASALLLDLK-AELAAYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEK---AKDEVNCLRVAAASL---- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2258 tlaqeeaekqKEDAEREarkraKTEESALRQKELA--------EDELEKQRkladataqqkfsaeQELIRLKAETENSEQ 2329
Cdd:pfam05701 327 ----------RSELEKE-----KAELASLRQREGMasiavsslEAELNRTK--------------SEIALVQAKEKEARE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2330 QRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEillQSKSRAEEESRSNTEKSKQMLEVEASklRELAEEAAKLR 2409
Cdd:pfam05701 378 KMVELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAE---QAKAAASTVESRLEAVLKEIEAAKAS--EKLALAAIKAL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2410 AVSEEAKRQRQIAE------------DEAARQRAEAERILKEKLAAINdatrlkTEAEIAlkeKEAENERLRRLAEdeay 2477
Cdd:pfam05701 453 QESESSAESTNQEDsprgvtlsleeyYELSKRAHEAEELANKRVAEAV------SQIEEA---KESELRSLEKLEE---- 519
|
570
....*....|....*...
gi 1835643837 2478 qrklLEEQATQHKQDIEE 2495
Cdd:pfam05701 520 ----VNREMEERKEALKI 533
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2597-3000 |
6.04e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.41 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2597 ADEKEAARqrkaaleevERLKAKAEEAKRQKELAEKEAErqiqlaqeaalkkidaeekahtaiVQQKEQEmlqtrkQEQS 2676
Cdd:pfam02029 2 EDEEEAAR---------ERRRRAREERRRQKEEEEPSGQ------------------------VTESVEP------NEHN 42
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2677 ILDKLKEEAERAKRAAEdadfartraEQEAALSRQQVEEAERlkQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQ 2756
Cdd:pfam02029 43 SYEEDSELKPSGQGGLD---------EEEAFLDRTAKREERR--QKRLQEALERQKEFDPTIADEKESVAERKENNEEEE 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2757 AALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVK 2836
Cdd:pfam02029 112 NSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVK 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2837 IQMEELIKLKLRIEEEN----KMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEddlaNQRALAEK 2912
Cdd:pfam02029 192 YESKVFLDQKRGHPEVKsqngEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQE----KESEEFEK 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2913 MLKEKMQAIQEASRLKAEAEmlQKQKELAQEQARKFQEDKeqiEQQLAKETEGFQKSLEAERRQqleitAEAERLKLQVL 2992
Cdd:pfam02029 268 LRQKQQEAELELEELKKKRE--ERRKLLEEEEQRRKQEEA---ERKLREEEEKRRMKEEIERRR-----AEAAEKRQKLP 337
|
....*...
gi 1835643837 2993 EMSRAQAK 3000
Cdd:pfam02029 338 EDSSSEGK 345
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2904-3131 |
6.60e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2904 ANQRALAEKMLKEKMQAIQEasrlkaeaemLQKQKELAQEQARKFQEDKEQIEQQLAKEtegfQKSLEAERRQQLEITAE 2983
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE----------LEKELAALKKEEKALLKQLAALERRIAAL----ARRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2984 AERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNK------LHQTELATKERMA-VVQTLEIQRQQsgkEAEELRRAIAE 3056
Cdd:COG4942 85 LAELEKEIAELRAELEAQKEELAELLRALYRLGRQpplallLSPEDFLDAVRRLqYLKYLAPARRE---QAEELRADLAE 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 3057 LEHEKEKLKREAELLQKNSQKMQVAQQ--EQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQK 3131
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAalEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2547-2688 |
6.64e-07 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 53.94 E-value: 6.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2547 ELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEK-EAARQRKAALEEVERLKAKAEEAKR 2625
Cdd:pfam13904 43 KLEGLKLERQPLEAYENWLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKyQEWLQRKARQQTKKREESHKQKAAE 122
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2626 QKELAEKEAERQIqlAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERA 2688
Cdd:pfam13904 123 SASKSLAKPERKV--SQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2063-2489 |
6.68e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 56.07 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2063 LETMQKHKANAEDELQELRARAEKAEQQkkaaQEEAERLRKQVkdeTQKKREAEEELKRKVQAEKEAAREKQRAVEDLEK 2142
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQ----QARLDELEALI---DQWLAELEQVIALRRAGGLEAALALVRSGEGKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2143 FRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEA 2222
Cdd:COG5278 151 MDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2223 EKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKL 2302
Cdd:COG5278 231 ALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2303 ADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRS 2382
Cdd:COG5278 311 AAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVEL 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2383 NTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKE 2462
Cdd:COG5278 391 EVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAA 470
|
410 420
....*....|....*....|....*..
gi 1835643837 2463 AENERLRRLAEDEAYQRKLLEEQATQH 2489
Cdd:COG5278 471 VAALAALAAAAAALAEAEAAAALAAAA 497
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2238-2498 |
7.01e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.62 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2238 QKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAErEARKRAKTEESALRQKELAEdeleKQRKLADATAQQKFSAEQEL 2317
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAE-KQRAAEQARQKELEQRAAAE----KAAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2318 IRLKAETENSEQQRLlleeelfrlknevnEAIQKRKEMEEelAKVRAEMEillqSKSRAEEESRSNTEKSKQMLEVEAsK 2397
Cdd:TIGR02794 122 EEAKAKQAAEAKAKA--------------EAEAERKAKEE--AAKQAEEE----AKAKAAAEAKKKAEEAKKKAEAEA-K 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2398 LRELAEEAAKLRAVSEEAKRQRQIAEDEAARqRAEAERILKEKLAAINDATRLKTEAEIAL-KEKEAENERLRRLAEDEA 2476
Cdd:TIGR02794 181 AKAEAEAKAKAEEAKAKAEAAKAKAAAEAAA-KAEAEAAAAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAAAGS 259
|
250 260
....*....|....*....|..
gi 1835643837 2477 YQRKLleeqATQHKQDIEEKII 2498
Cdd:TIGR02794 260 EVDKY----AAIIQQAIQQNLY 277
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1943-2136 |
7.93e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 7.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1943 LRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQ 2022
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2023 ELQQLRQNSDME------------------------IKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQ 2078
Cdd:COG4942 109 LLRALYRLGRQPplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2079 ELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRA 2136
Cdd:COG4942 189 ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2753-3187 |
8.09e-07 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 56.17 E-value: 8.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2753 HAEQAALKQKQLADEEMDKHKKFAEKTLrqKSQVEQELTKVKLQLEETDHQKTL-LDEELQRLKEEVtdamrqkaqveee 2831
Cdd:NF033838 36 HAEEVRGGNNPTVTSSGNESQKEHAKEV--ESHLEKILSEIQKSLDKRKHTQNVaLNKKLSDIKTEY------------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2832 lfkvkiqMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKlaEDDLANQRALAE 2911
Cdd:NF033838 101 -------LYELNVLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQK--EEDRRNYPTNTY 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2912 KMLKEKmqaIQEASRLKAEAEMlqkqkELAQEQARKFQeDKEQIEQQLAKetegfqksLEAERrqqleitAEAERLKLQV 2991
Cdd:NF033838 172 KTLELE---IAESDVEVKKAEL-----ELVKEEAKEPR-DEEKIKQAKAK--------VESKK-------AEATRLEKIK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2992 LEMSRAQAKAEEDA-SKFKKKAEEIGNKLHQTELATKERMAVVQTL------EIQRQQSGKEAEELRRAIAELEHEKEKl 3064
Cdd:NF033838 228 TDREKAEEEAKRRAdAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPatpdkkENDAKSSDSSVGEETLPSPSLKPEKKV- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3065 kREAELLQKNSQKMQVAQQEQLRQETQVlqTTFlseKQLLLE-REKYIEEEKAKLENLYED--EVRKAQKLKQEQEHqmk 3141
Cdd:NF033838 307 -AEAEKKVEEAKKKAKDQKEEDRRNYPT--NTY---KTLELEiAESDVKVKEAELELVKEEakEPRNEEKIKQAKAK--- 377
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1835643837 3142 hlEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEK 3187
Cdd:NF033838 378 --VESKKAEATRLEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQ 421
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3006-3228 |
8.50e-07 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 56.10 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3006 SKFKKKAEEIGNKLHQTElatkERMAVVQTL--EIQRQQS--GKEAEELRRAiAELEHEKEKLKREAELLQKNSQKmqvA 3081
Cdd:COG1196 168 SKYKERKEEAERKLEATE----ENLERLEDIlgELERQLEplERQAEKAERY-RELKEELKELEAELLLLKLRELE---A 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3082 QQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLyEDEVRKAQKLKQEQEHQMKHLEEEKDQLKvsmddamKKQ 3161
Cdd:COG1196 240 ELEELEAELEELEAELEELEAELAELEAELEELRLELEEL-ELELEEAQAEEYELLAELARLEQDIARLE-------ERR 311
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 3162 KEAEENVRRKQDELQQLDKKRQEQEklladenrklrEKLEQMEEEHRIALAQTREMRTQTDDLAGNL 3228
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELE-----------EELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
|
| EF-hand_7 |
pfam13499 |
EF-hand domain pair; |
6876-6939 |
8.57e-07 |
|
EF-hand domain pair;
Pssm-ID: 463900 [Multi-domain] Cd Length: 67 Bit Score: 49.56 E-value: 8.57e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 6876 KSRILDIFRSIDRDQDGRISQQEFIESV--LSSKFPTNSLEMNAVASIFDYNGDGFIDYYEFVSAL 6939
Cdd:pfam13499 1 EEKLKEAFKLLDSDGDGYLDVEELKKLLrkLEEGEPLSDEEVEELFKEFDLDKDGRISFEEFLELY 66
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2457-2701 |
8.65e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.16 E-value: 8.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2457 ALKEKEAENERLRRLAEDEAYQRKLLEEQATQHK------QDIEEKIILLKKSSdNELERQKNIVEDTLRQRRIIEeeir 2530
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKallkqlAALERRIAALARRI-RALEQELAALEAELAELEKEI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2531 ilkvnfekasvgkSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAAL 2610
Cdd:COG4942 93 -------------AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2611 EEVERLKAKAEEAKRQKE--LAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERA 2688
Cdd:COG4942 160 AELAALRAELEAERAELEalLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 1835643837 2689 KRAAEDADFARTR 2701
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2809-3024 |
9.68e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2809 EELQRLKEEVTDAMRQKAQVEeelFKVKIQMEELIKLKLRIEEENKmlimkdKDSTQKLLVEEAEKMrqvAEEAARLSIE 2888
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRK---KKEQQQAEELQQKQAAEQERLK------QLEKERLAAQEQKKQ---AEEAAKQAAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2889 AQeaarmrKLAEDDLANQRALAEKMLKEKMQAIQEASRlKAEAEmlQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQK 2968
Cdd:PRK09510 130 KQ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAE--AKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2969 ---SLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTEL 3024
Cdd:PRK09510 201 kkaEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1674-2142 |
1.12e-06 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 55.79 E-value: 1.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1674 QKMDQVYSLSSIYLEKLKTINlVIRSTQGAEEVVRTYEDQLKEVHAVPSDSKELEATKAELKKLRSQVEghqplfntlea 1753
Cdd:NF033838 85 QNVALNKKLSDIKTEYLYELN-VLKEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAE----------- 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1754 dlNKAKDVNEQMLRSH---SERDVDLDRYREKVQqllerwqailvqidLRQRELDQLGRQLRYYRETyewliKWIKDAKQ 1830
Cdd:NF033838 153 --KKAKDQKEEDRRNYptnTYKTLELEIAESDVE--------------VKKAELELVKEEAKEPRDE-----EKIKQAKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1831 RQEQIQSvpitdsktmkehllqEKKLLDEIESNRDKVDEcqkYAKQYIDA-IKDYELQLVTYKAQVEP-----------V 1898
Cdd:NF033838 212 KVESKKA---------------EATRLEKIKTDREKAEE---EAKRRADAkLKEAVEKNVATSEQDKPkrrakrgvlgeP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1899 ASPAKKPKVQSTSDSIIQEyvdlrtryselTTLTSQYI---KFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQlAKQT 1975
Cdd:NF033838 274 ATPDKKENDAKSSDSSVGE-----------ETLPSPSLkpeKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYK-TLEL 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1976 QLAEAHAKAK-AQAEKEAEELQRRMQEEVSKREVVAVDAEqqkqtiqqelqqlrqnsdmeiKSKAKQIEEVEYNRRKIEE 2054
Cdd:NF033838 342 EIAESDVKVKeAELELVKEEAKEPRNEEKIKQAKAKVESK---------------------KAEATRLEKIKTDRKKAEE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2055 EihivrlqletmQKHKANAEDELQELRARAEK---AEQQKKAAqEEAERLRKQVKDETQKKREAEEELKRKvqAEKEAAR 2131
Cdd:NF033838 401 E-----------AKRKAAEEDKVKEKPAEQPQpapAPQPEKPA-PKPEKPAEQPKAEKPADQQAEEDYARR--SEEEYNR 466
|
490
....*....|.
gi 1835643837 2132 EKQRAVEDLEK 2142
Cdd:NF033838 467 LTQQQPPKTEK 477
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2342-2598 |
1.13e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 55.60 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQK----RKEMEEElakvRAEMEILLQsksRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLR--AVSEEA 2415
Cdd:PRK00409 515 KEKLNELIASleelERELEQK----AEEAEALLK---EAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIkeAKKEAD 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2416 KRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKteaEIALKEKEAENERLRrlAEDEAYQRKLleeqatqhkqdiEE 2495
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAHELIEARKRLNKANEKK---EKKKKKQKEKQEELK--VGDEVKYLSL------------GQ 650
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2496 KIILLKKSSDNELERQKNIVEdtlrqrriieeeiriLKVNfekasvgksdleleLNQLKNIAEETQRSKEKAEQEAEKQR 2575
Cdd:PRK00409 651 KGEVLSIPDDKEAIVQAGIMK---------------MKVP--------------LSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
250 260
....*....|....*....|....*.
gi 1835643837 2576 QLALEEE---QRRKEAEEKVRKILAD 2598
Cdd:PRK00409 702 TVSLELDlrgMRYEEALERLDKYLDD 727
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2071-2313 |
1.13e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2071 ANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEA 2150
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2151 ERRMKQAevekERQIKVAQEVAQQSAAAELNSKRM---SFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKARE 2227
Cdd:COG3883 92 ARALYRS----GGSVSYLDVLLGSESFSDFLDRLSalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2228 EAEKELEKwHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATA 2307
Cdd:COG3883 168 AAKAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
....*.
gi 1835643837 2308 QQKFSA 2313
Cdd:COG3883 247 AGAGAA 252
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2927-3226 |
1.20e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 56.11 E-value: 1.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2927 LKAEAEMLQKQKELAQEQARkFQEDKEQIEQQlaketEGFQKSLEAErrqqleITAEAERLKLqVLEMSRAQAKAEedas 3006
Cdd:COG3096 288 LELRRELFGARRQLAEEQYR-LVEMARELEEL-----SARESDLEQD------YQAASDHLNL-VQTALRQQEKIE---- 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3007 KFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEEL---------------RRAIA------ELEhEKEKLK 3065
Cdd:COG3096 351 RYQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLksqladyqqaldvqqTRAIQyqqavqALE-KARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3066 REAELLQKNSQKMQVAQQEQLRQETQVLqttFLSEKQLLLEREKYIEEEKA-KLENLYEDEVRKAQKLKQEQE-----HQ 3139
Cdd:COG3096 430 GLPDLTPENAEDYLAAFRAKEQQATEEV---LELEQKLSVADAARRQFEKAyELVCKIAGEVERSQAWQTAREllrryRS 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3140 MKHLEEEKDQLKVSMDDAmKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRT 3219
Cdd:COG3096 507 QQALAQRLQQLRAQLAEL-EQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
....*..
gi 1835643837 3220 QTDDLAG 3226
Cdd:COG3096 586 QLEQLRA 592
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2865-3202 |
1.23e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.54 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2865 QKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQ 2944
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2945 ARKFQEDKEQIEQQLAKETEGFQKSLEAERRQqleitaEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIgnklhqtEL 3024
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKEL------EKEEEREEDERILEYLKEKAEREEEREAEREEI-------EE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3025 ATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQttflsekqll 3104
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKER---------- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3105 lEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAeenvrrKQDELQQLDKKRQE 3184
Cdd:pfam13868 251 -RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAE------REEELEEGERLREE 323
|
330
....*....|....*...
gi 1835643837 3185 QEKLLADENRKLREKLEQ 3202
Cdd:pfam13868 324 EAERRERIEEERQKKLKE 341
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3745-3781 |
1.23e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 1.23e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1835643837 3745 IRLLDAQLATGGIIDPVNSHRVPLDIAYKRGYLDEET 3781
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1961-2129 |
1.23e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.17 E-value: 1.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1961 RRRLAEVEAQLAKQT---QLAEAHAKAKA-------QAEKEAEELQRRMQEEVSKREvvaVDAEQQKQTIQQELQQLRqn 2030
Cdd:PRK12704 25 RKKIAEAKIKEAEEEakrILEEAKKEAEAikkeallEAKEEIHKLRNEFEKELRERR---NELQKLEKRLLQKEENLD-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2031 sdmeikskaKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQqkkAAQEEA-ERLRKQVKDET 2109
Cdd:PRK12704 100 ---------RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG---LTAEEAkEILLEKVEEEA 167
|
170 180
....*....|....*....|....*
gi 1835643837 2110 QKK-----REAEEELKRkvQAEKEA 2129
Cdd:PRK12704 168 RHEaavliKEIEEEAKE--EADKKA 190
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2898-3185 |
1.28e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 55.50 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2898 LAEDDLANQRALAEKMLKEKMQAiQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQ 2977
Cdd:pfam05483 65 LKDSDFENSEGLSRLYSKLYKEA-EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQEN 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2978 LEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAE-ELRRAIAE 3056
Cdd:pfam05483 144 KDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEK 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3057 LEHEKEKLKREAELLQKNSQKMQVAQQEQlrqETQVLQTTFLsekqlllerekyIEEEKAKLENLYEDEVRKAQKLKQEQ 3136
Cdd:pfam05483 224 IQHLEEEYKKEINDKEKQVSLLLIQITEK---ENKMKDLTFL------------LEESRDKANQLEEKTKLQDENLKELI 288
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1835643837 3137 EHQmKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQ 3185
Cdd:pfam05483 289 EKK-DHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQ 336
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2092-2521 |
1.29e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2092 KAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERqikVAQEV 2171
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK---LEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2172 AQQSAAAELNSKRMSFAEKTAQLElSLKQEHITVTHLQEEAERLKKlhdeaekareeaekELEKWHQKANEALRLRLQAE 2251
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEA--------------ELAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2252 EVAHKKTLAQ-EEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQrKLADATAQQKFSAEQELIRLKAETENSEQQ 2330
Cdd:COG4717 191 EEELQDLAEElEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2331 RLLLE----------------EELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVE 2394
Cdd:COG4717 270 SLILTiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2395 ASKLRELAEEAAKLRAVSEEAKRQ--------------RQIAEDEAARQRAEAERI-LKEKLAAINDATR--LKTEAEIA 2457
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAallaeagvedeeelRAALEQAEEYQELKEELEeLEEQLEELLGELEelLEALDEEE 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2458 LKEKEAENERLRRLAEDEayQRKLLEEQAtqhkqDIEEKIILLKKSSD-NELERQKNIVEDTLRQ 2521
Cdd:COG4717 430 LEEELEELEEELEELEEE--LEELREELA-----ELEAELEQLEEDGElAELLQELEELKAELRE 487
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2574-2826 |
1.29e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.77 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2574 QRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQkelaEKEAERQIQLAQEAALKKIDAEE 2653
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2654 KAHTAIVQQKEQEMLQTRK-QEQSILDKLKEEAerakrAAEDADFARTRAEQEAALSRQQVEEAERLKQRaeeeaqakaq 2732
Cdd:COG4942 94 ELRAELEAQKEELAELLRAlYRLGRQPPLALLL-----SPEDFLDAVRRLQYLKYLAPARREQAEELRAD---------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2733 aQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEEtdhqktlLDEELQ 2812
Cdd:COG4942 159 -LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE-------LEALIA 230
|
250
....*....|....
gi 1835643837 2813 RLKEEVTDAMRQKA 2826
Cdd:COG4942 231 RLEAEAAAAAERTP 244
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1949-2160 |
1.43e-06 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 55.01 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1949 EEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLR 2028
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2029 QNSDMEIKSKAKQIEEVEYNRRKieeeihivrlqletmqkhkanaedelqelraRAEKAEQQKKAAQEEAERLRKQVKDE 2108
Cdd:pfam05262 259 NLPKPADTSSPKEDKQVAENQKR-------------------------------EIEKAQIEIKKNDEEALKAKDHKAFD 307
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2109 TqkKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVE 2160
Cdd:pfam05262 308 L--KQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
2679-2798 |
1.45e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 54.88 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2679 DKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEA-------------QAKAQAQDEAEKLRKEAE 2745
Cdd:PRK12472 193 ETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELkradkalaaaktdEAKARAEERQQKAAQQAA 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2746 LEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKtlrqKSQVEQELTKVKLQLE 2798
Cdd:PRK12472 273 EAATQLDTAKADAEAKRAAAAATKEAAKAAAAK----KAETAKAATDAKLALE 321
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1954-2200 |
1.46e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 55.34 E-value: 1.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1954 EKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAvdAEQQKQTIQQELQQLRQNSDM 2033
Cdd:PRK05035 465 EKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIA--AREARKAQARARQAEKQAAAA 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2034 EIKSKAkqieeveynrrKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKA---EQQKKAAQEEAErlrkqvkDETQ 2110
Cdd:PRK05035 543 ADPKKA-----------AVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAiarAKAKKAAQQAAS-------AEPE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2111 KKREAEEELKRKVQAEKEAAREKQRAVEDLEKfRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEK 2190
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAE-PEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAA 683
|
250
....*....|
gi 1835643837 2191 TAQLELSLKQ 2200
Cdd:PRK05035 684 IARAKAKKAA 693
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2557-3004 |
1.47e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 55.05 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2557 AEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRqkelaekeAER 2636
Cdd:COG3064 41 EERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAA--------AEK 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2637 QIQLAQEAalKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEA 2716
Cdd:COG3064 113 AAAAAEKE--KAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2717 ERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQ 2796
Cdd:COG3064 191 EAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2797 LEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMR 2876
Cdd:COG3064 271 AAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2877 QVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIE 2956
Cdd:COG3064 351 AAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAA 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1835643837 2957 QQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEED 3004
Cdd:COG3064 431 GAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2714-2855 |
1.51e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 55.17 E-value: 1.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2714 EEAERLKQRAEEEAQ-----AKAQAQDEAEKLRKEAELEAAKR----AHAEQAALKQKQLADEEMDKHKKFAEKTLRQKS 2784
Cdd:PRK12704 38 EEAKRILEEAKKEAEaikkeALLEAKEEIHKLRNEFEKELRERrnelQKLEKRLLQKEENLDRKLELLEKREEELEKKEK 117
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2785 QVEQELTKVKLQLEETDHQKTLLDEELQRL----KEEVTDAMRQkaQVEEELfkvKIQMEELIKlklRIEEENKM 2855
Cdd:PRK12704 118 ELEQKQQELEKKEEELEELIEEQLQELERIsgltAEEAKEILLE--KVEEEA---RHEAAVLIK---EIEEEAKE 184
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
2711-2814 |
1.57e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 51.88 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2711 QQVEEAE-RLKQRAEEEAQAK---AQAQDEAEKLRKEAE-------LEAAKRAHAEQAALKQKQLADEEMDKHKKFAEkt 2779
Cdd:PRK07352 57 QALKEAEeRLRQAAQALAEAQqklAQAQQEAERIRADAKaraeairAEIEKQAIEDMARLKQTAAADLSAEQERVIAQ-- 134
|
90 100 110
....*....|....*....|....*....|....*...
gi 1835643837 2780 LRQKSqVEQELTKVKLQLEET---DHQKTLLDEELQRL 2814
Cdd:PRK07352 135 LRREA-AELAIAKAESQLPGRldeDAQQRLIDRSIANL 171
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2710-3093 |
1.59e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 54.15 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2710 RQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQe 2789
Cdd:pfam13868 2 RENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEE- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2790 ltkvklQLEETDHQKTLLDEELQRLKEEVTDAMRQkaqveeelfkvkIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLV 2869
Cdd:pfam13868 81 ------QIEEREQKRQEEYEEKLQEREQMDEIVER------------IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEW 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2870 EEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRAlaEKMLKEKMQAIQEasrlkaeaEMLQKQKELAQEQARKFQ 2949
Cdd:pfam13868 143 KELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE--KEREIARLRAQQE--------KAQDEKAERDELRAKLYQ 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2950 EDKEQIEQQLAKEtegfqkslEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEignklhQTELATKER 3029
Cdd:pfam13868 213 EEQERKERQKERE--------EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRK------QAEDEEIEQ 278
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 3030 MavvqTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVL 3093
Cdd:pfam13868 279 E----EAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2662-2961 |
1.70e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 54.27 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2662 QKEQEMLQTRKQEQSILDKLK-------EEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQR----AEEEAQAK 2730
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELRrrdqkrqETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRADRRekqvIEKESRWR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2731 AQAQDEaEKLRKeaelEAAKRAHAEQAALKQKQladEEMDKHKKFAEKTLRQksQVEQELTKvklQLEETDHQKTLLDEE 2810
Cdd:pfam15558 98 EQAEDQ-ENQRQ----EKLERARQEAEQRKQCQ---EQRLKEKEEELQALRE--QNSLQLQE---RLEEACHKRQLKERE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2811 LQRLKEEVTDAMRQKAQVEEELFKVKIQMEEL-----IKLKLRIEEENKMLIMKDKDSTQKLLV-EEAEKMRQVAEEAAR 2884
Cdd:pfam15558 165 EQKKVQENNLSELLNHQARKVLVDCQAKAEELlrrlsLEQSLQRSQENYEQLVEERHRELREKAqKEEEQFQRAKWRAEE 244
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2885 LSIEAQEAARM-RKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKfQEDKEQIEQQLAK 2961
Cdd:pfam15558 245 KEEERQEHKEAlAELADRKIQQARQVAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHR-EGIKEAIKKKEQR 321
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1941-2170 |
1.85e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.95 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1941 ETLRRLNDEEKAAEKLKEEERRRLAEVEAQL-AKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVD-----AE 2014
Cdd:PRK05035 465 EKAAREARHKKAAEARAAKDKDAVAAALARVkAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKqaaaaAD 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2015 QQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEihIVRLQLETMQKHKANAEDELQELRARAEKAeqqKKAA 2094
Cdd:PRK05035 545 PKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAA--IARAKAKKAAQQAASAEPEEQVAEVDPKKA---AVAA 619
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2095 QEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEkfrSQAEEAERRMKQ---AEVEKERQIKVAQE 2170
Cdd:PRK05035 620 AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQAN---AEPEEAEDPKKAavaAAIARAKAKKAAQQ 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2994-3198 |
1.86e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2994 MSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKE---RMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAEL 3070
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEaeeKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3071 LQKNSQKMQVaqQEQLRQETQVLQTtFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQL 3150
Cdd:COG4717 128 LPLYQELEAL--EAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3151 KvsmddamKKQKEAEENVRRKQDELQQLDKKRQ--EQEKLLADENRKLRE 3198
Cdd:COG4717 205 Q-------QRLAELEEELEEAQEELEELEEELEqlENELEAAALEERLKE 247
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2554-2693 |
1.92e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 55.15 E-value: 1.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2554 KNIAEETQRSKEKAEQEAEKQRQLAleeEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKA-EEAKRQKELAEK 2632
Cdd:COG1193 506 RELLGEESIDVEKLIEELERERREL---EEEREEAERLREELEKLREELEEKLEELEEEKEEILEKArEEAEEILREARK 582
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 2633 EAERQIQlaqeaALKKIDAEEKAhtaiVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAE 2693
Cdd:COG1193 583 EAEELIR-----ELREAQAEEEE----LKEARKKLEELKQELEEKLEKPKKKAKPAKPPEE 634
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1939-2150 |
1.94e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 55.13 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1939 ITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEahakakaqAEKEAEELQRRMQEEVSKREVVAVDAEQQKQ 2018
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEE--------QERQQQVERLRQQEEERKRKKLELEKEKRDR 486
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2019 TIQQELQqlRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHivrlqletmQKHKANAEDElqelraRAEKAEQQKKAAQEEA 2098
Cdd:pfam17380 487 KRAEEQR--RKILEKELEERKQAMIEEERKRKLLEKEME---------ERQKAIYEEE------RRREAEEERRKQQEME 549
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2099 ERLRKQvkdetQKKREAEEELKRKVQAEKEaaREKQRAVEDLEKFRSQAEEA 2150
Cdd:pfam17380 550 ERRRIQ-----EQMRKATEERSRLEAMERE--REMMRQIVESEKARAEYEAT 594
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4539-4576 |
2.03e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.48 E-value: 2.03e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1835643837 4539 QRFLEGTSCIAGVYVEASKERFSVYQAMKKGFIRPGTA 4576
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2865-3201 |
2.06e-06 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 55.06 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2865 QKLLVEEAEKMRQVAEEAARLSIEAQEaarmRKLAEDDlaNQRALAEKMLKEKM--QAIQEASRLKAEAEMLQKQKELAQ 2942
Cdd:PRK10929 60 RKGSLERAKQYQQVIDNFPKLSAELRQ----QLNNERD--EPRSVPPNMSTDALeqEILQVSSQLLEKSRQAQQEQDRAR 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2943 EQArkfqEDKEQIEQQlakETEGFQKSLEAERRQQLEIT--------------AEAERLKLQV--LEMSRAQAKAEEDAS 3006
Cdd:PRK10929 134 EIS----DSLSQLPQQ---QTEARRQLNEIERRLQTLGTpntplaqaqltalqAESAALKALVdeLELAQLSANNRQELA 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3007 K-----FKKKAEEIGNKLHQTElatkermavvQTLEIQRQQSGKEAEELRRAIAELEHE-----KEKLKREAEL---LQK 3073
Cdd:PRK10929 207 RlrselAKKRSQQLDAYLQALR----------NQLNSQRQREAERALESTELLAEQSGDlpksiVAQFKINRELsqaLNQ 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3074 NSQKMQV--AQQEQLRQET-QVLQT--TFLSEKQLLLEREKYIEEEKAKLENLyeDEVRKAQKLKQEqehqMKHLEEEkd 3148
Cdd:PRK10929 277 QAQRMDLiaSQQRQAASQTlQVRQAlnTLREQSQWLGVSNALGEALRAQVARL--PEMPKPQQLDTE----MAQLRVQ-- 348
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3149 qlKVSMDDAMKKQKEAEENvrrKQDELQQLDKkrqEQEKLLADENRKLREKLE 3201
Cdd:PRK10929 349 --RLRYEDLLNKQPQLRQI---RQADGQPLTA---EQNRILDAQLRTQRELLN 393
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1926-2319 |
2.11e-06 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 55.19 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1926 SELTTLTSQyikfITETLRRLNDEEKAAEKLKEEErrrLAEVEAQLAKQ----TQLAEAHAKAKAQAEKEAE--ELQRRM 1999
Cdd:PRK10246 380 EQLRQWQQQ----LTHAEQKLNALPAITLTLTADE---VAAALAQHAEQrplrQRLVALHGQIVPQQKRLAQlqVAIQNV 452
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2000 QEEVSKREVVAVDAEQQKQTIQQELQQLrqnsdmeikskaKQIEEVEYNRRKIEEEihivRLQLETMQ--------KHKA 2071
Cdd:PRK10246 453 TQEQTQRNAALNEMRQRYKEKTQQLADV------------KTICEQEARIKDLEAQ----RAQLQAGQpcplcgstSHPA 516
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2072 NAEDELQEL---RARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAE 2148
Cdd:PRK10246 517 VEAYQALEPgvnQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQEEQALTQQWQAVCASLNITLQPQD 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2149 -------EAERRMKQAEVEKERQIKVAQEVAQQ----SAAAELNSKRMSFAEKTAQLELSL------------------- 2198
Cdd:PRK10246 597 diqpwldAQEEHERQLRLLSQRHELQGQIAAHNqqiiQYQQQIEQRQQQLLTALAGYALTLpqedeeaswlatrqqeaqs 676
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2199 -KQEHITVTHLQEEAERLKKLHD----EAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKED--- 2270
Cdd:PRK10246 677 wQQRQNELTALQNRIQQLTPLLEtlpqSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQfdt 756
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2271 -------AEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQkfsAEQELIR 2319
Cdd:PRK10246 757 alqasvfDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQTLVTQ---TAQALAQ 809
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2672-2933 |
2.11e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.49 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2672 KQEQSILDklkeeAERAKRAAE---DADFARTRAEQEAAlsrQQVEEAERLKQRAEEEAQA----KAQAQDEAEKLRKEA 2744
Cdd:COG2268 180 EDENNYLD-----ALGRRKIAEiirDARIAEAEAERETE---IAIAQANREAEEAELEQEReietARIAEAEAELAKKKA 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2745 ELEA---AKRAHAEQAALKQKQLADEEMDKHKKFAEKtlrqksQVEQELTKVKLQLEEtdhqktlldEELQRLKEEVTDA 2821
Cdd:COG2268 252 EERReaeTARAEAEAAYEIAEANAEREVQRQLEIAER------EREIELQEKEAEREE---------AELEADVRKPAEA 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2822 MRQKAQVEEELfKVKIQMEELIK----LKLRIEEENKMlimkdkdSTQKLLVEEAEKMRQVAEEAARlSIEAQEAARMRK 2897
Cdd:COG2268 317 EKQAAEAEAEA-EAEAIRAKGLAeaegKRALAEAWNKL-------GDAAILLMLIEKLPEIAEAAAK-PLEKIDKITIID 387
|
250 260 270
....*....|....*....|....*....|....*.
gi 1835643837 2898 LAEDDLANQRALAEKMLKeKMQAIQEASRLKAEAEM 2933
Cdd:COG2268 388 GGNGGNGAGSAVAEALAP-LLESLLEETGLDLPGLL 422
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1926-2136 |
2.12e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 55.23 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1926 SELTTLTSQYIKFITE---TLRRLNDEEKAAE---KLKEEERRRLAEV---EAQLAKQTQLA-EAHAKAKAQA-EKEAEE 1994
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAEAdrqRLEQEKQQQLAAIsgsQSQLESTDQNAlETNGQAQRDAiLEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1995 LQRRMQEEVSKREVV---AVDAEQQKQ------------TIQQELQQLRQNSDMEIKSKAKQIEEveyNRRKIEEEIHIV 2059
Cdd:NF012221 1618 VTKELTTLAQGLDALdsqATYAGESGDqwrnpfagglldRVQEQLDDAKKISGKQLADAKQRHVD---NQQKVKDAVAKS 1694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2060 RLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQ---VKDETQKK--REAEEELKRKVQAEKEAAREKQ 2134
Cdd:NF012221 1695 EAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDanaAANDAQSRgeQDASAAENKANQAQADAKGAKQ 1774
|
..
gi 1835643837 2135 RA 2136
Cdd:NF012221 1775 DE 1776
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2864-3031 |
2.18e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.70 E-value: 2.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2864 TQKLLVEEAEKMR-QVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASR-LKAEAEMLQKQKELA 2941
Cdd:TIGR02794 69 RQKKLEQQAEEAEkQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAkAKAEAEAERKAKEEA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2942 QEQARkfqEDKEQIEQQLAKetegfQKSLEAERRQQLEITAEAERlklqvlemsRAQAKAEEDASK---FKKKAEEIGNK 3018
Cdd:TIGR02794 149 AKQAE---EEAKAKAAAEAK-----KKAEEAKKKAEAEAKAKAEA---------EAKAKAEEAKAKaeaAKAKAAAEAAA 211
|
170
....*....|...
gi 1835643837 3019 LHQTELATKERMA 3031
Cdd:TIGR02794 212 KAEAEAAAAAAAE 224
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2720-3007 |
2.20e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 54.65 E-value: 2.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2720 KQRAEEEAQAKAQAQDEAEKL-----RKEAELEAAKR---AHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSqvEQELT 2791
Cdd:pfam05667 261 LAGTEATSGASRSAQDLAELLssfsgSSTTDTGLTKGsrfTHTEKLQFTNEAPAATSSPPTKVETEEELQQQR--EEELE 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2792 KVKLQLEETDHQKTLLDEELQRLK------EEVTDAMRQKAQVEEELFKVKIQMEELIKlklriEEENKMLIMkdkdstQ 2865
Cdd:pfam05667 339 ELQEQLEDLESSIQELEKEIKKLEssikqvEEELEELKEQNEELEKQYKVKKKTLDLLP-----DAEENIAKL------Q 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2866 KLLVEEAEKMRQVAE--EAARLSIEAQEAARMRKLAEDDLANQRALAE-KMLKEKMQAIQEASRLKAEA-EMLQKQKELA 2941
Cdd:pfam05667 408 ALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiKELREKIKEVAEEAKQKEELyKQLVAEYERL 487
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2942 QEQA------RKFQEDKEQIEQQlakeTEGFQKSLEAERRQQLEI---TAEAERLKLQVLEMSRAQAKAEEDASK 3007
Cdd:pfam05667 488 PKDVsrsaytRRILEIVKNIKKQ----KEEITKILSDTKSLQKEInslTGKLDRTFTVTDELVFKDAKKDESVRK 558
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1911-2147 |
2.56e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 54.45 E-value: 2.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1911 SDSIIQEyvdLRTRYSELTTLTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKqtqLAEAHAKAKAQAEK 1990
Cdd:PRK00409 500 PENIIEE---AKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEK---LQEEEDKLLEEAEK 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1991 EAEElqrrmqeevskrevvAVdaEQQKQTIQQELQQLRQNSDMEIKS-KAKQIEEveyNRRKIEEEIHIvrlqLETMQKH 2069
Cdd:PRK00409 574 EAQQ---------------AI--KEAKKEADEIIKELRQLQKGGYASvKAHELIE---ARKRLNKANEK----KEKKKKK 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2070 KANAEDELQE-----LRARAEKAE----QQKKAAQEEAERLRKQVK-DETQKKREAEEELKRKVQAEKEAAREKQ----- 2134
Cdd:PRK00409 630 QKEKQEELKVgdevkYLSLGQKGEvlsiPDDKEAIVQAGIMKMKVPlSDLEKIQKPKKKKKKKPKTVKPKPRTVSleldl 709
|
250
....*....|....*....
gi 1835643837 2135 ------RAVEDLEKFRSQA 2147
Cdd:PRK00409 710 rgmryeEALERLDKYLDDA 728
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2878-3069 |
2.57e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 2.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2878 VAEEAARLSIEAQEAARMRKLAEDDLANQralAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQ 2957
Cdd:PRK09510 60 VVEQYNRQQQQQKSAKRAEEQRKKKEQQQ---AEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2958 QLAKETEGFQKSLEAERRQQLEITAEAERLKlQVLEMSRAQAKAEEDAskfKKKAEEignklhqtelatkerMAVVQTLE 3037
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA-KKKAEAEAAKKAAAEA---KKKAEA---------------EAAAKAAA 197
|
170 180 190
....*....|....*....|....*....|..
gi 1835643837 3038 IQRQQSGKEAEElrRAIAElehEKEKLKREAE 3069
Cdd:PRK09510 198 EAKKKAEAEAKK--KAAAE---AKKKAAAEAK 224
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2567-3259 |
2.58e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2567 AEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQkeLAEKEAerqiqlaQEAAL 2646
Cdd:TIGR00606 166 SEGKALKQKFDEIFSATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQ--ITSKEA-------QLESS 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2647 KKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQR-AEE 2725
Cdd:TIGR00606 237 REIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRtVRE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2726 EAQAKAQAQDEAEKLRKEAELeaakrahaeqaaLKQKqladeemdkhkkfaektlrqKSQVEQELTKVKLQLEETDHQKT 2805
Cdd:TIGR00606 317 KERELVDCQRELEKLNKERRL------------LNQE--------------------KTELLVEQGRLQLQADRHQEHIR 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2806 LLDEELQRLkeevtdAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLImkdkdstQKLLVEEAEKMRQVAEEAARL 2885
Cdd:TIGR00606 365 ARDSLIQSL------ATRLELDGFERGPFSERQIKNFHTLVIERQEDEAKTA-------AQLCADLQSKERLKQEQADEI 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2886 SIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASR-LKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETE 2964
Cdd:TIGR00606 432 RDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRiLELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA 511
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2965 GFQKSLEAERRQQLEITAEAERLKlQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSG 3044
Cdd:TIGR00606 512 DLDRKLRKLDQEMEQLNHHTTTRT-QMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTR 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3045 KEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKqllLEREKYIEEEKAKLENLYED 3124
Cdd:TIGR00606 591 DRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEE---IEKSSKQRAMLAGATAVYSQ 667
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3125 EVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQME 3204
Cdd:TIGR00606 668 FITQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIP 747
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 3205 EEHRIALAQTREMRTQTDDLAGNLPLTPTVvtqtkaMPNGRDALDGLTQNGMTEQ 3259
Cdd:TIGR00606 748 ELRNKLQKVNRDIQRLKNDIEEQETLLGTI------MPEEESAKVCLTDVTIMER 796
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2113-2743 |
2.62e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 54.44 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2113 REAEEELKRKVQAEKEaarekqRAVEDLEKFRSQAEEAERRM---KQAEVEKERQIKVAQEVAQ-----QSAAAELNSKR 2184
Cdd:pfam10174 111 PELTEENFRRLQSEHE------RQAKELFLLRKTLEEMELRIetqKQTLGARDESIKKLLEMLQskglpKKSGEEDWERT 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2185 MSFAEKTAQ---LELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQ 2261
Cdd:pfam10174 185 RRIAEAEMQlghLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGL 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2262 EEAEKQKEDAE-----REARKRAKTEESALRQkELAEDELEK---QRKLADATAQQkfSAEQELIRLKAETENSEQQRLL 2333
Cdd:pfam10174 265 LHTEDREEEIKqmevyKSHSKFMKNKIDQLKQ-ELSKKESELlalQTKLETLTNQN--SDCKQHIEVLKESLTAKEQRAA 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2334 LEeelfrlKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSntekSKQMLEVEASKLRELAEeaaKLRAVSE 2413
Cdd:pfam10174 342 IL------QTEVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRD----LKDMLDVKERKINVLQK---KIENLQE 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2414 EAK-RQRQIAEdeaarqraeaeriLKEKLAAI-----NDATRLKTEAEiALKEKEAENERLRRLAEDEAYQRKLLEEQAT 2487
Cdd:pfam10174 409 QLRdKDKQLAG-------------LKERVKSLqtdssNTDTALTTLEE-ALSEKERIIERLKEQREREDRERLEELESLK 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2488 QHKQDIEEKIILL------KKSSDNEL-ERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDL----ELEL------ 2550
Cdd:pfam10174 475 KENKDLKEKVSALqpelteKESSLIDLkEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkahNAEEavrtnp 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2551 ---NQLKNIAEETQRSKEKAEQ-EAEKQRQL-ALEEEQRRKEAEEKvrKILADEKEAARQRKAALEEVERLKAKAEEAKR 2625
Cdd:pfam10174 555 einDRIRLLEQEVARYKEESGKaQAEVERLLgILREVENEKNDKDK--KIAELESLTLRQMKEQNKKVANIKHGQQEMKK 632
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2626 qkelaekeaeRQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSIldKLKEEAERAKRAAEDADFARTRAEQe 2705
Cdd:pfam10174 633 ----------KGAQLLEEARRREDNLADNSQQLQLEELMGALEKTRQELDAT--KARLSSTQQSLAEKDGHLTNLRAER- 699
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2706 aalsRQQVEEAERLKQRA---------------EEEAQAKAQAQDEAEKLRKE 2743
Cdd:pfam10174 700 ----RKQLEEILEMKQEAllaaisekdaniallELSSSKKKKTQEEVMALKRE 748
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
6878-6941 |
2.76e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 50.18 E-value: 2.76e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 6878 RILDIFRSIDRDQDGRISQQEFIESVLSSKFPTNSLEMnAVASIfDYNGDGFIDYYEFVSALHP 6941
Cdd:COG5126 70 FARAAFDLLDTDGDGKISADEFRRLLTALGVSEEEADE-LFARL-DTDGDGKISFEEFVAAVRD 131
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2545-2742 |
2.84e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.23 E-value: 2.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2545 DLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKaaleeveRLKAKAEEAK 2624
Cdd:COG1579 14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIK-------KYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2625 RQKELaekeaerqiqlaqEAALKKIDAEEKAhtaiVQQKEQEMLQTRKQEQSILDKLKEEaeRAKRAAEDADFARTRAEQ 2704
Cdd:COG1579 87 NNKEY-------------EALQKEIESLKRR----ISDLEDEILELMERIEELEEELAEL--EAELAELEAELEEKKAEL 147
|
170 180 190
....*....|....*....|....*....|....*...
gi 1835643837 2705 EAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRK 2742
Cdd:COG1579 148 DEELAELEAELEELEAEREELAAKIPPELLALYERIRK 185
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2565-2649 |
2.86e-06 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 50.13 E-value: 2.86e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2565 EKAEQEAEKQRQlalEEEQRRKEAEEKVRKILAD-----EKEAARQRKAALEEVERLKAKA-EEAKRQKELAEKEAERQI 2638
Cdd:cd06503 43 EKAKEEAEELLA---EYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAkAEIEQEKEKALAELRKEV 119
|
90
....*....|..
gi 1835643837 2639 -QLAQEAALKKI 2649
Cdd:cd06503 120 aDLAVEAAEKIL 131
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2695-3119 |
2.95e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 2.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2695 ADFARTRAE-----QEAALSRQQVEEAERlkQRAEEeaqakaqaQDEAEKLRKEAELEAAKRAHAEQaalkQKQLADEem 2769
Cdd:PRK04863 272 ADYMRHANErrvhlEEALELRRELYTSRR--QLAAE--------QYRLVEMARELAELNEAESDLEQ----DYQAASD-- 335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2770 dkHKKFAEKTLRQKSQVEQ---ELTKVKLQLEEtdhQKTLLDEelqrLKEEVTDAMRQKAQVEEELFKVKIQmeeLIKLK 2846
Cdd:PRK04863 336 --HLNLVQTALRQQEKIERyqaDLEELEERLEE---QNEVVEE----ADEQQEENEARAEAAEEEVDELKSQ---LADYQ 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2847 LRIEEENKMLIMKDKdstQKLLVEEAEKMRQVAEEAARLSIEAQEAARmrklAEDDLANQRALaekMLKEKMQAIQEASR 2926
Cdd:PRK04863 404 QALDVQQTRAIQYQQ---AVQALERAKQLCGLPDLTADNAEDWLEEFQ----AKEQEATEELL---SLEQKLSVAQAAHS 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2927 LKAEAEMLQKQ--KELAQEQA-RKFQEDKEQIEQQLAketegfqkslEAERRQQLeitaeaeRLKLQVLEMS-RAQAKAE 3002
Cdd:PRK04863 474 QFEQAYQLVRKiaGEVSRSEAwDVARELLRRLREQRH----------LAEQLQQL-------RMRLSELEQRlRQQQRAE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3003 EDASKFKKKaeeignkLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQ 3082
Cdd:PRK04863 537 RLLAEFCKR-------LGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQ 609
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3083 Q--EQLRQE-----------TQVLQTTFLSEKQLLLEREKyIEEEKAKLE 3119
Cdd:PRK04863 610 DalARLREQsgeefedsqdvTEYMQQLLERERELTVERDE-LAARKQALD 658
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2665-2766 |
2.97e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 50.54 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2665 QEMLQTRKQeqsildKLKEEAERAKRAAEDADFARTRAEQEAALSRQQ----VEEAErlKQRAEEEAQAKAQAQDEAEKL 2740
Cdd:PRK05759 30 MKALEERQK------KIADGLAAAERAKKELELAQAKYEAQLAEARAEaaeiIEQAK--KRAAQIIEEAKAEAEAEAARI 101
|
90 100
....*....|....*....|....*.
gi 1835643837 2741 RKEAELEAAKRAHAEQAALKqKQLAD 2766
Cdd:PRK05759 102 KAQAQAEIEQERKRAREELR-KQVAD 126
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5957-6052 |
3.06e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 3.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5957 YQEAMQRLFNWLDTAEARLSEEFlVGGDLDMVKRQLLDLKEFKRELYQRKVELESLHHRTLPVK----CEDKETSTRLND 6032
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASED-LGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIeeghPDAEEIEERLEE 81
|
90 100
....*....|....*....|
gi 1835643837 6033 FRQRWERLEEEVVDRQHQLE 6052
Cdd:smart00150 82 LNERWEELKELAEERRQKLE 101
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1716-2493 |
3.42e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.46 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1716 EVHAVPSDSKELEATKAELKKLRSQVEGHQplfnTLEADLNKAKDVNEQMLRShsERDVDLDRYREKVQQLLERWQAILV 1795
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDE----TLIASRQEERQETSAELNQ--LLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1796 QIDLRQRELDQLGRQLRYYRETYewlikwIKDAKQRQEQIQSVPITDSKTMKEHLLQEKKLLD---EIESNRDKVDECQK 1872
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDAD------IETAAADQEQLPSWQSELENLEERLKALTGKHQDvtaKYNRRRSKIKEQNN 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1873 YA----KQYIDAIKD-YELQLVTYKAQVEPVASPAKKPKVQSTSDSIIQEYvDLRTRYSELTTLTSQYIkFITETLRRLN 1947
Cdd:pfam12128 390 RDiagiKDKLAKIREaRDRQLAVAEDDLQALESELREQLEAGKLEFNEEEY-RLKSRLGELKLRLNQAT-ATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1948 DEEKAAEKLKEEERRRLAEVEAqlakqtqLAEAHAKAKAQAEKEAEELQrrmQEEVSKREVVAVDAEQQKQTIQQE---L 2024
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVER-------LQSELRQARKRRDQASEALR---QASRRLEERQSALDELELQLFPQAgtlL 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2025 QQLRQNSDMEIKSKAKQIE-----------EVEYNRRKIEEEIHIVRLQLETMQKHKANAEDElqELRARAEKAEQQKKA 2093
Cdd:pfam12128 538 HFLRKEAPDWEQSIGKVISpellhrtdldpEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE--ELRERLDKAEEALQS 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2094 AQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEaAREKQRAVEDlekfrsqaeeaerRMKQAEVEKERQIKVAQEVAQ 2173
Cdd:pfam12128 616 AREKQAAAEEQLVQANGELEKASREETFARTALKN-ARLDLRRLFD-------------EKQSEKDKKNKALAERKDSAN 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2174 QSaaaelnskRMSFAEKTAQLELSLKQehitvthlqeeaerlkklhdeaekareeaekELEKWHQKANEALRLRLQAEEV 2253
Cdd:pfam12128 682 ER--------LNSLEAQLKQLDKKHQA-------------------------------WLEEQKEQKREARTEKQAYWQV 722
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2254 AHKKTLAQEEAEKQKEDAEREARKRakteesalRQKELAEDeleKQRKLAdataqQKFSAEQELIRLKAETEN---SEQQ 2330
Cdd:pfam12128 723 VEGALDAQLALLKAAIAARRSGAKA--------ELKALETW---YKRDLA-----SLGVDPDVIAKLKREIRTlerKIER 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2331 RLLLEEELFRLKNEVNEA-IQKRKEMEEELAKVRAEMEILLQSKSRAEEESRsnTEKSKQMLEVEASK--LRELAEEAAK 2407
Cdd:pfam12128 787 IAVRRQEVLRYFDWYQETwLQRRPRLATQLSNIERAISELQQQLARLIADTK--LRRAKLEMERKASEkqQVRLSENLRG 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2408 LRAvseeakRQRQIAEDEAARQRAEAERILKEKLAAINDaTRLKTEAEIALKEKEAEN-----ERLRRLAEDEAYQRkLL 2482
Cdd:pfam12128 865 LRC------EMSKLATLKEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYVEHfknviADHSGSGLAETWES-LR 936
|
810
....*....|.
gi 1835643837 2483 EEQATQHKQDI 2493
Cdd:pfam12128 937 EEDHYQNDKGI 947
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2261-2480 |
3.54e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 53.27 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2261 QEEAEKQKEDAEREARKRAKTEESALRQKELAEDE----LEKQRKLADAtaQQKFSAEQElirlkaetenseqqrlllee 2336
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQErlkqLEKERLAAQE--QKKQAEEAA-------------------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2337 elfrlknevNEAIQKRKEMEEELAKVRAemeillQSKSRAEEESRSNTEKSKQMlEVEASKlreLAEEAAKLRAVSEEAK 2416
Cdd:PRK09510 125 ---------KQAALKQKQAEEAAAKAAA------AAKAKAEAEAKRAAAAAKKA-AAEAKK---KAEAEAAKKAAAEAKK 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2417 RQRQIAEDEA---ARQRAEAERILK-EKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRK 2480
Cdd:PRK09510 186 KAEAEAAAKAaaeAKKKAEAEAKKKaAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1939-2146 |
3.60e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 51.75 E-value: 3.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1939 ITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSK-REVVAVDAEQQK 2017
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERK 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2018 QTIQQELQQLRQnsdmEIKSKAKQIEEveynrrkieeeihiVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQ-- 2095
Cdd:COG1842 94 AELEAQAEALEA----QLAQLEEQVEK--------------LKEALRQLESKLEELKAKKDTLKARAKAAKAQEKVNEal 155
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2096 ---------EEAERLRKQVkDETQKKREAEEELKRKVQAEKE-AAREKQRAVED-LEKFRSQ 2146
Cdd:COG1842 156 sgidsddatSALERMEEKI-EEMEARAEAAAELAAGDSLDDElAELEADSEVEDeLAALKAK 216
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2350-2480 |
3.66e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.72 E-value: 3.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2350 QKRKEMEEELAKVRAEMEILLQSKSRAEEEsrsnTEKSKQMLEVEASKLRELAEEAAKL------RAVS---EEAKRQRQ 2420
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAE----LAKKKAEERREAETARAEAEAAYEIaeanaeREVQrqlEIAERERE 291
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2421 I--AEDEAARQRAEAERILKEKLAAinDATRLKTEAeialkEKEAENERLRRLAEDEAYQRK 2480
Cdd:COG2268 292 IelQEKEAEREEAELEADVRKPAEA--EKQAAEAEA-----EAEAEAIRAKGLAEAEGKRAL 346
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2765-3006 |
3.74e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 53.30 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2765 ADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIK 2844
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2845 -LKLRIEEENKMLIMKDKDSTQKLLvEEAEKMRQVAEEAARLsIEAQEAARmrklaeDDLANQRALAEkmlkekmQAIQE 2923
Cdd:COG3883 94 aLYRSGGSVSYLDVLLGSESFSDFL-DRLSALSKIADADADL-LEELKADK------AELEAKKAELE-------AKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2924 ASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEE 3003
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
...
gi 1835643837 3004 DAS 3006
Cdd:COG3883 239 AAA 241
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2061-2217 |
3.77e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 3.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2061 LQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKrKVQAEKEAAREKQRAV--- 2137
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-EVEARIKKYEEQLGNVrnn 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2138 EDLEKFRSQAEEAERRMKQAEvEKERQIKVAQEVAQ---QSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAER 2214
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLE-DEILELMERIEELEeelAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
...
gi 1835643837 2215 LKK 2217
Cdd:COG1579 168 LAA 170
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2343-3069 |
3.80e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 54.19 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2343 NEVNEAIQKRKEMEEELAKVRaemEILLQSKSRAEEESRSNTEKS--KQMLEVE---AS--------------------- 2396
Cdd:COG3096 278 NERRELSERALELRRELFGAR---RQLAEEQYRLVEMARELEELSarESDLEQDyqaASdhlnlvqtalrqqekieryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2397 KLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERiLKEKLA---------------------AINDATRLKTEAE 2455
Cdd:COG3096 355 DLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDS-LKSQLAdyqqaldvqqtraiqyqqavqALEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2456 IALKEKEAENERLRRlAEDEAYQRKLLEEQ----ATQHKQDIEEKIILLKKSSDnELERQKniVEDTLRQRRIIEEEIRI 2531
Cdd:COG3096 434 LTPENAEDYLAAFRA-KEQQATEEVLELEQklsvADAARRQFEKAYELVCKIAG-EVERSQ--AWQTARELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2532 LKVNFEKASVGKSDLELELNQLKN---IAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKA 2608
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNaerLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2609 ALEEVERLKAKAEEAKRQKELAEKEAErqiQLAQEAAlkkiDAEE-KAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAER 2687
Cdd:COG3096 590 LRARIKELAARAPAWLAAQDALERLRE---QSGEALA----DSQEvTAAMQQLLEREREATVERDELAARKQALESQIER 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAAEDADfARTRAEQEA----------------------AL---SRQQ--VEEAERLKQRAEEEA---------QAKA 2731
Cdd:COG3096 663 LSQPGGAED-PRLLALAERlggvllseiyddvtledapyfsALygpARHAivVPDLSAVKEQLAGLEdcpedlyliEGDP 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2732 QAQDEAekLRKEAELEAAKRAHAEQAALkqkqladeemdKHKKFAEKTLRQKSQVEQELTKVKLQLEETD--HQKTLLD- 2808
Cdd:COG3096 742 DSFDDS--VFDAEELEDAVVVKLSDRQW-----------RYSRFPEVPLFGRAAREKRLEELRAERDELAeqYAKASFDv 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2809 EELQRL--------------------KEEVTDAMRQKAQVEEELFKVKIQM----EELIKLKLRIEEENKML----IMKD 2860
Cdd:COG3096 809 QKLQRLhqafsqfvgghlavafapdpEAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLAD 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2861 KDSTQKllVEEAEKMRQVAEEAAR-----------------------LSIEAQEAARMRKLAEDDLANQRALAekmLKEK 2917
Cdd:COG3096 889 ETLADR--LEELREELDAAQEAQAfiqqhgkalaqleplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFA---LSEV 963
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2918 MQ-----AIQEASRLKAEA----EMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQkSLEAERRQQLEITAEAERlK 2988
Cdd:COG3096 964 VQrrphfSYEDAVGLLGENsdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ-E 1041
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2989 LQVLEMsRAQAKAEEDAskfKKKAEEIGNKLHQTelatkeRMAVVQtLEIQRQQSGKEAEELRRAIAELEHEKEKLKREA 3068
Cdd:COG3096 1042 LEELGV-QADAEAEERA---RIRRDELHEELSQN------RSRRSQ-LEKQLTRCEAEMDSLQKRLRKAERDYKQEREQV 1110
|
.
gi 1835643837 3069 E 3069
Cdd:COG3096 1111 V 1111
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2589-2725 |
4.05e-06 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 50.42 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2589 EEKVRKILADEKEAARQRKaALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDA--EEKAHTAIVQQKEQE 2666
Cdd:pfam05672 9 AEEAARILAEKRRQAREQR-EREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERrrEEEERQRKAEEEAEE 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 2667 MLQTRKQEQSILDKLKEEAERakRAAEDAdfARTRAEQEaalSRQQVEEAERL--KQRAEE 2725
Cdd:pfam05672 88 REQREQEEQERLQKQKEEAEA--KAREEA--ERQRQERE---KIMQQEEQERLerKKRIEE 141
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2886-3229 |
4.06e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 4.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2886 SIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEG 2965
Cdd:COG4717 50 RLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2966 FQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMavvQTLEIQRQQSGK 3045
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL---QDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3046 EAEELRRAIAELEHEKEKLKREAELLQKnsQKMQVAQQEQLRQETQVLQTT----------------------------- 3096
Cdd:COG4717 207 RLAELEEELEEAQEELEELEEELEQLEN--ELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3097 -FLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDaMKKQKEAEENVRRKQDEL 3175
Cdd:COG4717 285 lLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDR-IEELQELLREAEELEEEL 363
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 3176 qQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDLAGNLP 3229
Cdd:COG4717 364 -QLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLG 416
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2541-2771 |
4.07e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 54.07 E-value: 4.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2541 VGKSDLELELNQLKNIAEE---TQRS---KEKAEQ-----EAEKQRQL-ALEEEQRRKEAEEKvrkiLADEKEAARQRKA 2608
Cdd:NF012221 1535 VATSESSQQADAVSKHAKQddaAQNAladKERAEAdrqrlEQEKQQQLaAISGSQSQLESTDQ----NALETNGQAQRDA 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2609 ALEE-----------VERLKAKAEEAKRQKELAEKEAER---------QIQL--AQEAALKKIDAEEKAHTA-------I 2659
Cdd:NF012221 1611 ILEEsravtkelttlAQGLDALDSQATYAGESGDQWRNPfagglldrvQEQLddAKKISGKQLADAKQRHVDnqqkvkdA 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2660 VQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKA-QAQDEAE 2738
Cdd:NF012221 1691 VAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKAnQAQADAK 1770
|
250 260 270
....*....|....*....|....*....|...
gi 1835643837 2739 KLrKEAELEAAKRAHAEQAALKQKQLADEEMDK 2771
Cdd:NF012221 1771 GA-KQDESDKPNRQGAAGSGLSGKAYSVEGVAE 1802
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1906-2165 |
4.12e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.87 E-value: 4.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1906 KVQSTSDSIIQEYVD--LRTRYSElttlTSQYIKFITETLRRLNDE----EKAAEKLKEEER------------RRLAEV 1967
Cdd:COG3206 149 LAAAVANALAEAYLEqnLELRREE----ARKALEFLEEQLPELRKEleeaEAALEEFRQKNGlvdlseeaklllQQLSEL 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1968 EAQLAK-QTQLAEAhaKAKAQAEKEAEELQRRMQEEVSKREVVAvDAEQQKQTIQQELQQLRQN---SDMEIKSKAKQIE 2043
Cdd:COG3206 225 ESQLAEaRAELAEA--EARLAALRAQLGSGPDALPELLQSPVIQ-QLRAQLAELEAELAELSARytpNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2044 EVeynRRKIEEEIhivrlqletmqkhkanaEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEeLKRKV 2123
Cdd:COG3206 302 AL---RAQLQQEA-----------------QRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR-LEREV 360
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1835643837 2124 QAEkeaarekqravedlekfRSQAEEAERRMKQAEVEKERQI 2165
Cdd:COG3206 361 EVA-----------------RELYESLLQRLEEARLAEALTV 385
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1772-2279 |
4.27e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 4.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1772 RDVDLDRYREKVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQSVpitdsktmKEHLL 1851
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAE--------LEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1852 QEKKLLDEIESNRDKVDECQKYAKQyidaIKDYELQLVTYKAQvepvaspakkpkvqstsdsiIQEYVDLRTRYSELTtl 1931
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALEAE----LAELPERLEELEER--------------------LEELRELEEELEELE-- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1932 tsqyikfitetlrrlNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEevSKREVVAV 2011
Cdd:COG4717 170 ---------------AELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE--LEEELEQL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2012 DAEQQKQTIQQELQQLRQ------------NSDMEIKSKAKQIEEV-----------EYNRRKIEEEIHIVRLQLETMQK 2068
Cdd:COG4717 233 ENELEAAALEERLKEARLllliaaallallGLGGSLLSLILTIAGVlflvlgllallFLLLAREKASLGKEAEELQALPA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2069 HKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAE 2148
Cdd:COG4717 313 LEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2149 EAERRmkqaeVEKERQIKVAQEvaqQSAAAELNSKRMSFAEKTAQLElslKQEHITVTHLQEEAERLKKLHDEAekaree 2228
Cdd:COG4717 393 QAEEY-----QELKEELEELEE---QLEELLGELEELLEALDEEELE---EELEELEEELEELEEELEELREEL------ 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 2229 aekelekwhQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRA 2279
Cdd:COG4717 456 ---------AELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2071-2142 |
4.50e-06 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 49.36 E-value: 4.50e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2071 ANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQK-----KREAEEELKR-KVQAEKEAAREKQRAVEDLEK 2142
Cdd:cd06503 40 EEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKikeeiLAEAKEEAERiLEQAKAEIEQEKEKALAELRK 117
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1544-2142 |
4.51e-06 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 54.29 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1544 DSENFLPDDRMQIEREYNNCIQKYEQLLRTQEkgeqdevtckNYISQLKDIRLQLEGCESRTIHKIRTPMEKDPIKECSQ 1623
Cdd:TIGR01612 1111 DEINKIKDDIKNLDQKIDHHIKALEEIKKKSE----------NYIDEIKAQINDLEDVADKAISNDDPEEIEKKIENIVT 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1624 RISEQQQIHfelEGIKKNLNKVSEktlkvlAQKEQSSSspllrteHEITHQKMDQVYSLSSIYLEKLKtinlviRSTQGA 1703
Cdd:TIGR01612 1181 KIDKKKNIY---DEIKKLLNEIAE------IEKDKTSL-------EEVKGINLSYGKNLGKLFLEKID------EEKKKS 1238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1704 EEVVRTYEDQLKEVHAVPSDSKELEA-------TKAELKKLRSQVEGHQPLF-----------------------NTLEA 1753
Cdd:TIGR01612 1239 EHMIKAMEAYIEDLDEIKEKSPEIENemgiemdIKAEMETFNISHDDDKDHHiiskkhdenisdirekslkiiedFSEES 1318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1754 DLNKAKDVNEQMLRSHSERDVDLDRYREKVQQL-----LERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKD- 1827
Cdd:TIGR01612 1319 DINDIKKELQKNLLDAQKHNSDINLYLNEIANIynilkLNKIKKIIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDd 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1828 --AKQRQEQIQSVP--------ITDSKTMKEHLLQEKKLLDEIESNRDKVD----------ECQKYAKQYIDAIK----- 1882
Cdd:TIGR01612 1399 inLEECKSKIESTLddkdidecIKKIKELKNHILSEESNIDTYFKNADENNenvlllfkniEMADNKSQHILKIKkdnat 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1883 ---DYEL-QLVTYKAQVEPVASPAKKPKVQSTSDSIIQEyvdlrtryselttltsQYIKFITETLRRLNDEE--KAAEKL 1956
Cdd:TIGR01612 1479 ndhDFNInELKEHIDKSKGCKDEADKNAKAIEKNKELFE----------------QYKKDVTELLNKYSALAikNKFAKT 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1957 KEEERRRLAEVEaqlakqtqlaEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTI--QQELQQLrQNSDME 2034
Cdd:TIGR01612 1543 KKDSEIIIKEIK----------DAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKAAIdiQLSLENF-ENKFLK 1611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2035 IKSKAKQIEEVEYNRRKIEEEIHIVRLQL-ETMQKHKANAEDELQE----LRARAEKAEQQKKAAQEEAERLRKQVKDET 2109
Cdd:TIGR01612 1612 ISDIKKKINDCLKETESIEKKISSFSIDSqDTELKENGDNLNSLQEflesLKDQKKNIEDKKKELDELDSEIEKIEIDVD 1691
|
650 660 670
....*....|....*....|....*....|...
gi 1835643837 2110 QKKREAEEELKRKVQAEKEAAREKQRAVEDLEK 2142
Cdd:TIGR01612 1692 QHKKNYEIGIIEKIKEIAIANKEEIESIKELIE 1724
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1961-2126 |
4.71e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 51.85 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1961 RRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRrmqeEVSKREVVAVDAEQQKQTIQQELQQLRQNSdmEIKSKAK 2040
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRNNK--EYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2041 QIEEVEYNRRKIEEEIhivrlqLETMQKHKAnAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELK 2120
Cdd:COG1579 97 EIESLKRRISDLEDEI------LELMERIEE-LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
....*.
gi 1835643837 2121 RKVQAE 2126
Cdd:COG1579 170 AKIPPE 175
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1704-2175 |
4.97e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.90 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1704 EEVVRTYEDQLKEVHAVPSDSKELEATKAELKKLRSQ---VEGHQPLFNTL---------------------EADLNKAK 1759
Cdd:TIGR00606 618 EEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQramLAGATAVYSQFitqltdenqsccpvcqrvfqtEAELQEFI 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1760 DVNEQMLRSHSERdvdLDRYREKVQQLLERWQAILVQIDLRQRELDQLgrqlryyretyewlikwIKDAKQRQEQIQSVP 1839
Cdd:TIGR00606 698 SDLQSKLRLAPDK---LKSTESELKKKEKRRDEMLGLAPGRQSIIDLK-----------------EKEIPELRNKLQKVN 757
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1840 iTDSKTMKEHLLQEKKLLDEIESNRDKVDECQKYakqyIDAIKDYELQLVTYKAQVEPVASPAKKPKVQSTSDSIIQEYV 1919
Cdd:TIGR00606 758 -RDIQRLKNDIEEQETLLGTIMPEEESAKVCLTD----VTIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQ 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1920 DLRTRYSELTTLTSQYIKFITETLRRLNDEEKAAEKLKEE---------ERRRLAEVEAQLAKQTQ-LAEAHAKAKAQA- 1988
Cdd:TIGR00606 833 EKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqigtnlqRRQQFEEQLVELSTEVQsLIREIKDAKEQDs 912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1989 --EKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQL------------------RQNSDMEIKSKAKQIEEVEYN 2048
Cdd:TIGR00606 913 plETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdienkiqdgkddyLKQKETELNTVNAQLEECEKH 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2049 RRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELkRKVQAEKE 2128
Cdd:TIGR00606 993 QEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENI-DLIKRNHV 1071
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1835643837 2129 AAREKQRAVEDlEKFRSQAEEAERRMKQAEvEKERQIKVAQEVAQQS 2175
Cdd:TIGR00606 1072 LALGRQKGYEK-EIKHFKKELREPQFRDAE-EKYREMMIVMRTTELV 1116
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4336-4369 |
5.05e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 5.05e-06
10 20 30
....*....|....*....|....*....|....
gi 1835643837 4336 LLDAQAATGFIIDPVKNEMLTVDEAVRKGVVGPE 4369
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2859-3069 |
5.17e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 5.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2859 KDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRAL---AEKMLKEKMQAIQEASRLKAEAEM-L 2934
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAeL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2935 QKQKELAQEQARKFQEDKEQIEQQLAKETEGFqksLEAERRQQL------EITAEAERLKLQVLEMSRAQAKAEEDASKF 3008
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLALLLSPEDF---LDAVRRLQYlkylapARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 3009 KKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAE 3069
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2150-2310 |
5.21e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 52.95 E-value: 5.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2150 AERRMKQAEVEKERQIKVAQ---EVAQQSAAAELNSKRMSFAEKTAqlELSLKQEHitvthLQEEAERLKklhdeaekar 2226
Cdd:COG2268 199 RDARIAEAEAERETEIAIAQanrEAEEAELEQEREIETARIAEAEA--ELAKKKAE-----ERREAETAR---------- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2227 EEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADAT 2306
Cdd:COG2268 262 AEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAE 341
|
....
gi 1835643837 2307 AQQK 2310
Cdd:COG2268 342 GKRA 345
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2971-3221 |
5.22e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2971 EAERRQQLEITAEAERlklQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTEL---ATKERMAVVQTLEIQRQQSGKEA 3047
Cdd:PRK04863 278 ANERRVHLEEALELRR---ELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQdyqAASDHLNLVQTALRQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3048 EELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQ---------VLQTTFLSEKQL--LLER--------- 3107
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEEVDELKSQladyqqaldVQQTRAIQYQQAvqALERakqlcglpd 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3108 ------EKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHleEEKDQL------KVSMDDAMKKQKEAE---------- 3165
Cdd:PRK04863 435 ltadnaEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQF--EQAYQLvrkiagEVSRSEAWDVARELLrrlreqrhla 512
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 3166 ---ENVRRKQDELQQLDKKRQEQEKLLADENRK-------------LREKLEQMEEEHRIALAQTREMRTQT 3221
Cdd:PRK04863 513 eqlQQLRMRLSELEQRLRQQQRAERLLAEFCKRlgknlddedeleqLQEELEARLESLSESVSEARERRMAL 584
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2249-2437 |
5.24e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.89 E-value: 5.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2249 QAEEVAHKKTLAQEEAEKQKEDAEREARKR-AKTEESALRQKELAED----ELEKQRKLADATAQQKFSAeqeliRLKAE 2323
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQKQAAEQERLKQlEKERLAAQEQKKQAEEaakqAALKQKQAEEAAAKAAAAA-----KAKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2324 TENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEK-SKQMLEVEASKLRELA 2402
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAeAKKKAAAEAKAAAAKA 230
|
170 180 190
....*....|....*....|....*....|....*
gi 1835643837 2403 EEAAKlrAVSEEAKRQRQIAEDEAARQRAEAERIL 2437
Cdd:PRK09510 231 AAEAK--AAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
2582-2752 |
6.32e-06 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 50.65 E-value: 6.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2582 EQRRKEAEEKVRKILAD-EKEAARQRKAAL----EEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAH 2656
Cdd:pfam12072 26 EAKIGSAEELAKRIIEEaKKEAETKKKEALleakEEIHKLRAEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2657 TAIvQQKEQEMlqtrKQEQSILDKLKEEAERAKRAaedadfARTRAEQEAALSRqqvEEA-ERLKQRAEEEAQakaqaQD 2735
Cdd:pfam12072 106 ESL-EKKEKEL----EAQQQQLEEKEEELEELIEE------QRQELERISGLTS---EEAkEILLDEVEEELR-----HE 166
|
170 180
....*....|....*....|
gi 1835643837 2736 EAEKLRK---EAELEAAKRA 2752
Cdd:pfam12072 167 AAVMIKEieeEAKEEADKKA 186
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2093-2429 |
6.52e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 53.03 E-value: 6.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2093 AAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVA 2172
Cdd:pfam15709 171 AERELIDKAKRRKGTKTDKTKTPKREREGKVHGEAEAAVGKSRESKAEKKSELISKGKKTGAKRKRTQKERNLEVAAELS 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2173 ----QQSAAAELNSKRMSFAEK-------------------TAQLELSLKQEHITVTHLQEEAERLKK------LHDEAE 2223
Cdd:pfam15709 251 gpdvINSKETEDASERGAFSSDsvvedpwlsskydaeesqvSIDGRSSPTQTFVVTGNMESEEERSEEdpskalLEKREQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2224 KAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAktEESALRQKELAEDEL-----EK 2298
Cdd:pfam15709 331 EKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRF--EEIRLRKQRLEEERQrqeeeER 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2299 QRKLADATAQQKFSAEQELIRLKAEtenseqQRLLLEEELFRLKNEVNEaiQKRKEMEEELA---KVRAEMeillQSKSR 2375
Cdd:pfam15709 409 KQRLQLQAAQERARQQQEEFRRKLQ------ELQRKKQQEEAERAEAEK--QRQKELEMQLAeeqKRLMEM----AEEER 476
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2376 AEEESRSNTEKSKQMLEVEASKLRElaEEAAKLraVSEEAKRQRQiaedEAARQ 2429
Cdd:pfam15709 477 LEYQRQKQEAEEKARLEAEERRQKE--EEAARL--ALEEAMKQAQ----EQARQ 522
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2716-2895 |
6.58e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2716 AERLKQRAEEEAQA-KAQAQDEAEKLRKEAELEAAKRAHaeqaalKQKQLADEEM-DKHKKFA--EKTLRQKsqvEQELT 2791
Cdd:PRK12704 29 AEAKIKEAEEEAKRiLEEAKKEAEAIKKEALLEAKEEIH------KLRNEFEKELrERRNELQklEKRLLQK---EENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2792 KvklQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKlriEEENKMLIMkdkDSTQKLLVEE 2871
Cdd:PRK12704 100 R---KLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLT---AEEAKEILL---EKVEEEARHE 170
|
170 180
....*....|....*....|....
gi 1835643837 2872 AEKMRQVAEEAARLsiEAQEAARM 2895
Cdd:PRK12704 171 AAVLIKEIEEEAKE--EADKKAKE 192
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4541-4579 |
6.65e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 46.17 E-value: 6.65e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 4541 FLEGTSCIAGVYVEASKERFSVYQAMKKGFIRPGTAFEL 4579
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1782-2505 |
6.76e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1782 KVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQeqiqsvpitdsKTMKEHLLQEKKLLDEIE 1861
Cdd:TIGR04523 34 EEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQI-----------KDLNDKLKKNKDKINKLN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1862 SNRDKVDECQKYAKQYIDAIKDyelQLVTYKAQVEPVASPAKKPKVQSTSDSiiQEYVDLRTRYSELTTLTSQYIKFITE 1941
Cdd:TIGR04523 103 SDLSKINSEIKNDKEQKNKLEV---ELNKLEKQKKENKKNIDKFLTEIKKKE--KELEKLNNKYNDLKKQKEELENELNL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1942 TLRRLNDEEKAAEKLKEEERR---RLAEVEAQLAKQTQLaeahakakaqaEKEAEELQRRMQEevskrevvavdAEQQKQ 2018
Cdd:TIGR04523 178 LEKEKLNIQKNIDKIKNKLLKlelLLSNLKKKIQKNKSL-----------ESQISELKKQNNQ-----------LKDNIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2019 TIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKaaqeea 2098
Cdd:TIGR04523 236 KKQQEINEKTT----EISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKE------ 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2099 ERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVaqevaqqsaaa 2178
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK----------- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2179 eLNSKRMSFAEKTAQLELSLKQEHITVthlqEEAERLKKLHDEAEKAREEAEKELEKWHQkanealrlRLQAEEVAHKKT 2258
Cdd:TIGR04523 375 -LKKENQSYKQEIKNLESQINDLESKI----QNQEKLNQQKDEQIKKLQQEKELLEKEIE--------RLKETIIKNNSE 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2259 LaqEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSeqqrllleeel 2338
Cdd:TIGR04523 442 I--KDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL----------- 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2339 frlKNEVNEAIQKRKEMEEELAKVRAEM-EILLQSKSRAEEESRSNTEKSKQMLEVEaskLRELAEEAAKLRAVSEEAKR 2417
Cdd:TIGR04523 509 ---EEKVKDLTKKISSLKEKIEKLESEKkEKESKISDLEDELNKDDFELKKENLEKE---IDEKNKEIEELKQTQKSLKK 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2418 QRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKI 2497
Cdd:TIGR04523 583 KQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWP 662
|
....*...
gi 1835643837 2498 ILLKKSSD 2505
Cdd:TIGR04523 663 EIIKKIKE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2618-2852 |
6.96e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 6.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2618 AKAEEAKRQKELaeKEAERQIQlAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSIldklkeEAERAKRAAEDADF 2697
Cdd:COG4942 18 QADAAAEAEAEL--EQLQQEIA-ELEKELAALKKEEKALLKQLAALERRIAALARRIRAL------EQELAALEAELAEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2698 ARTRAEQEAALSRQQVEEAERLKQraeeeAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAE 2777
Cdd:COG4942 89 EKEIAELRAELEAQKEELAELLRA-----LYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2778 KTLRQKSQVEQELTKVKLQLEEtdhQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEE 2852
Cdd:COG4942 164 ALRAELEAERAELEALLAELEE---ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1720-1894 |
7.42e-06 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 50.91 E-value: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1720 VPSDSKELEATKAELKKLRSQVEGHQPLFNTLEAdlnkakdVNEQMLRSHSERDVDLdryREKVQQLLERWQAILVQIDL 1799
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNE-------LGEQLIEEGHPDAEEI---QERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1800 RQRELDQLGRQLRYYRETYEwLIKWIKDAKQRQEQIQsvPITDSKTMKEHLLQEKKLLDEIESNRDKVDECQKYAKQYID 1879
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1835643837 1880 AIKDYELQLVTYKAQ 1894
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2431-2658 |
7.58e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 52.52 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2431 AEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKiillkkssDNELER 2510
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA--------EAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2511 QKNIVEDTLRQRRIIEEEIRILKVNFEKAS-------------VGKSDLELeLNQLKNIAEETQRSKEKAEQEAEKQRQL 2577
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVLLGSESfsdfldrlsalskIADADADL-LEELKADKAELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2578 ALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHT 2657
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
.
gi 1835643837 2658 A 2658
Cdd:COG3883 243 A 243
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2159-2466 |
7.83e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.03 E-value: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2159 VEKERQIKVA-QEVAQQSAAAELNSKRmsFAEKTAQLElslkqehitvthlQEEAERLKKlhdeaekareeaekelekwH 2237
Cdd:PRK05035 428 VQYYRQAKAEiRAIEQEKKKAEEAKAR--FEARQARLE-------------REKAAREAR-------------------H 473
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2238 QKANEALRLRLQ------AEEVAHKKTLAQEEAEKQKED--------AEREARKRAKTEESAlrQKELAEDELEKQRKLA 2303
Cdd:PRK05035 474 KKAAEARAAKDKdavaaaLARVKAKKAAATQPIVIKAGArpdnsaviAAREARKAQARARQA--EKQAAAAADPKKAAVA 551
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2304 DATAqqkfsaeqeliRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKemeeelAKvRAEMEILLQSKsrAEEESRSN 2383
Cdd:PRK05035 552 AAIA-----------RAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAK------AK-KAAQQAASAEP--EEQVAEVD 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2384 TEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIA-LKEKE 2462
Cdd:PRK05035 612 PKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIArAKAKK 691
|
....
gi 1835643837 2463 AENE 2466
Cdd:PRK05035 692 AAQQ 695
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3418-3454 |
7.85e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 7.85e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1835643837 3418 IRLLEAQIATGGIIDPVDSHRLPLEVAYKRNYFDEEM 3454
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
650-757 |
7.91e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 49.27 E-value: 7.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 650 QKKTFTKWVNK---------HLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR----EKGRMRFHKLQNVQIALDYL 716
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1835643837 717 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 757
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2353-2964 |
8.00e-06 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 52.90 E-value: 8.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2353 KEMEEELaKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAK----LRAVSEE------AKRQRQIA 2422
Cdd:pfam10174 77 QALQDEL-RAQRDLNQLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHERQAKelflLRKTLEEmelrieTQKQTLGA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2423 EDEAARQRAE----------AERILKEKLAAINDATRLKTEAEIALKEKEAENERLRrlaedEAYQRKLlEEQATQHKQD 2492
Cdd:pfam10174 156 RDESIKKLLEmlqskglpkkSGEEDWERTRRIAEAEMQLGHLEVLLDQKEKENIHLR-----EELHRRN-QLQPDPAKTK 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2493 IEEKIILLKKSSDNELERQKNIVEDTLRqrriieeeirILKVNfekASVGKSDLELELNQLKNIAEETQRSKEKAEQeae 2572
Cdd:pfam10174 230 ALQTVIEMKDTKISSLERNIRDLEDEVQ----------MLKTN---GLLHTEDREEEIKQMEVYKSHSKFMKNKIDQ--- 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2573 kqrqlaLEEEQRRKEAE--------EKVRKILADEKE----------AARQRKAALE-EVERLKAKAEE-----AKRQKE 2628
Cdd:pfam10174 294 ------LKQELSKKESEllalqtklETLTNQNSDCKQhievlkesltAKEQRAAILQtEVDALRLRLEEkesflNKKTKQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2629 LAEKEAERQIQLAQEAALK--------KIDAEEKAHTAIVQQ---KEQEMLQTRKQEQS--------------------- 2676
Cdd:pfam10174 368 LQDLTEEKSTLAGEIRDLKdmldvkerKINVLQKKIENLQEQlrdKDKQLAGLKERVKSlqtdssntdtalttleealse 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2677 ---ILDKLKEEAERAKRA--AEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKR 2751
Cdd:pfam10174 448 kerIIERLKEQREREDRErlEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVE 527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2752 AHAEQAALKQKQL--ADEEMDKHKKFAEKTLRQKsQVEQEltkVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVE 2829
Cdd:pfam10174 528 QKKEECSKLENQLkkAHNAEEAVRTNPEINDRIR-LLEQE---VARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA 603
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2830 E----ELFKVKIQMEELIKLKLRIEEENKMLIMKD----------KDSTQKLLVEEA----EKMRQVAEEA-ARLSIEAQ 2890
Cdd:pfam10174 604 EleslTLRQMKEQNKKVANIKHGQQEMKKKGAQLLeearrrednlADNSQQLQLEELmgalEKTRQELDATkARLSSTQQ 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2891 eaarmrKLAEDD--LANQRALAEKMLKEKMQ--------AIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLA 2960
Cdd:pfam10174 684 ------SLAEKDghLTNLRAERRKQLEEILEmkqeallaAISEKDANIALLELSSSKKKKTQEEVMALKREKDRLVHQLK 757
|
....
gi 1835643837 2961 KETE 2964
Cdd:pfam10174 758 QQTQ 761
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2459-2754 |
8.10e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 52.29 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2459 KEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIE--EKIILLKKSSDNELERQKNIVEDTLRQrriieeeirilkvnf 2536
Cdd:PRK07735 5 KDLEDLKKEAARRAKEEARKRLVAKHGAEISKLEEEnrEKEKALPKNDDMTIEEAKRRAAAAAKA--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2537 eKASvgksdlELELNQLKNIAEETQRSKEKAEQEA--EKQRQLALEEEQRRKEAEEkvrkiLADEKEAARQRKAALEEve 2614
Cdd:PRK07735 70 -KAA------ALAKQKREGTEEVTEEEKAKAKAKAaaAAKAKAAALAKQKREGTEE-----VTEEEKAAAKAKAAAAA-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2615 rlKAKAEEAKRQKELAEKEA-ERQIQLAQEAALKKIDAEEKAHTAIVQQKEQemlqtrkQEQSILDKLKEEAERAKRAAE 2693
Cdd:PRK07735 136 --KAKAAALAKQKREGTEEVtEEEEETDKEKAKAKAAAAAKAKAAALAKQKA-------AEAGEGTEEVTEEEKAKAKAK 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2694 DADFARTRAeqeAALSRQQVEEA------ERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHA 2754
Cdd:PRK07735 207 AAAAAKAKA---AALAKQKASQGngdsgdEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4749-4781 |
8.49e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 8.49e-06
10 20 30
....*....|....*....|....*....|...
gi 1835643837 4749 VRKRRVVIVDPETGKEMSVYEAYRKGLIDQQTY 4781
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| FRQ1 |
COG5126 |
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms]; |
6845-6954 |
8.60e-06 |
|
Ca2+-binding protein, EF-hand superfamily [Signal transduction mechanisms];
Pssm-ID: 444056 [Multi-domain] Cd Length: 137 Bit Score: 49.02 E-value: 8.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6845 TAQQRLQELqdFAHFDfgVWRKRYLEW--ISRMKSRILD-IFRSIDRDQDGRISQQEFIESVLSSKFPTNSLEMNAVASI 6921
Cdd:COG5126 2 LQRRKLDRR--FDLLD--ADGDGVLERddFEALFRRLWAtLFSEADTDGDGRISREEFVAGMESLFEATVEPFARAAFDL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1835643837 6922 FDYNGDGFIDYYEF---VSALHPSRDTLR---KSLDADQ 6954
Cdd:COG5126 78 LDTDGDGKISADEFrrlLTALGVSEEEADelfARLDTDG 116
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4076-4112 |
8.91e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 8.91e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1835643837 4076 IRILEAQIATGGIIDPVHSHRVPVDIAYKRGYFDEEM 4112
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2038-2693 |
9.07e-06 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 52.72 E-value: 9.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2038 KAKQIEEVEynRRKIeeeihiVRLQLETMQKhkanaedELQELRARAEKAEQQKKAAQEEAERLRKQVkdetqkkreaeE 2117
Cdd:pfam05701 27 KAHRIQTVE--RRKL------VELELEKVQE-------EIPEYKKQSEAAEAAKAQVLEELESTKRLI-----------E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2118 ELKRKVQ-AEKEAAREKQraveDLEKFRSQAEEAERRM-KQAEVEKERQIKVAQEvAQQSAAAELNSKRMsfaektaqlE 2195
Cdd:pfam05701 81 ELKLNLErAQTEEAQAKQ----DSELAKLRVEEMEQGIaDEASVAAKAQLEVAKA-RHAAAVAELKSVKE---------E 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2196 L-SLKQEHITVTHLQEEAErlkklhdeaekareeaekelekwhQKANEAlrlrlqaeevahkkTLAQEEAEKQKEDAERE 2274
Cdd:pfam05701 147 LeSLRKEYASLVSERDIAI------------------------KRAEEA--------------VSASKEIEKTVEELTIE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2275 ARKRAKTEESAlrqkELAEDELEKQR-KLADATAQQKFSAEQELIRLKAETEnseqqrllleeelfrlknEVNEAIQKRK 2353
Cdd:pfam05701 189 LIATKESLESA----HAAHLEAEEHRiGAALAREQDKLNWEKELKQAEEELQ------------------RLNQQLLSAK 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2354 EMEEE-------LAKVRAEMEILLQSKSRAEEESRSNTEKSKQML-EVEASKLRELAEEAAKLRAVSEEAKRQRQIAede 2425
Cdd:pfam05701 247 DLKSKletasalLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIqAALASAKKELEEVKANIEKAKDEVNCLRVAA--- 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2426 aARQRAEAERiLKEKLAAINdatRLKTEAEIALKEKEAENERLRrlAEDEAYQRKllEEQATQHKQDIEEKiilLKKSSd 2505
Cdd:pfam05701 324 -ASLRSELEK-EKAELASLR---QREGMASIAVSSLEAELNRTK--SEIALVQAK--EKEAREKMVELPKQ---LQQAA- 390
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2506 NELERQKNIVE---DTLRQRriieeeirilKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEkqrqlALEEE 2582
Cdd:pfam05701 391 QEAEEAKSLAQaarEELRKA----------KEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIK-----ALQES 455
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2583 QRRKEAEekvrkilaDEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQ 2662
Cdd:pfam05701 456 ESSAEST--------NQEDSPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKLEEVNREMEER 527
|
650 660 670
....*....|....*....|....*....|.
gi 1835643837 2663 KEQEMLQTRKQEQSILDKLKEEAERAKRAAE 2693
Cdd:pfam05701 528 KEALKIALEKAEKAKEGKLAAEQELRKWRAE 558
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2678-3061 |
9.34e-06 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.99 E-value: 9.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2678 LDKLKEEAERAKRAAED--ADFARTRAEQEAAlsRQQVEEAERLKQRAEEEaqakaQAQDEAEKLRKEAELEAAKRAHAE 2755
Cdd:pfam19220 36 IEAILRELPQAKSRLLEleALLAQERAAYGKL--RRELAGLTRRLSAAEGE-----LEELVARLAKLEAALREAEAAKEE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2756 QA-ALKQKQLADEEmdkhkkfAEKTLRQKSQVEQELTkvkLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFK 2834
Cdd:pfam19220 109 LRiELRDKTAQAEA-------LERQLAAETEQNRALE---EENKALREEAQAAEKALQRAEGELATARERLALLEQENRR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2835 VKIQMEE----LIKLKLRIEEENKMLimkdkdstqkllveEAEKMRQVAEEAarlSIEAQEAARMRKLAEDDLANQRALA 2910
Cdd:pfam19220 179 LQALSEEqaaeLAELTRRLAELETQL--------------DATRARLRALEG---QLAAEQAERERAEAQLEEAVEAHRA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2911 EKM-LKEKMQAIQeaSRLKAEAEMLQKQKELAQEQARKFQE-DKEQIEQQLAKET-EGFQKSLEAERRQQLEITAEAERL 2987
Cdd:pfam19220 242 ERAsLRMKLEALT--ARAAATEQLLAEARNQLRDRDEAIRAaERRLKEASIERDTlERRLAGLEADLERRTQQFQEMQRA 319
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2988 KLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLH-QTELATKERMAVVQTLEIQRqqsgkeaeelRRAIAELEHEK 3061
Cdd:pfam19220 320 RAELEERAEMLTKALAAKDAALERAEERIASLSdRIAELTKRFEVERAALEQAN----------RRLKEELQRER 384
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2688-3027 |
9.57e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 51.83 E-value: 9.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2688 AKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADE 2767
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2768 EMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKL 2847
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDEL 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2848 RIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKM--QAIQEAS 2925
Cdd:COG4372 189 LKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEieELELAIL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2926 RLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDA 3005
Cdd:COG4372 269 VEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLV 348
|
330 340
....*....|....*....|..
gi 1835643837 3006 SKFKKKAEEIGNKLHQTELATK 3027
Cdd:COG4372 349 GLLDNDVLELLSKGAEAGVADG 370
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2979-3233 |
9.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2979 EITAEAERLKLQVLEMSRAQAKAEeDASKFKKKAEEIgNKLHQTELATKERMAVVQTLE--IQRQQSGKEAEELRRAIAE 3056
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALE-DAREQIELLEPI-RELAERYAAARERLAELEYLRaaLRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3057 LEHEKEKLKREAELLQknsqkmqvAQQEQLRQETQVLqttflsekqllleREKYIEEEKAKLENLyEDEVRKAQKLKQEQ 3136
Cdd:COG4913 300 LRAELARLEAELERLE--------ARLDALREELDEL-------------EAQIRGNGGDRLEQL-EREIERLERELEER 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3137 EHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRiALAQTR- 3215
Cdd:COG4913 358 ERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA-SLERRKs 436
|
250 260
....*....|....*....|..
gi 1835643837 3216 ----EMRTQTDDLAGNLPLTPT 3233
Cdd:COG4913 437 nipaRLLALRDALAEALGLDEA 458
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2091-2673 |
9.71e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.00 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2091 KKAAQEEAERLRKQVKD---------ETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEK 2161
Cdd:COG4913 220 EPDTFEAADALVEHFDDlerahealeDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2162 ERQIKVAQEVAQQSAAAELnskrmsfaEKTAQLELSLKQEHitvthLQEEAERLKKLhdeaekareeaEKELEKWHQKAN 2241
Cdd:COG4913 300 LRAELARLEAELERLEARL--------DALREELDELEAQI-----RGNGGDRLEQL-----------EREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2242 EALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEkqRKLADATAQQKfSAEQELIRLK 2321
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE--AALRDLRRELR-ELEAEIASLE 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2322 AetenseqqrllleeelfrlkNEVN---EAIQKRKEMEEELAKVRAEMEI---LLQSKSRaEEESRSNTEK----SKQML 2391
Cdd:COG4913 433 R--------------------RKSNipaRLLALRDALAEALGLDEAELPFvgeLIEVRPE-EERWRGAIERvlggFALTL 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2392 EVEASKLRELAE--EAAKLRA--VSEEAKRQRQIAEDEAARQRAEAERI----------LKEKLAAINDATRLKTEAEI- 2456
Cdd:COG4913 492 LVPPEHYAAALRwvNRLHLRGrlVYERVRTGLPDPERPRLDPDSLAGKLdfkphpfrawLEAELGRRFDYVCVDSPEELr 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2457 ----------------ALKEKEAENERLRR--LAEDEAYQRKLLEEQATQHKQDIEEkiillkksSDNELERQKNIVEDT 2518
Cdd:COG4913 572 rhpraitragqvkgngTRHEKDDRRRIRSRyvLGFDNRAKLAALEAELAELEEELAE--------AEERLEALEAELDAL 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2519 LRQRRIIEEEiriLKVNFEKASVGKSDLEL-ELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILA 2597
Cdd:COG4913 644 QERREALQRL---AEYSWDEIDVASAEREIaELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK 720
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2598 DEKEAARQRKAALEEVERLKAKAEEAKRQkELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQ 2673
Cdd:COG4913 721 ELEQAEEELDELQDRLEAAEDLARLELRA-LLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2541-2752 |
9.74e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.47 E-value: 9.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2541 VGKSDLELELNQLKNIAEETQRSKEKaEQEAEKQRQLAleeeqrrkEAEEKVRKILAD-EKEaARQRKAALEEVE-RLKA 2618
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRILEEAKK-EAEAIKKEALL--------EAKEEIHKLRNEfEKE-LRERRNELQKLEkRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2619 KAEEAKRQKELAEKEAERqiqlaqeaalkkidaeekahtaiVQQKEQEMlqtrKQEQSILDKLKEEAERAKRAAEDadfa 2698
Cdd:PRK12704 94 KEENLDRKLELLEKREEE-----------------------LEKKEKEL----EQKQQELEKKEEELEELIEEQLQ---- 142
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2699 rtRAEQEAALSRqqvEEA-ERLKQRAEEEAQAKAQAQ-DEAEklrKEAELEAAKRA 2752
Cdd:PRK12704 143 --ELERISGLTA---EEAkEILLEKVEEEARHEAAVLiKEIE---EEAKEEADKKA 190
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1932-2163 |
9.95e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 9.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1932 TSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEElqrRMQEEVSKREVVAV 2011
Cdd:pfam02029 92 TIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE---EGEEEEDKSEEAEE 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2012 DAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKI---EEEIHIVRLQLETMQKHKANAEDELQELRARAE--- 2085
Cdd:pfam02029 169 VPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSqngEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEaeq 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2086 KAEQQKKAAQEEAERLRKQVKdetQKKREAE---EELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKE 2162
Cdd:pfam02029 249 KLEELRRRRQEKESEEFEKLR---QKQQEAElelEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERR 325
|
.
gi 1835643837 2163 R 2163
Cdd:pfam02029 326 R 326
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2071-2142 |
1.05e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 49.02 E-value: 1.05e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2071 ANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKRE-----AEEELKRKV-QAEKEAAREKQRAVEDLEK 2142
Cdd:COG0711 41 AEAERAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEeakaeAEAEAERIIaQAEAEIEQERAKALAELRA 118
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2024-2325 |
1.07e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2024 LQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLE----TMQKHKANAEDELQELRARAEKAEQQKKAAQEEAE 2099
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWErqrrELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2100 RLRKQvKDETQKKREAEEELKRKVQAEKEAAREKQRAVE-DLEKFRSQAEEAERRMKQAEVEKER-QIKVAQ-EVAQQSA 2176
Cdd:pfam07888 112 ELSEE-KDALLAQRAAHEARIRELEEDIKTLTQRVLEREtELERMKERAKKAGAQRKEEEAERKQlQAKLQQtEEELRSL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2177 AAELNSKRMSFAEKTAQLeLSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKAN---------EALRLR 2247
Cdd:pfam07888 191 SKEFQELRNSLAQRDTQV-LQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEglgeelssmAAQRDR 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2248 LQAEevAHKKTLAQEEAEKQKEDAE---REARKRAKTEESALRQKelAEDELEKQRKLADATAQ-QKFSAEQELIRLKAE 2323
Cdd:pfam07888 270 TQAE--LHQARLQAAQLTLQLADASlalREGRARWAQERETLQQS--AEADKDRIEKLSAELQRlEERLQEERMEREKLE 345
|
..
gi 1835643837 2324 TE 2325
Cdd:pfam07888 346 VE 347
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1943-2049 |
1.08e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 52.71 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1943 LRRLNDEEKAaeklkEEERRRLAEVEAQLAKQTQ----LAEAHAKAKA-QAEKEAEELQRRMQEEVSKREVVAvDAEQQK 2017
Cdd:PTZ00491 685 RQKMHDKAKA-----EEQRTKLLELQAESAAVESsgqsRAEALAEAEArLIEAEAEVEQAELRAKALRIEAEA-ELEKLR 758
|
90 100 110
....*....|....*....|....*....|..
gi 1835643837 2018 QTIQQELQQLRQNSDMEIKsKAKQIEEVEYNR 2049
Cdd:PTZ00491 759 KRQELELEYEQAQNELEIA-KAKELADIEATK 789
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2544-2758 |
1.15e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2544 SDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEA--------------------- 2602
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvllgsesfsdfld 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2603 --------ARQRKAALEEVERLKAKAEEAKRQkelAEKEAERQIQLAQEAALKKIDAEEKahtaiVQQKEQEMLQTRKQE 2674
Cdd:COG3883 120 rlsalskiADADADLLEELKADKAELEAKKAE---LEAKLAELEALKAELEAAKAELEAQ-----QAEQEALLAQLSAEE 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2675 QSILDKlKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHA 2754
Cdd:COG3883 192 AAAEAQ-LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAG 270
|
....
gi 1835643837 2755 EQAA 2758
Cdd:COG3883 271 AAGA 274
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2085-2315 |
1.25e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2085 EKAEQQKKAAQEEAERLRKQvkdetqKKREAEEE-LKRKVQAEKEAaREKQRAVEDLEKFRSQAEEAERRmKQAEVEKER 2163
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKE------ALLEAKEEiHKLRNEFEKEL-RERRNELQKLEKRLLQKEENLDR-KLELLEKRE 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2164 QikvaqevaqqsaaaELNSKRMSfaektaqlelslkqehitVTHLQEEAERLKKlhdeaekareeaekELEKWHQKANEA 2243
Cdd:PRK12704 110 E--------------ELEKKEKE------------------LEQKQQELEKKEE--------------ELEELIEEQLQE 143
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2244 LrlrlqaEEVAhkkTLAQEEA-----EKQKEDAEREARKRAKTEEsalrqkELAEDELEKQRKLADATAQQKFSAEQ 2315
Cdd:PRK12704 144 L------ERIS---GLTAEEAkeillEKVEEEARHEAAVLIKEIE------EEAKEEADKKAKEILAQAIQRCAADH 205
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2183-2787 |
1.27e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.05 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2183 KRMSFAEKTAQLELsLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKAnEALRLRLQAEEVAHKKtlaQE 2262
Cdd:pfam05557 19 KQMELEHKRARIEL-EKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA-ELNRLKKKYLEALNKK---LN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2263 EAEKQKEDAE----------REARKRAKTEESALRQKELAEDELEKQRKLADATAQQkfsAEQELIRLKAETEnseqqrl 2332
Cdd:pfam05557 94 EKESQLADARevisclknelSELRRQIQRAELELQSTNSELEELQERLDLLKAKASE---AEQLRQNLEKQQS------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2333 lleeelfrlknEVNEAIQKRKEMEEELAKVRAEMEILlqSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRavS 2412
Cdd:pfam05557 164 -----------SLAEAEQRIKELEFEIQSQEQDSEIV--KNSKSELARIPELEKELERLREHNKHLNENIENKLLLK--E 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2413 EEAKRQRQIAEDEAARQRAEAERILKEKLaaindatrlktEAEIALKEKEAENERLRrLAEDEAYQRKLLEEQAtqhkqd 2492
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLELEKEKL-----------EQELQSWVKLAQDTGLN-LRSPEDLSRRIEQLQQ------ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2493 iEEKIILLKKSSDNELERQKNIVEDTLRQRRiieeeirilkvnfekasvgksdleleLNQLKNIAEETQRSKEKAEQEAE 2572
Cdd:pfam05557 291 -REIVLKEENSSLTSSARQLEKARRELEQEL--------------------------AQYLKKIEDLNKKLKRHKALVRR 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2573 KQRQLALEEEQRR--KEAEEKVRKILAdEKEAARQRKAALEEVERL----KAKAEEAKRQKELAEKEAERQIQLAQeaal 2646
Cdd:pfam05557 344 LQRRVLLLTKERDgyRAILESYDKELT-MSNYSPQLLERIEEAEDMtqkmQAHNEEMEAQLSVAEEELGGYKQQAQ---- 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2647 kkidAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAErakraAEDADFARTRAEQEAALSR---QQVEEAERLK--- 2720
Cdd:pfam05557 419 ----TLERELQALRQQESLADPSYSKEEVDSLRRKLETLE-----LERQRLREQKNELEMELERrclQGDYDPKKTKvlh 489
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2721 QRAEEEAQAKAQAQDEAEKLRKEAEleaAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVE 2787
Cdd:pfam05557 490 LSMNPAAEAYQQRKNQLEKLQAEIE---RLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2063-2313 |
1.32e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 51.90 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2063 LETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAErlrkqvKDETQKKREAE--EELKRKVQAE---KEAAREKQRav 2137
Cdd:PRK07735 7 LEDLKKEAARRAKEEARKRLVAKHGAEISKLEEENRE------KEKALPKNDDMtiEEAKRRAAAAakaKAAALAKQK-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2138 edlekfRSQAEEAerrmkqAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKK 2217
Cdd:PRK07735 79 ------REGTEEV------TEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQK 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2218 LHDEAEKAREEAEKELEKWHQKANEALRLR---LQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESAL-RQKE--- 2290
Cdd:PRK07735 147 REGTEEVTEEEEETDKEKAKAKAAAAAKAKaaaLAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALaKQKAsqg 226
|
250 260
....*....|....*....|....*
gi 1835643837 2291 --LAEDELEKQRKLADATAQQKFSA 2313
Cdd:PRK07735 227 ngDSGDEDAKAKAIAAAKAKAAAAA 251
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2661-2789 |
1.33e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2661 QQKEQEMLQTRKQEQsildklkeeaeRAKRAAEDADfaRTRAEQEAALSRQQVEEAERLKQR-----AEEEAQAKAQAQD 2735
Cdd:PRK09510 66 RQQQQQKSAKRAEEQ-----------RKKKEQQQAE--ELQQKQAAEQERLKQLEKERLAAQeqkkqAEEAAKQAALKQK 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2736 EAEKLRKEAELEAAKRAHAEQ--AALKQKQLADEEMDKHKKFAEKTLRQKSQVEQE 2789
Cdd:PRK09510 133 QAEEAAAKAAAAAKAKAEAEAkrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAE 188
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2723-3096 |
1.39e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.22 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2723 AEEEAQAKAQAQDEAEKLRKEAELEAakrahaEQAALKQkQLADeemdkhkkfAEKTLRQKSQVEQELTKVKLQLEETDH 2802
Cdd:PRK11281 31 SNGDLPTEADVQAQLDALNKQKLLEA------EDKLVQQ-DLEQ---------TLALLDKIDRQKEETEQLKQQLAQAPA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2803 QKTLLDEELQRLKEEVTDAMRQK------AQVEEELFKVKIQMEE-----------LIKLK--------------LRIEE 2851
Cdd:PRK11281 95 KLRQAQAELEALKDDNDEETRETlstlslRQLESRLAQTLDQLQNaqndlaeynsqLVSLQtqperaqaalyansQRLQQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2852 ENKMLimKDKDSTQKLLVEEAEKMRQvAEEAArlsIEAQEAARmRKLAED-----DLANQR----ALAEKMLKEKMQAIQ 2922
Cdd:PRK11281 175 IRNLL--KGGKVGGKALRPSQRVLLQ-AEQAL---LNAQNDLQ-RKSLEGntqlqDLLQKQrdylTARIQRLEHQLQLLQ 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2923 EA--SRLKAEAEMlQKQKELAQEQARKFQED----KE-----QIEQQLAKETEG----FQKSLEAerRQQLEITAEAER- 2986
Cdd:PRK11281 248 EAinSKRLTLSEK-TVQEAQSQDEAARIQANplvaQEleinlQLSQRLLKATEKlntlTQQNLRV--KNWLDRLTQSERn 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2987 LKLQV------LEMSR---AQAKAEEDASKFKKKAEEIGN-KLHQTELaTKER------MAVVQTLEiqRQQSGKEAEEL 3050
Cdd:PRK11281 325 IKEQIsvlkgsLLLSRilyQQQQALPSADLIEGLADRIADlRLEQFEI-NQQRdalfqpDAYIDKLE--AGHKSEVTDEV 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 3051 RRAIAELehekekLKREAELL-----QKNSQKM-----QVAQQeQLRQETQVLQTT 3096
Cdd:PRK11281 402 RDALLQL------LDERRELLdqlnkQLNNQLNlainlQLNQQ-QLLSVSDSLQST 450
|
|
| EH |
cd00052 |
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and ... |
6881-6940 |
1.41e-05 |
|
Eps15 homology domain; found in proteins implicated in endocytosis, vesicle transport, and signal transduction. The alignment contains a pair of EF-hand motifs, typically one of them is canonical and binds to Ca2+, while the other may not bind to Ca2+. A hydrophobic binding pocket is formed by residues from both EF-hand motifs. The EH domain binds to proteins containing NPF (class I), [WF]W or SWG (class II), or H[TS]F (class III) sequence motifs.
Pssm-ID: 238009 [Multi-domain] Cd Length: 67 Bit Score: 46.06 E-value: 1.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 6881 DIFRSIDRDQDGRISQQEFIESVLSSKFPTNSLemnavASIFDY---NGDGFIDYYEFVSALH 6940
Cdd:cd00052 3 QIFRSLDPDGDGLISGDEARPFLGKSGLPRSVL-----AQIWDLadtDKDGKLDKEEFAIAMH 60
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2051-2195 |
1.42e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 49.82 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2051 KIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKRE--AEEELKRKVQAEKE 2128
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREdlAREALERKAELEAQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2129 AAREKQ---RAVEDLEKFRSQAEEAERRMKQAEVEKER---QIKVAQ---EVAQQSAAAELNSKRMSFA---EKTAQLE 2195
Cdd:COG1842 100 AEALEAqlaQLEEQVEKLKEALRQLESKLEELKAKKDTlkaRAKAAKaqeKVNEALSGIDSDDATSALErmeEKIEEME 178
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1955-2435 |
1.54e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.95 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1955 KLKEEERRRLAEVEAQLAKQTQLAEAHAK-AKAQAE-----KEAEELQRRMQEEVSKREVVAVDAEqqkqtiqqelqqlr 2028
Cdd:pfam05701 104 KLRVEEMEQGIADEASVAAKAQLEVAKARhAAAVAElksvkEELESLRKEYASLVSERDIAIKRAE-------------- 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2029 qnsdmEIKSKAKQIEeveynrRKIEE---EIHIVRLQLETMQKhkanAEDELQELRARAEKAEQQK--------KAAQEE 2097
Cdd:pfam05701 170 -----EAVSASKEIE------KTVEEltiELIATKESLESAHA----AHLEAEEHRIGAALAREQDklnwekelKQAEEE 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2098 AERLRKQV--KDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKE-RQIKVAQEvaqq 2174
Cdd:pfam05701 235 LQRLNQQLlsAKDLKSKLETASALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAALASAKKElEEVKANIE---- 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2175 SAAAELNSKRMSFAEKTAQLE------LSLKQEH----ITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEAL 2244
Cdd:pfam05701 311 KAKDEVNCLRVAAASLRSELEkekaelASLRQREgmasIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAA 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2245 RlrlQAEEVAHKKTLAQEEAEKQKEDAErEARKRAKTEESALR--QKE-LAEDELEkqrKLADATAQqkfsAEQElirlk 2321
Cdd:pfam05701 391 Q---EAEEAKSLAQAAREELRKAKEEAE-QAKAAASTVESRLEavLKEiEAAKASE---KLALAAIK----ALQE----- 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2322 AETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMeEELAKVRAeMEILLQSKSRAEEESRSntekskqmLEVEASKLREL 2401
Cdd:pfam05701 455 SESSAESTNQEDSPRGVTLSLEEYYELSKRAHEA-EELANKRV-AEAVSQIEEAKESELRS--------LEKLEEVNREM 524
|
490 500 510
....*....|....*....|....*....|....*..
gi 1835643837 2402 AEEAAKLRAVSEEAKRQRQ---IAEDEAARQRAEAER 2435
Cdd:pfam05701 525 EERKEALKIALEKAEKAKEgklAAEQELRKWRAEHEQ 561
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2620-3019 |
1.55e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 51.58 E-value: 1.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2620 AEEAKRQKElAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFAR 2699
Cdd:COG3064 1 AQEALEEKA-AEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2700 TRAEQEAALSRQQVE-EAERLKQRAEEEA---QAKAQAQDE-AEKLRKEAELEAAKRAhAEQAALKQKQLADEEMDKHKK 2774
Cdd:COG3064 80 AEAEKAAAEAEKKAAaEKAKAAKEAEAAAaaeKAAAAAEKEkAEEAKRKAEEEAKRKA-EEERKAAEAEAAAKAEAEAAR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2775 FAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENK 2854
Cdd:COG3064 159 AAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2855 MLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEML 2934
Cdd:COG3064 239 ATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2935 QKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEE 3014
Cdd:COG3064 319 AAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGG 398
|
....*
gi 1835643837 3015 IGNKL 3019
Cdd:COG3064 399 GLLGL 403
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
2570-2690 |
1.57e-05 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 51.14 E-value: 1.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2570 EAEKQRQLALEEEQRRKEAEEKVRkilADEKEAARQRKAaleEVERLKAKaeeakRQKELAEKEAERQIQLAQEAALKKI 2649
Cdd:pfam07767 206 EAEKKRLKEEEKLERVLEKIAESA---ATAEAREEKRKT---KAQRNKEK-----RRKEEEREAKEEKALKKKLAQLERL 274
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1835643837 2650 DAEEKAhtaiVQQKEQEMLQTRKQEQSILDKLKEEAERAKR 2690
Cdd:pfam07767 275 KEIAKE----IAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2292-2488 |
1.69e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2292 AEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEM----- 2366
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2367 ------------EILLQSKSRAEEESRSntekskQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAE 2434
Cdd:COG3883 94 alyrsggsvsylDVLLGSESFSDFLDRL------SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2435 RILKEKLAAINDATRLKteAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQ 2488
Cdd:COG3883 168 AAKAELEAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2716-2945 |
1.71e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.94 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2716 AERLKQRAEEEAQAKAQAQDEAEKLRKEAEleaakRAHAEQAALKQKQL---ADEEmdkhkkfAEKTLRQKSQVEQELTK 2792
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE-----EAEAALEEFRQKNGlvdLSEE-------AKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2793 VKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKA--QVEEELFKVKIQMEELiklKLRIEEENKMLimkdkdstQKLLVE 2870
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAEL---SARYTPNHPDV--------IALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2871 EAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAE--------MLQKQKELAQ 2942
Cdd:COG3206 300 IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvarelyesLLQRLEEARL 379
|
...
gi 1835643837 2943 EQA 2945
Cdd:COG3206 380 AEA 382
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2903-3207 |
1.72e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 50.97 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2903 LANQRALAEKMLKEKMQAiqeasrlkaEAEMLQKQKELAQEQARKFQEDKEQIE--QQLAKETEGFQKSLEAERRQQLEI 2980
Cdd:pfam15905 50 PATARKVKSLELKKKSQK---------NLKESKDQKELEKEIRALVQERGEQDKrlQALEEELEKVEAKLNAAVREKTSL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2981 TAEAERLKLQVLEMSRA----QAKAEEDASKFKKKA--EEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAI 3054
Cdd:pfam15905 121 SASVASLEKQLLELTRVnellKAKFSEDGTQKKMSSlsMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3055 AELEHEKEKLKREaellqKNSQKMQVAQQEQLRQETQvlqttflsekQLLLEREKYiEEEKAKLENLYEDEVRKAQKLKQ 3134
Cdd:pfam15905 201 AQLEEKLVSTEKE-----KIEEKSETEKLLEYITELS----------CVSEQVEKY-KLDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3135 EqehqmkhLEEEKDQLKVSMDDAMKKQKEAEEnvrrkqdELQQLDKKRQEQEKLLADENRKLREKLEQMEEEH 3207
Cdd:pfam15905 265 S-------LEEKEQELSKQIKDLNEKCKLLES-------EKEELLREYEEKEQTLNAELEELKEKLTLEEQEH 323
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
645-753 |
1.72e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 47.67 E-value: 1.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 645 ERDRVQKKTFTKWVNKhlIKAQRHVSDLYEDLRDGHNLISLLEV---------LSGDNLPREKGRMRfhKLQNVQIALDY 715
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1835643837 716 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 753
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1947-2435 |
1.79e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 51.58 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1947 NDEEKAAEKLKEEerrRLAEVEAQlakQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQ 2026
Cdd:COG3064 4 ALEEKAAEAAAQE---RLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2027 LRQNSDMEIKSKAKQIEEvEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVK 2106
Cdd:COG3064 78 KLAEAEKAAAEAEKKAAA-EKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2107 DETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMS 2186
Cdd:COG3064 157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2187 FAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEK 2266
Cdd:COG3064 237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2267 QKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVN 2346
Cdd:COG3064 317 VLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2347 EAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEA 2426
Cdd:COG3064 397 GGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAV 476
|
....*....
gi 1835643837 2427 ARQRAEAER 2435
Cdd:COG3064 477 LADLLLLGG 485
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2059-2171 |
1.80e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 52.01 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2059 VRLQLETMQKHKANAEDELQELRARAEKAEQ-QKKAAQEEAERLRKQVKDetqkKREAEEELKRKVQAEKEAAREKQRAV 2137
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKeQDEASFERLAELRDELAE----LEEELEALKARWEAEKELIEEIQELK 477
|
90 100 110
....*....|....*....|....*....|....
gi 1835643837 2138 EDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEV 2171
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2579-2947 |
1.80e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 51.22 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2579 LEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERL--KAKAEEAKRQKELAEKEAERQiqlAQEAALKKIDAEEKAH 2656
Cdd:pfam19220 40 LRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRlsAAEGELEELVARLAKLEAALR---EAEAAKEELRIELRDK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2657 TAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEdadfARTRAEQEAALSRQQV----EEAERLKQRAEEeaqakaQ 2732
Cdd:pfam19220 117 TAQAEALERQLAAETEQNRALEEENKALREEAQAAEK----ALQRAEGELATARERLalleQENRRLQALSEE------Q 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2733 AQDEAEKLRKEAELEAAKRAHAEQAALKQKQLAdeemdkhkkfAEKTLRQKSQVEQELTKVKLQLEETDHQKTLldEELQ 2812
Cdd:pfam19220 187 AAELAELTRRLAELETQLDATRARLRALEGQLA----------AEQAERERAEAQLEEAVEAHRAERASLRMKL--EALT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2813 -------RLKEEVTDAMRQKaqvEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLveEAEKMRQVAEEAARL 2885
Cdd:pfam19220 255 araaateQLLAEARNQLRDR---DEAIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQ--EMQRARAELEERAEM 329
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2886 ---SIEAQEAARMRklAEDDLANQR----ALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQ---EQARK 2947
Cdd:pfam19220 330 ltkALAAKDAALER--AEERIASLSdriaELTKRFEVERAALEQANRRLKEELQRERAERALAQgalEIARE 399
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2680-2947 |
2.01e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.49 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2680 KLKEEAERAKRAAEdadfARTRAEQ-EAALSRQQVEEAERLKQRAEeeaQAKAQAQDeaeklrkeAELEAAKRAHAEQAA 2758
Cdd:PRK05035 437 EIRAIEQEKKKAEE----AKARFEArQARLEREKAAREARHKKAAE---ARAAKDKD--------AVAAALARVKAKKAA 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2759 LKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQ 2838
Cdd:PRK05035 502 ATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAA 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2839 MEELI-KLKLRIEEENkmlimKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARM--RKLAEDDLANQRALAEKMLK 2915
Cdd:PRK05035 582 VAAAIaRAKAKKAAQQ-----AASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANaePEEPVDPRKAAVAAAIARAK 656
|
250 260 270
....*....|....*....|....*....|....*
gi 1835643837 2916 EKMQAIQEASRLKAEAEMLQKQK---ELAQEQARK 2947
Cdd:PRK05035 657 ARKAAQQQANAEPEEAEDPKKAAvaaAIARAKAKK 691
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1941-2325 |
2.11e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 51.57 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1941 ETLRRLNDEEKAAEKLKeeerrrlAEVEAQLAKQTQL-AEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAvdaeqqkqt 2019
Cdd:pfam05701 233 EELQRLNQQLLSAKDLK-------SKLETASALLLDLkAELAAYMESKLKEEADGEGNEKKTSTSIQAALA--------- 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2020 iqqelqqlrqnsdmeikSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAE 2099
Cdd:pfam05701 297 -----------------SAKKELEEVKANIEKAKDEVNCLRVAAASLRSELEKEKAELASLRQREGMASIAVSSLEAELN 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2100 RLRKQVKDETQKKREAEE---ELKRKVQ-AEKEAAREK---QRAVEDLEKFRSQAEEA-------ERRMKQAEVEKErQI 2165
Cdd:pfam05701 360 RTKSEIALVQAKEKEAREkmvELPKQLQqAAQEAEEAKslaQAAREELRKAKEEAEQAkaaastvESRLEAVLKEIE-AA 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2166 KVAQEVAQQSAAAELNSKrmSFAEKTAQLELSLKqehITVThLQEEAERLKKLHDeaekareeaekelekwhqkanealr 2245
Cdd:pfam05701 439 KASEKLALAAIKALQESE--SSAESTNQEDSPRG---VTLS-LEEYYELSKRAHE------------------------- 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2246 lrlqAEEVAHKKTlaqEEAEKQKEDA-EREARKRAKTEEsALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAET 2324
Cdd:pfam05701 488 ----AEELANKRV---AEAVSQIEEAkESELRSLEKLEE-VNREMEERKEALKIALEKAEKAKEGKLAAEQELRKWRAEH 559
|
.
gi 1835643837 2325 E 2325
Cdd:pfam05701 560 E 560
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2789-3208 |
2.22e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2789 ELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEEliklKLRIEEEnkmliMKDKDSTQKLL 2868
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDM----KNRYESE-----IKTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2869 VEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKF 2948
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRY 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2949 QEDKEQIE---------QQLAKETEGFQKSLEAERRQQLEITAEaerlklqvleMSRAQAKAEEDASKFKKKAEEIGNKL 3019
Cdd:PRK01156 349 DDLNNQILelegyemdyNSYLKSIESLKKKIEEYSKNIERMSAF----------ISEILKIQEIDPDAIKKELNEINVKL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3020 HQTElatkermavvqtleiqrqqsgKEAEELRRAIAELEHEKEKLKREAELLQKNSQkmqvaqqeqlrqeTQVLQTTFLS 3099
Cdd:PRK01156 419 QDIS---------------------SKVSSLNQRIRALRENLDELSRNMEMLNGQSV-------------CPVCGTTLGE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3100 EKQLLLeREKYiEEEKAKLEnlyeDEVRKAqklkqeqEHQMKHLEEEKDQLKvSMDDAMKKQKeaeenVRRKQDELQQLD 3179
Cdd:PRK01156 465 EKSNHI-INHY-NEKKSRLE----EKIREI-------EIEVKDIDEKIVDLK-KRKEYLESEE-----INKSINEYNKIE 525
|
410 420 430
....*....|....*....|....*....|.
gi 1835643837 3180 KKRQEQEKLLADENR--KLREKLEQMEEEHR 3208
Cdd:PRK01156 526 SARADLEDIKIKINElkDKHDKYEEIKNRYK 556
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3344-3377 |
2.24e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 2.24e-05
10 20 30
....*....|....*....|....*....|....
gi 1835643837 3344 LLEAQAASGFIIDPVKNKRLSVNEAVKENVIGPE 3377
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
3046-3164 |
2.29e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 51.62 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3046 EAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLErekyIEEEKAKLENLYEDE 3125
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEE----IQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 3126 VRKAQKLKQEQEHQMKH----------------------------LEEEKDQLkVSMDDAMKK----QKEA 3164
Cdd:COG0542 488 PELEKELAELEEELAELapllreevteediaevvsrwtgipvgklLEGEREKL-LNLEEELHErvigQDEA 557
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2889-3165 |
2.36e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 51.56 E-value: 2.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2889 AQEAARMRKLAEDDLANQRALAE--KMLKEKMQAIQEAS----RLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKE 2962
Cdd:COG3206 96 LERVVDKLNLDEDPLGEEASREAaiERLRKNLTVEPVKGsnviEISYTSPDPELAAAVANALAEAYLEQNLELRREEARK 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2963 TEGFQKSLEAERRQQLEitaEAERlKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQ 3042
Cdd:COG3206 176 ALEFLEEQLPELRKELE---EAEA-ALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGS 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3043 SGKEAEELRR--AIAELEHEKEKLKRE-AELLQK---NSQKMQVAQQE------QLRQETQVLQTTFLSEKQLLLEREKY 3110
Cdd:COG3206 252 GPDALPELLQspVIQQLRAQLAELEAElAELSARytpNHPDVIALRAQiaalraQLQQEAQRILASLEAELEALQAREAS 331
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 3111 IEEEKAKLENLYEDEVRKAQKLKQeqehqmkhLEEEKDQLKVSMDDAMKKQKEAE 3165
Cdd:COG3206 332 LQAQLAQLEARLAELPELEAELRR--------LEREVEVARELYESLLQRLEEAR 378
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1943-2195 |
2.44e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 51.18 E-value: 2.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1943 LRRLNDEEKAAEKlKEEERRRLAEveaQLakqTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQ 2022
Cdd:pfam05667 232 ASRLTPEEYRKRK-RTKLLKRIAE---QL---RSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTE 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2023 ELQ--QLRQNSDMEIKSKAKQIEEVEYNRrkiEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAER 2100
Cdd:pfam05667 305 KLQftNEAPAATSSPPTKVETEEELQQQR---EEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2101 LRKQVKdetQKKR------EAEE---ELKRKVQAEKE-----AAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKErQIK 2166
Cdd:pfam05667 382 LEKQYK---VKKKtldllpDAEEniaKLQALVDASAQrlvelAGQWEKHRVPLIEEYRALKEAKSNKEDESQRKLE-EIK 457
|
250 260
....*....|....*....|....*....
gi 1835643837 2167 VAQEVAQQsAAAELNSKRMSFAEKTAQLE 2195
Cdd:pfam05667 458 ELREKIKE-VAEEAKQKEELYKQLVAEYE 485
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2410-2645 |
2.46e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.58 E-value: 2.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2410 AVSEEAKRQRQiaeDEAARQRAEAERilkEKLAaindatrlKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQH 2489
Cdd:PRK09510 59 AVVEQYNRQQQ---QQKSAKRAEEQR---KKKE--------QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2490 KQdieekiillkkssdnELERQKNIVEDTLRQRriieeeirilkvnfEKASVGKSDLELELNQLKNIAEETQRSKEKAE- 2568
Cdd:PRK09510 125 KQ---------------AALKQKQAEEAAAKAA--------------AAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEa 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2569 ---QEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKrqKELAEKEAERQIQLAQEAA 2645
Cdd:PRK09510 176 akkAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA--KAAAEKAAAAKAAEKAAAA 253
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1920-2185 |
2.50e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1920 DLRTRYSELTTLTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLaEAHAKAKAQAEKEAEELQRRM 1999
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2000 QEEVSKREVVAVDAEQQKQTIQQELQQLRQNS---DMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDE 2076
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEELrslSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2077 LQELRARAEKAEqqkkAAQEEAERLRKQVKDETQKKREAEEELKR-KVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMK 2155
Cdd:pfam07888 236 LEELRSLQERLN----ASERKVEGLGEELSSMAAQRDRTQAELHQaRLQAAQLTLQLADASLALREGRARWAQERETLQQ 311
|
250 260 270
....*....|....*....|....*....|
gi 1835643837 2156 QAEVEKERQIKVAQEVaqQSAAAELNSKRM 2185
Cdd:pfam07888 312 SAEADKDRIEKLSAEL--QRLEERLQEERM 339
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1615-2158 |
2.52e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 51.44 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1615 KDPIKECSQRIS-------EQQQIHFELEGIKKNLNKvSEKTLKVLAQKEQSSSSPLLRTEHEITHQKmDQVYSLSSIyL 1687
Cdd:PRK01156 172 KDVIDMLRAEISnidyleeKLKSSNLELENIKKQIAD-DEKSHSITLKEIERLSIEYNNAMDDYNNLK-SALNELSSL-E 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1688 EKLKTINLVIRSTQGAEEVVRTYEDQLKEVHavpSDSKELEATKAELK--------KLRSQVEGHQPLFNTLEADLNKAK 1759
Cdd:PRK01156 249 DMKNRYESEIKTAESDLSMELEKNNYYKELE---ERHMKIINDPVYKNrnyindyfKYKNDIENKKQILSNIDAEINKYH 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1760 DVneqmLRSHSERDVDLDRYREKVQQLLERWQAILvqiDLRQRELDQLGrqlryYRETYEWLIKWIKDAKQRQEQIQSVP 1839
Cdd:PRK01156 326 AI----IKKLSVLQKDYNDYIKKKSRYDDLNNQIL---ELEGYEMDYNS-----YLKSIESLKKKIEEYSKNIERMSAFI 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1840 ITDSKTMKEHLLQEKKLLDEIESNRDKVDECQKYAKQYIDAIKDYELQLvtyKAQVEPVASPAKKPKVQSTSDSiiQEYV 1919
Cdd:PRK01156 394 SEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDEL---SRNMEMLNGQSVCPVCGTTLGE--EKSN 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1920 DLRTRYSELTTLTSQYIKFITETLRRLNDEEKAAEKLKEeeRRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRM 1999
Cdd:PRK01156 469 HIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKE--YLESEEINKSINEYNKIESARADLEDIKIKINELKDKHD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2000 QEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELqe 2079
Cdd:PRK01156 547 KYEEIKNRYKSLKLEDLDSKRTSWLNALAVISLIDIETNRSRSNEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREI-- 624
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2080 lraraekaeqqkkaaQEEAERLRKQvKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAE 2158
Cdd:PRK01156 625 ---------------ENEANNLNNK-YNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEITSRINDIEDNLKKSR 687
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1991-2409 |
2.53e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 51.36 E-value: 2.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1991 EAEELQRRMQEE---VSKREVVAVDAEQQKQTIQQELQQLRQNSDME---IKSKAKQIEEVEYNRRKIEEEIHIVRLQLE 2064
Cdd:pfam10174 346 EVDALRLRLEEKesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKerkINVLQKKIENLQEQLRDKDKQLAGLKERVK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2065 TMQKHKANAEDELQELR-ARAEKaEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDL-EK 2142
Cdd:pfam10174 426 SLQTDSSNTDTALTTLEeALSEK-ERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLkEH 504
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2143 FRSQAEEA---ERRMKQAEVEKER----------QIKVAQEVAQQSAAAElnskrmSFAEKTAQLELSLKQEHITVTHLQ 2209
Cdd:pfam10174 505 ASSLASSGlkkDSKLKSLEIAVEQkkeecsklenQLKKAHNAEEAVRTNP------EINDRIRLLEQEVARYKEESGKAQ 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2210 EEAERLKKLHDEAEKAREEAEKELEKWHQKAneALRLRLQAEEVAHKKTLAQEEAEKQKEDAErEARKRAKTEESALRQK 2289
Cdd:pfam10174 579 AEVERLLGILREVENEKNDKDKKIAELESLT--LRQMKEQNKKVANIKHGQQEMKKKGAQLLE-EARRREDNLADNSQQL 655
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2290 ELAE--DELEKQRKLADATAQQKFSAEQELirlkAETENSEqqrllleeelfrlkneVNEAIQKRKEMEEELakvraEM- 2366
Cdd:pfam10174 656 QLEElmGALEKTRQELDATKARLSSTQQSL----AEKDGHL----------------TNLRAERRKQLEEIL-----EMk 710
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1835643837 2367 -EILLQSKSraeeESRSNTekskQMLEVEASKLRELAEEAAKLR 2409
Cdd:pfam10174 711 qEALLAAIS----EKDANI----ALLELSSSKKKKTQEEVMALK 746
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1725-2158 |
2.62e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1725 KELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKD----VNEQMlrSHSERdvdLDRYREKVQQLLERWQAILVQIDLR 1800
Cdd:PRK04863 300 RQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDhlnlVQTAL--RQQEK---IERYQADLEELEERLEEQNEVVEEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1801 QRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQsvpitdskTMKEHLLQEKKLLDEIESNRDKVDECQKYAKQYIDa 1880
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQ--------TRAIQYQQAVQALERAKQLCGLPDLTADNAEDWLE- 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1881 ikdyelqlvTYKAQvepvaspakkpkvqstSDSIIQEYVDLRTRYSELTTLTSQYIKfITETLRRLNDE---EKAAEKLK 1957
Cdd:PRK04863 446 ---------EFQAK----------------EQEATEELLSLEQKLSVAQAAHSQFEQ-AYQLVRKIAGEvsrSEAWDVAR 499
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1958 EEERRrlAEVEAQLAKQTQLAEAHAKakaqaekeaeELQRRMQEEvskREVVAVDAEQQKQTIQQ-----ELQQLRQNSD 2032
Cdd:PRK04863 500 ELLRR--LREQRHLAEQLQQLRMRLS----------ELEQRLRQQ---QRAERLLAEFCKRLGKNlddedELEQLQEELE 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2033 MEIKSKAKQIEEVEYNRRKIEEEIhivrlqletmqkhkanaeDELQELRARAEKAEQQKKAAQEEAERLRKQVkDETQKK 2112
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQL------------------EQLQARIQRLAARAPAWLAAQDALARLREQS-GEEFED 625
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1835643837 2113 REAEEELkRKVQAEKEaaREKQRAVEDLEKFRSQAEEAERRMKQAE 2158
Cdd:PRK04863 626 SQDVTEY-MQQLLERE--RELTVERDELAARKQALDEEIERLSQPG 668
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1944-2141 |
2.71e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.77 E-value: 2.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1944 RRLNDEEKAAEKLKE---------EERRRLAEVEAQLAKQTQLAEAHAKAKAQ-----AEKEAEELQRRMQEEVSKREVV 2009
Cdd:pfam05262 185 ALREDNEKGVNFRRDmtdlkeresQEDAKRAQQLKEELDKKQIDADKAQQKADfaqdnADKQRDEVRQKQQEAKNLPKPA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2010 AVDAEQQKQTIQQELQQLRQNSDMEIKSKAkqieeveynrrkieeeihivrlqlETMQKHKANAEDELQELRARAEKAEQ 2089
Cdd:pfam05262 265 DTSSPKEDKQVAENQKREIEKAQIEIKKND------------------------EEALKAKDHKAFDLKQESKASEKEAE 320
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2090 QKkaaQEEAERLRKQVKDETQKKReaeEELKRKVQAEKEAAREKQRAVEDLE 2141
Cdd:pfam05262 321 DK---ELEAQKKREPVAEDLQKTK---PQVEAQPTSLNEDAIDSSNPVYGLK 366
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2779-3201 |
2.77e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 51.05 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2779 TLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVK-------IQMEELIKLKLRIEE 2851
Cdd:pfam07888 8 TLEEESHGEEGGTDMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERYKrdreqweRQRRELESRVAELKE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2852 ENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDdlanQRALAEKMLKEKMqaiqEASRLKAEA 2931
Cdd:pfam07888 88 ELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIRELEED----IKTLTQRVLERET----ELERMKERA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2932 EMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQ--KSLEAERrqqleitaEAERLKLQvlemsraqakaeEDASKFK 3009
Cdd:pfam07888 160 KKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQelRNSLAQR--------DTQVLQLQ------------DTITTLT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3010 KKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAelLQKNSQKMQVAQQE-QLRQ 3088
Cdd:pfam07888 220 QKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQAR--LQAAQLTLQLADASlALRE 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3089 EtqvlQTTFLSEKQLLLERekyIEEEKAKLENLyEDEVRKAQKLKQEQEHQMKHLE----EEKDQLKVSMDDAMKKQKEA 3164
Cdd:pfam07888 298 G----RARWAQERETLQQS---AEADKDRIEKL-SAELQRLEERLQEERMEREKLEvelgREKDCNRVQLSESRRELQEL 369
|
410 420 430
....*....|....*....|....*....|....*..
gi 1835643837 3165 EENVRRKQDELQQLDKKRQEqeklLADENRKLREKLE 3201
Cdd:pfam07888 370 KASLRVAQKEKEQLQAEKQE----LLEYIRQLEQRLE 402
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2098-2309 |
2.82e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2098 AERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLekfRSQAEEAERRMKQAEVEKER---QIKVAQEVAQQ 2174
Cdd:COG2268 195 AEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETA---RIAEAEAELAKKKAEERREAetaRAEAEAAYEIA 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2175 SAAAELnskrmsfaEKTAQLELSLKQEHITVthlqEEAERLKKLhdeaekareeaeKELEKWHQKANEALRLRLQAEEVA 2254
Cdd:COG2268 272 EANAER--------EVQRQLEIAEREREIEL----QEKEAEREE------------AELEADVRKPAEAEKQAAEAEAEA 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2255 hkktlaqeEAEKQKEDAEREA-RKRAKTE-ESALRQKELAEDELEKQRKLADATAQQ 2309
Cdd:COG2268 328 --------EAEAIRAKGLAEAeGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAKP 376
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2008-2193 |
2.89e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.60 E-value: 2.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2008 VVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEK- 2086
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2087 ------------------------------------AEQQK------KAAQEEAERLRKQVKDETQKKREAEEELKRKVQ 2124
Cdd:COG3883 92 aralyrsggsvsyldvllgsesfsdfldrlsalskiADADAdlleelKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2125 AEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ 2193
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
650-757 |
3.06e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 47.75 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 650 QKKTFTKWVNK---------HLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR----EKGRMRFHKLQNVQIALDYL 716
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1835643837 717 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 757
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIEL 145
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1993-2158 |
3.07e-05 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 51.01 E-value: 3.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1993 EELQRRMQEEVSKREVVAVDAEQQKQTIQQElqqlrqnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMqkhkan 2072
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEE----------EIRRLEEQVERLEAEVEELEAELEEKDERIERL------ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2073 aEDELQELR--ARAEKAEQQK-KAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQA-E 2148
Cdd:COG2433 447 -ERELSEARseERREIRKDREiSRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAiR 525
|
170
....*....|
gi 1835643837 2149 EAERRMKQAE 2158
Cdd:COG2433 526 RLEEEYGLKE 535
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2685-2783 |
3.10e-05 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 47.85 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2685 AERAKRAAEDADFARtRAEQEAALSRQQVEEaerlkqraeEEAQAKAQAQ---DEAEKlRKEAELEAAKrAHAEQAALKQ 2761
Cdd:PRK05759 34 EERQKKIADGLAAAE-RAKKELELAQAKYEA---------QLAEARAEAAeiiEQAKK-RAAQIIEEAK-AEAEAEAARI 101
|
90 100
....*....|....*....|..
gi 1835643837 2762 KQLADEEMDKHKKFAEKTLRQK 2783
Cdd:PRK05759 102 KAQAQAEIEQERKRAREELRKQ 123
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2565-2662 |
3.23e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 47.47 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2565 EKAEQEAEKQRQlalEEEQRRKEAEEKVRKILAD-----EKEAARQRKAALEEVERLKAKAE-EAKRQKELAEKEAERQI 2638
Cdd:COG0711 44 ERAKEEAEAALA---EYEEKLAEARAEAAEIIAEarkeaEAIAEEAKAEAEAEAERIIAQAEaEIEQERAKALAELRAEV 120
|
90 100
....*....|....*....|....*..
gi 1835643837 2639 -QLAQEAALKKIDAE--EKAHTAIVQQ 2662
Cdd:COG0711 121 aDLAVAIAEKILGKEldAAAQAALVDR 147
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2677-2783 |
3.26e-05 |
|
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase
Pssm-ID: 440475 [Multi-domain] Cd Length: 152 Bit Score: 47.47 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2677 ILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAErlKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKR-AHAE 2755
Cdd:COG0711 25 ILKALDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEAR--AEAAEIIAEARKEAEAIAEEAKAEAEAEAERIiAQAE 102
|
90 100 110
....*....|....*....|....*....|...
gi 1835643837 2756 QAALKQKQLADEEMDKH-----KKFAEKTLRQK 2783
Cdd:COG0711 103 AEIEQERAKALAELRAEvadlaVAIAEKILGKE 135
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2874-3014 |
3.53e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 50.48 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2874 KMRQVAEEAARLSIEAQEAARmRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKE 2953
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAE-EKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2954 QIEQQLAK--ETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEE 3014
Cdd:PRK12705 106 QLEEREKAlsARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE 168
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2718-2888 |
3.53e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 50.48 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2718 RLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAAlkQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQL 2797
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQ--QRQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2798 EETDHQKTLLDEELQRLKEEvtdamrqKAQVEEELFKVKIQMEELIK------LKLRIEEENKMLIMKDKDSTQKLLVEE 2871
Cdd:PRK12705 105 NQLEEREKALSARELELEEL-------EKQLDNELYRVAGLTPEQARklllklLDAELEEEKAQRVKKIEEEADLEAERK 177
|
170 180
....*....|....*....|...
gi 1835643837 2872 AEK-----MRQVAEE-AARLSIE 2888
Cdd:PRK12705 178 AQNilaqaMQRIASEtASDLSVS 200
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
787-863 |
3.57e-05 |
|
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409034 Cd Length: 98 Bit Score: 46.14 E-value: 3.57e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 787 DNFTTSWRDGRLFNAIIHRHKPVLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSS 863
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQ 95
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2345-2647 |
3.72e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 49.92 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2345 VNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRsntEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAED 2424
Cdd:pfam13868 28 IAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKE---EERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2425 EAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKK-- 2502
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKer 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2503 -----SSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELEL---NQLKNIAEETQRSKEKAEQEAEKQ 2574
Cdd:pfam13868 185 eiarlRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELqqaREEQIELKERRLAEEAEREEEEFE 264
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2575 RQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALE-EVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALK 2647
Cdd:pfam13868 265 RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEErEEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2892-3155 |
3.74e-05 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 50.40 E-value: 3.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2892 AARMRKLAEDdLANQRALAE--KMLKEKMQAIQEasrlkaEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKS 2969
Cdd:PHA02562 149 APARRKLVED-LLDISVLSEmdKLNKDKIRELNQ------QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2970 LEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQ--TELATKERMAVVQTLEIQRQQSGKEA 3047
Cdd:PHA02562 222 YDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQfqKVIKMYEKGGVCPTCTQQISEGPDRI 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3048 EELRRAIAELEHEKEKLKREAELLQKnsqkmQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENL------ 3121
Cdd:PHA02562 302 TKIKDKLKELQHSLEKLDTAIDELEE-----IMDEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAIEELqaefvd 376
|
250 260 270
....*....|....*....|....*....|....
gi 1835643837 3122 YEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMD 3155
Cdd:PHA02562 377 NAEELAKLQDELDKIVKTKSELVKEKYHRGIVTD 410
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2687-2906 |
3.94e-05 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 50.64 E-value: 3.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2687 RAKRAAEDADFARTRAEQEAALSRQQVE-EAERLKQRAEEEAQAkaqaqdeaekLRKEAELEAAKRAHAEQaalkqkqla 2765
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRGKAErDAEHIKKTAKRESKA----------LKKELLLEAKEEARKYR--------- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2766 dEEMDKHKKFAEKTLRQksqVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQ-MEELIK 2844
Cdd:PRK00106 86 -EEIEQEFKSERQELKQ---IESRLTERATSLDRKDENLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQkKAELER 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2845 LKLRIEEENKMLIMKD--KDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAArMRKLAEDDLANQ 2906
Cdd:PRK00106 162 VAALSQAEAREIILAEteNKLTHEIATRIREAEREVKDRSDKMAKDLLAQA-MQRLAGEYVTEQ 224
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1752-2186 |
4.01e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 50.85 E-value: 4.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1752 EADLNKAKDVNEQMLRSHSERDVDLDRYR-EKVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQ 1830
Cdd:COG5022 834 ETEEVEFSLKAEVLIQKFGRSLKAKKRFSlLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVNLELESEIIELKK 913
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1831 rqeQIQSVPITDSKTMKEHLLQEKKLLDEIES------NRDKVDECQKY----------AKQYIDAIKDYELQLVTYKAQ 1894
Cdd:COG5022 914 ---SLSSDLIENLEFKTELIARLKKLLNNIDLeegpsiEYVKLPELNKLhevesklketSEEYEDLLKKSTILVREGNKA 990
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1895 VEPVASPAKKPKVQSTSDSIIQEYVD-LRTRYSELTTLTSQY--IKFITETLRRLNDEEKAAEKLKEEERRRLAEVEA-Q 1970
Cdd:COG5022 991 NSELKNFKKELAELSKQYGALQESTKqLKELPVEVAELQSASkiISSESTELSILKPLQKLKGLLLLENNQLQARYKAlK 1070
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1971 LAKQTQLAEAHAKAKAQA----EKEAEELqrrmQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVE 2046
Cdd:COG5022 1071 LRRENSLLDDKQLYQLEStenlLKTINVK----DLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVF 1146
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2047 YNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQK-KAAQEEAERLRKQVKDETQKKRE----------- 2114
Cdd:COG5022 1147 QKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQSALYDEKsKLSSSEVNDLKNELIALFSKIFSgwprgdklkkl 1226
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2115 ------AEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMS 2186
Cdd:COG5022 1227 isegwvPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNSIDNLLSSYKLEEEVLPATINSLLQYINVGLFNALRTK 1304
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
2871-3004 |
4.20e-05 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 49.21 E-value: 4.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2871 EAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRalaekmlkekMQAIQEASRlKAEAEMLQKQKELA--QEQARKF 2948
Cdd:pfam12037 77 KIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKR----------YQDQLEAQR-RRNEELLRKQEESVakQEAMRIQ 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2949 QEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKlqvLEMSRAQAKAEED 3004
Cdd:pfam12037 146 AQRRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLN---LEQLREKANEERE 198
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
3056-3212 |
4.60e-05 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 49.63 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3056 ELEHEKEKLKREAELLQKNSQKMQVAQQeQLRQETQVLQTTFLSEKQLLLEREKYIEEE----KAKLENLYEDEVRKAQK 3131
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKP-KLRDRKDALEEELRQLKQLEDELEDCDPTEldraKEKLKKLLQEIMIKVKK 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3132 LKQeqehqmkhLEEEKDQLKVSMDDAMKKQKEAEenvrrkqDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIAL 3211
Cdd:smart00787 227 LEE--------LEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTGWKI 291
|
.
gi 1835643837 3212 A 3212
Cdd:smart00787 292 T 292
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1725-2513 |
4.60e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 50.72 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1725 KELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKD----VNEQMlrSHSERdvdLDRYREKVQQLLERW--QAILV--- 1795
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnlVQTAL--RQQEK---IERYQEDLEELTERLeeQEEVVeea 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1796 ---------QIDLRQRELDQLGRQLRYYRET----------YEWLIKwikdAKQRQEQIQSVPITDSKTMKEHLL----Q 1852
Cdd:COG3096 374 aeqlaeaeaRLEAAEEEVDSLKSQLADYQQAldvqqtraiqYQQAVQ----ALEKARALCGLPDLTPENAEDYLAafraK 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1853 EKKLLDEIESNRDKVDECQKYAKQYIDAikdYELqlvtykaqVEPVASPAKKPKVQSTSDSIIQEYVDLRTRYSELTTLT 1932
Cdd:COG3096 450 EQQATEEVLELEQKLSVADAARRQFEKA---YEL--------VCKIAGEVERSQAWQTARELLRRYRSQQALAQRLQQLR 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1933 SQYikfitETLRRLNDEEKAAEKLKEEERRR--------------LAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRR 1998
Cdd:COG3096 519 AQL-----AELEQRLRQQQNAERLLEEFCQRigqqldaaeeleelLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1999 MQeEVSKREVVAVDAEQQKQTIQ----------QELQQLRQNsdMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQletmqk 2068
Cdd:COG3096 594 IK-ELAARAPAWLAAQDALERLReqsgealadsQEVTAAMQQ--LLEREREATVERDELAARKQALESQIERLS------ 664
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2069 HKANAEDelQELRARAEK------AEQQKKAAQEEA-------------------ERLRKQVK----------------- 2106
Cdd:COG3096 665 QPGGAED--PRLLALAERlggvllSEIYDDVTLEDApyfsalygparhaivvpdlSAVKEQLAgledcpedlyliegdpd 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2107 --DETQkkREAEEELKRK-VQAEK---------------EAAREKQravedLEKFRSQAEEAERRMKQAEVEKERQIKVA 2168
Cdd:COG3096 743 sfDDSV--FDAEELEDAVvVKLSDrqwrysrfpevplfgRAAREKR-----LEELRAERDELAEQYAKASFDVQKLQRLH 815
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2169 QE----VAQQSA-------AAELNSKRmsfaEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWH 2237
Cdd:COG3096 816 QAfsqfVGGHLAvafapdpEAELAALR----QRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQANLLADETL 891
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2238 QKANEALRLRLQAEEVA------HKKTLAQEE-------AEKQKEDAEREARKRAKTEESALRQKELAEDELeKQRKLAd 2304
Cdd:COG3096 892 ADRLEELREELDAAQEAqafiqqHGKALAQLEplvavlqSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEV-VQRRPH- 969
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2305 ataqqkFSAEQELIRLkaeTENSeqqrllleeelfrlknEVNEAIQKR-KEMEEELAKVRAEMEillQSKSRAEEESRSN 2383
Cdd:COG3096 970 ------FSYEDAVGLL---GENS----------------DLNEKLRARlEQAEEARREAREQLR---QAQAQYSQYNQVL 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2384 TEkSKQMLEVEASKLRELAEEAAKLravseeakrqrQIAEDEAARQRAEAERI-LKEKLAAiNDATRLKTEAEIALKEKE 2462
Cdd:COG3096 1022 AS-LKSSRDAKQQTLQELEQELEEL-----------GVQADAEAEERARIRRDeLHEELSQ-NRSRRSQLEKQLTRCEAE 1088
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2463 AEN--ERLRRLAEDEAYQRklleEQATQHKQDIEekiILLKKSSDNELERQKN 2513
Cdd:COG3096 1089 MDSlqKRLRKAERDYKQER----EQVVQAKAGWC---AVLRLARDNDVERRLH 1134
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
2063-2153 |
4.64e-05 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 46.54 E-value: 4.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2063 LETMQKHKANAEDELQELRARAEK----AEQQKKAAQEEAERLRKQVKDETQKKREAeeelkRKVQAEKEAAREKQRAVE 2138
Cdd:pfam00430 28 LDKRRELIADEIAEAEERRKDAAAalaeAEQQLKEARAEAQEIIENAKKRAEKLKEE-----IVAAAEAEAERIIEQAAA 102
|
90
....*....|....*
gi 1835643837 2139 DLEKFRSQAEEAERR 2153
Cdd:pfam00430 103 EIEQEKDRALAELRQ 117
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2559-2767 |
4.86e-05 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 50.06 E-value: 4.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2559 ETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQrkaaleEVERLKAKAEEAKRQKELAEKEAERQI 2638
Cdd:pfam04747 59 ELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEARRA------EAEAKKRAAQEEEHKQWKAEQERIQKE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2639 QLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQ------EQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQ 2712
Cdd:pfam04747 133 QEKKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKAstpapvEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEIT 212
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2713 VEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADE 2767
Cdd:pfam04747 213 GKKNKKNKKKSESEATAAPASVEQVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSE 267
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2378-2633 |
5.02e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2378 EESRSNTEKSKQML---EVEASKLRELAEEAAKLRAVSEEAKRQRQiaEDEAARQRAEAERilKEKLAAINDATRLKTEA 2454
Cdd:pfam15709 312 EEERSEEDPSKALLekrEQEKASRDRLRAERAEMRRLEVERKRREQ--EEQRRLQQEQLER--AEKMREELELEQQRRFE 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2455 EIALKEKEAENERLRRLAED--EAYQRKLLEEQATQHKQDIEEKIillkkssdNELERQKNIVEdtlrqrriieeeiril 2532
Cdd:pfam15709 388 EIRLRKQRLEEERQRQEEEErkQRLQLQAAQERARQQQEEFRRKL--------QELQRKKQQEE---------------- 443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2533 kvnFEKASVGKSDLELELNQLkniAEETQRSKEKAEQE-AEKQRQLALEEEQRRKEAEEKVRKiladEKEAARqrkaale 2611
Cdd:pfam15709 444 ---AERAEAEKQRQKELEMQL---AEEQKRLMEMAEEErLEYQRQKQEAEEKARLEAEERRQK----EEEAAR------- 506
|
250 260
....*....|....*....|..
gi 1835643837 2612 everlkAKAEEAKRQKELAEKE 2633
Cdd:pfam15709 507 ------LALEEAMKQAQEQARQ 522
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2624-2810 |
5.28e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2624 KRQKELAEKEAERQIQLAQEAA-LKKIDAEEKAhtaivqQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRA 2702
Cdd:pfam05262 180 KKVVEALREDNEKGVNFRRDMTdLKERESQEDA------KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2703 EQEAALSRQ--QVEEAERLKQRAEEEAQAKAQAQDEAEKlrKEAELEAAKRAHAEQAALKQKQLADEEMDKhkkfAEKTL 2780
Cdd:pfam05262 254 QQEAKNLPKpaDTSSPKEDKQVAENQKREIEKAQIEIKK--NDEEALKAKDHKAFDLKQESKASEKEAEDK----ELEAQ 327
|
170 180 190
....*....|....*....|....*....|
gi 1835643837 2781 RQKSQVEQELTKVKlqlEETDHQKTLLDEE 2810
Cdd:pfam05262 328 KKREPVAEDLQKTK---PQVEAQPTSLNED 354
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2666-2771 |
5.35e-05 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 46.28 E-value: 5.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2666 EMLQTRkqEQSILDKLkEEAERAKRAAEDAdfartRAEQEAALsrqqvEEAErlKQRAEEEAQAKAQAQDEAEKLRKEAE 2745
Cdd:cd06503 26 KALDER--EEKIAESL-EEAEKAKEEAEEL-----LAEYEEKL-----AEAR--AEAQEIIEEARKEAEKIKEEILAEAK 90
|
90 100
....*....|....*....|....*..
gi 1835643837 2746 LEAAK-RAHAEQAALKQKQLADEEMDK 2771
Cdd:cd06503 91 EEAERiLEQAKAEIEQEKEKALAELRK 117
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1940-2187 |
5.42e-05 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 49.96 E-value: 5.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1940 TETLRRLNDEEKAAEKLKEEERRRLAEVEAQLA-------KQTQLAEAHAKAK-AQAEKEAEELQRRMQEEVSKREvvaV 2011
Cdd:COG5185 274 AESSKRLNENANNLIKQFENTKEKIAEYTKSIDikkatesLEEQLAAAEAEQElEESKRETETGIQNLTAEIEQGQ---E 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2012 DAEQQKQTIQQELQQLRQNSDMEIKSkaKQIEEVEYNRRKIEEEIHIVRLQ--------LETMQKHKANAEDELQELRAR 2083
Cdd:COG5185 351 SLTENLEAIKEEIENIVGEVELSKSS--EELDSFKDTIESTKESLDEIPQNqrgyaqeiLATLEDTLKAADRQIEELQRQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2084 AEKAEQQKKAAQEEaerLRKQVKDETQKKREAEEELKRKVQAE-KEAAREKQRAVEDLEKFRSQAEEAERRMKqaevEKE 2162
Cdd:COG5185 429 IEQATSSNEEVSKL---LNELISELNKVMREADEESQSRLEEAyDEINRSVRSKKEDLNEELTQIESRVSTLK----ATL 501
|
250 260
....*....|....*....|....*
gi 1835643837 2163 RQIKVAQEVAQQSAAAELNSKRMSF 2187
Cdd:COG5185 502 EKLRAKLERQLEGVRSKLDQVAESL 526
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2062-2468 |
5.47e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.91 E-value: 5.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2062 QLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLE 2141
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2142 KFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDE 2221
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2222 AEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRK 2301
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2302 LADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESR 2381
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2382 SNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEK 2461
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
....*..
gi 1835643837 2462 EAENERL 2468
Cdd:COG5278 511 AAAEAAL 517
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2741-3003 |
5.76e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.87 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2741 RKEAELEAAKRAHAEqAALKQ--KQLADEEMDKHK-KFAEKTLrqkSQVEQELTKVKLQLE-----ETDHQKTLLDEELQ 2812
Cdd:COG2268 116 RDPEEIEELAEEKLE-GALRAvaAQMTVEELNEDReKFAEKVQ---EVAGTDLAKNGLELEsvaitDLEDENNYLDALGR 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2813 RLKEEVT-DAMRQKAQVEEELfKVKI----QMEELIKLKLRIEEENKMLIMKDKDSTQKllVEEAEKMRQVAEEAARLSI 2887
Cdd:COG2268 192 RKIAEIIrDARIAEAEAERET-EIAIaqanREAEEAELEQEREIETARIAEAEAELAKK--KAEERREAETARAEAEAAY 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2888 EAQEAARMRKLAEDDLANQR----ALAEKMLKEKMQAIQEASRLKAEAEmlqKQKELAQEQArkfqeDKEQIEQQLAKET 2963
Cdd:COG2268 269 EIAEANAEREVQRQLEIAERereiELQEKEAEREEAELEADVRKPAEAE---KQAAEAEAEA-----EAEAIRAKGLAEA 340
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1835643837 2964 EGFQKslEAERRQQLEITAEAERLkLQVL-EMSRAQAKAEE 3003
Cdd:COG2268 341 EGKRA--LAEAWNKLGDAAILLML-IEKLpEIAEAAAKPLE 378
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
647-746 |
5.76e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 46.11 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 647 DRVQKKTFTKWVNKHLIKA--QRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKG--RMRFHKLQNVQIALDYLKHRQVK 722
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1835643837 723 LVNIRNDDIADGNPKLTLGLIWTI 746
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2545-2763 |
5.84e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 48.28 E-value: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2545 DLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILAdekeaarqrKAALEEVERLKAKAEEAK 2624
Cdd:COG1842 34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLA---------REALERKAELEAQAEALE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2625 RQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMlqtRKQEQSILDKLKEEaerakraaedadfartraEQ 2704
Cdd:COG1842 105 AQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKA---QEKVNEALSGIDSD------------------DA 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2705 EAALsrqqveeaERLKQRAEEEaQAKAQAQDE---AEKLRKE-AELEAAKRAHAEQAALKQKQ 2763
Cdd:COG1842 164 TSAL--------ERMEEKIEEM-EARAEAAAElaaGDSLDDElAELEADSEVEDELAALKAKM 217
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2879-3201 |
5.85e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.87 E-value: 5.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2879 AEEAARLSIEAQEAARMRKLAEDDLANQraLAEKMLKEKMQAIQEASRLKA--------EAEMLQKQKELAQEQARKFQE 2950
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQ--VTESVEPNEHNSYEEDSELKPsgqggldeEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2951 DKEQiEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVlemSRAQAKAEEDASKFKKKAEEiGNKLHQTELATKERM 3030
Cdd:pfam02029 82 ALER-QKEFDPTIADEKESVAERKENNEEEENSSWEKEEKR---DSRLGRYKEEETEIREKEYQ-ENKWSTEVRQAEEEG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3031 AVVQ--TLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQK---NSQKMQVAQQE--QLRQETQVLQTTFLSEKQL 3103
Cdd:pfam02029 157 EEEEdkSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKrghPEVKSQNGEEEvtKLKVTTKRRQGGLSQSQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3104 LLEREKYIEEEKaKLENLY----EDEVRKAQKLKQEQEHQMKHLEEekdqLKVSMDDAMKKQKEAEEnvRRKQDELQQld 3179
Cdd:pfam02029 237 EEEAEVFLEAEQ-KLEELRrrrqEKESEEFEKLRQKQQEAELELEE----LKKKREERRKLLEEEEQ--RRKQEEAER-- 307
|
330 340
....*....|....*....|..
gi 1835643837 3180 KKRQEQEKlladenRKLREKLE 3201
Cdd:pfam02029 308 KLREEEEK------RRMKEEIE 323
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2403-2799 |
5.93e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 50.14 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2403 EEAAKLRAVSEEAKRQRQIAEDEAARQRAEaerilKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLL 2482
Cdd:pfam09731 73 SAVTGESKEPKEEKKQVKIPRQSGVSSEVA-----EEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAV 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2483 EEQATqhkqdiEEKIILLKKSSDNElerqKNIVEDTLRQRRIieeeirilkvnfEKASVGKSDLELELNQLKNIAEETQR 2562
Cdd:pfam09731 148 AKEAK------DDAIQAVKAHTDSL----KEASDTAEISREK------------ATDSALQKAEALAEKLKEVINLAKQS 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2563 SKEKAEQEAEKQRQLALEEEQRRKEAEEKVrkiladekEAARQRKAALEEVERLKAKAEEaKRQKELAEKEAERQIQLAQ 2642
Cdd:pfam09731 206 EEEAAPPLLDAAPETPPKLPEHLDNVEEKV--------EKAQSLAKLVDQYKELVASERI-VFQQELVSIFPDIIPVLKE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2643 EAALKKIDAE---EKAHTAIvQQKEQEMLQTRKQEQsildKLKEEAERAKRAAEDADFARTRAEQEAALSrqqveeAERL 2719
Cdd:pfam09731 277 DNLLSNDDLNsliAHAHREI-DQLSKKLAELKKREE----KHIERALEKQKEELDKLAEELSARLEEVRA------ADEA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2720 KQRAEEEAQAKAQAQDEAEKLRKEaeLEAAKRAHAEQAalkQKQLADEEMDKHKKFAEKTlrqKSQVEQELTKVKLQLEE 2799
Cdd:pfam09731 346 QLRLEFEREREEIRESYEEKLRTE--LERQAEAHEEHL---KDVLVEQEIELQREFLQDI---KEKVEEERAGRLLKLNE 417
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
760-867 |
6.00e-05 |
|
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409161 Cd Length: 114 Bit Score: 45.95 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 760 QSEDMTAKEKLLLWSQRMTEGyqgLHCDNFTTSWRDGRLFNAIIHRHKPVLI-DMNKVYRQTNLENLDQAFNVAERDLGV 838
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1835643837 839 TRLLDPEDVDVPQPDEKSIITYVSSMYDA 867
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1221-1313 |
6.03e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 45.40 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1221 HAFVSAATKELMWLNDKEEEEVNFDWSDRNTNMAAKKENYSGLMRELELKEKKIKEIQISGDRLQREDHPGKQTVEAFQA 1300
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1835643837 1301 ALQTQWSWMLQLC 1313
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2815-3145 |
6.16e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 49.26 E-value: 6.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2815 KEEVTDAMRQKAQVEEELFKV---KIQMEELIKLKLRIEEENKMlimkdkdstqkllveeaeKMRQVAEEAARLSIEAQE 2891
Cdd:pfam15558 19 EEQRMRELQQQAALAWEELRRrdqKRQETLERERRLLLQQSQEQ------------------WQAEKEQRKARLGREERR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2892 AARMRK----LAEDDLANQRALAEKMLKEKMQ-AIQEASRLKaeaemlQKQKELAQEQARKFQEDKEQIEQQL-AKETEG 2965
Cdd:pfam15558 81 RADRREkqviEKESRWREQAEDQENQRQEKLErARQEAEQRK------QCQEQRLKEKEEELQALREQNSLQLqERLEEA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2966 FQKSLEAERRQQLEITAE--AERLKLQVLEMSRA-QAKAEEDASKfkkkaeeigNKLHQTELATKERMA--VVQTLEIQR 3040
Cdd:pfam15558 155 CHKRQLKEREEQKKVQENnlSELLNHQARKVLVDcQAKAEELLRR---------LSLEQSLQRSQENYEqlVEERHRELR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3041 QQSGKEAEELRRA-IAELEHEKEKLKREAELLQKNSQKMQVAQQ---EQLRQETQ-VLQTTFLSEKQLLLEREKYIEEEK 3115
Cdd:pfam15558 226 EKAQKEEEQFQRAkWRAEEKEEERQEHKEALAELADRKIQQARQvahKTVQDKAQrARELNLEREKNHHILKLKVEKEEK 305
|
330 340 350
....*....|....*....|....*....|
gi 1835643837 3116 AKLENLYEDEVRKAQKLKQEQEHQMKHLEE 3145
Cdd:pfam15558 306 CHREGIKEAIKKKEQRSEQISREKEATLEE 335
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2890-3174 |
6.17e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.22 E-value: 6.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2890 QEAARMRKLAEDDLANQRALAEKMlkekmqaiqeasrlKAEAEmlqKQKeLAQEQArkfqedkeqieQQLAkETEGFQKS 2969
Cdd:NF012221 1542 QQADAVSKHAKQDDAAQNALADKE--------------RAEAD---RQR-LEQEKQ-----------QQLA-AISGSQSQ 1591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2970 LEAERRQQLEITAEAERlklqvlemsraqakaeeDAskFKKKAEEIgnklhqtelaTKERMAVVQTLEI---QRQQSGKE 3046
Cdd:NF012221 1592 LESTDQNALETNGQAQR-----------------DA--ILEESRAV----------TKELTTLAQGLDAldsQATYAGES 1642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3047 AEELRRAIAE--LEHEKEKLKREAELLQK---NSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENL 3121
Cdd:NF012221 1643 GDQWRNPFAGglLDRVQEQLDDAKKISGKqlaDAKQRHVDNQQKVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKR 1722
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 3122 YEDEVRK---AQKLKQEQEHQMKHLEEEKDQ-LKVSMDDAMKKQKEAEENvrrKQDE 3174
Cdd:NF012221 1723 KDDALAKqneAQQAESDANAAANDAQSRGEQdASAAENKANQAQADAKGA---KQDE 1776
|
|
| EFh_PEF_ALG-2_like |
cd16185 |
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein ... |
6883-6956 |
6.38e-05 |
|
EF-hand, calcium binding motif, found in homologs of mammalian apoptosis-linked gene 2 protein (ALG-2); The family includes some homologs of mammalian apoptosis-linked gene 2 protein (ALG-2) mainly found in lower eukaryotes, such as a parasitic protist Leishmarua major and a cellular slime mold Dictyostelium discoideum. These homologs contains five EF-hand motifs. Due to the presence of unfavorable residues at the Ca2+-coordinating positions, their non-canonical EF4 and EF5 hands may not bind Ca2+. Two Dictyostelium PEF proteins are the prototypes of this family. They may bind to cytoskeletal proteins and/or signal-transducing proteins localized to detergent-resistant membranes named lipid rafts, and occur as monomers or weak homo- or heterodimers like ALG-2. They can serve as a mediator for Ca2+ signaling-related Dictyostehum programmed cell death (PCD).
Pssm-ID: 320060 [Multi-domain] Cd Length: 163 Bit Score: 46.82 E-value: 6.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6883 FRSIDRDQDGRISQQEfIESVLSSKFPTNSLEM-NAVASIFDYNGDGFIDYYEFVsALHP----------SRDTLR-KSL 6950
Cdd:cd16185 6 FRAVDRDRSGSIDVNE-LQKALAGGGLLFSLATaEKLIRMFDRDGNGTIDFEEFA-ALHQflsnmqngfeQRDTSRsGRL 83
|
....*.
gi 1835643837 6951 DADQIQ 6956
Cdd:cd16185 84 DANEVH 89
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2077-2174 |
6.41e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.83 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2077 LQELRARAEKAEQQKKAAQEEAERLRKQVKDETQK--------KREAEEELKRKVQAEKEAAREKQRAVEDLEKF----- 2143
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKlqeeedklLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGgyasv 604
|
90 100 110
....*....|....*....|....*....|..
gi 1835643837 2144 -RSQAEEAERRMKQAEVEKERQIKVAQEVAQQ 2174
Cdd:PRK00409 605 kAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
2014-2201 |
6.49e-05 |
|
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 trasnmembrane helices, followed by a C-terminal coiled-coil region. Macoilin is a highly conserved protein present in eukaryotes. Macoilin appears to be found in the ER and be involved in the function of neurons.
Pssm-ID: 462859 [Multi-domain] Cd Length: 670 Bit Score: 49.85 E-value: 6.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2014 EQQKQTIQQELQQLRQNsDMEIKSkakQIEEVEYNRRKIEEEIHivrlqletmQKHKANaeDELQElraRAEKAEQQKKA 2093
Cdd:pfam09726 401 EQDIKKLKAELQASRQT-EQELRS---QISSLTSLERSLKSELG---------QLRQEN--DLLQT---KLHNAVSAKQK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2094 AQEEAERLRKQVKDETQKKREAE----EELKRKVQAEKEAAREKQRA----VEDLEKFRSQAEEAERRMKQAEVE---KE 2162
Cdd:pfam09726 463 DKQTVQQLEKRLKAEQEARASAEkqlaEEKKRKKEEEATAARAVALAaasrGECTESLKQRKRELESEIKKLTHDiklKE 542
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1835643837 2163 RQIKVAQEVAQQSAAAELNSKR----MS----FAEKTAQLELSLKQE 2201
Cdd:pfam09726 543 EQIRELEIKVQELRKYKESEKDtevlMSalsaMQDKNQHLENSLSAE 589
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2655-2899 |
6.55e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2655 AHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDadfaRTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQ 2734
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQ----LAALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2735 DEAEKLRKEAELEAAKRAHAEQAALKQKQLA----DEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEE 2810
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPPLAlllsPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2811 LQRLKEEVTDAMRQKAQVEEElfkVKIQMEELIKLKLRIEEENKMLimKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQ 2890
Cdd:COG4942 173 RAELEALLAELEEERAALEAL---KAERQKLLARLEKELAELAAEL--AELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
....*....
gi 1835643837 2891 EAARMRKLA 2899
Cdd:COG4942 248 FAALKGKLP 256
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2636-2804 |
6.61e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 50.02 E-value: 6.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2636 RQIQLAQEAALKKIDAEEKaHTAivQQKEQEMlQTRKQEQSILDKLKEEAERAKraaedadfartraeqeaaLSRQQvee 2715
Cdd:PTZ00491 651 KSVQLAIEITTKSQEAAAR-HQA--ELLEQEA-RGRLERQKMHDKAKAEEQRTK------------------LLELQ--- 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2716 AERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAK-RAHAEQAalkqkqLADEEMDKHKKFAEKTLR-QKSQVEQELTKV 2793
Cdd:PTZ00491 706 AESAAVESSGQSRAEALAEAEARLIEAEAEVEQAElRAKALRI------EAEAELEKLRKRQELELEyEQAQNELEIAKA 779
|
170
....*....|.
gi 1835643837 2794 KlQLEETDHQK 2804
Cdd:PTZ00491 780 K-ELADIEATK 789
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2555-2759 |
6.77e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.62 E-value: 6.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2555 NIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEaeekvrkiladekeaarqrkaaleeverlkaKAEEAKRQKELAEKEA 2634
Cdd:pfam05262 195 NFRRDMTDLKERESQEDAKRAQQLKEELDKKQI-------------------------------DADKAQQKADFAQDNA 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2635 ERQIQLAQEAALKKIDAEEKAHTaivqqkeqemlQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALS-RQQV 2713
Cdd:pfam05262 244 DKQRDEVRQKQQEAKNLPKPADT-----------SSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDlKQES 312
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1835643837 2714 EEAERLKQRAEEEAQAKaqAQDEAEKLRKEAELEAAKRAHAEQAAL 2759
Cdd:pfam05262 313 KASEKEAEDKELEAQKK--REPVAEDLQKTKPQVEAQPTSLNEDAI 356
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2071-2433 |
6.82e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 6.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2071 ANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKrkvQAEKEAAREKQRAVEDLEKfrsQAEEA 2150
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELK---PSGQGGLDEEEAFLDRTAK---REERR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2151 ERRMKQAEvekERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDeaekareeae 2230
Cdd:pfam02029 76 QKRLQEAL---ERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQE---------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2231 kelEKWHQKANEAlrlrlqAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESaLRQKELAEDELEKQRKLADATAQQk 2310
Cdd:pfam02029 143 ---NKWSTEVRQA------EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE-KKVKYESKVFLDQKRGHPEVKSQN- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2311 fsAEQELIRLKaETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELA-KVRAEMEILLQSKSRAE---EESRSNTEK 2386
Cdd:pfam02029 212 --GEEEVTKLK-VTTKRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQeKESEEFEKLRQKQQEAElelEELKKKREE 288
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1835643837 2387 SKQMLEVEASKlRELAEEAAKLRavSEEAKRQRQiaeDEAARQRAEA 2433
Cdd:pfam02029 289 RRKLLEEEEQR-RKQEEAERKLR--EEEEKRRMK---EEIERRRAEA 329
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2897-3088 |
6.88e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 6.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2897 KLAEDDLANQRALAEKMLKE-KMQAIQEASRLKAEAEMLQKQ--KELAQEQARKFQEDKEQiEQQLAKETegfQKSLEAE 2973
Cdd:pfam15709 332 KASRDRLRAERAEMRRLEVErKRREQEEQRRLQQEQLERAEKmrEELELEQQRRFEEIRLR-KQRLEEER---QRQEEEE 407
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2974 RRQQLEITAEAERL---------KLQVLEMSRAQAKAEE-DASKFKKKAEEIGNKLHQTELAtkeRMAVVQTLEIQRQQs 3043
Cdd:pfam15709 408 RKQRLQLQAAQERArqqqeefrrKLQELQRKKQQEEAERaEAEKQRQKELEMQLAEEQKRLM---EMAEEERLEYQRQK- 483
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1835643837 3044 gKEAEElrRAIAELEHEKEKLKREAELLQKNSQKMqvaQQEQLRQ 3088
Cdd:pfam15709 484 -QEAEE--KARLEAEERRQKEEEAARLALEEAMKQ---AQEQARQ 522
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2342-2656 |
6.90e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 6.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEEsrsnTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQI 2421
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE----LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2422 AEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLK 2501
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2502 KSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKA-EQEAEKQRQLALE 2580
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELlEEVILKEIEELEL 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2581 EEQRRKEAEEKVRKILADEKEAAR-QRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAH 2656
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEeAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADL 342
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2067-2164 |
7.17e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.57 E-value: 7.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2067 QKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKrkvQAEKEAAREKQRAVEDLEKFRSQ 2146
Cdd:pfam05672 26 QREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQR---KAEEEAEEREQREQEEQERLQKQ 102
|
90
....*....|....*...
gi 1835643837 2147 AEEAERRMkQAEVEKERQ 2164
Cdd:pfam05672 103 KEEAEAKA-REEAERQRQ 119
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
649-750 |
7.20e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 45.87 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 649 VQKKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMRF----HKLQNVQIALDYLKHRQVKLV 724
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1835643837 725 NIRNDDIADGNPKLTLGLIWTIILHF 750
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
3060-3208 |
7.30e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 48.73 E-value: 7.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3060 EKEKLKREAELLQKNSQKMQVAQQEQLrQETQVLQTTFLSEKQLLLEREKYIEEEKAKLEnlyedEVRKAQKLKQEQEHQ 3139
Cdd:cd16269 150 DREKLVEKYRQVPRKGVKAEEVLQEFL-QSKEAEAEAILQADQALTEKEKEIEAERAKAE-----AAEQERKLLEEQQRE 223
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 3140 MKHLEEEKdqlKVSMDDAMKKQKEAEENVRRKQDELQQ--LDKKRQEQEKLLADENRKLREKLEQMEEEHR 3208
Cdd:cd16269 224 LEQKLEDQ---ERSYEEHLRQLKEKMEEERENLLKEQEraLESKLKEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1955-2308 |
7.40e-05 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 49.26 E-value: 7.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1955 KLKEEERRRlaeveaQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAvDAEQQKQTIQQELQQLRQnsdme 2034
Cdd:pfam15558 16 RHKEEQRMR------ELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQA-EKEQRKARLGREERRRAD----- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2035 ikSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDEtQKKRE 2114
Cdd:pfam15558 84 --RREKQVIEKESRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEAC-HKRQL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2115 AEEELKRKVQAEKEAAR----------EKQRAVEDL--------------EKFRSQAEEAERRMKQAEVEKERQIKVAQE 2170
Cdd:pfam15558 161 KEREEQKKVQENNLSELlnhqarkvlvDCQAKAEELlrrlsleqslqrsqENYEQLVEERHRELREKAQKEEEQFQRAKW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2171 VAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVthlQEEAERLKKLHdeaekareeaekeLEKwhQKANEALRLRLQA 2250
Cdd:pfam15558 241 RAEEKEEERQEHKEALAELADRKIQQARQVAHKTV---QDKAQRARELN-------------LER--EKNHHILKLKVEK 302
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2251 EEVAHKKTLaqeeaekqKEDAEREARKRakteESALRQKELAedeLEKQRKLADATAQ 2308
Cdd:pfam15558 303 EEKCHREGI--------KEAIKKKEQRS----EQISREKEAT---LEEARKTARASFH 345
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2039-2212 |
7.43e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.62 E-value: 7.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2039 AKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEE- 2117
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKp 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2118 ----ELKRKVQAEKEAAREKQRAVEDLEKfrsQAEEAERRMKQAEVEKERQIKvAQEVAQQSAAAELNSKRMSFAEKTAQ 2193
Cdd:pfam05262 264 adtsSPKEDKQVAENQKREIEKAQIEIKK---NDEEALKAKDHKAFDLKQESK-ASEKEAEDKELEAQKKREPVAEDLQK 339
|
170
....*....|....*....
gi 1835643837 2194 LELSLKQEhitVTHLQEEA 2212
Cdd:pfam05262 340 TKPQVEAQ---PTSLNEDA 355
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2915-3088 |
7.85e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.10 E-value: 7.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2915 KEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQiEQQLAKETEGFQKSLEAERrqqleitAEAErlklqvlem 2994
Cdd:COG2268 203 IAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEA-EAELAKKKAEERREAETAR-------AEAE--------- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2995 sRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTL--------EIQRQQSGKEAEelrraiAELEHEKEKLKR 3066
Cdd:COG2268 266 -AAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELeadvrkpaEAEKQAAEAEAE------AEAEAIRAKGLA 338
|
170 180
....*....|....*....|..
gi 1835643837 3067 EAELLQKNSQKMQVAQQEQLRQ 3088
Cdd:COG2268 339 EAEGKRALAEAWNKLGDAAILL 360
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1551-3184 |
7.91e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 50.05 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1551 DDRMQIEREYNNCIQKYEQLLrtqekgeqDEVTcknYISQLKdirlqLEgcesrtihkirtpmekdpIKECSQRISEQQq 1630
Cdd:TIGR01612 572 EDSIHLEKEIKDLFDKYLEID--------DEII---YINKLK-----LE------------------LKEKIKNISDKN- 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1631 ihfelEGIKK--NLNKVSEKTLKVLaqKEQSSSSPLLRTEHEithQKMDQVYS-----LSSIYLEKLKTINLVIRSTQgA 1703
Cdd:TIGR01612 617 -----EYIKKaiDLKKIIENNNAYI--DELAKISPYQVPEHL---KNKDKIYStikseLSKIYEDDIDALYNELSSIV-K 685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1704 EEVVRTYEDQLK------------------EVHAVPSDSKELEATKAELKKLRSQVEGH------QPLFNTLEADLNKAK 1759
Cdd:TIGR01612 686 ENAIDNTEDKAKlddlkskidkeydkiqnmETATVELHLSNIENKKNELLDIIVEIKKHihgeinKDLNKILEDFKNKEK 765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1760 DVNEQMLRSHSERDvDLDRYREKVQQLLERWQAILVQIDLRQRELDQlgrqlryyreTYEWLIKWIKDAKQRQEQIQSVp 1839
Cdd:TIGR01612 766 ELSNKINDYAKEKD-ELNKYKSKISEIKNHYNDQINIDNIKDEDAKQ----------NYDKSKEYIKTISIKEDEIFKI- 833
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1840 ITDSKTMKEHLLQEKKLLDEIESN-RDKVDECQKYAKQYIDAIKD--YELQLVTYKAQVEPvaspaKKPKVQSTSDSIIQ 1916
Cdd:TIGR01612 834 INEMKFMKDDFLNKVDKFINFENNcKEKIDSEHEQFAELTNKIKAeiSDDKLNDYEKKFND-----SKSLINEINKSIEE 908
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1917 EYVDLRTRYSelttlTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVeaqlaKQTQLAEahakaKAQAEKEAEELQ 1996
Cdd:TIGR01612 909 EYQNINTLKK-----VDEYIKICENTKESIEKFHNKQNILKEILNKNIDTI-----KESNLIE-----KSYKDKFDNTLI 973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1997 RRMQE-EVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKA-KQIEEVEYNRRKIEEEIhivrlqlETMQKHKANAE 2074
Cdd:TIGR01612 974 DKINElDKAFKDASLNDYEAKNNELIKYFNDLKANLGKNKENMLyHQFDEKEKATNDIEQKI-------EDANKNIPNIE 1046
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2075 DELQElrARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQaekeaarekqravedLEKFrsqaeeaerrm 2154
Cdd:TIGR01612 1047 IAIHT--SIYNIIDEIEKEIGKNIELLNKEILEEAEINITNFNEIKEKLK---------------HYNF----------- 1098
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2155 kqAEVEKERQIKVAQEVAQqsaaaelnskrmsfaektaqLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELE 2234
Cdd:TIGR01612 1099 --DDFGKEENIKYADEINK--------------------IKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLE 1156
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2235 KWHQKAnealrlrLQAEEVahkktlaqEEAEKQKEDAEREARKRAKTEESAlrQKELAE-DELEKQRKLADATAQQKFSA 2313
Cdd:TIGR01612 1157 DVADKA-------ISNDDP--------EEIEKKIENIVTKIDKKKNIYDEI--KKLLNEiAEIEKDKTSLEEVKGINLSY 1219
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2314 EQELIRLKAET-ENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELA---KVRAEMEILLQSKSRAEEESRSNTEKSKQ 2389
Cdd:TIGR01612 1220 GKNLGKLFLEKiDEEKKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGiemDIKAEMETFNISHDDDKDHHIISKKHDEN 1299
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2390 MLEVEASKLReLAEEAAKLRAVSEeAKRQRQIAEDEAARQRAEAERILKE-----KLAAINDATRLKTEAEIALKEKEAE 2464
Cdd:TIGR01612 1300 ISDIREKSLK-IIEDFSEESDIND-IKKELQKNLLDAQKHNSDINLYLNEianiyNILKLNKIKKIIDEVKEYTKEIEEN 1377
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2465 NERLR-RLAEDEAYQRKLLEE----------QATQHKQDIEEKIILLKKSSDNELERQKNIveDTLRQRRIIEEEIRILK 2533
Cdd:TIGR01612 1378 NKNIKdELDKSEKLIKKIKDDinleeckskiESTLDDKDIDECIKKIKELKNHILSEESNI--DTYFKNADENNENVLLL 1455
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2534 V-NFEKASV------------GKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKI--LAD 2598
Cdd:TIGR01612 1456 FkNIEMADNksqhilkikkdnATNDHDFNINELKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYsaLAI 1535
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2599 EKEAARQRKAA---LEEVERLKAK-AEEAKRQKELAEKEAERQIQLAQEAAlkKIDAEEKAHTAI---VQQKEQEMLQTR 2671
Cdd:TIGR01612 1536 KNKFAKTKKDSeiiIKEIKDAHKKfILEAEKSEQKIKEIKKEKFRIEDDAA--KNDKSNKAAIDIqlsLENFENKFLKIS 1613
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2672 KQEQSILDKLKEEAERAKRAAedadfARTRAEQEAALSrQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRK-EAELEAAK 2750
Cdd:TIGR01612 1614 DIKKKINDCLKETESIEKKIS-----SFSIDSQDTELK-ENGDNLNSLQEFLESLKDQKKNIEDKKKELDElDSEIEKIE 1687
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2751 rahaeqaalkqkqladEEMDKHKKFAEKTLrqksqVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEE 2830
Cdd:TIGR01612 1688 ----------------IDVDQHKKNYEIGI-----IEKIKEIAIANKEEIESIKELIEPTIENLISSFNTNDLEGIDPNE 1746
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2831 ELFKVKIQM----EELIKLKLRI----EEENKMLIMKDKDSTQKLLVEEaEKMRQVAEEAARLS----IEAQEAARM--- 2895
Cdd:TIGR01612 1747 KLEEYNTEIgdiyEEFIELYNIIagclETVSKEPITYDEIKNTRINAQN-EFLKIIEIEKKSKSylddIEAKEFDRIinh 1825
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2896 --RKL--AEDDLANQRALAEKMLKEKMQAIQEASRLKAEA---EMLQKQKELAQEQARK----FQEDKEQIEQQLAKETE 2964
Cdd:TIGR01612 1826 fkKKLdhVNDKFTKEYSKINEGFDDISKSIENVKNSTDENllfDILNKTKDAYAGIIGKkyysYKDEAEKIFINISKLAN 1905
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2965 GFQKSLEAE------RRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEI 3038
Cdd:TIGR01612 1906 SINIQIQNNsgidlfDNINIAILSSLDSEKEDTLKFIPSPEKEPEIYTKIRDSYDTLLDIFKKSQDLHKKEQDTLNIIFE 1985
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3039 QRQ--QSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQvaqqeQLRQETQVLQTTFLSEKQ-LLLEREKYIEEEK 3115
Cdd:TIGR01612 1986 NQQlyEKIQASNELKDTLSDLKYKKEKILNDVKLLLHKFDELN-----KLSCDSQNYDTILELSKQdKIKEKIDNYEKEK 2060
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3116 AKL---------ENLYEDEVRKAQKLKQEQEHQMK---HLEEEKD-------QLKvSMDDAMKKQ-KEAEENVRRKQDEL 3175
Cdd:TIGR01612 2061 EKFgidfdvkamEEKFDNDIKDIEKFENNYKHSEKdnhDFSEEKDniiqskkKLK-ELTEAFNTEiKIIEDKIIEKNDLI 2139
|
....*....
gi 1835643837 3176 QQLDKKRQE 3184
Cdd:TIGR01612 2140 DKLIEMRKE 2148
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1949-2176 |
7.93e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 49.21 E-value: 7.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1949 EEKAAEKLKEEERRRL-AEVEAQLAKQTQlaEAHAKAKAQAEKEAEELqrrmqEEVSKREVVAVDAEQQKQTIQQELQQL 2027
Cdd:PRK07735 11 KKEAARRAKEEARKRLvAKHGAEISKLEE--ENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAALAKQKREGTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2028 RQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDElQELRARAEKAEQQKKAAQEEAERLRKQVKD 2107
Cdd:PRK07735 84 EVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAA-AAAKAKAAALAKQKREGTEEVTEEEEETDK 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2108 ETQKKREAEeelKRKVQAEKEAAREKQRAVEDLEKfRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSA 2176
Cdd:PRK07735 163 EKAKAKAAA---AAKAKAAALAKQKAAEAGEGTEE-VTEEEKAKAKAKAAAAAKAKAAALAKQKASQGN 227
|
|
| SprA-related |
pfam12118 |
SprA-related family; This family of bacterial proteins has a conserved HEXXH motif, suggesting ... |
2563-2656 |
7.96e-05 |
|
SprA-related family; This family of bacterial proteins has a conserved HEXXH motif, suggesting they are putative peptidases of zincin fold. Proteins in this family are typically between 234 to 465 amino acids in length. Most members are annotated as being SprA-related.
Pssm-ID: 432342 Cd Length: 335 Bit Score: 49.00 E-value: 7.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2563 SKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQ 2642
Cdd:pfam12118 109 EAEKAAKEAKQQKLAEALGGEREPFSQEKVQRQVDAQVTQDSNAQQMQRENDIEKQREQVKIRQQEMQSAQKAELAQAAQ 188
|
90
....*....|....
gi 1835643837 2643 EAALKKIDAEEKAH 2656
Cdd:pfam12118 189 VRQLEARDAEVKAH 202
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3033-3202 |
8.06e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 8.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3033 VQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKmqvAQQEQLRQETQVLQTtflsekqlllerEKYIE 3112
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED---LEKEIKRLELEIEEV------------EARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3113 EEKAKLENL--------YEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQE 3184
Cdd:COG1579 77 KYEEQLGNVrnnkeyeaLQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*...
gi 1835643837 3185 QEKLLADENRKLREKLEQ 3202
Cdd:COG1579 157 ELEELEAEREELAAKIPP 174
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2964-3216 |
8.08e-05 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 48.65 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2964 EGFQKSLEAERRQQL----EITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTL--- 3036
Cdd:pfam15905 27 QRFRKQKAAESQPNLnnskDASTPATARKVKSLELKKKSQKNLKESKDQKELEKEIRALVQERGEQDKRLQALEEELekv 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3037 EIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQK------NSQKMQVAQQE--QLRQETQVLQTTFLSEKQ----LL 3104
Cdd:pfam15905 107 EAKLNAAVREKTSLSASVASLEKQLLELTRVNELLKAkfsedgTQKKMSSLSMElmKLRNKLEAKMKEVMAKQEgmegKL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3105 LEREKYIEEEKAKLENLyEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKE---AEENVRRKQDELQQLDKK 3181
Cdd:pfam15905 187 QVTQKNLEHSKGKVAQL-EEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDiaqLEELLKEKNDEIESLKQS 265
|
250 260 270
....*....|....*....|....*....|....*
gi 1835643837 3182 RQEQEKLLADENRKLREKLEQMEEEHRIALAQTRE 3216
Cdd:pfam15905 266 LEEKEQELSKQIKDLNEKCKLLESEKEELLREYEE 300
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
626-757 |
8.15e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 46.16 E-value: 8.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 626 ETVPVVGVSEMEEPTPAEDERDRVQKKTFTKWVNK---------HLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR 696
Cdd:cd21324 1 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 697 ----EKGRMRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 757
Cdd:cd21324 81 rtinKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1949-2152 |
8.45e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 8.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1949 EEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHakakaQAEKEAEELQRRMQEEVSKREVvAVDAEQQKQTIQQELQQLR 2028
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAE-----KMREELELEQQRRFEEIRLRKQ-RLEEERQRQEEEERKQRLQ 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2029 QNSDMEiksKAKQIEEvEYnRRKIEEeihivrLQLETMQKHKANAEDELQELRARAEK-AEQQKK----AAQEEAERLRK 2103
Cdd:pfam15709 414 LQAAQE---RARQQQE-EF-RRKLQE------LQRKKQQEEAERAEAEKQRQKELEMQlAEEQKRlmemAEEERLEYQRQ 482
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1835643837 2104 QVKDETQKKREAEEelkrKVQAEKEAAREKqravedLEKFRSQAEEAER 2152
Cdd:pfam15709 483 KQEAEEKARLEAEE----RRQKEEEAARLA------LEEAMKQAQEQAR 521
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1951-2514 |
8.47e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.44 E-value: 8.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1951 KAAEKLKEEERRRLAEVEAQLakqtqlaeAHAKAKAQaEKEAEELQRRmqEEVSKREVVAVDAEQQKQtiqqeLQQLrqn 2030
Cdd:pfam10174 174 KKSGEEDWERTRRIAEAEMQL--------GHLEVLLD-QKEKENIHLR--EELHRRNQLQPDPAKTKA-----LQTV--- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2031 sdmeIKSKAKQIEEVEYNRRKIEEEIHIVRL--------------QLETMQKHKANAEDELQELRARAEKAEQQKKAAQE 2096
Cdd:pfam10174 235 ----IEMKDTKISSLERNIRDLEDEVQMLKTngllhtedreeeikQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQT 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2097 EAERLRKQVKDETQKKREAEEELKRK------VQAEKEAAR-----------EKQRAVEDLEKFRSQAEEAERRMKQAEV 2159
Cdd:pfam10174 311 KLETLTNQNSDCKQHIEVLKESLTAKeqraaiLQTEVDALRlrleekesflnKKTKQLQDLTEEKSTLAGEIRDLKDMLD 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2160 EKERQIKVAQEVAQ--QSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEE-------AERLKKLHDEAEKAREEAE 2230
Cdd:pfam10174 391 VKERKINVLQKKIEnlQEQLRDKDKQLAGLKERVKSLQTDSSNTDTALTTLEEAlsekeriIERLKEQREREDRERLEEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2231 KELEKWHQKANEalRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARK--RAKTEESALRQKELAEDELEKQRKLADATAQ 2308
Cdd:pfam10174 471 ESLKKENKDLKE--KVSALQPELTEKESSLIDLKEHASSLASSGLKKdsKLKSLEIAVEQKKEECSKLENQLKKAHNAEE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2309 QKFSAEQELIRLKaetenseqqrllleeelfRLKNEVneaiqkrKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSK 2388
Cdd:pfam10174 549 AVRTNPEINDRIR------------------LLEQEV-------ARYKEESGKAQAEVERLLGILREVENEKNDKDKKIA 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2389 QMLEVEASKLRELAEEAAKLRAVSEEAKRQRqIAEDEAARQRAE------AERILKEKLAAIN------DATRLK-TEAE 2455
Cdd:pfam10174 604 ELESLTLRQMKEQNKKVANIKHGQQEMKKKG-AQLLEEARRREDnladnsQQLQLEELMGALEktrqelDATKARlSSTQ 682
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2456 IALKEKEAENERLRrlaedeAYQRKLLEEqATQHKQD-----IEEK---IILLKKSSDNELERQKNI 2514
Cdd:pfam10174 683 QSLAEKDGHLTNLR------AERRKQLEE-ILEMKQEallaaISEKdanIALLELSSSKKKKTQEEV 742
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2551-2764 |
8.49e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 8.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2551 NQLKNIAEETQRSKEKAEQEAEKQRQlALEEeqrrkeAEEKVRKILADEK--EAARQRKAALEEVERLKAKAEEAKRQke 2628
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRK-ELEE------AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAE-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2629 LAEKEAERQiQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEE-----AERAKRAA------EDADF 2697
Cdd:COG3206 235 LAEAEARLA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdviALRAQIAAlraqlqQEAQR 313
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2698 ARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAEleaAKRAHAEQAALKQKQL 2764
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVE---VARELYESLLQRLEEA 377
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1992-2314 |
8.64e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 8.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1992 AEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKA 2071
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEE----ELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2072 NAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRkvqaEKEAAREKQRAVEDLEKFRSQAEEAE 2151
Cdd:COG4372 105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKE----LEEQLESLQEELAALEQELQALSEAE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2152 RRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEK 2231
Cdd:COG4372 181 AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEI 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2232 elekwHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKF 2311
Cdd:COG4372 261 -----EELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
...
gi 1835643837 2312 SAE 2314
Cdd:COG4372 336 LAE 338
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2928-3140 |
8.73e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2928 KAEAEMLQKQKELAQEQARKFQEDKEQIEQQlaKETEGFQKSLEAERRQQLEITAEAErlklqvlEMSRAQAKAEEDASK 3007
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ--AEEAEKQRAAEQARQKELEQRAAAE-------KAAKQAEQAAKQAEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3008 FKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQvAQQEQLR 3087
Cdd:TIGR02794 117 KQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAK-AKAEEAK 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3088 QETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQM 3140
Cdd:TIGR02794 196 AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2556-2924 |
8.87e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 8.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2556 IAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAE 2635
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2636 RQIQLAQEAALKKIDAEEKAHTAIVQQKE-QEMLQTRKQEQSILDKLKEEAErAKRAAEDADFARTRAEQEAALSRQQVE 2714
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEElQEELEELQKERQDLEQQRKQLE-AQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2715 EAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVK 2794
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2795 LQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEenkmLIMKDKDSTQKLLVEEAEK 2874
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA----LLLNLAALSLIGALEDALL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2875 MRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEA 2924
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2544-2874 |
9.43e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2544 SDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEA 2623
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2624 KRQKELAEKEAErQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEdadfartRAE 2703
Cdd:COG4372 121 QKERQDLEQQRK-QLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELL-------KEA 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2704 QEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQK 2783
Cdd:COG4372 193 NRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKD 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2784 SQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDS 2863
Cdd:COG4372 273 TEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLD 352
|
330
....*....|.
gi 1835643837 2864 TQKLLVEEAEK 2874
Cdd:COG4372 353 NDVLELLSKGA 363
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1939-2150 |
9.90e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1939 ITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQ 2018
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2019 T---------------IQQELQQLrQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKhkanAEDELQELRAr 2083
Cdd:COG3883 98 SggsvsyldvllgsesFSDFLDRL-SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEA----LKAELEAAKA- 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2084 aeKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEA 2150
Cdd:COG3883 172 --ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
643-747 |
1.01e-04 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 45.52 E-value: 1.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 643 EDERdrvqkKTFTKWVNK---------HLIKAQRHVSDLYEDLRDGHNLISLLEVLSGD-------NLPREKGRM--RFH 704
Cdd:cd21294 5 EDER-----REFTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDtidervlNKPPRKNKPlnNFQ 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1835643837 705 KLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 747
Cdd:cd21294 80 MIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2601-2755 |
1.09e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.61 E-value: 1.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2601 EAARQRKAALEEVERLKAKAEEAKRQKELAEKEAErqiqlAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQsiLDK 2680
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELE-----DLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNKE--YEA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2681 LKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAE-RLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAE 2755
Cdd:COG1579 94 LQKEIESLKRRISDLEDEILELMERIEELEEELAELEaELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
3031-3201 |
1.11e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.30 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3031 AVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLK--REAELLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLERE 3108
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEkqRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3109 KYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEK---DQLKVSMDDAMKKQKEAEENVRRK--QDELQQLDKKRQ 3183
Cdd:TIGR02794 127 KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKkkaEEAKKKAEAEAKAKAEAEAKAKAEeaKAKAEAAKAKAA 206
|
170
....*....|....*...
gi 1835643837 3184 EQEKLLADENRKLREKLE 3201
Cdd:TIGR02794 207 AEAAAKAEAEAAAAAAAE 224
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2260-2749 |
1.12e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 48.88 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2260 AQEEAEKQKEDAEREARKRAKTEESALRQ-KELAEDELEKQRKLADATAQQkfsAEQELIRLKAETENSEQQRLLLEEEL 2338
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEaEQKAKEEAEEERLAELEAKRQ---AEEEAREAKAEAEQRAAELAAEAAKK 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2339 FRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKqmleveasklrelAEEAAKLRAvsEEAKRQ 2418
Cdd:COG3064 79 LAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRK-------------AEEEAKRKA--EEERKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2419 RQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKII 2498
Cdd:COG3064 144 AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2499 LLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLA 2578
Cdd:COG3064 224 RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2579 LEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTA 2658
Cdd:COG3064 304 AAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADV 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2659 IVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAE 2738
Cdd:COG3064 384 EEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALL 463
|
490
....*....|.
gi 1835643837 2739 KLRKEAELEAA 2749
Cdd:COG3064 464 GILKAVALDGG 474
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2698-3156 |
1.12e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.13 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2698 ARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEK---LRKEAELEAAKRAHAEQAAlkqKQLADEemdkhkk 2774
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQviaLRRAGGLEAALALVRSGEG---KALMDE------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2775 faektLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENK 2854
Cdd:COG5278 154 -----IRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2855 MLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEML 2934
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2935 QKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEE 3014
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3015 IGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQ 3094
Cdd:COG5278 389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 3095 TTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDD 3156
Cdd:COG5278 469 AAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1944-2170 |
1.13e-04 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 48.38 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1944 RRLNDEEKAAEKLKEEERRRLAEV-EAQLA--KQTQLAEAHAKAKAQAE-----KEAEELQRRMQEEVSKREVVA----- 2010
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEdlRRQLDTLTVERARLQLEldnlrLAAEDFRQKYEDELNLRTSAEndlvg 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2011 ------------VDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEE----VEY-NRRKIE--EEIHIVRLQLETM-QKHK 2070
Cdd:pfam00038 108 lrkdldeatlarVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSDtqvnVEMdAARKLDltSALAEIRAQYEEIaAKNR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2071 ANAED----ELQELRARAEKAEQQKKAAQEEAERLRKQVKdetqkKREAEEELKRKVQAEKEAARE--KQRAVEDLEKFR 2144
Cdd:pfam00038 188 EEAEEwyqsKLEELQQAAARNGDALRSAKEEITELRRTIQ-----SLEIELQSLKKQKASLERQLAetEERYELQLADYQ 262
|
250 260
....*....|....*....|....*.
gi 1835643837 2145 SQAEEAERRMKQAEVEKERQIKVAQE 2170
Cdd:pfam00038 263 ELISELEAELQETRQEMARQLREYQE 288
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2256-2450 |
1.15e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2256 KKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQElirlKAETENSEQQRLLLE 2335
Cdd:PRK09510 71 QKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ----KQAEEAAAKAAAAAK 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2336 EELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEK-SKQMLEVEAsklRELAEEAAKLRAVSEE 2414
Cdd:PRK09510 147 AKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAeAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 1835643837 2415 AKRQRQIAEDEAARQRAEAERILKEKLAAINDATRL 2450
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| DUF1663 |
pfam07909 |
Protein of unknown function (DUF1663); The members of this family are hypothetical proteins ... |
2067-2509 |
1.18e-04 |
|
Protein of unknown function (DUF1663); The members of this family are hypothetical proteins expressed by Trypanosoma cruzi, a eukaryotic parasite that causes Chagas' disease in humans. This region is found as multiple copies per protein.
Pssm-ID: 116521 [Multi-domain] Cd Length: 514 Bit Score: 49.04 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2067 QKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDE----TQKKREAEEELKRKVQAE--KEAAREKQRAVEDL 2140
Cdd:pfam07909 10 KEERVNVQRRVSSWRKLQLREAEHARAGRECIEAAEAAAEDEdsslTSPISSYAVNLGFSPQPDeaLNATHEKDGGPLSF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2141 EKFRSQAEEAERRMKqAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQ-----EEAERL 2215
Cdd:pfam07909 90 EPSWAISFDAAEALA-AEEDAARGQLVGEESSRVFHVVHDRIGREDAAGHHWVPEDALDAEERRETASRkclelEEAAAF 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2216 KKLHDEAEKAREEAEKELEKWHQKANEALrlrlQAEEVAHKKTLAQEEaekqKEDAEREARKRAKTEESALRQK-----E 2290
Cdd:pfam07909 169 DEIGEMMFQDRLIQAELRSARHEKAEEAL----AAEEDAAMCILAEEE----REDTYGLHRDAIDSEEHADRRRieageA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2291 LAED-ELEKQRKLADATaQQKFSAEQELIRLKAETENSEQQRLLLEEELF---RLKNEVNEAIQK-RKEMEE-ELAKVRA 2364
Cdd:pfam07909 241 AAEDfEEEKGEETADAK-DWFFSAFELALEALAAEEDAARGKLVLEEREGnygKHRDAIDSEEQAtMNCLEKgEAAAVDA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2365 EMEILLQ-SKSRAE--EESRSNT-EKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDE----------AARQR 2430
Cdd:pfam07909 320 GSTLAANfSKSEQElgEEYEEATdEIADEAIAAEEDIIIHRNKAAARGELVGEEREDMCGLHKDAidsetttgehAVRKL 399
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2431 AEAERILKEKLAAindATRLKTEAEIALKEKEAENERLRRLAEDEayqrkLLEEQATQHKQDIEEKIILLKKSSDNELE 2509
Cdd:pfam07909 400 AHPPRLSVQKLSS---QTPLTTTNYNVLIETTTCIERDEAAARDE-----LLDEEILQLIKIIEETRLILTNKTNNDGE 470
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2582-2803 |
1.31e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.29 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2582 EQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAErqiqlAQEAALKKIDAEEKAHTAIVQ 2661
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID-----KLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2662 QKEQEMlQTRKQEQSILDKLKEeAERAKRAAEDADFARTRAEQEAALSRQQ---VEEAERLKQRAEEEAQAKAQAQDEAE 2738
Cdd:COG3883 90 ERARAL-YRSGGSVSYLDVLLG-SESFSDFLDRLSALSKIADADADLLEELkadKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2739 KLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQ 2803
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
2762-3120 |
1.33e-04 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 49.08 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2762 KQLADEEMDKHK--KFAEKTLRQKSQVEQELTKVKLQLEETDHQKTL-LDEELQRLKEEVTDAMRQKAQVEEELFKVKIQ 2838
Cdd:PLN03229 386 GKMDTEELLKHRmlKFRKIGGFQEGVPVDPERKVNMKKREAVKTPVReLEGEVEKLKEQILKAKESSSKPSELALNEMIE 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2839 meeliKLKLRIEEE--NKMLIMKDKDstqkllveeaeKMRQVAEEAARLSIEAQE-----AARMRKLAED-DLANQRALA 2910
Cdd:PLN03229 466 -----KLKKEIDLEytEAVIAMGLQE-----------RLENLREEFSKANSQDQLmhpvlMEKIEKLKDEfNKRLSRAPN 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2911 EKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQE--DKEQIEQQLAKETEGFQKSlEAERRQQL--EITAEAER 2986
Cdd:PLN03229 530 YLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEvmDRPEIKEKMEALKAEVASS-GASSGDELddDLKEKVEK 608
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2987 LKLQV-LEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKermavvqtLEIQRQQSGKEAEELRRAiAELEHEKEKLK 3065
Cdd:PLN03229 609 MKKEIeLELAGVLKSMGLEVIGVTKKNKDTAEQTPPPNLQEK--------IESLNEEINKKIERVIRS-SDLKSKIELLK 679
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3066 REaelLQKNSQKMQVAQQ---EQLRQE-----TQVLQTTFLSEKQLLLEREKYIEEEKAKLEN 3120
Cdd:PLN03229 680 LE---VAKASKTPDVTEKekiEALEQQikqkiAEALNSSELKEKFEELEAELAAARETAAESN 739
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1829-2148 |
1.35e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.90 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1829 KQRQEQIQSVPITDSKTMKEHLLQEKKLLDEIESNRDKvdecqkyAKQYIDAIKDYELQLVTYKAQVEPVASPAKKPKVQ 1908
Cdd:PRK10929 29 TQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLER-------AKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPN 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1909 STSDSIIQEYVDLRTRYSELTTLTSQYikfiTETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQA 1988
Cdd:PRK10929 102 MSTDALEQEILQVSSQLLEKSRQAQQE----QDRAREISDSLSQLPQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1989 ekeaeelqrrMQEEVSKREVVaVDaeqqkqtiQQELQQLRQNsdmeikskakqieeveyNRRKIeeeihiVRLQLETMQK 2068
Cdd:PRK10929 178 ----------LQAESAALKAL-VD--------ELELAQLSAN-----------------NRQEL------ARLRSELAKK 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2069 HKANAEDELQELRA-----RAEKAEQqkkaAQEEAERLRKQ-------VKDETQKKREAEEELKRKVQ-------AEKEA 2129
Cdd:PRK10929 216 RSQQLDAYLQALRNqlnsqRQREAER----ALESTELLAEQsgdlpksIVAQFKINRELSQALNQQAQrmdliasQQRQA 291
|
330
....*....|....*....
gi 1835643837 2130 AREKQRAVEDLEKFRSQAE 2148
Cdd:PRK10929 292 ASQTLQVRQALNTLREQSQ 310
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2703-2811 |
1.40e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 49.18 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2703 EQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKE--------AELEAAKRA-HAEQAALKQKQLADEemdkhk 2773
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQElvaleglaAELEEKQQElEAQLEQLQEKAAETS------ 211
|
90 100 110
....*....|....*....|....*....|....*...
gi 1835643837 2774 kfAEKTLRQKSQVEQELTKVKLQLEETdhqKTLLDEEL 2811
Cdd:PRK11448 212 --QERKQKRKEITDQAAKRLELSEEET---RILIDQQL 244
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
5957-6053 |
1.40e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 44.62 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5957 YQEAMQRLFNWLDTAEARLSEEFLvGGDLDMVKRQLLDLKEFKRELYQRKVELESLHHRTLPVKCED----KETSTRLND 6032
Cdd:pfam00435 6 FFRDADDLESWIEEKEALLSSEDY-GKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGhyasEEIQERLEE 84
|
90 100
....*....|....*....|.
gi 1835643837 6033 FRQRWERLEEEVVDRQHQLEA 6053
Cdd:pfam00435 85 LNERWEQLLELAAERKQKLEE 105
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5271-5360 |
1.60e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 44.24 E-value: 1.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5271 LEMILSWVSDMEDLISnQKPPSSEVKVVKAQLQEQKLLQRLLEERRPRLERV------LQDMQTSESGEENAKHGSLQAR 5344
Cdd:smart00150 7 ADELEAWLEEKEQLLA-SEDLGKDLESVEALLKKHEAFEAELEAHEERVEALnelgeqLIEEGHPDAEEIEERLEELNER 85
|
90
....*....|....*.
gi 1835643837 5345 WEALIQQADTRNRRLE 5360
Cdd:smart00150 86 WEELKELAEERRQKLE 101
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2013-2393 |
1.66e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2013 AEQQKQTIQQELQQLRQNSDMEIKSKakqiEEVEYNRRKIEEEIhivrlqlETMQKHKANAEDELQELRARAEKAEQQKK 2092
Cdd:pfam02029 8 ARERRRRAREERRRQKEEEEPSGQVT----ESVEPNEHNSYEED-------SELKPSGQGGLDEEEAFLDRTAKREERRQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2093 AAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDlEKFRSQAEEAERRMKQAEVEKERQ--IKVAQE 2170
Cdd:pfam02029 77 KRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDS-RLGRYKEEETEIREKEYQENKWSTevRQAEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2171 VAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQA 2250
Cdd:pfam02029 156 GEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2251 EEvahKKTLAQEEAEKqkedaerearkraKTEESALRQKELAEDELEKQRkladataQQKFSAEQELIRLKAETEnseqq 2330
Cdd:pfam02029 236 RE---EEAEVFLEAEQ-------------KLEELRRRRQEKESEEFEKLR-------QKQQEAELELEELKKKRE----- 287
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2331 rllleeelfrLKNEVNEAIQKRKEMEEELAKVRAEMEillqSKSRAEEESRSNTEKSKQMLEV 2393
Cdd:pfam02029 288 ----------ERRKLLEEEEQRRKQEEAERKLREEEE----KRRMKEEIERRRAEAAEKRQKL 336
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2797-3200 |
1.70e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 48.60 E-value: 1.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2797 LEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQME-ELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKM 2875
Cdd:pfam09731 51 LGEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQsGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKAL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2876 RQVAEEAARLSIEAQEAArmrKLAEDDLANQRALAEKMLKEKMQAiQEASRLKAEAEMLQKQKELAqeqarkfqEDKEQI 2955
Cdd:pfam09731 131 EEVLKEAISKAESATAVA---KEAKDDAIQAVKAHTDSLKEASDT-AEISREKATDSALQKAEALA--------EKLKEV 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2956 EQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEI------------------GN 3017
Cdd:pfam09731 199 INLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVfqqelvsifpdiipvlkeDN 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3018 KLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQEtqvlqttf 3097
Cdd:pfam09731 279 LLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEAQLRLE-------- 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3098 lSEKQLLLEREKYIEEEKAKLENLYEDEvrkAQKLKQEqehqmkhLEEEKDQLKVSMDDAMKKQKEAEENVRRKQdeLQQ 3177
Cdd:pfam09731 351 -FEREREEIRESYEEKLRTELERQAEAH---EEHLKDV-------LVEQEIELQREFLQDIKEKVEEERAGRLLK--LNE 417
|
410 420
....*....|....*....|...
gi 1835643837 3178 LDKKRQEQEKLLADENRKLREKL 3200
Cdd:pfam09731 418 LLANLKGLEKATSSHSEVEDENR 440
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4039-4070 |
1.74e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.74e-04
10 20 30
....*....|....*....|....*....|..
gi 1835643837 4039 KLLSAEKAVTGYKDPYSGKTISVFEAMKKGLI 4070
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2051-2196 |
1.76e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 46.60 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2051 KIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKRE--AEEELKRKVQAEKE 2128
Cdd:pfam04012 19 KAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEelAREALAEKKSLEKQ 98
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2129 AAREKQ---RAVEDLEKFRSQAEEAERRMKQAEVEK------ERQIKVAQEVAQQSAAAELNSKRMSFAE-KTAQLEL 2196
Cdd:pfam04012 99 AEALETqlaQQRSAVEQLRKQLAALETKIQQLKAKKnllkarLKAAKAQEAVQTSLGSLSTSSATDSFERiEEKIEER 176
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2375-2631 |
1.80e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2375 RAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQiAEDEAARQRAEAERILKEKLAAINDATrlKTEA 2454
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERL-AAQEQKKQAEEAAKQAALKQKQAEEAA--AKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2455 EIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKiillKKSsdnelerqknivedtlrqrriieeeirilkv 2534
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAK----KKA------------------------------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2535 nfEKASVGKSDLElelnqlkniaeetqrSKEKAEQEAEKQRQlALEEEQRRKEAEEKVRKILADEKEAARQRKAAleeve 2614
Cdd:PRK09510 188 --EAEAAAKAAAE---------------AKKKAEAEAKKKAA-AEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAA----- 244
|
250
....*....|....*..
gi 1835643837 2615 rlkAKAEEAKRQKELAE 2631
Cdd:PRK09510 245 ---KAAEKAAAAKAAAE 258
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2538-2659 |
1.86e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.67 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2538 KASVGKSDLELE-----LNQLKNIAEETQRSKEKAEQEAEKQR--------QLALEEEQRRKEAEEKVRKILADEKEAAR 2604
Cdd:PRK00409 508 KKLIGEDKEKLNeliasLEELERELEQKAEEAEALLKEAEKLKeeleekkeKLQEEEDKLLEEAEKEAQQAIKEAKKEAD 587
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2605 QRKAALEEVERLKAKAEEAKRQkelaeKEAERQIQLAQEAALKKIDAEEKAHTAI 2659
Cdd:PRK00409 588 EIIKELRQLQKGGYASVKAHEL-----IEARKRLNKANEKKEKKKKKQKEKQEEL 637
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2909-3220 |
2.13e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 2.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2909 LAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLA---KETEGFQKSLEAERRQQLEITAEAE 2985
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEqarEELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2986 RLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLK 3065
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3066 REAELLQKNSQKMQVAQ-----QEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQM 3140
Cdd:COG4372 164 EELAALEQELQALSEAEaeqalDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3141 KHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQ 3220
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2537-2642 |
2.15e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 48.41 E-value: 2.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2537 EKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQR-KAALEEVER 2615
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAaETSQERKQK 217
|
90 100
....*....|....*....|....*....
gi 1835643837 2616 LKAKAEEAKRQKELAEKEAERQI--QLAQ 2642
Cdd:PRK11448 218 RKEITDQAAKRLELSEEETRILIdqQLRK 246
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
5366-5560 |
2.21e-04 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 46.28 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5366 AQAFQESLSAFQDWLCATEKHLAELWQVDScLSQIQEAHQQIQVLCKDVRLKSGELDRVLENGQKVLELASGEEELLtQE 5445
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDD-LESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEI-QE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5446 KLDSLRVRYLITAQSSAAILQRLEQTLEASSCVDpSQEDFSLWLSRMEKEVASHgSWDEDREGMLSTVDRDK-FEQIIEL 5524
Cdd:cd00176 80 RLEELNQRWEELRELAEERRQRLEEALDLQQFFR-DADDLEQWLEEKEAALASE-DLGKDLESVEELLKKHKeLEEELEA 157
|
170 180 190
....*....|....*....|....*....|....*.
gi 1835643837 5525 EHTKISRIEDRLEELRHIRLDPSQLQSQLRDHKILA 5560
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNE 193
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2033-2139 |
2.28e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 48.15 E-value: 2.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2033 MEIKSKAKQIEEVEYNRRKIEEEIH-IVRLQLETMQKHKANAEDELQELRARAEKAE---QQKKAAQEEAERLRKQVKDE 2108
Cdd:COG0542 404 MEIDSKPEELDELERRLEQLEIEKEaLKKEQDEASFERLAELRDELAELEEELEALKarwEAEKELIEEIQELKEELEQR 483
|
90 100 110
....*....|....*....|....*....|.
gi 1835643837 2109 TQKKREAEEELKRKVQAEKEAAREKQRAVED 2139
Cdd:COG0542 484 YGKIPELEKELAELEEELAELAPLLREEVTE 514
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1920-2164 |
2.29e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1920 DLRTRYSELTTLTSQYIkfitETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQ----TQLAEAHAKAKAQAEKEAEEL 1995
Cdd:COG1340 12 ELEEKIEELREEIEELK----EKRDELNEELKELAEKRDELNAQVKELREEAQELrekrDELNEKVKELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1996 QRRMQEEVSKREVVA--VDAEQQKQTIQQELQQLR---QNSDM----------EIKSKAKQIEEVEyNRRKIEEEIHIVR 2060
Cdd:COG1340 88 NELREELDELRKELAelNKAGGSIDKLRKEIERLEwrqQTEVLspeeekelveKIKELEKELEKAK-KALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2061 LQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDL 2140
Cdd:COG1340 167 AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKEL 246
|
250 260
....*....|....*....|....
gi 1835643837 2141 EKFRSQAEEAERRMKQAEVEKERQ 2164
Cdd:COG1340 247 KKLRKKQRALKREKEKEELEEKAE 270
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2537-2938 |
2.32e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.73 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2537 EKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAalEEVERL 2616
Cdd:COG3064 42 ERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKA--AAAAEK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2617 KAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDAD 2696
Cdd:COG3064 120 EKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2697 FARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFA 2776
Cdd:COG3064 200 AAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLV 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2777 EKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEElFKVKIQMEELIKLKLRIEEENKML 2856
Cdd:COG3064 280 VVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA-ASLEAALSLLAAGAAAAAAGAGAL 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2857 IMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQK 2936
Cdd:COG3064 359 ATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLV 438
|
..
gi 1835643837 2937 QK 2938
Cdd:COG3064 439 KL 440
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3097-3214 |
2.35e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3097 FLSEKQLLL---EREKYIEEEKAKLENLYEDEVRKAQ----KLKQEQE-----------HQMKHLEEEKDQLKVSMDDAM 3158
Cdd:PRK12704 27 KIAEAKIKEaeeEAKRILEEAKKEAEAIKKEALLEAKeeihKLRNEFEkelrerrnelqKLEKRLLQKEENLDRKLELLE 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 3159 KKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKL------------REKLEQMEEEHRIALAQT 3214
Cdd:PRK12704 107 KREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELerisgltaeeakEILLEKVEEEARHEAAVL 174
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3104-3206 |
2.36e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 48.28 E-value: 2.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3104 LLEREKYIEEEKAKLENLyedeVRKAQKLKQEQEHQMKHLEEEKDQLKVSMD----DAMKKQKEAEENVRRKQDELQQLd 3179
Cdd:PRK00409 525 LEELERELEQKAEEAEAL----LKEAEKLKEELEEKKEKLQEEEDKLLEEAEkeaqQAIKEAKKEADEIIKELRQLQKG- 599
|
90 100
....*....|....*....|....*..
gi 1835643837 3180 KKRQEQEKLLADENRKLREKLEQMEEE 3206
Cdd:PRK00409 600 GYASVKAHELIEARKRLNKANEKKEKK 626
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
3031-3192 |
2.42e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3031 AVVQTL-EIQRQQSG-KEAEELRRAIAE--LEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQTtflSEKQLLLE 3106
Cdd:PRK09510 59 AVVEQYnRQQQQQKSaKRAEEQRKKKEQqqAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA---ALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3107 REKYIEEEKAKLENlyEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDdaMKKQKEAEENVRRKQDELQQLDKKRQEQE 3186
Cdd:PRK09510 136 EAAAKAAAAAKAKA--EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE--AKKKAEAEAAAKAAAEAKKKAEAEAKKKA 211
|
....*.
gi 1835643837 3187 KLLADE 3192
Cdd:PRK09510 212 AAEAKK 217
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1724-2034 |
2.42e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1724 SKELEATKAELKKLRSQVEghqplfnTLEADLNKAKDVNEQMLRSHSERDVDldryreKVQQLLERWQAILVQIDLRQRE 1803
Cdd:TIGR02169 750 EQEIENVKSELKELEARIE-------ELEEDLHKLEEALNDLEARLSHSRIP------EIQAELSKLEEEVSRIEARLRE 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1804 LDQLGRQLRYYRETYEwliKWIKDAKQRQEQIQSvpitdsktmkehllQEKKLLDEIESNRDKVDECQKYAKQYIDAIKD 1883
Cdd:TIGR02169 817 IEQKLNRLTLEKEYLE---KEIQELQEQRIDLKE--------------QIKSIEKEIENLNGKKEELEEELEELEAALRD 879
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1884 YELQLVTYKAQVEPVAspAKKPKVQSTSDSIIQEYVDLRTRYSELttltsqyikfiTETLRRLNDEEKAAEKLKEE---- 1959
Cdd:TIGR02169 880 LESRLGDLKKERDELE--AQLRELERKIEELEAQIEKKRKRLSEL-----------KAKLEALEEELSEIEDPKGEdeei 946
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 1960 --ERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIqQELQQLRQNSDME 2034
Cdd:TIGR02169 947 peEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI-EEYEKKKREVFME 1022
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4410-4446 |
2.51e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 2.51e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1835643837 4410 LKLLDAQLATGGIIDPRFGFHLPVEIAYQRGYFNRET 4446
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2380-2818 |
2.56e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.98 E-value: 2.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2380 SRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEialK 2459
Cdd:pfam15964 291 AQTHTNVHMQTIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELE---R 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2460 EKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKA 2539
Cdd:pfam15964 368 QKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDV 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2540 SVGKSDLELELNQLKNIAEETQrsKEKAEQEAEKQRQLALEEEQRRKeaeekvrkiLADEKEAARQRkaaLEEVERLKAK 2619
Cdd:pfam15964 448 TKVCGEMRYQLNQTKMKKDEAE--KEHREYRTKTGRQLEIKDQEIEK---------LGLELSESKQR---LEQAQQDAAR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2620 A-EEAKRQKELAeKEAERQIQLA---QEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDklKEEAERAKRAAEDA 2695
Cdd:pfam15964 514 ArEECLKLTELL-GESEHQLHLTrleKESIQQSFSNEAKAQALQAQQREQELTQKMQQMEAQHD--KTVNEQYSLLTSQN 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2696 DFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKE-AELEAAKRAHAEQAALKQKQLadEEMDKHKK 2774
Cdd:pfam15964 591 TFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYLQDRLEKLQKRnEELEEQCVQHGRMHERMKQRL--RQLDKHCQ 668
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1835643837 2775 FAEKTLRQKSQVEQELTKvklqleetdhQKTLLDEELQRLKEEV 2818
Cdd:pfam15964 669 ATAQQLVQLLSKQNQLFK----------ERQNLTEEVQSLRSQV 702
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
2477-2800 |
2.57e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 48.39 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2477 YQRKLLEEQATQHKQDIEEKIILlkKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLEL-ELNQLKN 2555
Cdd:PLN03188 947 HEHKLLKEKYENHPEVLRTKIEL--KRVQDELEHYRNFYDMGEREVLLEEIQDLRSQLQYYIDSSLPSARKRnSLLKLTY 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2556 IAEETQRSKEKAEQEA-EKQRQLALEEEQRR-KEAEEK---VRKILADEKEAARqrkaALeeVERLKAKAEEAKRQKEla 2630
Cdd:PLN03188 1025 SCEPSQAPPLNTIPEStDESPEKKLEQERLRwTEAESKwisLAEELRTELDASR----AL--AEKQKHELDTEKRCAE-- 1096
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2631 ekEAERQIQLAQEAALKKIDaeekaHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSR 2710
Cdd:PLN03188 1097 --ELKEAMQMAMEGHARMLE-----QYADLEEKHIQLLARHRRIQEGIDDVKKAAARAGVRGAESKFINALAAEISALKV 1169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2711 QQVEEAERLKqraEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFaEKTLRQKSQVEQEL 2790
Cdd:PLN03188 1170 EREKERRYLR---DENKSLQAQLRDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEQEAAEAY-KQIDKLKRKHENEI 1245
|
330
....*....|
gi 1835643837 2791 TKVKLQLEET 2800
Cdd:PLN03188 1246 STLNQLVAES 1255
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2798-3003 |
2.83e-04 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 45.81 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2798 EETDHQKTLLDEELQRLKEEVTDAMRQ-KAQVEEEL-FKVKIQ-MEELIKLKLRIEEENKMlimkdKDSTQKLLVEEAEk 2874
Cdd:pfam15665 14 AEIQALKEAHEEEIQQILAETREKILQyKSKIGEELdLKRRIQtLEESLEQHERMKRQALT-----EFEQYKRRVEERE- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2875 MRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKA-EAEMLQKQKelaQEQARKFQEDKE 2953
Cdd:pfam15665 88 LKAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAKHRqEIQELLTTQ---RAQSASSLAEQE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2954 QIEQQLAKETEGFQKSLEAERRQQLEITAEAERlklqvlEMSRAQAKAEE 3003
Cdd:pfam15665 165 KLEELHKAELESLRKEVEDLRKEKKKLAEEYEQ------KLSKAQAFYER 208
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
2582-2637 |
2.90e-04 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 47.18 E-value: 2.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2582 EQRRKEAEEKVRKILADEK-EAARQRKAALEEVERLKAKAEE-AKRQKELAEKEAERQ 2637
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEERaEEAQEKKEEAKKKEREEKLAKLsPEEQRKYEEKERKKE 320
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4885-4921 |
2.93e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.93e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1835643837 4885 DPSEETGPIAGILDTDTLEKISITEAMHRSLVDNITG 4921
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2052-2361 |
3.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2052 IEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAR 2131
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2132 EKQRAVEDLEKFRSQAEEAERRMKQaeVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHIT-----VT 2206
Cdd:COG4372 109 EAEELQEELEELQKERQDLEQQRKQ--LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAeaeqaLD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2207 HLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESAL 2286
Cdd:COG4372 187 ELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELA 266
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2287 RQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAK 2361
Cdd:COG4372 267 ILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELAD 341
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1920-2261 |
3.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.20 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1920 DLRTRYSELTTLTSQYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEahaKAKAQAEKEAEELQRRM 1999
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELE---QLEEELEELNEQLQAAQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2000 QEEVSKREVVAvDAEQQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQE 2079
Cdd:COG4372 94 AELAQAQEELE-SLQEEAEELQEELEELQK----ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2080 LRARAEKAEQQKkaAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEV 2159
Cdd:COG4372 169 LEQELQALSEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2160 EKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQK 2239
Cdd:COG4372 247 DKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAK 326
|
330 340
....*....|....*....|..
gi 1835643837 2240 ANEALRLRLQAEEVAHKKTLAQ 2261
Cdd:COG4372 327 KLELALAILLAELADLLQLLLV 348
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
2563-2765 |
3.11e-04 |
|
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a number of Proteobacteria. The N-terminal 30 residue region tends to by Lys/Arg-rich, and is followed by a membrane-spanning region. This is followed by an acidic low-complexity region of variable length and a well-conserved C-terminal domain of two tandem regions matched by pfam05036 (Sporulation related repeat), found in several cell division and sporulation proteins. The role of FtsN as a suppressor for other cell division mutations is poorly understood; it may involve cell wall hydrolysis. [Cellular processes, Cell division]
Pssm-ID: 274041 [Multi-domain] Cd Length: 298 Bit Score: 46.99 E-value: 3.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2563 SKEKAEQEAEKQRQLALEEEQRRK---EAEEKVRKILADEKeaarqRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQ 2639
Cdd:TIGR02223 51 SKQANEPETLQPKNQTENGETAADlppKPEERWSYIEELEA-----REVLINDPEEPSNGGGVEESAQLTAEQRQLLEQM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2640 LAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARtrAEQEAALSRQQVEEAERL 2719
Cdd:TIGR02223 126 QADMRAAEKVLATAPSEQTVAVEARKQTAEKKPQKARTAEAQKTPVETEKIASKVKEAKQ--KQKALPKQTAETQSNSKP 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1835643837 2720 KQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLA 2765
Cdd:TIGR02223 204 IETAPKADKADKTKPKPKEKAERAAALQCGAYANKEQAESVRAKLA 249
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1992-2477 |
3.23e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 3.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1992 AEELQRRMQEEVSKREVVAvDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEihiVRLQLETMQKHKA 2071
Cdd:COG3064 1 AQEALEEKAAEAAAQERLE-QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE---AEQRAAELAAEAA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2072 NAEDELQELRARAEKAEQQKKA-AQEEAERLRKQVKDETQKKREAEEELKRKVQAE-KEAAREKQRAVEDLEKFRSQAEE 2149
Cdd:COG3064 77 KKLAEAEKAAAEAEKKAAAEKAkAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEaKRKAEEERKAAEAEAAAKAEAEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2150 AERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEA 2229
Cdd:COG3064 157 ARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2230 EKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQ 2309
Cdd:COG3064 237 VEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2310 KFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQ 2389
Cdd:COG3064 317 VLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2390 MLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLR 2469
Cdd:COG3064 397 GGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAV 476
|
....*...
gi 1835643837 2470 RLAEDEAY 2477
Cdd:COG3064 477 LADLLLLG 484
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2082-2153 |
3.29e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 44.77 E-value: 3.29e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2082 ARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKV------QAEKEAAREKQRAVEDLEKFRSQAEEAERR 2153
Cdd:PRK05759 45 AAAERAKKELELAQAKYEAQLAEARAEAAEIIEQAKKRAAQIieeakaEAEAEAARIKAQAQAEIEQERKRAREELRK 122
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2950-3163 |
3.34e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 47.25 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2950 EDKEQIEQQLAKETEGFQKSLEAERRQQLEitaeAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKER 3029
Cdd:pfam15709 310 ESEEERSEEDPSKALLEKREQEKASRDRLR----AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRR 385
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3030 MAVV----QTLEIQRQQsgkEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQvlqttflSEKQLLL 3105
Cdd:pfam15709 386 FEEIrlrkQRLEEERQR---QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAE-------AEKQRQK 455
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3106 EREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEE-----KDQLKVSMDDAMKKQKE 3163
Cdd:pfam15709 456 ELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEErrqkeEEAARLALEEAMKQAQE 518
|
|
| PRK13735 |
PRK13735 |
conjugal transfer mating pair stabilization protein TraG; Provisional |
1909-2113 |
3.34e-04 |
|
conjugal transfer mating pair stabilization protein TraG; Provisional
Pssm-ID: 184287 [Multi-domain] Cd Length: 942 Bit Score: 47.82 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1909 STSDSIIQEYVDLRTR---YSELTT------------LTSQYIKFITEtlRRLNDEEK----AAEKLKEEERRRLAE--V 1967
Cdd:PRK13735 723 NSAKQSYDQYTTNMTRsheYAEMASrtesmsgqmsenLSQQFAQYVMK--HAPQDAEAiltnTSSPEIAERRRAMAWsfV 800
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1968 EAQLakQTQLAEAHAKAKAqaekeaeELQRRMQEEVSKREVVAVDAEQQKQtiQQELQQLRQNSDM--EIKSK-AKQIEE 2044
Cdd:PRK13735 801 QEQV--QPGVDNAWRESRG-------DIGKGMESVPSGGGSQDIIADHQGH--QAIIEQRTQDSGIrnDVKHQvDNMVTE 869
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2045 VEYNRRKIEEEIH----IVRLQLETMQKHKaNAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKR 2113
Cdd:PRK13735 870 YEGNIGDTQNSIRgeenTVKGQYSELQNHH-KTEALSQNNKYNEEKSAQERMPGADSPEELMKRAKEYQDKHK 941
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2543-2730 |
3.40e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2543 KSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEE 2622
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2623 ------------------------------------AKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQE 2666
Cdd:COG4942 109 llralyrlgrqpplalllspedfldavrrlqylkylAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2667 MLQTRKQEQ-SILDKL-KEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAK 2730
Cdd:COG4942 189 ALEALKAERqKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2678-2814 |
3.46e-04 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 44.17 E-value: 3.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2678 LDKLKEEAERAKRAAEDADFARTRAEQEaalSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEA-ELEAAKRAHAEQ 2756
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQED---LEKQAEIAREAQQNYERELVLHAEDIKALQALREELnELKAEIAELKAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2757 AALKQKQLADEEmdkhkkfaEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRL 2814
Cdd:pfam07926 80 AESAKAELEESE--------ESWEEQKKELEKELSELEKRIEDLNEQNKLLHDQLESL 129
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4998-5035 |
3.54e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 3.54e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1835643837 4998 QRFLEVQYLTGGLIEPDLPNRVNLDEALRKGIIDARTA 5035
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
3062-3224 |
3.56e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.45 E-value: 3.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3062 EKLKREAELLQKNSQK------MQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLyEDEVRKAQKLKQE 3135
Cdd:COG4717 49 ERLEKEADELFKPQGRkpelnlKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEEL-REELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3136 QEH--QMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQ 3213
Cdd:COG4717 128 LPLyqELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170
....*....|.
gi 1835643837 3214 TREMRTQTDDL 3224
Cdd:COG4717 208 LAELEEELEEA 218
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2347-2782 |
3.61e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2347 EAIQKRKEMEEELAKvRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEA 2426
Cdd:COG3064 19 EQAEAEKRAAAEAEQ-KAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2427 ARQRAEAER-ILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSD 2505
Cdd:COG3064 98 AKAAKEAEAaAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2506 NELERQKNIVEDTLRQRRIIEEEIRILKVNfekASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRR 2585
Cdd:COG3064 178 AAAALVAAAAAAVEAADTAAAAAAALAAAA---AAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2586 KEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQ 2665
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2666 EMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAE 2745
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430
....*....|....*....|....*....|....*..
gi 1835643837 2746 LEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQ 2782
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGI 451
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2999-3166 |
3.90e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2999 AKAEEDASKFKKKAE-EIGNKLHQTELATKERMavvqtlEIQRQQSGKEAEELRRAIAELEH----EKEKLKREAELLQK 3073
Cdd:PRK12704 34 KEAEEEAKRILEEAKkEAEAIKKEALLEAKEEI------HKLRNEFEKELRERRNELQKLEKrllqKEENLDRKLELLEK 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3074 NSQKMQVAQQEQLRQETQVlqttflseKQLLLEREKYIEEEKAKLE---NLYEDEVRKA--QKLKQEQEHQMKHLeeekd 3148
Cdd:PRK12704 108 REEELEKKEKELEQKQQEL--------EKKEEELEELIEEQLQELErisGLTAEEAKEIllEKVEEEARHEAAVL----- 174
|
170
....*....|....*....
gi 1835643837 3149 qLKVSMDDAMKK-QKEAEE 3166
Cdd:PRK12704 175 -IKEIEEEAKEEaDKKAKE 192
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2679-3106 |
4.12e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 47.36 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2679 DKLKEEAERAKrAAEDADFARTRAEQEAALSrqQVEEAerlkQRAEEEAQAKAQAQDEAEKLRKEAeleaakrahaeqaa 2758
Cdd:PRK10929 26 KQITQELEQAK-AAKTPAQAEIVEALQSALN--WLEER----KGSLERAKQYQQVIDNFPKLSAEL-------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2759 lkQKQLADEEmDKHKKFAEKTlrQKSQVEQELTKVKLQLEETDHQktlLDEELQRLKEeVTDAMRQKAQVEEELFKVKIQ 2838
Cdd:PRK10929 85 --RQQLNNER-DEPRSVPPNM--STDALEQEILQVSSQLLEKSRQ---AQQEQDRARE-ISDSLSQLPQQQTEARRQLNE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2839 MEELIKLK---LRIEEENKMLIMKDKDSTQKLLVEEAEkmrqvaeeAARLSieaqeaarmrklaeddlANQRalaekmlk 2915
Cdd:PRK10929 156 IERRLQTLgtpNTPLAQAQLTALQAESAALKALVDELE--------LAQLS-----------------ANNR-------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2916 ekmqaiQEASRLKAEaeMLQKQkelaqeqarkfqedkeqiEQQLAKETEGFQKSLEAERRQQLEITAE-AERLKLQVLEM 2994
Cdd:PRK10929 203 ------QELARLRSE--LAKKR------------------SQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2995 SRA---QAKAEEDASK-FKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQ------SGKEAEELRRAIAEL-EHEK-E 3062
Cdd:PRK10929 257 PKSivaQFKINRELSQaLNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVARLpEMPKpQ 336
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1835643837 3063 KLKRE-AEL-LQKNSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLE 3106
Cdd:PRK10929 337 QLDTEmAQLrVQRLRYEDLLNKQPQLRQIRQADGQPLTAEQNRILD 382
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
2056-2176 |
4.16e-04 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 46.37 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2056 IHIVRLQLEtmqkhKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEElkrkvQAEKEAAREKQR 2135
Cdd:COG0330 153 IEVVDVEIK-----DIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAII-----EAEAYREAQILR 222
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1835643837 2136 AVEDLEKFRSQAEEAErrmKQAEVEKERQIKVAQEVAQQSA 2176
Cdd:COG0330 223 AEGEAEAFRIVAEAYS---AAPFVLFYRSLEALEEVLSPNS 260
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4298-4336 |
4.23e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 41.16 E-value: 4.23e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 4298 YLYGTGCVAGIQIPTTKEIISFYQALKRGLISPEVAHVL 4336
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
2238-2768 |
4.55e-04 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 47.32 E-value: 4.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2238 QKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLAD----ATAQQKFSA 2313
Cdd:COG5271 330 LAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSAddeeASADGGTSP 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2314 EQELIRLKAETENSEQQRLLLEEELFRLKNEvnEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEV 2393
Cdd:COG5271 410 TSDTDEEEEEADEDASAGETEDESTDVTSAE--DDIATDEEADSLADEEEEAEAELDTEEDTESAEEDADGDEATDEDDA 487
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2394 EASKLRELAEEAAKLRAVSEEAKRQRQIA-----EDEAARQRAEAERIL-----KEKLAAINDATRLKTEAEIALKEK-- 2461
Cdd:COG5271 488 SDDGDEEEAEEDAEAEADSDELTAEETSAddgadTDAAADPEDSDEDALedeteGEENAPGSDQDADETDEPEATAEEde 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2462 --EAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKA 2539
Cdd:COG5271 568 pdEAEAETEDATENADADETEESADESEEAEASEDEAAEEEEADDDEADADADGAADEEETEEEAAEDEAAEPETDASEA 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2540 SVGKSDLELEL-----NQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKIL--ADEKEAARQRKAALEE 2612
Cdd:COG5271 648 ADEDADAETEAeasadESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASeeADAEEADTEADGTAEE 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2613 VERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAA 2692
Cdd:COG5271 728 AEEAAEEAESADEEAASLPDEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEEAEAAAEEKEKVADEDQDTD 807
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2693 EDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQ-AKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEE 2768
Cdd:COG5271 808 EDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAeDDEEDDDAAAAKDVDADLDLDADLAADEHEAEEAQEAETD 884
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1522-2125 |
4.67e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 47.20 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1522 EDYKQALRNLETHYQEFMRDSQDSENFLPDDRMQIER---EYNNCIQKYEQLLRTQEKGEQDEVTCKNYISQLKDI--RL 1596
Cdd:PRK01156 186 DYLEEKLKSSNLELENIKKQIADDEKSHSITLKEIERlsiEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAesDL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1597 QLEGCESRTIHKIR---TPMEKDPIKECSQRISEQQQIHFELEGIKKNLNKVSEKTLKVLAQKEQSSSSPLLRTEHEITH 1673
Cdd:PRK01156 266 SMELEKNNYYKELEerhMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1674 QKMDQVYSLSSIYLEKLKTINLVIRSTQGAEEVVRTYEDQLKEVHAVPSDS-KELEATKAELKKLRSQVEGHQPLFNTLE 1752
Cdd:PRK01156 346 SRYDDLNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEIlKIQEIDPDAIKKELNEINVKLQDISSKV 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1753 ADLNKAKDVneqmLRSHserdvdLDRYREKVQQLLERWQAILVQIDLRQrelDQLGRQLRYYREtyewlikwikDAKQRQ 1832
Cdd:PRK01156 426 SSLNQRIRA----LREN------LDELSRNMEMLNGQSVCPVCGTTLGE---EKSNHIINHYNE----------KKSRLE 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1833 EQIQSVPItDSKTMKEHLLQEKKLLDEIESnrdkvDECQKYAKQYiDAIKDYELQLVTYKAQVEPVASPAKKpkvqstSD 1912
Cdd:PRK01156 483 EKIREIEI-EVKDIDEKIVDLKKRKEYLES-----EEINKSINEY-NKIESARADLEDIKIKINELKDKHDK------YE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1913 SIIQEYV-----DLRTRYSELTTLTSQYIKFITETLRRLNDEEKaaEKLKEEERRrLAEVEAQLAKQTQLAEAHAKakaQ 1987
Cdd:PRK01156 550 EIKNRYKslkleDLDSKRTSWLNALAVISLIDIETNRSRSNEIK--KQLNDLESR-LQEIEIGFPDDKSYIDKSIR---E 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1988 AEKEAEELQRRMQEevskrevvAVDAEQQKQTIQQELQQLRQNSdMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQ 2067
Cdd:PRK01156 624 IENEANNLNNKYNE--------IQENKILIEKLRGKIDNYKKQI-AEIDSIIPDLKEITSRINDIEDNLKKSRKALDDAK 694
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2068 KHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQA 2125
Cdd:PRK01156 695 ANRARLESTIEILRTRINELSDRINDINETLESMKKIKKAIGDLKRLREAFDKSGVPA 752
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2686-3018 |
4.73e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2686 ERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLA 2765
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2766 DEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKL 2845
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2846 KLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAA-----RLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQA 2920
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAeaeklIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2921 IQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAK 3000
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....*...
gi 1835643837 3001 AEEDASKFKKKAEEIGNK 3018
Cdd:COG4372 326 KKLELALAILLAELADLL 343
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2581-2824 |
4.73e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.87 E-value: 4.73e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2581 EEQRRKEAEEKVRKILADEKEAARQRKAAleevERLKAKAEEAKRQKElaEKEAERQIQlaqeaalkkidaEEKAHTAIV 2660
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRA----ERAEMRRLEVERKRR--EQEEQRRLQ------------QEQLERAEK 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2661 QQKEQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTR-AEQEAAlsRQQVEEAERLKQRAEEEAQAKAQAQDEAEK 2739
Cdd:pfam15709 374 MREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLqAAQERA--RQQQEEFRRKLQELQRKKQQEEAERAEAEK 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2740 LRKEaELEaakrahaEQAALKQKQLAdeEMDKHKKFaeKTLRQKSQVEQeltKVKLQLEETDHQktllDEELQRLKEEvt 2819
Cdd:pfam15709 452 QRQK-ELE-------MQLAEEQKRLM--EMAEEERL--EYQRQKQEAEE---KARLEAEERRQK----EEEAARLALE-- 510
|
....*
gi 1835643837 2820 DAMRQ 2824
Cdd:pfam15709 511 EAMKQ 515
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
2049-2142 |
4.81e-04 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 43.84 E-value: 4.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2049 RRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAeqqKKAAQEEAERLRKQVKDETQKKREAEEElkrkvQAEKE 2128
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEAEQQLKEARAEAQEI---IENAKKRAEKLKEEIVAAAEAEAERIIE-----QAAAE 103
|
90
....*....|....
gi 1835643837 2129 AAREKQRAVEDLEK 2142
Cdd:pfam00430 104 IEQEKDRALAELRQ 117
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
3134-3236 |
5.09e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 47.00 E-value: 5.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3134 QEQEHQMKHLEEEKDQLKVSMDDAMKKQKEA-EENVRRKQDELQQLdKKRQEQEKLLADENRKLREKLEQMEEEHRIALA 3212
Cdd:COG0542 414 DELERRLEQLEIEKEALKKEQDEASFERLAElRDELAELEEELEAL-KARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100
....*....|....*....|....
gi 1835643837 3213 QTREMRTQtddLAGNLPLTPTVVT 3236
Cdd:COG0542 493 ELAELEEE---LAELAPLLREEVT 513
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2753-2916 |
5.12e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.69 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2753 HAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEEL 2832
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2833 FKVKIQME------ELIKLKLRIEE-ENKML-IMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLA 2904
Cdd:COG1579 83 GNVRNNKEyealqkEIESLKRRISDlEDEILeLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 1835643837 2905 NQRALAEKMLKE 2916
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3708-3739 |
5.19e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 5.19e-04
10 20 30
....*....|....*....|....*....|..
gi 1835643837 3708 KLLSAEKAVTGYKDPYTGNTISLFQALKRGLI 3739
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2871-3216 |
5.19e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 5.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2871 EAEKMRQVAE-EAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASrLKAEAEMLQkQKELAQEQARKFQ 2949
Cdd:pfam05557 15 QNEKKQMELEhKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEA-LREQAELNR-LKKKYLEALNKKL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2950 EDKEQIEQQlAKETEGFQKSLEAERRQQLEITAEAerLKLQVLEMSRAQAKAEEdaskFKKKAEEIGNKLHQTELATKER 3029
Cdd:pfam05557 93 NEKESQLAD-AREVISCLKNELSELRRQIQRAELE--LQSTNSELEELQERLDL----LKAKASEAEQLRQNLEKQQSSL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3030 MAV---VQTLEIQRQQSGKEAEELRRA------IAELEHEKEKLKREAELLQKNSQkmqvaQQEQLRQETQVLQTTflse 3100
Cdd:pfam05557 166 AEAeqrIKELEFEIQSQEQDSEIVKNSkselarIPELEKELERLREHNKHLNENIE-----NKLLLKEEVEDLKRK---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3101 kqllLEREKYIEEEKAKLE---NLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLK--VSMDDAMKKQKEAEEN-VRRKQDE 3174
Cdd:pfam05557 237 ----LEREEKYREEAATLElekEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEqlQQREIVLKEENSSLTSsARQLEKA 312
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1835643837 3175 LQQLDKKRQEQEKLLADENRKLREKLEQMEEEHRIALAQTRE 3216
Cdd:pfam05557 313 RRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKE 354
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2617-2774 |
5.23e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.93 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2617 KAKAEEAKRQKELAEKEAerQIQLAQEAALKKIDAEEkahtaivqqkeqemlqTRKQeqsildKLKEEAERAKRAAEDAD 2696
Cdd:PTZ00491 662 KSQEAAARHQAELLEQEA--RGRLERQKMHDKAKAEE----------------QRTK------LLELQAESAAVESSGQS 717
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2697 FARTRAEQEAALSRQQVE-EAERLKQRAEE-EAQAkaqaqdEAEKLRKEAELEAA-KRAHAEQAALKQKQLADEEMDKHK 2773
Cdd:PTZ00491 718 RAEALAEAEARLIEAEAEvEQAELRAKALRiEAEA------ELEKLRKRQELELEyEQAQNELEIAKAKELADIEATKFE 791
|
.
gi 1835643837 2774 K 2774
Cdd:PTZ00491 792 R 792
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2031-2195 |
5.25e-04 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 46.60 E-value: 5.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2031 SDMEIKSKAKQIEEVEYNRRKIEEEihivRLQLETMQKHKANAEdELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQ 2110
Cdd:pfam04747 56 ASLELTEQPQQVEKVKKSEKKKAQK----QIAKDHEAEQKVNAK-KAAEKEARRAEAEAKKRAAQEEEHKQWKAEQERIQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2111 KKREAEEELKRKVQAEKEaaREKQRAVEDLEKfrsqAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEK 2190
Cdd:pfam04747 131 KEQEKKEADLKKLQAEKK--KEKAVKAEKAEK----AEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEP 204
|
....*
gi 1835643837 2191 TAQLE 2195
Cdd:pfam04747 205 AEQVQ 209
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2074-2191 |
5.33e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 47.25 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2074 EDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKrKVQAEKEAAREKQRAV--EDLEKFRSQAEEAE 2151
Cdd:PRK11448 148 QQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQ-ELEAQLEQLQEKAAETsqERKQKRKEITDQAA 226
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1835643837 2152 RRMKQAEVEKERQIKvaqevaQQSAAA--ELNSKRMSFAEKT 2191
Cdd:PRK11448 227 KRLELSEEETRILID------QQLRKAgwEADSKTLRFSKGA 262
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2743-3058 |
5.48e-04 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 46.10 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2743 EAELEAAKRAHAEqaALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQ---LEE-----TDHQKTLLDEELQRL 2814
Cdd:pfam09728 17 EEKLAALCKKYAE--LLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAkskLEKlcrelQKQNKKLKEESKKLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2815 KEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDstqklLVEEAEKMRQVAEEAARlSIEAQEAAR 2894
Cdd:pfam09728 95 KEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEELREKLKS-----LIEQYELRELHFEKLLK-TKELEVQLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2895 MRKLAEDDLANQRALAEKMLKekmqaiqEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKsleaer 2974
Cdd:pfam09728 169 EAKLQQATEEEEKKAQEKEVA-------KARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTT------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2975 rqqleitaeaerLKLQVLEMSRAQAKAEEDASKFKKKAEeignKLHQTELATKErmavvqtleiQRQQSGKEAEELRRAI 3054
Cdd:pfam09728 236 ------------FKKEMEKMSKKIKKLEKENLTWKRKWE----KSNKALLEMAE----------ERQKLKEELEKLQKKL 289
|
....
gi 1835643837 3055 AELE 3058
Cdd:pfam09728 290 EKLE 293
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2247-2410 |
5.48e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2247 RLQAEEVAHKKTL-AQEEAEKQKEDAEREARKR---AKTEESALRQKelaEDELEKQrkladataqqkfsaEQELIRLKA 2322
Cdd:PRK12704 48 KKEAEAIKKEALLeAKEEIHKLRNEFEKELRERrneLQKLEKRLLQK---EENLDRK--------------LELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2323 ETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELAKVRAE--MEILLQsksRAEEESRsnTEKSKQMLEVEasklrE 2400
Cdd:PRK12704 111 ELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGLTAEeaKEILLE---KVEEEAR--HEAAVLIKEIE-----E 180
|
170
....*....|
gi 1835643837 2401 LAEEAAKLRA 2410
Cdd:PRK12704 181 EAKEEADKKA 190
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2622-3206 |
5.83e-04 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 46.74 E-value: 5.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2622 EAKRQKELAEKEAERQIQLAQEAalkKIDAEEKAHTAIVQQKEQEMLQTRK------QEQSILDKLKEEAERAKRAAEDA 2695
Cdd:pfam10174 40 ELKKERALRKEEAARISVLKEQY---RVTQEENQHLQLTIQALQDELRAQRdlnqllQQDFTTSPVDGEDKFSTPELTEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2696 DFARTRAEQEaalsrQQVEEAERLKQRAEEeaqakAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKkf 2775
Cdd:pfam10174 117 NFRRLQSEHE-----RQAKELFLLRKTLEE-----MELRIETQKQTLGARDESIKKLLEMLQSKGLPKKSGEEDWERT-- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2776 aektlRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKA-QVEEELFKVKI-QMEELIK---LKLRIE 2850
Cdd:pfam10174 185 -----RRIAEAEMQLGHLEVLLDQKEKENIHLREELHRRNQLQPDPAKTKAlQTVIEMKDTKIsSLERNIRdleDEVQML 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2851 EENKMLIMKDKDSTQKLLveEA---------EKMRQVAEEAARLSIEAQeaARMRKLaeDDLANQRALAEK---MLKEKM 2918
Cdd:pfam10174 260 KTNGLLHTEDREEEIKQM--EVykshskfmkNKIDQLKQELSKKESELL--ALQTKL--ETLTNQNSDCKQhieVLKESL 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2919 QAI-QEASRLKAEAEMLqkqkelaqeqaRKFQEDKEQIeqqLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRA 2997
Cdd:pfam10174 334 TAKeQRAAILQTEVDAL-----------RLRLEEKESF---LNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKERKINVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2998 QAKAEEDASKFKKKAEEIGNKlhqtelatKERmavVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKnsQK 3077
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAGL--------KER---VKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDR--ER 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3078 MQvaQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEekdqlKVSMDDA 3157
Cdd:pfam10174 467 LE--ELESLKKENKDLKEKVSALQPELTEKESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEE-----CSKLENQ 539
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 3158 MKKQKEAEENVRRKQ---DELQQLDK----KRQEQEKLLADENRkLREKLEQMEEE 3206
Cdd:pfam10174 540 LKKAHNAEEAVRTNPeinDRIRLLEQevarYKEESGKAQAEVER-LLGILREVENE 594
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1558-2104 |
5.86e-04 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 47.04 E-value: 5.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1558 REYNNCIQKYEQLLRTQEKGEQdevtcKNYISQLKDirlqLEGCESRTIHKIRTP--MEKDPIKECSQRI----SEQQQI 1631
Cdd:pfam15921 291 RSQANSIQSQLEIIQEQARNQN-----SMYMRQLSD----LESTVSQLRSELREAkrMYEDKIEELEKQLvlanSELTEA 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1632 HFELEGIKKNLNKVSEKTLKVLA-----------QKEQSSSSPLLRTEHEITHQKMDQVYSLSSIYLEKLKTINLVIRST 1700
Cdd:pfam15921 362 RTERDQFSQESGNLDDQLQKLLAdlhkrekelslEKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSE 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1701 -QGA-EEVVRTYEDQLKEVHAVPSDSKELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRSHSERDVDLDR 1778
Cdd:pfam15921 442 cQGQmERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEATNAEITK 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1779 YREKVQQLLERWQAILVQID-LR--QRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQiqsvpitDSKTMKEHLLQEKK 1855
Cdd:pfam15921 522 LRSRVDLKLQELQHLKNEGDhLRnvQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQ-------HGRTAGAMQVEKAQ 594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1856 LLDEIESNRDKVDECqKYAKQYIDAiKDYELQLVTYKAQVEPV----ASPAKKPKVQSTSDSIIQEYVDLRTRYSELTTL 1931
Cdd:pfam15921 595 LEKEINDRRLELQEF-KILKDKKDA-KIRELEARVSDLELEKVklvnAGSERLRAVKDIKQERDQLLNEVKTSRNELNSL 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1932 TSQYiKFITETLRRLNDE-EKAAEKLKEEERRRLAEVEA--QLAKQTQLAEAHAKAKAQAEKEAEELQR----RMQEEVS 2004
Cdd:pfam15921 673 SEDY-EVLKRNFRNKSEEmETTTNKLKMQLKSAQSELEQtrNTLKSMEGSDGHAMKVAMGMQKQITAKRgqidALQSKIQ 751
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2005 KREVVAVDAEQQKQTIQQELQQLRQnsdmeikskakQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARA 2084
Cdd:pfam15921 752 FLEEAMTNANKEKHFLKEEKNKLSQ-----------ELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQF 820
|
570 580
....*....|....*....|
gi 1835643837 2085 EKAEQQKKAAQEEAERLRKQ 2104
Cdd:pfam15921 821 AECQDIIQRQEQESVRLKLQ 840
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2809-3005 |
6.11e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2809 EELQRLKEEVTDAmrqKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKllvEEAEKMRQVAEEAARlsie 2888
Cdd:TIGR02794 50 QQANRIQQQKKPA---AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAA---KQAEQAAKQAEEKQK---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2889 aQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRL-KAEAEMLQKQKElAQEQARKFQEDKEQIEQQlAKETEGFQ 2967
Cdd:TIGR02794 120 -QAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKaKAAAEAKKKAEE-AKKKAEAEAKAKAEAEAK-AKAEEAKA 196
|
170 180 190
....*....|....*....|....*....|....*...
gi 1835643837 2968 KSLEAERRQQLEITAEAERLKlQVLEMSRAQAKAEEDA 3005
Cdd:TIGR02794 197 KAEAAKAKAAAEAAAKAEAEA-AAAAAAEAERKADEAE 233
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
3054-3218 |
6.22e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.48 E-value: 6.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3054 IAELEHEKEKLKR----EAELLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRka 3129
Cdd:pfam15709 325 LEKREQEKASRDRlraeRAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3130 qklkQEQEHQMKHLEEEKDQlkvsmddamKKQKEAEENVRRKQDELQQldKKRQEQEKLLADENRKLREKLEQMEEEHRI 3209
Cdd:pfam15709 403 ----QEEEERKQRLQLQAAQ---------ERARQQQEEFRRKLQELQR--KKQQEEAERAEAEKQRQKELEMQLAEEQKR 467
|
....*....
gi 1835643837 3210 ALAQTREMR 3218
Cdd:pfam15709 468 LMEMAEEER 476
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2293-2512 |
6.32e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 6.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2293 EDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEMEEELaKVRAEMEillQS 2372
Cdd:TIGR02794 28 KPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL-EQRAAAE---KA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2373 KSRAEEESRSNTEKSKQMLEVEASKLRE--LAEEAAKLRAVSEEAKRQRQI-----AEDEAARQRAEAERILKEKLAAIN 2445
Cdd:TIGR02794 104 AKQAEQAAKQAEEKQKQAEEAKAKQAAEakAKAEAEAERKAKEEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKA 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2446 DATRlKTEAEIALKEKEAENERLRRLAEDEAYQ-RKLLEEQATQHKQDIEEKIILLKKSSDNELERQK 2512
Cdd:TIGR02794 184 EAEA-KAKAEEAKAKAEAAKAKAAAEAAAKAEAeAAAAAAAEAERKADEAELGDIFGLASGSNAEKQG 250
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
650-747 |
6.64e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 43.81 E-value: 6.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 650 QKKTFTKWVN---------KHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPR----EKGRMRFHKLQNVQIALDYL 716
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1835643837 717 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 747
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2871-3068 |
6.80e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2871 EAEKMRQVAEEAARLSiEAQEAARMRKlAEDDLANQRALAEkmLKEKmQAIQEASRLKAEAEMLQKQKELAQEQARKFQE 2950
Cdd:PRK05035 456 EARQARLEREKAAREA-RHKKAAEARA-AKDKDAVAAALAR--VKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQA 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2951 DKEQIEQQLAKETEGFQKSLEA-------ERRQQLEITAEAER----LKLQV-LEMSRAQA-KAEEDASKFKKKAEEIGN 3017
Cdd:PRK05035 531 RARQAEKQAAAAADPKKAAVAAaiarakaKKAAQQAANAEAEEevdpKKAAVaAAIARAKAkKAAQQAASAEPEEQVAEV 610
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 3018 KLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREA 3068
Cdd:PRK05035 611 DPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAA 661
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2262-2622 |
6.81e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 6.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2262 EEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRL 2341
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEE-AKRQRQ 2420
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2421 IAEDEAARQR---AEAERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKI 2497
Cdd:COG4372 166 LAALEQELQAlseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2498 ILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQL 2577
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1835643837 2578 ALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEE 2622
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
3054-3228 |
6.88e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 46.60 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3054 IAELEHEKEKLKREAELLQKNSQKMQVAQQEqLRQETQVLQT---TFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQ 3130
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDE-KRQQLERLRRereKAERYQALLKEKREYEGYELLKEKEALERQKEAIE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3131 KLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRK-QDELQQLDKKRQEQEKLLADENRKLREK---LEQMEEE 3206
Cdd:TIGR02169 244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKereLEDAEER 323
|
170 180
....*....|....*....|..
gi 1835643837 3207 HRIALAQTREMRTQTDDLAGNL 3228
Cdd:TIGR02169 324 LAKLEAEIDKLLAEIEELEREI 345
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
2950-3140 |
6.91e-04 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 44.40 E-value: 6.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2950 EDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKer 3029
Cdd:pfam14662 11 EDLQANNQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLEEARRSLLA-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3030 mavvqtleiQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMqVAQQEQLRQETQVLQTTFLSEKQLLLEREK 3109
Cdd:pfam14662 89 ---------QNKQLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKEL-LKSKACLKEQLHSCEDLACNRETILIEKTT 158
|
170 180 190
....*....|....*....|....*....|..
gi 1835643837 3110 YIEEEKAKLENLYEDEVR-KAQKLKQEQEHQM 3140
Cdd:pfam14662 159 QIEELKSTVEEYSSIEEElRAEKSRLESQLPD 190
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2545-2862 |
6.99e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2545 DLELELNQLKNIAEETQRSKEKAEQEAEKQRQlaleeeqRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAK 2624
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAE-------KRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2625 RQKELAEKEAERQIQLAQEAALKKIDaEEKAHTAIvqQKEQEMLQTR----KQEQSILDK---LKEEAERAKRAAEDADF 2697
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGS-IDKLRKEI--ERLEWRQQTEvlspEEEKELVEKikeLEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2698 ARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQD---EAEKLRKEAEleaakRAHAEqaALKQKQLADEEmdkHKK 2774
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIElykEADELRKEAD-----ELHKE--IVEAQEKADEL---HEE 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2775 FAEKtlrQKSQVEqeltkvklqleetdhqktlLDEELQRLKEEVTDAMRQKAQveEELFKVKIQMEELIKLKLRIEEENK 2854
Cdd:COG1340 232 IIEL---QKELRE-------------------LRKELKKLRKKQRALKREKEK--EELEEKAEEIFEKLKKGEKLTTEEL 287
|
....*...
gi 1835643837 2855 MLIMKDKD 2862
Cdd:COG1340 288 KLLQKSGL 295
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
622-762 |
6.99e-04 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 46.47 E-value: 6.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 622 ETGMETVPVVGVSEMEEPTpAEDERdrvQKKTFTKWVNKHLIKAQRHvsDLYEDLRDGHNLISLLEVLSGD---NLPREK 698
Cdd:COG5069 356 HPGQEPLEEEEKPEIEEFD-AEGEF---EARVFTFWLNSLDVSPEIT--NLFGDLRDQLILLQALSKKLMPmtvTHKLVK 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 699 GR-------MRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDIQVMGQSE 762
Cdd:COG5069 430 KQpasgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKDGCGLSDSD 506
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2967-3088 |
7.07e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.82 E-value: 7.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2967 QKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEignklhqtELAT------KERMAVVQTLEIQR 3040
Cdd:COG1842 36 EEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGRE--------DLARealerkAELEAQAEALEAQL 107
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3041 QQSGKEAEELRRAIAELEHEKEKLKREAELL--QKNSQKMQVAQQEQLRQ 3088
Cdd:COG1842 108 AQLEEQVEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEALSG 157
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2353-2654 |
7.30e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2353 KEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEveasKLRELAEEAAKLRAvseeakrQRQIAEDEAARQRAE 2432
Cdd:COG1340 11 EELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNA----QVKELREEAQELRE-------KRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2433 AERILKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQrklleeQATQHKQDIEEKIILLKKSSDNELERQK 2512
Cdd:COG1340 80 RDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ------QTEVLSPEEEKELVEKIKELEKELEKAK 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2513 NIVEdtlrqrriieeEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEK---AEQEAEKQRQLALEEEQRRKEAE 2589
Cdd:COG1340 154 KALE-----------KNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEmieLYKEADELRKEADELHKEIVEAQ 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2590 EKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERqiqlaqEAALKKIDAEEK 2654
Cdd:COG1340 223 EKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKA------EEIFEKLKKGEK 281
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
5847-5948 |
7.44e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 42.32 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5847 RFWHGFSELTITLNDTQQMVLDiEEASSDPDSIRTKLNTMQALREDVDNLQNDLDTLGILGVELMSSCGDmDKPNVTKSL 5926
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLAS-EDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHP-DAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1835643837 5927 DDLYATWNSLNKVWNEHYNKLE 5948
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4297-4333 |
7.69e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 7.69e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1835643837 4297 KYLYGTGCVAGIQIPTTKEIISFYQALKRGLISPEVA 4333
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2979-3218 |
7.70e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2979 EITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIAELE 3058
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3059 HEKEKLKREAELLQKNSQKMQVAQQEqLRQETQVLQTTFLS---EKQL---------LLEREKYIEEEKAKLENLYEdEV 3126
Cdd:COG1340 92 EELDELRKELAELNKAGGSIDKLRKE-IERLEWRQQTEVLSpeeEKELvekikelekELEKAKKALEKNEKLKELRA-EL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3127 RKAQKLKQEQEHQMKHLEEEKDQLKvsmdDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEE 3206
Cdd:COG1340 170 KELRKEAEEIHKKIKELAEEAQELH----EEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRELRKE 245
|
250
....*....|..
gi 1835643837 3207 HRIALAQTREMR 3218
Cdd:COG1340 246 LKKLRKKQRALK 257
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
2559-2627 |
7.78e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 45.75 E-value: 7.78e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 2559 ETQRSKEKAEQEAEKQRQLALEEEQRRKEAeEKVRKILA--DEKEAARQRKAALEEVERLKAKAEEAKRQK 2627
Cdd:pfam07767 242 KAQRNKEKRRKEEEREAKEEKALKKKLAQL-ERLKEIAKeiAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1944-2098 |
7.83e-04 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 46.10 E-value: 7.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1944 RRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQA-EKEAEELQRRMQEEVSKRevvavdAEQQKQTIQQ 2022
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAER------AEAEKQRQKE 456
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2023 ELQQL--RQNSDMEIKSKakqiEEVEYNRRKIEEEihivrlqletmqkhkanaEDELQELRARAEKAEQQKKAAQEEA 2098
Cdd:pfam15709 457 LEMQLaeEQKRLMEMAEE----ERLEYQRQKQEAE------------------EKARLEAEERRQKEEEAARLALEEA 512
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
3108-3216 |
8.04e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.31 E-value: 8.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3108 EKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKhleeekdqlkvsmDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEK 3187
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAK-------------EEIHKLRNEFEKELRERRNELQKLEKRLLQKEE 96
|
90 100
....*....|....*....|....*....
gi 1835643837 3188 LLADENRKLREKLEQMEEEHRIALAQTRE 3216
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQE 125
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1965-3144 |
8.05e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.58 E-value: 8.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1965 AEVEAQLAKQTQLAEAHAKAKAQAEKEAEElqrrMQEEVSKREVVAVDAEQQKQTIQQELQQLRQnSDMEIKSKAKQIEE 2044
Cdd:TIGR01612 540 KEIEAGLKESYELAKNWKKLIHEIKKELEE----ENEDSIHLEKEIKDLFDKYLEIDDEIIYINK-LKLELKEKIKNISD 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2045 --------------VEYNRRKIEEEIHIVRLQLEtmqKHKANAEDELQELRARAEKAEQQK--KAAQEEAERLRKQVKDE 2108
Cdd:TIGR01612 615 kneyikkaidlkkiIENNNAYIDELAKISPYQVP---EHLKNKDKIYSTIKSELSKIYEDDidALYNELSSIVKENAIDN 691
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2109 TQKKREAEEeLKRKVqaEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIkvaqevaQQSAAAELNSKRMSFA 2188
Cdd:TIGR01612 692 TEDKAKLDD-LKSKI--DKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHI-------HGEINKDLNKILEDFK 761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2189 EKTAQLElslkqehitvthlqeeaerlKKLHDEAEKAREeaekeLEKWHQKANEalrLRLQAEEVAHKKTLAQEEAeKQK 2268
Cdd:TIGR01612 762 NKEKELS--------------------NKINDYAKEKDE-----LNKYKSKISE---IKNHYNDQINIDNIKDEDA-KQN 812
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2269 EDAEREARKRAKTEESALRQ-----KELAEDELEKQRKLA--DATAQQKFSAEQELI-----RLKAE-TENSEQQRLLLE 2335
Cdd:TIGR01612 813 YDKSKEYIKTISIKEDEIFKiinemKFMKDDFLNKVDKFInfENNCKEKIDSEHEQFaeltnKIKAEiSDDKLNDYEKKF 892
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2336 EELFRLKNEVNEAIQKRKEMEEELAKVRAEMEILlqsksraeeesrSNTEKSKQMLEVEASKLRELAEEAAK-LRAVSEE 2414
Cdd:TIGR01612 893 NDSKSLINEINKSIEEEYQNINTLKKVDEYIKIC------------ENTKESIEKFHNKQNILKEILNKNIDtIKESNLI 960
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2415 AKRQRQIAEDEAARQRAEAERILKEklAAINDATRLKTEAeiaLKEKEAENERLRRLAEDEAYQRKLLEEQATQhkqDIE 2494
Cdd:TIGR01612 961 EKSYKDKFDNTLIDKINELDKAFKD--ASLNDYEAKNNEL---IKYFNDLKANLGKNKENMLYHQFDEKEKATN---DIE 1032
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2495 EKIILLKKSSDN-ELERQK---NIVEDTLRQrriieeeirilkvnfekasVGKsDLELeLNqlKNIAEETQRSKEKAEQE 2570
Cdd:TIGR01612 1033 QKIEDANKNIPNiEIAIHTsiyNIIDEIEKE-------------------IGK-NIEL-LN--KEILEEAEINITNFNEI 1089
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2571 AEKQRQLALEE---EQRRKEAEEkVRKILADEKEAARQRKAALEEVERLKAKAE----EAKRQKELAEKEAERqiqlaqe 2643
Cdd:TIGR01612 1090 KEKLKHYNFDDfgkEENIKYADE-INKIKDDIKNLDQKIDHHIKALEEIKKKSEnyidEIKAQINDLEDVADK------- 1161
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2644 aALKKIDAEEkahtaiVQQKEQEMLQTRKQEQSILDKLKE------EAERAKRAAEDA-DFARTRAEQEAALSRQQVEEA 2716
Cdd:TIGR01612 1162 -AISNDDPEE------IEKKIENIVTKIDKKKNIYDEIKKllneiaEIEKDKTSLEEVkGINLSYGKNLGKLFLEKIDEE 1234
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2717 ERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAeQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQEltkvKLQ 2796
Cdd:TIGR01612 1235 KKKSEHMIKAMEAYIEDLDEIKEKSPEIENEMGIEMDI-KAEMETFNISHDDDKDHHIISKKHDENISDIREK----SLK 1309
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2797 LEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEE------------ELFKVKIQMEELIKLKLRIEEENK---------- 2854
Cdd:TIGR01612 1310 IIEDFSEESDINDIKKELQKNLLDAQKHNSDINLylneianiynilKLNKIKKIIDEVKEYTKEIEENNKnikdeldkse 1389
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2855 MLIMKDKDS----TQKLLVEEA-------EKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAE--KMLKEKMQAI 2921
Cdd:TIGR01612 1390 KLIKKIKDDinleECKSKIESTlddkdidECIKKIKELKNHILSEESNIDTYFKNADENNENVLLLFKniEMADNKSQHI 1469
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2922 QEASR-------------LKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLK 2988
Cdd:TIGR01612 1470 LKIKKdnatndhdfnineLKEHIDKSKGCKDEADKNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKKDSEII 1549
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2989 LQvlEMSRAQAKAEEDASKFKKKAEEIGN-KLHQTELATKERMAVVQTLEIQRQQSGKEAEELRraIAELEHEKEKLKRE 3067
Cdd:TIGR01612 1550 IK--EIKDAHKKFILEAEKSEQKIKEIKKeKFRIEDDAAKNDKSNKAAIDIQLSLENFENKFLK--ISDIKKKINDCLKE 1625
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3068 AELLQKNSQKMQVAQQE-QLRQETQVLQT--TFLSEkqlLLEREKYIEEEKAKLENLYEdevrKAQKLKQEQEHQMKHLE 3144
Cdd:TIGR01612 1626 TESIEKKISSFSIDSQDtELKENGDNLNSlqEFLES---LKDQKKNIEDKKKELDELDS----EIEKIEIDVDQHKKNYE 1698
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1795-2158 |
8.33e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 8.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1795 VQIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQSVpITDSKtmkehLLQEKKLLDEIESNRDKVDECQKyA 1874
Cdd:PRK04863 837 AELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRL-LPRLN-----LLADETLADRVEEIREQLDEAEE-A 909
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1875 KQYIDAikdYELQLvtykAQVEPVAS-----PAKKPKVQSTSDSIIQEYVDLRTRYSELTTLTSQYIKF-ITETLRRLND 1948
Cdd:PRK04863 910 KRFVQQ---HGNAL----AQLEPIVSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsYEDAAEMLAK 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1949 EEKAAEKLK------EEERRR----LAEVEAQLAKQTQLaeaHAKAKAQAEKEAEELQRRMQeEVSKREVVAV-DAEQQK 2017
Cdd:PRK04863 983 NSDLNEKLRqrleqaEQERTRareqLRQAQAQLAQYNQV---LASLKSSYDAKRQMLQELKQ-ELQDLGVPADsGAEERA 1058
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2018 QTIQQELQQLRQNSDMEIKSKAKQIEEVEYNR-------RKIEEEIHIVRLQLET--------MQKHKAN---------- 2072
Cdd:PRK04863 1059 RARRDELHARLSANRSRRNQLEKQLTFCEAEMdnltkklRKLERDYHEMREQVVNakagwcavLRLVKDNgverrlhrre 1138
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2073 -AEDELQELRARAEKAEQQKKAAQEEAERLR-KQVKDETQKKREaeeelkRKVQ---AEKEAAREKQRA--------VED 2139
Cdd:PRK04863 1139 lAYLSADELRSMSDKALGALRLAVADNEHLRdVLRLSEDPKRPE------RKVQfyiAVYQHLRERIRQdiirtddpVEA 1212
|
410
....*....|....*....
gi 1835643837 2140 LEKFRSQAEEAERRMKQAE 2158
Cdd:PRK04863 1213 IEQMEIELSRLTEELTSRE 1231
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1931-2605 |
8.40e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.33 E-value: 8.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1931 LTSQYIKFITETLRRLNDEEKaaeklkeeerrrlaeveaQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVA 2010
Cdd:PRK10246 213 LTPEQVQSLTASLQVLTDEEK------------------QLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQALAAEE 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2011 VDAEQ-QKQTIQQELQQLRQNSDmeikSKAKQIEEVEYNRRKIEEeihiVRLQLETMQKHKAnaedelqELRARAEKAEQ 2089
Cdd:PRK10246 275 KAQPQlAALSLAQPARQLRPHWE----RIQEQSAALAHTRQQIEE----VNTRLQSTMALRA-------RIRHHAAKQSA 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2090 QKKAAQE-------EAERLR--------------KQVKDETQKKREAEE--ELKRKVQA-----------EKEAAREKQR 2135
Cdd:PRK10246 340 ELQAQQQslntwlaEHDRFRqwnnelagwraqfsQQTSDREQLRQWQQQltHAEQKLNAlpaitltltadEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2136 AVEDLEKFRS--QAEEAERRMKQAEVEKERQiKVAQEVAQQSAAaeLNSKRMSFAEKTaqlelslkQEHITVTHLQEEAE 2213
Cdd:PRK10246 420 EQRPLRQRLValHGQIVPQQKRLAQLQVAIQ-NVTQEQTQRNAA--LNEMRQRYKEKT--------QQLADVKTICEQEA 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2214 RLKKLhdeaekareeaekelekwhqkanEALRLRLQA----------EEVAHKKTLAQEEAEKQKEDAEREARKRAKTEE 2283
Cdd:PRK10246 489 RIKDL-----------------------EAQRAQLQAgqpcplcgstSHPAVEAYQALEPGVNQSRLDALEKEVKKLGEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2284 SALRQKELaeDELEKQRKLADATAQQKFSAEQELIRLKAETenseqqrLLLEEELFRLKNEVNEAIQKRKEMEEELAKVR 2363
Cdd:PRK10246 546 GAALRGQL--DALTKQLQRDESEAQSLRQEEQALTQQWQAV-------CASLNITLQPQDDIQPWLDAQEEHERQLRLLS 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2364 AEMEILLQSKSRAEEESR--SNTEKSKQMLEVE----ASKLRELAEEAAKLRAVSEEAKR-QRQIAEDEAARQRAEAERI 2436
Cdd:PRK10246 617 QRHELQGQIAAHNQQIIQyqQQIEQRQQQLLTAlagyALTLPQEDEEASWLATRQQEAQSwQQRQNELTALQNRIQQLTP 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2437 LKEKLAAINDATrlkTEAEIALKE--KEAENERLRRLAEDEAYQRKLLEEQA--TQHKQDIEEKI-------------IL 2499
Cdd:PRK10246 697 LLETLPQSDDLP---HSEETVALDnwRQVHEQCLSLHSQLQTLQQQDVLEAQrlQKAQAQFDTALqasvfddqqaflaAL 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2500 LKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKN-IAEETQRSKEKAEQEAEKQRQLA 2578
Cdd:PRK10246 774 LDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQeLAQLAQQLRENTTRQGEIRQQLK 853
|
730 740
....*....|....*....|....*..
gi 1835643837 2579 LEEEQRRKEaeekvRKILADEKEAARQ 2605
Cdd:PRK10246 854 QDADNRQQQ-----QALMQQIAQATQQ 875
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2838-2938 |
8.69e-04 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 45.36 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2838 QMEELiKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDD--LANQRALAE---- 2911
Cdd:cd03406 170 AMEAE-KTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEIEDEmhLAREKARADaeyy 248
|
90 100
....*....|....*....|....*..
gi 1835643837 2912 KMLKEKmqaiqEASRLKAEAEMLQKQK 2938
Cdd:cd03406 249 RALREA-----EANKLKLTPEYLELKK 270
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2049-2163 |
8.76e-04 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 42.60 E-value: 8.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2049 RRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEElKRKVQAEKE 2128
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEES-AEMEAEEKE 79
|
90 100 110
....*....|....*....|....*....|....*....
gi 1835643837 2129 A----AREKQRAVEDLEKfRSQAEEAERRMKQAEVEKER 2163
Cdd:pfam20492 80 QleaeLAEAQEEIARLEE-EVERKEEEARRLQEELEEAR 117
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
3039-3208 |
9.22e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 45.80 E-value: 9.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3039 QRQQSGKEAEELRRAiaeLEHEKEKLKREAELLQKNSQKMQVAQQEQLRQE-TQVLQTTFLSEKQLLLEREKYIEEEKAK 3117
Cdd:pfam15558 26 LQQQAALAWEELRRR---DQKRQETLERERRLLLQQSQEQWQAEKEQRKARlGREERRRADRREKQVIEKESRWREQAED 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3118 LENLYEDEVRKAQK----LKQEQEHQMKHLEEEKDQLKVSMDDAMkkQKEAEENVRRKQDELQQLDKKRQE---QEKLLA 3190
Cdd:pfam15558 103 QENQRQEKLERARQeaeqRKQCQEQRLKEKEEELQALREQNSLQL--QERLEEACHKRQLKEREEQKKVQEnnlSELLNH 180
|
170
....*....|....*...
gi 1835643837 3191 DENRKLREKLEQMEEEHR 3208
Cdd:pfam15558 181 QARKVLVDCQAKAEELLR 198
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
2553-2677 |
9.36e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 43.79 E-value: 9.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2553 LKNIAEETQRSKEKAEQEAE---KQRQLALEEEQRR-KEAEEKVRKILADEK---EAARQR--KAALEEVERLKAKAEea 2623
Cdd:PRK07352 44 LGKILEERREAILQALKEAEerlRQAAQALAEAQQKlAQAQQEAERIRADAKaraEAIRAEieKQAIEDMARLKQTAA-- 121
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2624 krqKELaEKEAERQI-QLAQEAALKKIDaeeKAHTAIvQQKEQEMLQTRKQEQSI 2677
Cdd:PRK07352 122 ---ADL-SAEQERVIaQLRREAAELAIA---KAESQL-PGRLDEDAQQRLIDRSI 168
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2702-2897 |
9.58e-04 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.84 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2702 AEQEAALSRQQVEEAERLKQ-RAEEEAQAKA-----QAQDEAEKLRKE--------AELEAAKRAH----AEQ--AALKQ 2761
Cdd:PRK11637 57 AAKEKSVRQQQQQRASLLAQlKKQEEAISQAsrklrETQNTLNQLNKQidelnasiAKLEQQQAAQerllAAQldAAFRQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2762 KQ-------LADEEMDKHKKFA----------EKTLRQKSQVEQELTKVKLQLEET-DHQKTLLDEE-LQRLKEEVTDAM 2822
Cdd:PRK11637 137 GEhtglqliLSGEESQRGERILayfgylnqarQETIAELKQTREELAAQKAELEEKqSQQKTLLYEQqAQQQKLEQARNE 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2823 RQK--AQVEEELFKVKIQMEELIKLKLRieeenkmliMKDKdstqkllVEEAEkmrqvAEEAARLSIEAQEAARMRK 2897
Cdd:PRK11637 217 RKKtlTGLESSLQKDQQQLSELRANESR---------LRDS-------IARAE-----REAKARAEREAREAARVRD 272
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
6498-6600 |
9.71e-04 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 42.31 E-value: 9.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6498 KFTDALQALMDWLYWAEPQLSEDvPIRGDKDLVSDLMDKHKIFQKELGKRASCVKTLKRSMRDLTrGSISTDSQWLQKQM 6577
Cdd:pfam00435 5 QFFRDADDLESWIEEKEALLSSE-DYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLI-DEGHYASEEIQERL 82
|
90 100
....*....|....*....|...
gi 1835643837 6578 EELNHRWEVVCKLSVGKQARLEA 6600
Cdd:pfam00435 83 EELNERWEQLLELAAERKQKLEE 105
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2673-2873 |
9.83e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 9.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2673 QEQSIldKLKEEAERAKRAAEDADfaRTRAEQEAALSRQQvEEAERLKQRAEEEAQAK-AQAQDEAEK-LRKEAELEAAK 2750
Cdd:PRK00409 526 EELER--ELEQKAEEAEALLKEAE--KLKEELEEKKEKLQ-EEEDKLLEEAEKEAQQAiKEAKKEADEiIKELRQLQKGG 600
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2751 rahaeQAALKQKQLADE--EMDKHKKFAEKTLRQKSQVEQELT---KVKLqleETDHQKTLLdeeLQRLKEEVtdamrqk 2825
Cdd:PRK00409 601 -----YASVKAHELIEArkRLNKANEKKEKKKKKQKEKQEELKvgdEVKY---LSLGQKGEV---LSIPDDKE------- 662
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2826 AQVEEELFKVKIQMEELIKLKLRIEEENKMLI-MKDKDSTQKLL-------VEEAE 2873
Cdd:PRK00409 663 AIVQAGIMKMKVPLSDLEKIQKPKKKKKKKPKtVKPKPRTVSLEldlrgmrYEEAL 718
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
2071-2174 |
9.90e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 43.79 E-value: 9.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2071 ANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEElkrkvQAEKEAAREKQRAVEDLEKFRSQAEEA 2150
Cdd:PRK07352 60 KEAEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIEK-----QAIEDMARLKQTAAADLSAEQERVIAQ 134
|
90 100
....*....|....*....|....*...
gi 1835643837 2151 ERR----MKQAEVEKERQIKVAQEVAQQ 2174
Cdd:PRK07352 135 LRReaaeLAIAKAESQLPGRLDEDAQQR 162
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2884-3180 |
9.94e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2884 RLSIEAQ-EAARMRKLAEDDlanqRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARkfqedkeQIEQQLAKe 2962
Cdd:PRK11281 38 EADVQAQlDALNKQKLLEAE----DKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQAPAKLR-------QAQAELEA- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2963 tegFQKSLEAERRQQLEiTAEAERLKLQVLEMSRAQAKAEEDASKFKkkAEEIGNKLH----QTELATkermAVVQTLEI 3038
Cdd:PRK11281 106 ---LKDDNDEETRETLS-TLSLRQLESRLAQTLDQLQNAQNDLAEYN--SQLVSLQTQperaQAALYA----NSQRLQQI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3039 QRQ-QSGKEAEELRRAiaeleHEKEKLKREAELLQknsqkMQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAK 3117
Cdd:PRK11281 176 RNLlKGGKVGGKALRP-----SQRVLLQAEQALLN-----AQNDLQRKSLEGNTQLQDLLQKQRDYLTARIQRLEHQLQL 245
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3118 LEnlyedEVRKAQKLKQEQEhQMKHLEEEKDQLKVSMDDAMkkQKEAEENVRRKQDELQQLDK 3180
Cdd:PRK11281 246 LQ-----EAINSKRLTLSEK-TVQEAQSQDEAARIQANPLV--AQELEINLQLSQRLLKATEK 300
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
2064-2135 |
1.03e-03 |
|
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.
Pssm-ID: 462322 Cd Length: 323 Bit Score: 45.25 E-value: 1.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2064 ETMQKHKANAEDELQELRARAEKAEQqkKAAQEEAERLRKQVKDETQKKREAEEELKRKvqaEKEAAREKQR 2135
Cdd:pfam07946 257 EALKKAKKTREEEIEKIKKAAEEERA--EEAQEKKEEAKKKEREEKLAKLSPEEQRKYE---EKERKKEQRK 323
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4373-4409 |
1.13e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1835643837 4373 RLLSAERAVTGYRDPYSEQMISLFQAMKKDLIPSEQA 4409
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
2589-2673 |
1.16e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 42.68 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2589 EEKVRKILADEKEAARQRK---AALEEVERLKAKAE-EAKRQKELAEKEAERQIQLAQEAALKKIDA-EEKAHTAIVQQK 2663
Cdd:pfam00430 29 DKRRELIADEIAEAEERRKdaaAALAEAEQQLKEARaEAQEIIENAKKRAEKLKEEIVAAAEAEAERiIEQAAAEIEQEK 108
|
90
....*....|
gi 1835643837 2664 EQEMLQTRKQ 2673
Cdd:pfam00430 109 DRALAELRQQ 118
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2029-2601 |
1.19e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2029 QNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAE---------QQKKAAQEEA- 2098
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNryeseiktaESDLSMELEKn 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2099 -------ERLRKQVKDETQKKRE-------------AEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKqaE 2158
Cdd:PRK01156 273 nyykeleERHMKIINDPVYKNRNyindyfkykndieNKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRYD--D 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2159 VEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQ 2238
Cdd:PRK01156 351 LNNQILELEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQ 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2239 KanealrlrlqaeevahKKTLAQEEAEKQKEDAEREARKRAKTEESALRQkelaedelEKQRKLADATAQQKFSAEQELI 2318
Cdd:PRK01156 431 R----------------IRALRENLDELSRNMEMLNGQSVCPVCGTTLGE--------EKSNHIINHYNEKKSRLEEKIR 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2319 RLKAETEN-SEQQRLLLEEELFRLKNEVNEAIQKRKEMEEelakVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASK 2397
Cdd:PRK01156 487 EIEIEVKDiDEKIVDLKKRKEYLESEEINKSINEYNKIES----ARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLED 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2398 LRELAEEAAKLRAVseeakrqRQIAEDEAARQRAEaerilkEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAY 2477
Cdd:PRK01156 563 LDSKRTSWLNALAV-------ISLIDIETNRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEAN 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2478 ----QRKLLEEQATQhKQDIEEKIILLKKSSDNELERQKNIVEDTLRQrriieeeirilkvnfekasvgkSDLELELNQL 2553
Cdd:PRK01156 630 nlnnKYNEIQENKIL-IEKLRGKIDNYKKQIAEIDSIIPDLKEITSRI----------------------NDIEDNLKKS 686
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2554 KNIAEETQRSKEKAEQEAEKQRQ------LALEEEQRRKEAEEKVRKILADEKE 2601
Cdd:PRK01156 687 RKALDDAKANRARLESTIEILRTrinelsDRINDINETLESMKKIKKAIGDLKR 740
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1961-2136 |
1.20e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 45.11 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1961 RRRLAEVEAQLAK-QTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAeqQKQTIQQELQQLRQNsdmeikska 2039
Cdd:pfam00529 57 QAALDSAEAQLAKaQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQA--AVKAAQAQLAQAQID--------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2040 kqieeveYNRRKIEEEI-HIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERL-RKQVKDETQKKREAEE 2117
Cdd:pfam00529 126 -------LARRRVLAPIgGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEvRSELSGAQLQIAEAEA 198
|
170
....*....|....*....
gi 1835643837 2118 ELKrkvQAEKEAAREKQRA 2136
Cdd:pfam00529 199 ELK---LAKLDLERTEIRA 214
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2070-2174 |
1.22e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2070 KANAEDELQELRARAEKAEQQKKA-AQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQravEDLEKFRSQAE 2148
Cdd:PRK12704 37 EEEAKRILEEAKKEAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL---ELLEKREEELE 113
|
90 100
....*....|....*....|....*.
gi 1835643837 2149 EAERRMKQAEVEKERQIKVAQEVAQQ 2174
Cdd:PRK12704 114 KKEKELEQKQQELEKKEEELEELIEE 139
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2589-2673 |
1.23e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.42 E-value: 1.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2589 EEKVRKILADEKEAARQRKAALEEVERLKAKA-EEAKRQKELAEKEAERQIQLAQEAALKKIDA-EEKAHTAIVQQKEQE 2666
Cdd:cd06503 32 EEKIAESLEEAEKAKEEAEELLAEYEEKLAEArAEAQEIIEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQEKEKA 111
|
....*..
gi 1835643837 2667 MLQTRKQ 2673
Cdd:cd06503 112 LAELRKE 118
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3633-3671 |
1.27e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.62 E-value: 1.27e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1835643837 3633 YLKGTTAIAGVLVEPTGEKLTFYDALKKNLLKPEVAYNL 3671
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
3037-3165 |
1.31e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.38 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3037 EIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQK----MQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIE 3112
Cdd:pfam05262 205 ERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKqrdeVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIE 284
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 3113 ----EEKAKLENLYEDEVRKAQKLKQE-----QEHQMKHLEEEKDQLKVSMD-DAMKKQKEAE 3165
Cdd:pfam05262 285 kaqiEIKKNDEEALKAKDHKAFDLKQEskaseKEAEDKELEAQKKREPVAEDlQKTKPQVEAQ 347
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
2680-2900 |
1.46e-03 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2680 KLKEEAERAKRAAEDAdfartraEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQ--DEAEKLRkeaelEAAKRAHA--- 2754
Cdd:COG0497 169 ALKKELEELRADEAER-------ARELDLLRFQLEELEAAALQPGEEEELEEERRrlSNAEKLR-----EALQEALEals 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2755 --EQAALkqKQLADeemdkhkkfAEKTLRQKSQVEQELTKVKLQLEETDHQktlLDE---ELQRLKEEV-TDAMRQkAQV 2828
Cdd:COG0497 237 ggEGGAL--DLLGQ---------ALRALERLAEYDPSLAELAERLESALIE---LEEaasELRRYLDSLeFDPERL-EEV 301
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2829 EEELFKVK-------IQMEELIKLKLRIEEENKMLiMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAArmRKLAE 2900
Cdd:COG0497 302 EERLALLRrlarkygVTVEELLAYAEELRAELAEL-ENSDERLEELEAELAEAEAELLEAAEKLSAARKKAA--KKLEK 377
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1542-2031 |
1.47e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 45.49 E-value: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1542 SQDSENFlpDDRMQI------EREYNNCIQKyEQLLRTQEKGEQDEVTCKNYISQLKDIRLQLEGCESrtihkirtpMEK 1615
Cdd:pfam15921 369 SQESGNL--DDQLQKlladlhKREKELSLEK-EQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEA---------LLK 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1616 DPIKECSQRISEQQQihfELEGIKKNLNKVSEKTLKVLAQKEQsssspLLRTEHEITHQKMdqvyslssiyleklktinl 1695
Cdd:pfam15921 437 AMKSECQGQMERQMA---AIQGKNESLEKVSSLTAQLESTKEM-----LRKVVEELTAKKM------------------- 489
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1696 virSTQGAEEVVRTYEDQLKEvhavpsDSKELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVN---EQMLRSHSER 1772
Cdd:pfam15921 490 ---TLESSERTVSDLTASLQE------KERAIEATNAEITKLRSRVDLKLQELQHLKNEGDHLRNVQtecEALKLQMAEK 560
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1773 DVDLDRYREKVQQLLE-------RWQAILVQIDLRQRELDQLGRQLRYYRetyewLIKWIKDAKQRQEQIQsvpITDSKT 1845
Cdd:pfam15921 561 DKVIEILRQQIENMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFK-----ILKDKKDAKIRELEAR---VSDLEL 632
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1846 MKEHLL----QEKKLLDEIESNRDKVDECQKYAKQYIDAI-KDYELQLVTYKAQVEPVASPAKKPKVQ--STSDSIIQEY 1918
Cdd:pfam15921 633 EKVKLVnagsERLRAVKDIKQERDQLLNEVKTSRNELNSLsEDYEVLKRNFRNKSEEMETTTNKLKMQlkSAQSELEQTR 712
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1919 VDLRT---------------------RYSELTTLTSQyIKFITETLRRLNDEEKAaekLKEEERRRLAEVEAQLAKQTQL 1977
Cdd:pfam15921 713 NTLKSmegsdghamkvamgmqkqitaKRGQIDALQSK-IQFLEEAMTNANKEKHF---LKEEKNKLSQELSTVATEKNKM 788
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 1978 AEAHAKAKAQaekeaeelQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNS 2031
Cdd:pfam15921 789 AGELEVLRSQ--------ERRLKEKVANMEVALDKASLQFAECQDIIQRQEQES 834
|
|
| SPFH_HflC |
cd03405 |
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ... |
2672-2750 |
1.51e-03 |
|
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model characterizes proteins similar to prokaryotic HflC (High frequency of lysogenization C). Although many members of the SPFH (or band 7) superfamily are lipid raft associated, prokaryote plasma membranes lack cholesterol and are unlikely to have lipid raft domains. Individual proteins of this SPFH domain superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Escherichia coli HflC is an integral membrane protein which may localize to the plasma membrane. HflC associates with another SPFH superfamily member (HflK) to form an HflKC complex. HflKC interacts with FtsH in a large complex termed the FtsH holo-enzyme. FtsH is an AAA ATP-dependent protease which exerts progressive proteolysis against membrane-embedded and soluble substrate proteins. HflKC can modulate the activity of FtsH. HflKC plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection.
Pssm-ID: 259803 [Multi-domain] Cd Length: 249 Bit Score: 44.40 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2672 KQEQSILDKLKEEAE---------RAKR-----AAEDADFARTRAE--QEAALSRQQ-VEEAERLKQRAEEEAQA-KAQA 2733
Cdd:cd03405 120 ELMEEILEQANEEAKeygievvdvRIKRidlpeEVSESVYERMRAEreRIAAEYRAEgEEEAEKIRAEADRERTViLAEA 199
|
90
....*....|....*..
gi 1835643837 2734 QDEAEKLRKEAELEAAK 2750
Cdd:cd03405 200 YREAEEIRGEGDAEAAR 216
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6279-6380 |
1.56e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.55 E-value: 1.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6279 EFHSSAQDLLKWISRTEDTLLTLPAASLvLETVTNQIQEHKVLLTEVNARGEKLAGLERSACRLKDySSKQDCAVIQNLV 6358
Cdd:smart00150 2 QFLRDADELEAWLEEKEQLLASEDLGKD-LESVEALLKKHEAFEAELEAHEERVEALNELGEQLIE-EGHPDAEEIEERL 79
|
90 100
....*....|....*....|..
gi 1835643837 6359 LTAQERLSKVQQCTVAKGRELE 6380
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2884-3040 |
1.58e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2884 RLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKM-QAIQEASRLKAEAE--MLQKQKELaQEQARKFQEDKEQIEQQLA 2960
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALlEAKEEIHKLRNEFEkeLRERRNEL-QKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2961 ------KETEGFQKSLEAERRQQLEITAEAERLK---LQVLE----MSRAQAK----------AEEDASKFKKKAEEign 3017
Cdd:PRK12704 104 llekreEELEKKEKELEQKQQELEKKEEELEELIeeqLQELErisgLTAEEAKeillekveeeARHEAAVLIKEIEE--- 180
|
170 180
....*....|....*....|....
gi 1835643837 3018 klHQTELATKE-RMAVVQTleIQR 3040
Cdd:PRK12704 181 --EAKEEADKKaKEILAQA--IQR 200
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1871-2305 |
1.60e-03 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 45.34 E-value: 1.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1871 QKYAKQYIDAIKDYELQLVTYKAQVEPVASPAKKPKVQSTSDSIIQEYVDLRTRYSELTTLTSQYIKFITETLRRLNDEE 1950
Cdd:COG4995 20 ALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALALALA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1951 KAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQN 2030
Cdd:COG4995 100 AAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAALAL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2031 SDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQ 2110
Cdd:COG4995 180 LALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2111 KKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEK 2190
Cdd:COG4995 260 LAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2191 TAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKED 2270
Cdd:COG4995 340 AAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAALALL 419
|
410 420 430
....*....|....*....|....*....|....*
gi 1835643837 2271 AEREARKRAKTEESALRQKELAEDELEKQRKLADA 2305
Cdd:COG4995 420 LALAAYAAARLALLALIEYIILPDRLYAFVQLYQL 454
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2554-2689 |
1.61e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2554 KNIAEEtqrsKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKiLADEKEAARQRKAALEEVER-LKAKAEEAKRQK-ELAE 2631
Cdd:PRK00409 509 KLIGED----KEKLNELIASLEELERELEQKAEEAEALLKE-AEKLKEELEEKKEKLQEEEDkLLEEAEKEAQQAiKEAK 583
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2632 KEAE------RQIQLAQEAALKKIDAEEkAHTAIvqQKEQEMLQTRKQEQSILDKLKEEAERAK 2689
Cdd:PRK00409 584 KEADeiikelRQLQKGGYASVKAHELIE-ARKRL--NKANEKKEKKKKKQKEKQEELKVGDEVK 644
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1522-2464 |
1.63e-03 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 45.81 E-value: 1.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1522 EDYKQALRNLETHYQEFMRDsQDSENFLPDDRMQIEREYNNCIQKYEQllrTQEKGEQDEVTCKNYIsqlKDIRLQlEGC 1601
Cdd:TIGR01612 758 EDFKNKEKELSNKINDYAKE-KDELNKYKSKISEIKNHYNDQINIDNI---KDEDAKQNYDKSKEYI---KTISIK-EDE 829
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1602 ESRTIHKIRTpMEKDPIKE----------CSQRISEQQQIHFELegIKKNLNKVSEKTLKVLAQKEQSSSSPLLRTEHEI 1671
Cdd:TIGR01612 830 IFKIINEMKF-MKDDFLNKvdkfinfennCKEKIDSEHEQFAEL--TNKIKAEISDDKLNDYEKKFNDSKSLINEINKSI 906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1672 --------THQKMDQVYSLSSIYLEKLKT-----------INLVIRSTQGAEEVVRTYEDQLKevHAVPSDSKELEA--T 1730
Cdd:TIGR01612 907 eeeyqninTLKKVDEYIKICENTKESIEKfhnkqnilkeiLNKNIDTIKESNLIEKSYKDKFD--NTLIDKINELDKafK 984
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1731 KAELKKLRSQVEGHQPLFNTLEADLNKAK--------DVNEQMLRSHSERDVDLDRYREKVQQLL---------ERWQAI 1793
Cdd:TIGR01612 985 DASLNDYEAKNNELIKYFNDLKANLGKNKenmlyhqfDEKEKATNDIEQKIEDANKNIPNIEIAIhtsiyniidEIEKEI 1064
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1794 LVQIDLRQRE-LDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQSVpiTDSKTMKEHLlqeKKLLDEIESNRDKVDECQK 1872
Cdd:TIGR01612 1065 GKNIELLNKEiLEEAEINITNFNEIKEKLKHYNFDDFGKEENIKYA--DEINKIKDDI---KNLDQKIDHHIKALEEIKK 1139
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1873 YAKQYIDAIKDY--ELQLVTYKA------------QVEPVASPAKKPKVQSTSDSIIQEYVDL---RTRYSELTTLTSQY 1935
Cdd:TIGR01612 1140 KSENYIDEIKAQinDLEDVADKAisnddpeeiekkIENIVTKIDKKKNIYDEIKKLLNEIAEIekdKTSLEEVKGINLSY 1219
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1936 IKFI-TETLRRLNDEEKAAEKLKEEERRRLAEVEaQLAKQTQLAEAHAKAKAQAEKEAEELQrrmqeevskrevVAVDAE 2014
Cdd:TIGR01612 1220 GKNLgKLFLEKIDEEKKKSEHMIKAMEAYIEDLD-EIKEKSPEIENEMGIEMDIKAEMETFN------------ISHDDD 1286
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2015 QQKQTIQQElqqlRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRA--------RAEK 2086
Cdd:TIGR01612 1287 KDHHIISKK----HDENISDIREKSLKIIEDFSEESDINDIKKELQKNLLDAQKHNSDINLYLNEIANiynilklnKIKK 1362
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2087 AEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAR-EKQRAVEDLEKFRSQAEEAERRMKQAEVEKERQI 2165
Cdd:TIGR01612 1363 IIDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKDDINLEECKSKiESTLDDKDIDECIKKIKELKNHILSEESNIDTYF 1442
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2166 KVAQEVAQQsaaAELNSKRMSFAEKTAQLELSLKQEHITVTH------LQEEAERLKKLHDEAEKAREEAEKELEKWHQK 2239
Cdd:TIGR01612 1443 KNADENNEN---VLLLFKNIEMADNKSQHILKIKKDNATNDHdfnineLKEHIDKSKGCKDEADKNAKAIEKNKELFEQY 1519
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2240 ANEALRLRLQAEEVAHKKTLAQeeaekQKEDAEREArkrakteesalrqKELaeDELEKQRKLADATAQQKFSA-EQELI 2318
Cdd:TIGR01612 1520 KKDVTELLNKYSALAIKNKFAK-----TKKDSEIII-------------KEI--KDAHKKFILEAEKSEQKIKEiKKEKF 1579
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2319 RLKAETENSeqqrllleeelfrlkNEVNEA---IQKRKE-MEEELAKVRaemEILLQSKSRAEEESRSNTEKSKQMLEVE 2394
Cdd:TIGR01612 1580 RIEDDAAKN---------------DKSNKAaidIQLSLEnFENKFLKIS---DIKKKINDCLKETESIEKKISSFSIDSQ 1641
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2395 ASKLRELAEEAAKLRAVSEEAKRQRQIAEDeaarQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAE 2464
Cdd:TIGR01612 1642 DTELKENGDNLNSLQEFLESLKDQKKNIED----KKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKE 1707
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
2351-2630 |
1.64e-03 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 45.31 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2351 KRKEMEEELAKVRAEM--EILLQSKSRAEEesrsnteksKQMLEVEASKLRE-----LAEEAAKLRAVSEEAKRQRQIAE 2423
Cdd:pfam04147 152 DDEEEEPERKKSKKEVmeEVIAKSKLHKYE---------RQKAKEEDEELREeldkeLKDLRSLLSGSKRPKPEQAKKPE 222
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2424 DEAARQRAEAE--RILKE----KLAAINDatRLKTEAEIALKEKE----AENERLRRL-----AEDEAYQRKLLEEQAtq 2488
Cdd:pfam04147 223 EKPDRKKPDDDydKLVRElafdKRAKPSD--RTKTEEELAEEEKErlekLEEERLRRMrgeedEEEEDGKKKKKHKSA-- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2489 hkQDIEEkiillkkssDNELERQKNIVEDTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAE 2568
Cdd:pfam04147 299 --DDLDD---------DFVVDDDDDDEEFGLGKGIKERPTATELGDEDEDDFIIDDDLVESESDLELDEEEEDEEEEDDE 367
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2569 QEAEkqrqlalEEEQRRKEAEEKVRKILADEKEaarqrkaaLEEVERLKAKAEEAKRQKELA 2630
Cdd:pfam04147 368 DEDE-------EEEEDDDDLSDLESEEDEEDDE--------FEEEKKKKKKKDEEGAKEELP 414
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2128-2636 |
1.65e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 45.62 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2128 EAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEK-----ERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ----LELSL 2198
Cdd:COG3899 723 EALRYLERALELLPPDPEEEYRLALLLELAEALYlagrfEEAEALLERALAARALAALAALRHGNPPASARayanLGLLL 802
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2199 KQEHITVTHLQEEAERLKKLHDEAEKAREEAEK--ELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREAR 2276
Cdd:COG3899 803 LGDYEEAYEFGELALALAERLGDRRLEARALFNlgFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAA 882
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2277 KRAKTEESALRQKELAEDELEKQRKLADATAqqkfsAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEAIQKRKEME 2356
Cdd:COG3899 883 AAALAAAAAAAARLLAAAAAALAAAAAAAAL-----AAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAA 957
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2357 EELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERI 2436
Cdd:COG3899 958 LALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALL 1037
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2437 LKEKLAAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVE 2516
Cdd:COG3899 1038 AAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALA 1117
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2517 DTLRQRRIIEEEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKIL 2596
Cdd:COG3899 1118 AALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLA 1197
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1835643837 2597 ADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAER 2636
Cdd:COG3899 1198 ALLALAARLAALLALALLALEAAALLLLLLLAALALAAAL 1237
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
5271-5361 |
1.66e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 41.54 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 5271 LEMILSWVSDMEDLISNQKPPSSEVKVvKAQLQEQKLLQRLLEERRPRLERV------LQDMQTSESGEENAKHGSLQAR 5344
Cdd:pfam00435 10 ADDLESWIEEKEALLSSEDYGKDLESV-QALLKKHKALEAELAAHQDRVEALnelaekLIDEGHYASEEIQERLEELNER 88
|
90
....*....|....*..
gi 1835643837 5345 WEALIQQADTRNRRLEQ 5361
Cdd:pfam00435 89 WEQLLELAAERKQKLEE 105
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2088-2317 |
1.70e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2088 EQQKKAAQEEAERLRKQVKDETQKKREAEEELKR--------KVQAEKEAAREKQRAVED-LEKFRSQAEEAERRMKQAE 2158
Cdd:COG3206 167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEfrqknglvDLSEEAKLLLQQLSELESqLAEARAELAEAEARLAALR 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2159 VEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKlhdeaekareeaekelekwhQ 2238
Cdd:COG3206 247 AQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA--------------------Q 306
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2239 KANEALRLRLQAEevahkktlAQEEAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQEL 2317
Cdd:COG3206 307 LQQEAQRILASLE--------AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEA 377
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1939-2158 |
1.71e-03 |
|
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.
Pssm-ID: 310534 [Multi-domain] Cd Length: 258 Bit Score: 44.33 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1939 ITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQ 2018
Cdd:pfam06008 17 INYNLENLTKQLQEYLSPENAHKIQIEILEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLID 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2019 TIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQletmqKHKANAEDELQELRARAEKAEQQKKAAQEEA 2098
Cdd:pfam06008 97 NIKEINEKVATLGENDFALPSSDLSRMLAEAQRMLGEIRSRDFG-----TQLQNAEAELKAAQDLLSRIQTWFQSPQEEN 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2099 ERLRKQVKDE----TQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAE 2158
Cdd:pfam06008 172 KALANALRDSlaeyEAKLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLE 235
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2702-2931 |
1.75e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2702 AEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEA--EKLRKEAELEAAKrahaEQAALKQKQLAD--EEMDKHKKFAE 2777
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELneEYNELQAELEALQ----AEIDKLQAEIAEaeAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2778 KTLRQKSQVEQELTKVKLQLEETD-----HQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEE 2852
Cdd:COG3883 90 ERARALYRSGGSVSYLDVLLGSESfsdflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 2853 nKMLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEA 2931
Cdd:COG3883 170 -KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2793-3037 |
1.76e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2793 VKLQLEETDHQKTLLDEELQRLKEEVTDAmrqkaqvEEEL--FKVKIQMEELiklklriEEENKMLIMKDKDSTQKLlve 2870
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEA-------EAALeeFRQKNGLVDL-------SEEAKLLLQQLSELESQL--- 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2871 eaekmrqVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEA-SRLKAEAEMLQKQKELAQEQARKFQ 2949
Cdd:COG3206 229 -------AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELeAELAELSARYTPNHPDVIALRAQIA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2950 EDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEE---DASKFKKKAEEIGNKLHQTELAT 3026
Cdd:COG3206 302 ALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlerEVEVARELYESLLQRLEEARLAE 381
|
250
....*....|.
gi 1835643837 3027 KERMAVVQTLE 3037
Cdd:COG3206 382 ALTVGNVRVID 392
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
2556-2629 |
1.76e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 45.25 E-value: 1.76e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2556 IAEETQRSKEK-AEQEAEKQRQlalEEEQRRKEAEekvrkiladekeaarqrKAAlEEVERLKAKAEEAKRQKEL 2629
Cdd:PLN02316 250 LLEEKRRELEKlAKEEAERERQ---AEEQRRREEE-----------------KAA-MEADRAQAKAEVEKRREKL 303
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1939-2067 |
1.86e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 44.21 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1939 ITETLRRlNDEEKAAEKLK---EEERRRLAEVEAQLAKQtqlaeahaKAKAQAEKEAEELQRRMQEEVSKREvvavdAEQ 2015
Cdd:cd03406 160 IPEAIRR-NYEAMEAEKTKlliAEQHQKVVEKEAETERK--------RAVIEAEKDAEVAKIQMQQKIMEKE-----AEK 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2016 QKQTIQQELQQLRQNS--DMEIKSKAKQIEEveyNRRKIEEEIhivrLQLETMQ 2067
Cdd:cd03406 226 KISEIEDEMHLAREKAraDAEYYRALREAEA---NKLKLTPEY----LELKKYQ 272
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2080-2178 |
2.01e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.04 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2080 LRARAEKAEQQKKAA---QEEAERLRKQVKDETQK-KREAEEELKrkvQAEKEAAREKQRAVEDLEkfrsqaEEAERRMK 2155
Cdd:cd06503 28 LDEREEKIAESLEEAekaKEEAEELLAEYEEKLAEaRAEAQEIIE---EARKEAEKIKEEILAEAK------EEAERILE 98
|
90 100
....*....|....*....|....*...
gi 1835643837 2156 QAEVEKERQIKVA-----QEVAQQSAAA 2178
Cdd:cd06503 99 QAKAEIEQEKEKAlaelrKEVADLAVEA 126
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2371-2637 |
2.21e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2371 QSKS--RAEEESRSNTEKSKQmlEVEASKLRELAEEAAKLrAVSEEAKRQRQiAEDEAARQRAEAEriLKEKLAAINDAT 2448
Cdd:PRK05035 433 QAKAeiRAIEQEKKKAEEAKA--RFEARQARLEREKAARE-ARHKKAAEARA-AKDKDAVAAALAR--VKAKKAAATQPI 506
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2449 RLKTEAEIALKEKEAEnERLRRLAEDEAYQRKLLEEQATQHKQDIEEKI--ILLKKSSDNELERQKNIVEDTLRQRRIIE 2526
Cdd:PRK05035 507 VIKAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDPKKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2527 EEIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAeekvrkiLADEKEAARQR 2606
Cdd:PRK05035 586 IARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-------VAAAIARAKAR 658
|
250 260 270
....*....|....*....|....*....|....*..
gi 1835643837 2607 KAALEEVERLKAKAEEAKRQK------ELAEKEAERQ 2637
Cdd:PRK05035 659 KAAQQQANAEPEEAEDPKKAAvaaaiaRAKAKKAAQQ 695
|
|
| NtpE |
COG1390 |
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal ... |
2560-2651 |
2.23e-03 |
|
Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 [Energy production and conversion]; Archaeal/vacuolar-type H+-ATPase subunit E/Vma4 is part of the Pathway/BioSystem: A/V-type ATP synthase
Pssm-ID: 441000 [Multi-domain] Cd Length: 196 Bit Score: 43.01 E-value: 2.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2560 TQRSKEKAEQEAEKQRQLALEE-EQRRKEAEEKVRKILADEKEAARQRkaALEEVERLKAKAEEAKRQKELAEKeaERQI 2638
Cdd:COG1390 8 IEEILEEAEAEAEEILEEAEEEaEKILEEAEEEAEEIKEEILEKAERE--AEREKRRIISSAELEARKELLEAK--EELI 83
|
90
....*....|...
gi 1835643837 2639 QLAQEAALKKIDA 2651
Cdd:COG1390 84 EEVFEEALEKLKN 96
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
2675-2779 |
2.31e-03 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 44.06 E-value: 2.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2675 QSILDKLKeeAERAKRAAEdadfarTRAEQEAAlsrQQVEEAERLKQRAEEEAQAKAQAQdeaeKLRKEAELEAAKR-AH 2753
Cdd:COG0330 171 DAMEDRMK--AEREREAAI------LEAEGYRE---AAIIRAEGEAQRAIIEAEAYREAQ----ILRAEGEAEAFRIvAE 235
|
90 100
....*....|....*....|....*.
gi 1835643837 2754 AEQAAlkQKQLADEEMDKHKKFAEKT 2779
Cdd:COG0330 236 AYSAA--PFVLFYRSLEALEEVLSPN 259
|
|
| MDN1 |
COG5271 |
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal ... |
2269-2821 |
2.41e-03 |
|
Midasin, AAA ATPase with vWA domain, involved in ribosome maturation [Translation, ribosomal structure and biogenesis];
Pssm-ID: 444083 [Multi-domain] Cd Length: 1028 Bit Score: 45.01 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2269 EDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETENSEQQRLLLEEELFRLKNEVNEA 2348
Cdd:COG5271 321 DTEIATADELAAADDEDDDDSAAEDAAEEAATAEDSAAEDTQDAEDEAAGEAADESEGADTDAAADEADAAADDSADDEE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2349 IQKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLR---ELAEEAAKLRAVSEEAKRQRQIAEDE 2425
Cdd:COG5271 401 ASADGGTSPTSDTDEEEEEADEDASAGETEDESTDVTSAEDDIATDEEADSladEEEEAEAELDTEEDTESAEEDADGDE 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2426 AARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENErlrrlaEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSD 2505
Cdd:COG5271 481 ATDEDDASDDGDEEEAEEDAEAEADSDELTAEETSADDGAD------TDAAADPEDSDEDALEDETEGEENAPGSDQDAD 554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2506 NELERQKNIVEDTLRQRRIIEEEIRI--------LKVNFEKASVGKSDLELELNQLKN--IAEETQRSKEKAEQEAEKQR 2575
Cdd:COG5271 555 ETDEPEATAEEDEPDEAEAETEDATEnadadeteESADESEEAEASEDEAAEEEEADDdeADADADGAADEEETEEEAAE 634
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2576 -QLALEEEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEK 2654
Cdd:COG5271 635 dEAAEPETDASEAADEDADAETEAEASADESEEEAEDESETSSEDAEEDADAAAAEASDDEEETEEADEDAETASEEADA 714
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2655 AHTAIVQQKEQEMLQTRKQEQS-----------ILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAErlkqrA 2723
Cdd:COG5271 715 EEADTEADGTAEEAEEAAEEAEsadeeaaslpdEADAEEEAEEAEEAEEDDADGLEEALEEEKADAEEAATDEE-----A 789
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2724 EEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQ 2803
Cdd:COG5271 790 EAAAEEKEKVADEDQDTDEDALLDEAEADEEEDLDGEDEETADEALEDIEAGIAEDDEEDDDAAAAKDVDADLDLDADLA 869
|
570
....*....|....*...
gi 1835643837 2804 KTLLDEELQRLKEEVTDA 2821
Cdd:COG5271 870 ADEHEAEEAQEAETDADA 887
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2551-2762 |
2.42e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2551 NQLK----NIAEetqrsKEKAEQEAEKQR-----QL------------ALEEEQRRKEAEEKVRKILADEKEAARQRKAA 2609
Cdd:PRK11637 47 DQLKsiqqDIAA-----KEKSVRQQQQQRasllaQLkkqeeaisqasrKLRETQNTLNQLNKQIDELNASIAKLEQQQAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2610 LEEVerLKAKAEEAKRQKE-------LAEKEAER-QIQLA-----QEAALKKIDAEEKAHTAIVQQKeQEMLQTRKQEQS 2676
Cdd:PRK11637 122 QERL--LAAQLDAAFRQGEhtglqliLSGEESQRgERILAyfgylNQARQETIAELKQTREELAAQK-AELEEKQSQQKT 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2677 ILDKLKEEaeraKRAAEDADFAR--TRAEQEAALSRQQVEEAE------RLKQR-AEEEAQAKAQAQDEAeklrkeaelE 2747
Cdd:PRK11637 199 LLYEQQAQ----QQKLEQARNERkkTLTGLESSLQKDQQQLSElranesRLRDSiARAEREAKARAEREA---------R 265
|
250
....*....|....*
gi 1835643837 2748 AAKRAHAEQAALKQK 2762
Cdd:PRK11637 266 EAARVRDKQKQAKRK 280
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2785-2967 |
2.42e-03 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 44.11 E-value: 2.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2785 QVEQELTKVKLQLEETDHQK--TLLDEELQRLKEEVTDA-----------MRQKAQVEEELFKVK---IQMEELIK--LK 2846
Cdd:cd16269 98 QLEEKKEEFCKQNEEASSKRcqALLQELSAPLEEKISQGsysvpggyqlyLEDREKLVEKYRQVPrkgVKAEEVLQefLQ 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2847 LRIEEENKMLIMkDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEddlaNQRALAE--KMLKEKMQaiQEA 2924
Cdd:cd16269 178 SKEAEAEAILQA-DQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLED----QERSYEEhlRQLKEKME--EER 250
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1835643837 2925 SRLKAEAEMLQKQKElaQEQARKFQEDKEQIEQQLAKETEGFQ 2967
Cdd:cd16269 251 ENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2552-2795 |
2.52e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 44.47 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2552 QLKNIAEETQRSKEKAEQEAEKQR-QLALEEEQRRKEAEekvrkiladeKEAARQRKAALeeverLKAKaEEAKRQKELA 2630
Cdd:PRK00106 25 KMKSAKEAAELTLLNAEQEAVNLRgKAERDAEHIKKTAK----------RESKALKKELL-----LEAK-EEARKYREEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2631 EKE--AERQiqlaqeaALKKIDAEEKAHTAIVQQKEQEMLQTRK----QEQSILDKLKEEAERAkraaedadfartraEQ 2704
Cdd:PRK00106 89 EQEfkSERQ-------ELKQIESRLTERATSLDRKDENLSSKEKtlesKEQSLTDKSKHIDERE--------------EQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2705 EAALSRQQVEEAERLKQRAEEEAQAKAQAQDEaEKLRKEAeleAAKRAHAEQaalkqkqladEEMDKHKKFAEKTLRQKS 2784
Cdd:PRK00106 148 VEKLEEQKKAELERVAALSQAEAREIILAETE-NKLTHEI---ATRIREAER----------EVKDRSDKMAKDLLAQAM 213
|
250
....*....|....*...
gi 1835643837 2785 Q-------VEQELTKVKL 2795
Cdd:PRK00106 214 QrlageyvTEQTITTVHL 231
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2957-3123 |
2.59e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2957 QQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTElATKERMAVVQTL 3036
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVR-NNKEYEALQKEI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3037 EIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEqLRQETQVLQTTflsEKQLLLEREKYIEEEKA 3116
Cdd:COG1579 99 ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAE-LDEELAELEAE---LEELEAEREELAAKIPP 174
|
....*..
gi 1835643837 3117 KLENLYE 3123
Cdd:COG1579 175 ELLALYE 181
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1944-2159 |
2.62e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.47 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1944 RRLNDEEKAAEKLKE-------------EERRRLAEVEAQLAKQ-----TQLAEAHAKAKAQAEKEAEE---------LQ 1996
Cdd:pfam02029 74 RRQKRLQEALERQKEfdptiadekesvaERKENNEEEENSSWEKeekrdSRLGRYKEEETEIREKEYQEnkwstevrqAE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1997 RRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKI---EEEIHIVRLQLETMQKHKAN- 2072
Cdd:pfam02029 154 EEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSqngEEEVTKLKVTTKRRQGGLSQs 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2073 ------------AEDELQELR-ARAEKAEQ--------QKKAAQEEAERLRKqvKDETQKKREAEEELKRKVQAEKEAAR 2131
Cdd:pfam02029 234 qereeeaevfleAEQKLEELRrRRQEKESEefeklrqkQQEAELELEELKKK--REERRKLLEEEEQRRKQEEAERKLRE 311
|
250 260 270
....*....|....*....|....*....|
gi 1835643837 2132 E--KQRAVEDLEKFRsqAEEAERRMKQAEV 2159
Cdd:pfam02029 312 EeeKRRMKEEIERRR--AEAAEKRQKLPED 339
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
651-709 |
2.66e-03 |
|
first calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409070 Cd Length: 106 Bit Score: 40.72 E-value: 2.66e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 651 KKTFTKWVNKHLIKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREK----GRMRFHKLQNV 709
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVV 65
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1963-2133 |
2.69e-03 |
|
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.
Pssm-ID: 460211 [Multi-domain] Cd Length: 175 Bit Score: 42.64 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1963 RLAEVEAQLAK-QTQLAEAHAKAKAQAEKEAEELQRRMQEEVSK-REVVAVDAEQQKQTIQQELQQLRQnsdmEIKSKAK 2040
Cdd:pfam01442 5 SLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQKDLEEvRAKLEPYLEELQAKLGQNVEELRQ----RLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2041 QIEevEYNRRKIEEeihiVRLQLET-MQKHKANAEDELQELRAR-AEKAEQQKKAAQEEAERLRKQVKDETQ----KKRE 2114
Cdd:pfam01442 81 ELR--KRLNADAEE----LQEKLAPyGEELRERLEQNVDALRARlAPYAEELRQKLAERLEELKESLAPYAEevqaQLSQ 154
|
170
....*....|....*....
gi 1835643837 2115 AEEELKRKVQAEKEAAREK 2133
Cdd:pfam01442 155 RLQELREKLEPQAEDLREK 173
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2719-2872 |
2.69e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2719 LKQRAEEEAQAKAQ-AQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQL 2797
Cdd:pfam05262 203 LKERESQEDAKRAQqLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKRE 282
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 2798 EETDHQKT-LLDEELQRLKEEVTDAMRQKAQVEEelfKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEA 2872
Cdd:pfam05262 283 IEKAQIEIkKNDEEALKAKDHKAFDLKQESKASE---KEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2870-3006 |
2.74e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.22 E-value: 2.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2870 EEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRalaekmlKEKMQAIQEASRL-------------------KAE 2930
Cdd:pfam05262 210 EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQR-------DEVRQKQQEAKNLpkpadtsspkedkqvaenqKRE 282
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2931 AEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGF--QKSLEAErRQQLEITAEAERLKLQVlemsRAQAKAEEDAS 3006
Cdd:pfam05262 283 IEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEaeDKELEAQ-KKREPVAEDLQKTKPQV----EAQPTSLNEDA 355
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2256-2476 |
2.75e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.38 E-value: 2.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2256 KKTLAQEEAEKQKEDAEREArkrakteESALRQKELAedelekqrkladataqqkfsAEQELIRLKAETENseqqrllle 2335
Cdd:PRK12704 32 KIKEAEEEAKRILEEAKKEA-------EAIKKEALLE--------------------AKEEIHKLRNEFEK--------- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2336 eelfrlknEVNEAIQKRKEMEEELakvraemeilLQSKSRAEEESRSNtEKSKQMLEVEASKLRELAEEAAKLRAVSEEA 2415
Cdd:PRK12704 76 --------ELRERRNELQKLEKRL----------LQKEENLDRKLELL-EKREEELEKKEKELEQKQQELEKKEEELEEL 136
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2416 -KRQRQIAEDEAARQRAEAERILKEKLaaindatRLKTEAEIALKEKEAENErlrrlAEDEA 2476
Cdd:PRK12704 137 iEEQLQELERISGLTAEEAKEILLEKV-------EEEARHEAAVLIKEIEEE-----AKEEA 186
|
|
| COG4223 |
COG4223 |
Uncharacterized conserved protein [Function unknown]; |
2546-2757 |
2.83e-03 |
|
Uncharacterized conserved protein [Function unknown];
Pssm-ID: 443367 [Multi-domain] Cd Length: 259 Bit Score: 43.50 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2546 LELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRK------ILADEKEAARQR----KAALEEVER 2615
Cdd:COG4223 39 LEARLAALRAALAAAREAVAAAAAAALEARLAALEAKAAAPEAEAAAAAraaalaLAAAALRAAVERgqpfAAELAALEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2616 LKAKAEEAKRQKELAEKEAERQIQLAQE---AALKKIDAEEKAHTaivqqkeqemlqtrkqEQSILDKLKEEAER----- 2687
Cdd:COG4223 119 LAPDAPALAALAAFAATGVPTLAALRAEfpaAARAALAAARAPEA----------------DASWLDRLLAFARSlvtvr 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2688 --AKRAAEDADFARTRAEqeAALSRQQVEEAerlkqRAEEEA---QAKAQAQDEAEKLRKEAELEAAKRAHAEQA 2757
Cdd:COG4223 183 rvGPVEGDDPDAILARAE--AALAAGDLAGA-----LAELEAlpeAAQAAAAPWIAKAEARLAADAALQALAAQA 250
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2442-3009 |
2.88e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 44.68 E-value: 2.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2442 AAINDATRLKTEAEIALKEKEAENERLRRLAEDEAYQRK--LLEEQATQHKQDiEEKIILLKKssDNELERQKNIVEDTL 2519
Cdd:COG5022 805 LLGSRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKaeVLIQKFGRSLKA-KKRFSLLKK--ETIYLQSAQRVELAE 881
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2520 RQRRIIEEEIRIL-----------KVNFEKASVGKSDLELELN-QLKNIAEETQ-----RSKEKAEQEAEKQRQLA--LE 2580
Cdd:COG5022 882 RQLQELKIDVKSIsslklvnleleSEIIELKKSLSSDLIENLEfKTELIARLKKllnniDLEEGPSIEYVKLPELNklHE 961
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2581 EEQRRKEAEEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEA----ERQIQLAQEAALKKIDAEEKAH 2656
Cdd:COG5022 962 VESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTkqlkELPVEVAELQSASKIISSESTE 1041
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2657 TAIVQ----------------QKEQEMLQTRKQEQSILDKLKEEAERAKR-----AAEDADFARTRAEQEAALSRQQVEE 2715
Cdd:COG5022 1042 LSILKplqklkgllllennqlQARYKALKLRRENSLLDDKQLYQLESTENllktiNVKDLEVTNRNLVKPANVLQFIVAQ 1121
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2716 AERLKQRAEEEA---QAKAQAQDEAEKLRK-EAELEAAKRAHAEQAALKQKQLAdeEMDKHKKFAEKTLRQK---SQVEQ 2788
Cdd:COG5022 1122 MIKLNLLQEISKflsQLVNTLEPVFQKLSVlQLELDGLFWEANLEALPSPPPFA--ALSEKRLYQSALYDEKsklSSSEV 1199
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2789 ELTKVKLQLEETDHQKTL-LDEELQRLKEEVTDA----MRQKAQVEEELFKVKIQ---MEELIKLKLRI-------EEEN 2853
Cdd:COG5022 1200 NDLKNELIALFSKIFSGWpRGDKLKKLISEGWVPteysTSLKGFNNLNKKFDTPAsmsNEKLLSLLNSIdnllssyKLEE 1279
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2854 KMLIMKDKDSTQKLLVE------------EAEKMRQVAEEAARLS---------------IEAQEAARMRKLAEDDLaNQ 2906
Cdd:COG5022 1280 EVLPATINSLLQYINVGlfnalrtkasslRWKSATEVNYNSEELDdwcrefeisdvdeelEELIQAVKVLQLLKDDL-NK 1358
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2907 RALAEKMLKEKMQAiqEASRLKAEAEMLQKQKELAQEQARKFQEDKeqIEQQLAKETEGFQKsLEAERRQQLEITAEAER 2986
Cdd:COG5022 1359 LDELLDACYSLNPA--EIQNLKSRYDPADKENNLPKEILKKIEALL--IKQELQLSLEGKDE-TEVHLSEIFSEEKSLIS 1433
|
650 660
....*....|....*....|...
gi 1835643837 2987 LKLQVLEMSRAQAKAEEDASKFK 3009
Cdd:COG5022 1434 LDRNSIYKEEVLSSLSALLTKEK 1456
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
2568-2650 |
2.89e-03 |
|
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex
Pssm-ID: 339878 [Multi-domain] Cd Length: 104 Bit Score: 40.88 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2568 EQEAEKQRQLALEEEQRRKEAEEKVRkilADEKEAARQRKAALEEVERLKAK-----AEEAKRQKELAEKEAERQIQLAQ 2642
Cdd:pfam16999 8 SELAEREAALDQQIEAARKEAEREVE---AAEAEAARILREAEAKAKALQAEyrqelAAETARIREEARARAEAEAQAVR 84
|
....*...
gi 1835643837 2643 EAALKKID 2650
Cdd:pfam16999 85 TRAEGRLQ 92
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2120-2466 |
2.90e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 2.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2120 KRKVQAEKEAA-REKQRAVEDLEkfrsqaeeAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTaqlelsl 2198
Cdd:PRK07735 5 KDLEDLKKEAArRAKEEARKRLV--------AKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKA------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2199 kqehitvthlqeeaerlkklhdeaekareeaekelekwhqkanEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKR 2278
Cdd:PRK07735 70 -------------------------------------------KAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAA 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2279 AKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAEtenseqqrllleeelfrlknevnEAIQKRKEMEEE 2358
Cdd:PRK07735 107 ALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTE-----------------------EVTEEEEETDKE 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2359 LAKVRAEMEILLQSKSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVS---EEAKRQRQIAEDEAARQRAEAER 2435
Cdd:PRK07735 164 KAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAAlakQKASQGNGDSGDEDAKAKAIAAA 243
|
330 340 350
....*....|....*....|....*....|.
gi 1835643837 2436 ilKEKLAAindATRLKTEAEIALKEKEAENE 2466
Cdd:PRK07735 244 --KAKAAA---AARAKTKGAEGKKEEEPKQE 269
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1954-2164 |
2.96e-03 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 44.29 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1954 EKLKEEERRRLAEVEAQLAKQTqlaEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNsDM 2033
Cdd:pfam19220 201 ETQLDATRARLRALEGQLAAEQ---AERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDR-DE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2034 EIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAE---KAEQQKKAAQEEAErlrkqvkDETQ 2110
Cdd:pfam19220 277 AIRAAERRLKEASIERDTLERRLAGLEADLERRTQQFQEMQRARAELEERAEmltKALAAKDAALERAE-------ERIA 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2111 KKREAEEELKRKVQAEKEAAREKQRA-VEDLekfrsQAEEAERRMKQAEVEKERQ 2164
Cdd:pfam19220 350 SLSDRIAELTKRFEVERAALEQANRRlKEEL-----QRERAERALAQGALEIARE 399
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2795-2989 |
2.97e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 43.37 E-value: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2795 LQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEenkmlimkDKDSTQKLLVEEAEK 2874
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLEL--------EIEEVEARIKKYEEQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2875 MRQV--AEEAARLSIEAQEAARMRKLAEDDlanqralaekmLKEKMQAIQEASRL--KAEAEMLQKQKELAQEQARkFQE 2950
Cdd:COG1579 82 LGNVrnNKEYEALQKEIESLKRRISDLEDE-----------ILELMERIEELEEElaELEAELAELEAELEEKKAE-LDE 149
|
170 180 190
....*....|....*....|....*....|....*....
gi 1835643837 2951 DKEQIEQQLAKETegfqksleaERRQQLEITAEAERLKL 2989
Cdd:COG1579 150 ELAELEAELEELE---------AEREELAAKIPPELLAL 179
|
|
| CC149 |
pfam09789 |
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as ... |
2976-3213 |
3.07e-03 |
|
Coiled-coil domain-containing protein 149-A; Members of this family have been annotated as being coiled-coil domain-containing protein 149, however they currently have no known function.
Pssm-ID: 462902 [Multi-domain] Cd Length: 314 Bit Score: 43.86 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2976 QQLEITAEAerlkLQVLEMSRAQAKAEEDasKFKKKAEeignKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRRAIA 3055
Cdd:pfam09789 2 RKLQSKVEA----LLILSKELEKCRQERD--QYKLMAE----QLQERYQGLKKQLRELKAGNNDFKPDDREQVNLIQLLR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3056 ELEHEKEKLKREAELLQknsQKMQVAQQE-QLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLyedevRKAQKLKQ 3134
Cdd:pfam09789 72 DSREQNKCLRLEVEELR---QKLNEAQGDiKLLREQIARQRLGGPDEGSISTRHFPLHEREELVKQL-----EKLRKKCQ 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3135 EQEHQMKHLEEEKDQLKVSMDdAMKkqkeaeENVRRKQDELQQL---DKKRQEQEKLLADENRKLREKLEQMEEEHRIAL 3211
Cdd:pfam09789 144 QLERDLQSVLDEKEELETERD-AYK------CKAHRLNHELNYIlggDESRIVDIDALIMENRYLQERLKQLEEEKELAK 216
|
..
gi 1835643837 3212 AQ 3213
Cdd:pfam09789 217 QT 218
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2920-3216 |
3.11e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 44.09 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2920 AIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLE----AERRQQLEITAEAERLKLQVLEM- 2994
Cdd:pfam02029 15 AREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDrtakREERRQKRLQEALERQKEFDPTIa 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2995 -------SRAQAKAEEDASKFKKKaEEIGNKLHQTELATKErmavVQTLEIQRQqsgKEAEELRRAIAELEHEKEKLKRE 3067
Cdd:pfam02029 95 dekesvaERKENNEEEENSSWEKE-EKRDSRLGRYKEEETE----IREKEYQEN---KWSTEVRQAEEEGEEEEDKSEEA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3068 AELLQKNSQKMQVaQQEQLRQETQVLqttflSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEK 3147
Cdd:pfam02029 167 EEVPTENFAKEEV-KDEKIKKEKKVK-----YESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3148 dqlkvsmddamKKQKEAE---ENVRRKQD-----ELQQLDKKRQEQEKLLA------DENRKLREKLEQMEEEHRiALAQ 3213
Cdd:pfam02029 241 -----------EVFLEAEqklEELRRRRQekeseEFEKLRQKQQEAELELEelkkkrEERRKLLEEEEQRRKQEE-AERK 308
|
...
gi 1835643837 3214 TRE 3216
Cdd:pfam02029 309 LRE 311
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2752-3021 |
3.15e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 43.43 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2752 AHAEQAALKQKQLA--DEEMDKHKKFAEKTLRQKSQV----EQELTKV--KLQLEETDHQ-----KTLLDEELQRLKEEV 2818
Cdd:pfam02841 37 AQIENSAAVQKAIAhyEQQMAQKVKLPTETLQELLDLhrdcEKEAIAVfmKRSFKDENQEfqkelVELLEAKKDDFLKQN 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2819 TDAMRQKAQVE-EELFKvkiQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQvAEEAARLSIEAQEAarmrk 2897
Cdd:pfam02841 117 EEASSKYCSALlQDLSE---PLEEKISQGTFSKPGGYKLFLEERDKLEAKYNQVPRKGVK-AEEVLQEFLQSKEA----- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2898 LAEDDLANQRALAEKmlkEKmqAIQEAsrlKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQ 2977
Cdd:pfam02841 188 VEEAILQTDQALTAK---EK--AIEAE---RAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEHVKQLIEKMEAEREQL 259
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1835643837 2978 LeitAEAERLKLQVLEMSRAQAKAEedaskFKKKAEEIGNKLHQ 3021
Cdd:pfam02841 260 L---AEQERMLEHKLQEQEELLKEG-----FKTEAESLQKEIQD 295
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
3062-3247 |
3.26e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.12 E-value: 3.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3062 EKLKREAELLQKnsqkmQVAQQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQmK 3141
Cdd:pfam07888 38 ECLQERAELLQA-----QEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS-E 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3142 HLEEEKDQLKVSMDDAMKKQKEAEENVR----RKQDELQQLDKKRQEQEKLLA------DENRKLREKLEQMEEEHRIAL 3211
Cdd:pfam07888 112 ELSEEKDALLAQRAAHEARIRELEEDIKtltqRVLERETELERMKERAKKAGAqrkeeeAERKQLQAKLQQTEEELRSLS 191
|
170 180 190
....*....|....*....|....*....|....*....
gi 1835643837 3212 AQTREMRT---QTDDLAGNLPLTPTVVTQTKAMPNGRDA 3247
Cdd:pfam07888 192 KEFQELRNslaQRDTQVLQLQDTITTLTQKLTTAHRKEA 230
|
|
| PTZ00440 |
PTZ00440 |
reticulocyte binding protein 2-like protein; Provisional |
2770-3224 |
3.32e-03 |
|
reticulocyte binding protein 2-like protein; Provisional
Pssm-ID: 240419 [Multi-domain] Cd Length: 2722 Bit Score: 44.82 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2770 DKHKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKT---LLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLK 2846
Cdd:PTZ00440 1035 EKGKEIEEKVDQYISLLEKMKTKLSSFHFNIDIKKYknpKIKEEIKLLEEKVEALLKKIDENKNKLIEIKNKSHEHVVNA 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2847 LRIEEENKMLIMKDKDSTQKLLvEEAEKMRQVAEEAARLSIEAQEAARMRKLAEddlanqRALAEKMLKEKMQAIQEASR 2926
Cdd:PTZ00440 1115 DKEKNKQTEHYNKKKKSLEKIY-KQMEKTLKELENMNLEDITLNEVNEIEIEYE------RILIDHIVEQINNEAKKSKT 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2927 LKAEAEMLQKQKELAQEQArkfqeDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLklqvlemsraqaKAEEDAS 3006
Cdd:PTZ00440 1188 IMEEIESYKKDIDQVKKNM-----SKERNDHLTTFEYNAYYDKATASYENIEELTTEAKGL------------KGEANRS 1250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3007 KFKKKAEEIGNKLHQtelatkermavvqtleiQRQQSGKEAEELRRAIAELEHEKE-----KLKREAELLQKNSQKmqva 3081
Cdd:PTZ00440 1251 TNVDELKEIKLQVFS-----------------YLQQVIKENNKMENALHEIKNMYEflisiDSEKILKEILNSTKK---- 1309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3082 QQEQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLENL----YEDEVRKAQKLKQEqehqmkhLEEEKDQLKVSMDDA 3157
Cdd:PTZ00440 1310 AEEFSNDAKKELEKTDNLIKQVEAKIEQAKEHKNKIYGSLedkqIDDEIKKIEQIKEE-------ISNKRKEINKYLSNI 1382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 3158 mKKQKEAEE----NVRRKQDELQQLDKKRQEQEKLLADEN-RKLREKLEQMEEEHRIALAQTREMRTQTDDL 3224
Cdd:PTZ00440 1383 -KSNKEKCDlhvrNASRGKDKIDFLNKHEAIEPSNSKEVNiIKITDNINKCKQYSNEAMETENKADENNDSI 1453
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2554-2651 |
3.49e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 41.69 E-value: 3.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2554 KNIAEETQRSkEKAEQEAEKqrqlaleeeqrrkeAEEKVRKILADEKEAARQ-----RKAALEEVERLKAKA-EEAKRQK 2627
Cdd:PRK05759 38 KKIADGLAAA-ERAKKELEL--------------AQAKYEAQLAEARAEAAEiieqaKKRAAQIIEEAKAEAeAEAARIK 102
|
90 100
....*....|....*....|....
gi 1835643837 2628 ELAEKEAERQIQLAQEAALKKIDA 2651
Cdd:PRK05759 103 AQAQAEIEQERKRAREELRKQVAD 126
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3671-3705 |
3.53e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 3.53e-03
10 20 30
....*....|....*....|....*....|....*
gi 1835643837 3671 LLEAQAGTGYIIDPVKNEKFPVEEAVKASVVGPEF 3705
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
645-753 |
3.61e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.13 E-value: 3.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 645 ERDRVQKKTFTKWVNKhlIKAQRHVSDLYEDLRDGHNLISLLEVL---------SGDNLPREKGRMRfhKLQNVQIALDY 715
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1835643837 716 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 753
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2919-3056 |
3.72e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 3.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2919 QAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQqLAKETEGFQKSLEaerrQQLEitaeaerlKLQvlemSRAQ 2998
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEG-LAAELEEKQQELE----AQLE--------QLQ----EKAA 208
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2999 AKAEEDASKFKKKAEEIGNKLHQTELATKermavvQTLEIQRQQSGKEA--EELR------------RAIAE 3056
Cdd:PRK11448 209 ETSQERKQKRKEITDQAAKRLELSEEETR------ILIDQQLRKAGWEAdsKTLRfskgarpekgrnLAIAE 274
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2661-2832 |
3.81e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 3.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2661 QQKEQEMLQTRKQEQSI---LDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEA 2737
Cdd:COG3883 19 QAKQKELSELQAELEAAqaeLDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2738 EKLRKEAEL--------EAAKRAHA-------EQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEEtdh 2802
Cdd:COG3883 99 GGSVSYLDVllgsesfsDFLDRLSAlskiadaDADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA--- 175
|
170 180 190
....*....|....*....|....*....|
gi 1835643837 2803 QKTLLDEELQRLKEEVTDAMRQKAQVEEEL 2832
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAEL 205
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2824-3003 |
3.89e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 43.79 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2824 QKAQVEEELFKVKIQMEELIKLKLRIEEENKMliMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDL 2903
Cdd:pfam15709 360 QRRLQQEQLERAEKMREELELEQQRRFEEIRL--RKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQR 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2904 ANQRALAEKMLKEKMQAIQEASRLKAEAEMLQkqkELAQEQARKFQEDKEQIEQQLAKETEgfqksleaERRQQLEitaE 2983
Cdd:pfam15709 438 KKQQEEAERAEAEKQRQKELEMQLAEEQKRLM---EMAEEERLEYQRQKQEAEEKARLEAE--------ERRQKEE---E 503
|
170 180
....*....|....*....|
gi 1835643837 2984 AERLKLQVLeMSRAQAKAEE 3003
Cdd:pfam15709 504 AARLALEEA-MKQAQEQARQ 522
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
6606-6707 |
3.93e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.39 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 6606 EEFHTLVHYFLERLSEAERTLKYGVIPEEEKALQECQKQQQELMSVLQCQKLALDCILSLGEEILNCCHPESiITIKSWL 6685
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDA-EEIEERL 79
|
90 100
....*....|....*....|..
gi 1835643837 6686 NVTKSRYQEVLNWAEQQGERIQ 6707
Cdd:smart00150 80 EELNERWEELKELAEERRQKLE 101
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2895-3069 |
3.99e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 3.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2895 MRKLAEDDLANQRALAEKMLKEkmqaiqeasrlkAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLE--A 2972
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE------------AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKrlL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2973 ERRQQLEITAEAERLKLQVLEMSRAQAKAEEDasKFKKKAEEIgNKLHQTELATKERMAVVQTLEIQRQQSGKEAEELRR 3052
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQ--ELEKKEEEL-EELIEEQLQELERISGLTAEEAKEILLEKVEEEARH 169
|
170
....*....|....*...
gi 1835643837 3053 AIAELEHEKEKL-KREAE 3069
Cdd:PRK12704 170 EAAVLIKEIEEEaKEEAD 187
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2943-3076 |
4.10e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2943 EQARKF-QEDKEQIEQQLAKeTEGFQKSLEAERRQQLEITAEAERLKLQVLE------------MSRAQAKAEEDASKFK 3009
Cdd:PRK00409 505 EEAKKLiGEDKEKLNELIAS-LEELERELEQKAEEAEALLKEAEKLKEELEEkkeklqeeedklLEEAEKEAQQAIKEAK 583
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 3010 KKAEEIGNKLHQTELATkermavvqtleiQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQ 3076
Cdd:PRK00409 584 KEADEIIKELRQLQKGG------------YASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1965-2322 |
4.18e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 4.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1965 AEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQR-RMQEEVSKREVvavdaEQQKQTIQQELQQLRQnsdmEIKSKAKQIE 2043
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRdREQWERQRREL-----ESRVAELKEELRQSRE----KHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2044 EVEYNRRKIEEEIHIVRLQletmqkhKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEElKRKV 2123
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQ-------RAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAE-RKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2124 QAEKEAAREKQRAV-EDLEKFRSQAEEaerrmkqaevekerqiKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEH 2202
Cdd:pfam07888 177 QAKLQQTEEELRSLsKEFQELRNSLAQ----------------RDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2203 ITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQAEEV-----------AHKKTLAQEEAEKQKEDA 2271
Cdd:pfam07888 241 SLQERLNASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQLADAslalregrarwAQERETLQQSAEADKDRI 320
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2272 EREARKRAKTEES---ALRQKELAEDELEKQRklaDATAQQKFSAEQELIRLKA 2322
Cdd:pfam07888 321 EKLSAELQRLEERlqeERMEREKLEVELGREK---DCNRVQLSESRRELQELKA 371
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3040-3187 |
4.24e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.05 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3040 RQQSGKEAEELRRAIAELehekEKLKREAEllQKNsqkmqvAQQEQLRQETQVLqttflsEKQLLLEREKYIEEEKAKLE 3119
Cdd:PRK00409 508 KKLIGEDKEKLNELIASL----EELERELE--QKA------EEAEALLKEAEKL------KEELEEKKEKLQEEEDKLLE 569
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1835643837 3120 NLyEDEVRKA-QKLKQEQEHQMKHLEEEKDqlkvsMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEK 3187
Cdd:PRK00409 570 EA-EKEAQQAiKEAKKEADEIIKELRQLQK-----GGYASVKAHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| ATP-synt_B |
pfam00430 |
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is ... |
2687-2783 |
4.25e-03 |
|
ATP synthase B/B' CF(0); Part of the CF(0) (base unit) of the ATP synthase. The base unit is thought to translocate protons through membrane (inner membrane in mitochondria, thylakoid membrane in plants, cytoplasmic membrane in bacteria). The B subunits are thought to interact with the stalk of the CF(1) subunits. This domain should not be confused with the ab CF(1) proteins (in the head of the ATP synthase) which are found in pfam00006
Pssm-ID: 425677 [Multi-domain] Cd Length: 132 Bit Score: 41.14 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2687 RAKRAAEDADFARTRAEQEAALsrqqvEEAERLKQRAEEEAQA-KAQAQDEAEKLRKEAEleaakrAHAEQAALKQKQLA 2765
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAAL-----AEAEQQLKEARAEAQEiIENAKKRAEKLKEEIV------AAAEAEAERIIEQA 100
|
90
....*....|....*...
gi 1835643837 2766 DEEMDKHKKFAEKTLRQK 2783
Cdd:pfam00430 101 AAEIEQEKDRALAELRQQ 118
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2745-2973 |
4.28e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 43.30 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2745 ELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEETdhQKtlldEELQRLKEEVTDAMRQ 2824
Cdd:TIGR02794 28 KPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQ--RA----AEQARQKELEQRAAAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2825 KAQVEEElfkvkiQMEELIKLKLRIEEENKMlimkdKDSTQKLLVEEAEKMRQVAEEAARLS-----IEAQEAARMRKLA 2899
Cdd:TIGR02794 102 KAAKQAE------QAAKQAEEKQKQAEEAKA-----KQAAEAKAKAEAEAERKAKEEAAKQAeeeakAKAAAEAKKKAEE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2900 EDDLANQRALAEKMLKEKmqAIQEASRLKAEAemlqkqkelAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAE 2973
Cdd:TIGR02794 171 AKKKAEAEAKAKAEAEAK--AKAEEAKAKAEA---------AKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
2672-2881 |
4.43e-03 |
|
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.
Pssm-ID: 459736 [Multi-domain] Cd Length: 235 Bit Score: 42.71 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2672 KQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAE-----L 2746
Cdd:pfam00261 4 QQIKEELDEAEERLKEAMKKLEEAEKRAEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADESErgrkvL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2747 EAAKRAHAEQAALKQKQLADEemdkhKKFAEKTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVT------- 2819
Cdd:pfam00261 84 ENRALKDEEKMEILEAQLKEA-----KEIAEEADRKYEEVARKLVVVEGDLERAEERAELAESKIVELEEELKvvgnnlk 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2820 --DAMRQKAQVEEELFKVKIQM--EELIKLKLRIEEENK--MLIMKDKDSTQKLLVEEAEKMRQVAEE 2881
Cdd:pfam00261 159 slEASEEKASEREDKYEEQIRFltEKLKEAETRAEFAERsvQKLEKEVDRLEDELEAEKEKYKAISEE 226
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2839-3226 |
4.59e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.73 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2839 MEELIKLKLRIEEENK---MLIMKDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMR-KLAEDDLANQRalaeKML 2914
Cdd:pfam07888 3 LDELVTLEEESHGEEGgtdMLLVVPRAELLQNRLEECLQERAELLQAQEAANRQREKEKERyKRDREQWERQR----REL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2915 KEKMQAIQEASRLKAE--AEMLQKQKELAQEQARKFQE-----DKEQIEQQLAKETEGFQKSLEaerRQQLEITAEAERL 2987
Cdd:pfam07888 79 ESRVAELKEELRQSREkhEELEEKYKELSASSEELSEEkdallAQRAAHEARIRELEEDIKTLT---QRVLERETELERM 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2988 KLQVLEMSRAQAKAEEDASKFKKKAEEIGNKLHQTELATK-------ERMAVVQTLEIQRQQSGKEAEELRRAIAELEHE 3060
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQelrnslaQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3061 KEKLKREAELLQKNSQKMQ---------VAQQEQLRQE-----TQVLQTTF-LSEKQLLLEREK-YIEEEKAKLENLYED 3124
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelssmAAQRDRTQAElhqarLQAAQLTLqLADASLALREGRaRWAQERETLQQSAEA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3125 EVRKAQKLKQEQEHQMKHLEEEKdqlkvsmddaMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKlEQME 3204
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEER----------MEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEK-EQLQ 384
|
410 420
....*....|....*....|..
gi 1835643837 3205 EEHRIALAQTREMRTQTDDLAG 3226
Cdd:pfam07888 385 AEKQELLEYIRQLEQRLETVAD 406
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2701-2930 |
4.66e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2701 RAEQEAALSRQQVEEAERLKQRAEEE-AQAKAQaQDEAEKLRKEAELEAAKRAHAEQAALKQkqlADEEMdkhkkfAEKT 2779
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQAlAQVIAN-QKRLERQLEELEAEAEKWEEKARLALEK---GREDL------AREA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2780 LRQKSQVEQELTKVKLQLEEtdhqktlLDEELQRLKEEVTdamrqkaqveeelfkvkiqmeeliKLKLRIEE-ENKMLIM 2858
Cdd:COG1842 90 LERKAELEAQAEALEAQLAQ-------LEEQVEKLKEALR------------------------QLESKLEElKAKKDTL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 2859 KDKDSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAE----DDLANQRALAEKM--LKEKMQAIQEASRLKAE 2930
Cdd:COG1842 139 KARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARaeaaAELAAGDSLDDELaeLEADSEVEDELAALKAK 216
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2954-3205 |
4.68e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.12 E-value: 4.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2954 QIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQ-VLEMSRAQAKAEEDA----SKFKKKAEEIGNKlHQTELATKE 3028
Cdd:PLN02939 45 QQKKKRGKNIAPKQRSSNSKLQSNTDENGQLENTSLRtVMELPQKSTSSDDDHnrasMQRDEAIAAIDNE-QQTNSKDGE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3029 RMAVVQTLEIQRQQSGKEAEELR------RAIAELE---HEKEKLKREAELLQ----KNSQKMQVAQQEQLRQE------ 3089
Cdd:PLN02939 124 QLSDFQLEDLVGMIQNAEKNILLlnqarlQALEDLEkilTEKEALQGKINILEmrlsETDARIKLAAQEKIHVEileeql 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3090 -------------------TQVLQTTFLSEKQLLLEREkyIEEEKAKLENLYEDEVRKAqKLKQEQEHQMKHLEEEKDQL 3150
Cdd:PLN02939 204 eklrnellirgateglcvhSLSKELDVLKEENMLLKDD--IQFLKAELIEVAETEERVF-KLEKERSLLDASLRELESKF 280
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1835643837 3151 KVSMDDAMKKQKEAEENVRRKQDELQQL---DKKRQEQEKLLADENRKLREKLEQMEE 3205
Cdd:PLN02939 281 IVAQEDVSKLSPLQYDCWWEKVENLQDLldrATNQVEKAALVLDQNQDLRDKVDKLEA 338
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1727-2101 |
4.77e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.14 E-value: 4.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1727 LEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNE--QMLRSHSERDVDLDRYREKvqqlLERWQAILVQIDLRQREL 1804
Cdd:COG4913 612 LAALEAELAELEEELAEAEERLEALEAELDALQERREalQRLAEYSWDEIDVASAERE----IAELEAELERLDASSDDL 687
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1805 DQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQSvpitdsktmkehllQEKKLLDEIESNRDKVDECQKYAKQYidaikdY 1884
Cdd:COG4913 688 AALEEQLEELEAELEELEEELDELKGEIGRLEK--------------ELEQAEEELDELQDRLEAAEDLARLE------L 747
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1885 ELQLVTYKAQVEPVASPAKkpKVQSTSDSIIQEYVDLRTRYSELTTLTSQYIK---FITETLRR-LNDEEKAAEKLKEEE 1960
Cdd:COG4913 748 RALLEERFAAALGDAVERE--LRENLEERIDALRARLNRAEEELERAMRAFNRewpAETADLDAdLESLPEYLALLDRLE 825
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1961 RRRLAEVEAQLAKQtqlaeahakAKAQAEKEAEELQRRMQEEVSkrevvavDAEQQKQTIQQELQQLRQNSDMEIKSKAK 2040
Cdd:COG4913 826 EDGLPEYEERFKEL---------LNENSIEFVADLLSKLRRAIR-------EIKERIDPLNDSLKRIPFGPGRYLRLEAR 889
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835643837 2041 QIEEVEYN--RRKIEEEihIVRLQLETMQKHKANAEDeLQELRARAEKAEQQkkAAQEEAERL 2101
Cdd:COG4913 890 PRPDPEVRefRQELRAV--TSGASLFDEELSEARFAA-LKRLIERLRSEEEE--SDRRWRARV 947
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1944-2084 |
4.82e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 43.11 E-value: 4.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1944 RRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHA---KAKAQAEKEAEELQRRmqEEVSKREVVavdAEQQKQTI 2020
Cdd:COG1566 79 TDLQAALAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAqlaAAQAQLDLAQRELERY--QALYKKGAV---SQQELDEA 153
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835643837 2021 QQELQQLRQNsdmeIKSKAKQIEEVEyNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARA 2084
Cdd:COG1566 154 RAALDAAQAQ----LEAAQAQLAQAQ-AGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1968-2162 |
4.91e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 43.74 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1968 EAQLAKQTQLAEAHaKAKAQAEKEAEELQRRMQEEVSKREvvavdaeQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEY 2047
Cdd:pfam15964 346 EANFEKTKALIQCE-QLKSELERQKERLEKELASQQEKRA-------QEKEALRKEMKKEREELGATMLALSQNVAQLEA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2048 NRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEE--------EL 2119
Cdd:pfam15964 418 QVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDqeieklglEL 497
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1835643837 2120 KRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQAEVEKE 2162
Cdd:pfam15964 498 SESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRLEKE 540
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2015-2177 |
4.94e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.54 E-value: 4.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2015 QQKQTIQQELQQLRQNSDMEIKSKAKQI--EEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKK 2092
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAAllEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2093 AAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREK--QRAVEDLEKFRSQAEEAERRMKQAEVEKERQIKVAQe 2170
Cdd:PRK12705 106 QLEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQ- 184
|
....*..
gi 1835643837 2171 VAQQSAA 2177
Cdd:PRK12705 185 AMQRIAS 191
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1124-1218 |
5.06e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 5.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1124 LRYLQELLLWVEENQRRINGAEWGVDLPSVESHLGSHRGLHQSIDEFRSKIERARADESQL---SPGSRGSYRDCLGKLD 1200
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1835643837 1201 LQYAKLLNSSKSRLRHLE 1218
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1970-2129 |
5.07e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.85 E-value: 5.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1970 QLAKQTQLA--------EAHAKAKAQA-EKEAE-ELQR-RMQEEVSkrevvavdAEQQKQTIqqeLQQLRQNSDMEIKSK 2038
Cdd:PTZ00491 648 SLQKSVQLAieittksqEAAARHQAELlEQEARgRLERqKMHDKAK--------AEEQRTKL---LELQAESAAVESSGQ 716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2039 AKQIEEVEYNRRKIEEEihivrlqletmqkhkanAEDELQELRARAEK------AEQQKKAAQEEAERLRKQVKDETQKK 2112
Cdd:PTZ00491 717 SRAEALAEAEARLIEAE-----------------AEVEQAELRAKALRieaeaeLEKLRKRQELELEYEQAQNELEIAKA 779
|
170
....*....|....*..
gi 1835643837 2113 REAEEELKRKVQAEKEA 2129
Cdd:PTZ00491 780 KELADIEATKFERIVEA 796
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2558-2739 |
5.14e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.38 E-value: 5.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2558 EETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILaDEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQ 2637
Cdd:pfam13904 6 EDMYGGEKQPEEESSKHRVPSLSLDSSSQSSSLTYARKL-EGLKLERQPLEAYENWLAAKQRQRQKELQAQKEEREKEEQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2638 iqlaqEAALKKIDAEEKaHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERAKRAAE-DADFARTRAEQ-EAALSRQQVEE 2715
Cdd:pfam13904 85 -----EAELRKRLAKEK-YQEWLQRKARQQTKKREESHKQKAAESASKSLAKPERKvSQEEAKEVLQEwERKKLEQQQRK 158
|
170 180
....*....|....*....|....
gi 1835643837 2716 AERLKQRAEEEAQAKAQAQDEAEK 2739
Cdd:pfam13904 159 REEEQREQLKKEEEEQERKQLAEK 182
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2862-3123 |
5.21e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.98 E-value: 5.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2862 DSTQKLLVEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQ----RALAEKMLKEKMQAIQEASRLKAEAEMLQKQ 2937
Cdd:COG1340 7 SSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQvkelREEAQELREKRDELNEKVKELKEERDELNEK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2938 KELAQEQARKFQE----------DKEQIEQQLAKETEGFQK---SLEAERRQQLEITAEAERLK--LQVLEMSRAQAKAE 3002
Cdd:COG1340 87 LNELREELDELRKelaelnkaggSIDKLRKEIERLEWRQQTevlSPEEEKELVEKIKELEKELEkaKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3003 EDASKFKKKAEEIGNKLhqtelatKERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKnsqkMQVAQ 3082
Cdd:COG1340 167 AELKELRKEAEEIHKKI-------KELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHE----EIIEL 235
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1835643837 3083 QEQLRQETQVLQTtfLSEKQLLLEREKYIEEEKAKLENLYE 3123
Cdd:COG1340 236 QKELRELRKELKK--LRKKQRALKREKEKEELEEKAEEIFE 274
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3304-3341 |
5.29e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 5.29e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1835643837 3304 KKYLQGKSSIAGLLLKPNNEKISIYQAMKRKLVTPGTA 3341
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2919-3119 |
5.29e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 5.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2919 QAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQ---LAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMS 2995
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEyneLQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2996 RAQAKAEEDASKFKK--KAEEIGNKLhqtelatkERMAVVQTLEiqrQQSGKEAEELRRAIAELEHEKEKLKREAELLQK 3073
Cdd:COG3883 93 RALYRSGGSVSYLDVllGSESFSDFL--------DRLSALSKIA---DADADLLEELKADKAELEAKKAELEAKLAELEA 161
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1835643837 3074 NSQKMQVAQQ--EQLRQETQVLQTTFLSEKQLLLEREKYIEEEKAKLE 3119
Cdd:COG3883 162 LKAELEAAKAelEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2398-2759 |
5.36e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.69 E-value: 5.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2398 LRELAEEAAKLRAVSEEAKRQRQIAEDEAARQRAEAERILKEKLAAI---NDATRLKTEAEIALKEKEAENERLRRLAED 2474
Cdd:COG3899 747 LLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARayaNLGLLLLGDYEEAYEFGELALALAERLGDR 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2475 EAYQRKLLEEQATQH-KQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILkvnfekasvgksDLELELNQL 2553
Cdd:COG3899 827 RLEARALFNLGFILHwLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAA------------LAAAAAAAA 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2554 KNIAEETQRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEkEAARQRKAALEEVERLKAKAEEAKRQKELAEKE 2633
Cdd:COG3899 895 RLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAA-AAAALAAAAAAAALAAALALAAAAAAAAAAALA 973
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2634 AERQIQLAQEAALKKIDAEEKAHTAIVQqkeQEMLQTRKQEQSILDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQV 2713
Cdd:COG3899 974 AAAAAAAAAAAAAAAAALEAAAAALLAL---LAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALA 1050
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1835643837 2714 EEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAAL 2759
Cdd:COG3899 1051 AAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAA 1096
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
2721-2889 |
5.37e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 43.18 E-value: 5.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2721 QRAEEEAQAkAQAQDEAEKLRKEAELEAAKRAHAEQAALKQkqladeEMDKHKKFAEKTLRQKSQVEQELTKVKLQLEET 2800
Cdd:pfam00529 57 QAALDSAEA-QLAKAQAQVARLQAELDRLQALESELAISRQ------DYDGATAQLRAAQAAVKAAQAQLAQAQIDLARR 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2801 dhqKTLLDEELqRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAEKMRQVAE 2880
Cdd:pfam00529 130 ---RVLAPIGG-ISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKL 205
|
....*....
gi 1835643837 2881 EAARLSIEA 2889
Cdd:pfam00529 206 DLERTEIRA 214
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1937-2105 |
5.38e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1937 KFITETlrRLNDEEKAAEKLKEEERRRlAEVEAQLAKQTQLAEAHaKAKAQAEKEAEE-------LQRRMQ--EEVSKRE 2007
Cdd:PRK12704 26 KKIAEA--KIKEAEEEAKRILEEAKKE-AEAIKKEALLEAKEEIH-KLRNEFEKELRErrnelqkLEKRLLqkEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2008 VVAVDAEQQK-QTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIhivrlqlETMQKHKANAE--DELQElRARA 2084
Cdd:PRK12704 102 LELLEKREEElEKKEKELEQKQQ----ELEKKEEELEELIEEQLQELERI-------SGLTAEEAKEIllEKVEE-EARH 169
|
170 180
....*....|....*....|....
gi 1835643837 2085 EKAEQQKKA---AQEEAERLRKQV 2105
Cdd:PRK12704 170 EAAVLIKEIeeeAKEEADKKAKEI 193
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2343-2498 |
5.39e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 42.22 E-value: 5.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2343 NEVNEAIQKRKEMEEELAKVRAEMEILLQSKSRAEEEsRSNTEKSKQMLEveaSKLRELAEEAAKLRAVSEEAKRQRQIA 2422
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLE---LEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2423 -----EDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAE-----NERLRRLAEDEAyQRKLLEEQATQHKQD 2492
Cdd:COG1579 93 alqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekkAELDEELAELEA-ELEELEAEREELAAK 171
|
....*.
gi 1835643837 2493 IEEKII 2498
Cdd:COG1579 172 IPPELL 177
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1941-2055 |
5.48e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 5.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1941 ETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEelqrRMQEEVSKREVVAVDAEQQKQTI 2020
Cdd:PRK11448 121 RTYGKDWDFKPGPFVPPEDPENLLHALQQEVLTLKQQLELQAREKAQSQALAE----AQQQELVALEGLAAELEEKQQEL 196
|
90 100 110
....*....|....*....|....*....|....*...
gi 1835643837 2021 QQELQQLRQNS---DMEIKSKAKQIEEVEYNRRKIEEE 2055
Cdd:PRK11448 197 EAQLEQLQEKAaetSQERKQKRKEITDQAAKRLELSEE 234
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1934-2124 |
5.53e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 5.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1934 QYIKFITETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKA---QAEKEAEELQRRMQEEVSKRevva 2010
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAklyQEEQERKERQKEREEAEKKA---- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2011 vdaEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLE-TMQKHKANAEDELQELRARAEKAEQ 2089
Cdd:pfam13868 232 ---RQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEkRRMKRLEHRRELEKQIEEREEQRAA 308
|
170 180 190
....*....|....*....|....*....|....*
gi 1835643837 2090 QKKAAQEEAERLRKQvkdETQKKREAEEELKRKVQ 2124
Cdd:pfam13868 309 EREEELEEGERLREE---EAERRERIEEERQKKLK 340
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
656-746 |
5.69e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 40.36 E-value: 5.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 656 KWVNKHLIKAQR---HVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRM---RFHKLQNVQIALDYLkhRQVKLVN-IRN 728
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1835643837 729 DDIADGNPKLTLGLIWTI 746
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2030-2302 |
5.95e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 5.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2030 NSDMEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLrKQVKDET 2109
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKEL-KEERDEL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2110 QKKReaeEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMkQAEV---EKERQI-----KVAQEVAQQSAAAELN 2181
Cdd:COG1340 84 NEKL---NELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQ-QTEVlspEEEKELvekikELEKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2182 SKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEAL----RLRLQAEEVAHKK 2257
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQekadELHEEIIELQKEL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1835643837 2258 TLAQEEAEKQKEdaEREARKRAKTEESALRQKELAEDELEKQRKL 2302
Cdd:COG1340 240 RELRKELKKLRK--KQRALKREKEKEELEEKAEEIFEKLKKGEKL 282
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3631-3668 |
6.01e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 6.01e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1835643837 3631 KKYLKGTTAIAGVLVEPTGEKLTFYDALKKNLLKPEVA 3668
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2071-2482 |
6.01e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 43.79 E-value: 6.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2071 ANAEDELQELRARaekaeqqkkaaQEEAERLRKQVKDETQKKREAEEELKRKVQA-------------EKEAARekqraV 2137
Cdd:COG3096 832 PDPEAELAALRQR-----------RSELERELAQHRAQEQQLRQQLDQLKEQLQLlnkllpqanlladETLADR-----L 895
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2138 EDLEKFRSQAEEAERRMKQ---AEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLEL-SLKQEHITVTHL--QEE 2211
Cdd:COG3096 896 EELREELDAAQEAQAFIQQhgkALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfALSEVVQRRPHFsyEDA 975
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2212 AERLKKLHDEaekareeaekelekwhqkaNEALRLRL-QAEEVAHKKTLAQEEAEKQKEDAERE-----ARKRAKTEESA 2285
Cdd:COG3096 976 VGLLGENSDL-------------------NEKLRARLeQAEEARREAREQLRQAQAQYSQYNQVlaslkSSRDAKQQTLQ 1036
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2286 LRQKELAEDELEkqrklADATAQQKfsAEQELIRLKAETENSEqqrllleeelfrlknevneaiQKRKEMEEELAKVRAE 2365
Cdd:COG3096 1037 ELEQELEELGVQ-----ADAEAEER--ARIRRDELHEELSQNR---------------------SRRSQLEKQLTRCEAE 1088
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2366 MEILLQSKSRAEEESRSntekskqmleveaskLRELAEEAAK----LRAVSEEAKRQRQIAEDEAARQRAeaerilkEKL 2441
Cdd:COG3096 1089 MDSLQKRLRKAERDYKQ---------------EREQVVQAKAgwcaVLRLARDNDVERRLHRRELAYLSA-------DEL 1146
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1835643837 2442 AAINDatrlktEAEIALKEKEAENERLR---RLAEDEAY-QRKLL 2482
Cdd:COG3096 1147 RSMSD------KALGALRLAVADNEHLRdalRLSEDPRRpERKVQ 1185
|
|
| BAR_Gvp36 |
cd07600 |
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 ... |
1980-2147 |
6.03e-03 |
|
The Bin/Amphiphysin/Rvs (BAR) domain of Saccharomyces cerevisiae Golgi vesicle protein of 36 kDa and similar proteins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions including organelle biogenesis, membrane trafficking or remodeling, and cell division and migration. Proteomic analysis shows that Golgi vesicle protein of 36 kDa (Gvp36) may be involved in vesicular trafficking and nutritional adaptation. A Saccharomyces cerevisiae strain deficient in Gvp36 shows defects in growth, in actin cytoskeleton polarization, in endocytosis, in vacuolar biogenesis, and in the cell cycle. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.
Pssm-ID: 153284 [Multi-domain] Cd Length: 242 Bit Score: 42.34 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1980 AHAKAKAqAEKEAEELQRRMQEEVSKrevvAVDAEQQKQTIQQELQQLRQNSDMEIKSK---------AKQIEEVEYNRR 2050
Cdd:cd07600 80 NHALSRA-ALASSLELKSLEPEDEDP----LSKALGKYSDAEEKIAEARLEQDQLIQKEfnaklretlNTSFQKAHKARK 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2051 KIEEEihivRLQLETMQKHKANAEDELQELRARA--EKAEQQKKAAQEEAERLRKQVKDETqkkrEAEEELKRKVQAEKE 2128
Cdd:cd07600 155 KVEDK----RLQLDTARAELKSAEPAEKQEAARVevETAEDEFVSATEEAVELMKEVLDNP----EPLQLLKELVKAQLA 226
|
170
....*....|....*....
gi 1835643837 2129 AARekqRAVEDLEKFRSQA 2147
Cdd:cd07600 227 YHK---TAAELLEELLSVL 242
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2675-2768 |
6.12e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 6.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2675 QSILDKLKEEAERAKRAAEDADFARtraEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAE----LEAAK 2750
Cdd:PRK11448 141 ENLLHALQQEVLTLKQQLELQAREK---AQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAetsqERKQK 217
|
90
....*....|....*...
gi 1835643837 2751 RAHAEQAALKQKQLADEE 2768
Cdd:PRK11448 218 RKEITDQAAKRLELSEEE 235
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1922-2056 |
6.13e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 42.66 E-value: 6.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1922 RTRYSELTTLTSQYIKFI----TETLRRLNDEEKAAEKLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEkeaeELqr 1997
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEE----LL-- 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 1998 RMQEEVSKREVVAVDAEQQKQTIQQELqQLRQNSDM-----EIKSKAKQIEEVE-YNRRKIEEEI 2056
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEA-ELRRETERakaeaEAEARAKEERENEdLNLEQLREKA 193
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2342-2494 |
6.15e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.47 E-value: 6.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEElAKVRAEMEILlqsKSRAEEEsrsntEKSKQMLEVEASKLRELAEEAAKLRAVSE-EAKRQRQ 2420
Cdd:PTZ00491 662 KSQEAAARHQAELLEQE-ARGRLERQKM---HDKAKAE-----EQRTKLLELQAESAAVESSGQSRAEALAEaEARLIEA 732
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2421 IAEDEAARQRAEAERILKeklaaindatrlktEAEIAL--KEKEAENERLRRLAEDE-AYQRKLLEEQATQHKQDIE 2494
Cdd:PTZ00491 733 EAEVEQAELRAKALRIEA--------------EAELEKlrKRQELELEYEQAQNELEiAKAKELADIEATKFERIVE 795
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2078-2176 |
6.43e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 6.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2078 QELRARAEKAEQQKKAaQEEAERLRKqvkdETQKKREAEEELKRKVQAEKEAAREKQRAVEDLEKFRSQAEEAERRMKQA 2157
Cdd:pfam05672 21 RQAREQREREEQERLE-KEEEERLRK----EELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEE 95
|
90
....*....|....*....
gi 1835643837 2158 EVEKERQIKVAQEVAQQSA 2176
Cdd:pfam05672 96 QERLQKQKEEAEAKAREEA 114
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
2049-2170 |
6.47e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.92 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2049 RRKIEEEIHIVRLQLETMQKHKANAEdeLQELRA---RAEKAEQQKKAAQE-EAERLRKqvKDETQKKREAEEELKRKVQ 2124
Cdd:PRK00247 291 RAQYREKQKEKKAFLWTLRRNRLRMI--ITPWRApelHAENAEIKKTRTAEkNEAKARK--KEIAQKRRAAEREINREAR 366
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1835643837 2125 AEKEAAREKQRAvedlekfRSQAEEAERRMKQAEVEKERQIKVAQE 2170
Cdd:PRK00247 367 QERAAAMARARA-------RRAAVKAKKKGLIDASPNEDTPSENEE 405
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2067-2191 |
6.47e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 6.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2067 QKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKqvkdETQKKREAEEELKRKVQAEKEAAREKQR--AVEDLEKFR 2144
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLLEEAEkeAQQAIKEAK 583
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1835643837 2145 SQAEEAERRMKQAEVEKERQIKvAQEVaqQSAAAELNSKRMSFAEKT 2191
Cdd:PRK00409 584 KEADEIIKELRQLQKGGYASVK-AHEL--IEARKRLNKANEKKEKKK 627
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1943-2318 |
6.56e-03 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 43.17 E-value: 6.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1943 LRRLNDEEKAAEKLKEEE--RRRLAEVEAQLAKQTQLAEAHAKAKAqAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTI 2020
Cdd:pfam03528 13 LEKENAEFYRLKQQLEAEfnQKRAKFKELYLAKEEDLKRQNAVLQE-AQVELDALQNQLALARAEMENIKAVATVSENTK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2021 QQELQQLRQNSDMEIKSKAKQIE------EVEYNRR-------------KIEEEIHIVRLQLETMQKHKaNAEDELqelr 2081
Cdd:pfam03528 92 QEAIDEVKSQWQEEVASLQAIMKetvreyEVQFHRRleqeraqwnqyreSAEREIADLRRRLSEGQEEE-NLEDEM---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2082 araekaeqqkKAAQEEAERLRKQVkdetqkkreaeeelkrkVQAEKEAAREKQRAVedlekfrsqaeEAERRMKQAEVEK 2161
Cdd:pfam03528 167 ----------KKAQEDAEKLRSVV-----------------MPMEKEIAALKAKLT-----------EAEDKIKELEASK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2162 ERQIKVAQEvaqqsaaaelnskrmsfAEKTAQ--LELSLKQEHITVTHLQEEAERLKK-LHD--EAEKAREEAEKELEKW 2236
Cdd:pfam03528 209 MKELNHYLE-----------------AEKSCRtdLEMYVAVLNTQKSVLQEDAEKLRKeLHEvcHLLEQERQQHNQLKHT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2237 HQKAN----EALRLRLQ----AEEVAHKKTLAQEEaEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQ 2308
Cdd:pfam03528 272 WQKANdqflESQRLLMRdmqrMESVLTSEQLRQVE-EIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETS 350
|
410
....*....|
gi 1835643837 2309 QKFSAEQELI 2318
Cdd:pfam03528 351 APLSNVEEQI 360
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
650-747 |
6.64e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 40.20 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 650 QKKTFTKWVNKHL---------IKAQRHVSDLYEDLRDGHNLISLLEVLSGDNLPREKGRMR-----FHKLQNVQIALDY 715
Cdd:cd21293 2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1835643837 716 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 747
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1796-2211 |
6.65e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.14 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1796 QIDLRQRELDQLGRQLRYYRETYEWLIKWIKDAKQRQEQIQSvpitdsktmkehllqekkLLDEIESNRDKVDECqkyaK 1875
Cdd:pfam05622 67 QLEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNEELTS------------------LAEEAQALKDEMDIL----R 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1876 QYIDAIKDYELQLVTYKAQVEPVASPAKKPKV-QSTSDSIIQEYVDLRTRYSELTTLTSQ---YIKFITETLRRLNDEEK 1951
Cdd:pfam05622 125 ESSDKVKKLEATVETYKKKLEDLGDLRRQVKLlEERNAEYMQRTLQLEEELKKANALRGQletYKRQVQELHGKLSEESK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1952 AAEKLKEEERRRLAEVEA-QLAKQTQLAEAHAKAKAQAE------KEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQEL 2024
Cdd:pfam05622 205 KADKLEFEYKKLEEKLEAlQKEKERLIIERDTLRETNEElrcaqlQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2025 QQLrqnsdmEIKSKAKQIEEVEYNRRKIEEeihiVRLQLETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQ 2104
Cdd:pfam05622 285 IRL------QHENKMLRLGQEGSYRERLTE----LQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2105 VKDETQKKREAEEELK--RKVQAEKEAAREkqrAVEDLE-KFRSQA-------EEAERR----MKQAEVEKERQIKVAQE 2170
Cdd:pfam05622 355 AEDSSLLKQKLEEHLEklHEAQSELQKKKE---QIEELEpKQDSNLaqkidelQEALRKkdedMKAMEERYKKYVEKAKS 431
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1835643837 2171 V-------AQQSAAAELNSKRMSFAEKTAQLE-LSLKQEHITVTHLQEE 2211
Cdd:pfam05622 432 ViktldpkQNPASPPEIQALKNQLLEKDKKIEhLERDFEKSKLQREQEE 480
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2012-2290 |
6.67e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.59 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2012 DAEQQKQTIQQELQQLRQnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQK 2091
Cdd:COG1340 12 ELEEKIEELREEIEELKE----KRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2092 KAAQEEAERLRKQvKDETQKKREAEEELKRKVQAEKeaaREKQRAVEDLEKFRSQAEEAERRMKQAEvEKERQIKVAQEV 2171
Cdd:COG1340 88 NELREELDELRKE-LAELNKAGGSIDKLRKEIERLE---WRQQTEVLSPEEEKELVEKIKELEKELE-KAKKALEKNEKL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2172 AQQSA-AAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKLHDEAEKAREEAEKELEKWHQKANEALRLRLQA 2250
Cdd:COG1340 163 KELRAeLKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELREL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1835643837 2251 EEVAHKKTLAQEEAEKQKEdaEREARKRAKTEESALRQKE 2290
Cdd:COG1340 243 RKELKKLRKKQRALKREKE--KEELEEKAEEIFEKLKKGE 280
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2153-2325 |
6.71e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 6.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2153 RMKQAEVEKERQIKVAQEVAQQsAAAELNSKRMSFAEKTAQLElslkQEHITVTHLQEEAErlkklhdeaekareeaeke 2232
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQ-QAEELQQKQAAEQERLKQLE----KERLAAQEQKKQAE------------------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2233 lekwhQKANEALRLRLQAEEVAHKktlaQEEAEKQKEDAER----EARKRAKTEESALRQKELAEDELEKQRKLADATAQ 2308
Cdd:PRK09510 122 -----EAAKQAALKQKQAEEAAAK----AAAAAKAKAEAEAkraaAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAA 192
|
170
....*....|....*..
gi 1835643837 2309 QKFSAEQElirLKAETE 2325
Cdd:PRK09510 193 AKAAAEAK---KKAEAE 206
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
2716-2884 |
6.72e-03 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 41.80 E-value: 6.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2716 AERLKQRAEEEA-QAKAQAQDEAEKLRKEAELEaakrahaeqaalkqkqlADEEMDKHKKFAEKTLRQKSQVEQELTKVK 2794
Cdd:pfam12072 25 AEAKIGSAEELAkRIIEEAKKEAETKKKEALLE-----------------AKEEIHKLRAEAERELKERRNELQRQERRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2795 LQLEET-DHQKTLLD---EELQRLKEEVTDAMRQKAQVEEEL-FKVKIQMEELIKL-KLRIEEENKMLImkdkDSTQKLL 2868
Cdd:pfam12072 88 LQKEETlDRKDESLEkkeESLEKKEKELEAQQQQLEEKEEELeELIEEQRQELERIsGLTSEEAKEILL----DEVEEEL 163
|
170
....*....|....*.
gi 1835643837 2869 VEEAEKMRQVAEEAAR 2884
Cdd:pfam12072 164 RHEAAVMIKEIEEEAK 179
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2342-2832 |
6.89e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 43.29 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2342 KNEVNEAIQKRKEMEEELAKVRAEMEILLQSksraEEESRSNTEKSKQMLEVEASKLRE----LAEEAAKLRAVSEEAKR 2417
Cdd:PRK04778 104 KHEINEIESLLDLIEEDIEQILEELQELLES----EEKNREEVEQLKDLYRELRKSLLAnrfsFGPALDELEKQLENLEE 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2418 QR-QIAEDEAARQRAEAERILkEKLAAINDATRLKTEaEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEK 2496
Cdd:PRK04778 180 EFsQFVELTESGDYVEAREIL-DQLEEELAALEQIME-EIPELLKELQTELPDQLQELKAGYRELVEEGYHLDHLDIEKE 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2497 IILLKKSSDNELErqkNIVEdtlrqrriieeeiriLKVnfEKASVGKSDLELELNQLKNIAEetqrskekAEQEAekqrq 2576
Cdd:PRK04778 258 IQDLKEQIDENLA---LLEE---------------LDL--DEAEEKNEEIQERIDQLYDILE--------REVKA----- 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2577 laleeeqrRKEAEEKVRKILADEKEAARQRKAALEEVERLKAK----AEEAKRQKELAE--KEAERQIQLAQEaalkKID 2650
Cdd:PRK04778 305 --------RKYVEKNSDTLPDFLEHAKEQNKELKEEIDRVKQSytlnESELESVRQLEKqlESLEKQYDEITE----RIA 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2651 AEEKAHTAIvqqkeQEMLqtrkqeQSILDKLKEeaerakraaedadfartraeqeaaLSRQQVEEAERLKQRAEEEaqak 2730
Cdd:PRK04778 373 EQEIAYSEL-----QEEL------EEILKQLEE------------------------IEKEQEKLSEMLQGLRKDE---- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2731 AQAQDEAEKLRKeaELEAAKRaHAE--------QAALKQKQLADEEMDkhkkfaektlrqksQVEQELTKVKLQLEETDH 2802
Cdd:PRK04778 414 LEAREKLERYRN--KLHEIKR-YLEksnlpglpEDYLEMFFEVSDEIE--------------ALAEELEEKPINMEAVNR 476
|
490 500 510
....*....|....*....|....*....|
gi 1835643837 2803 QKTLLDEELQRLKEEvTDAMRQKAQVEEEL 2832
Cdd:PRK04778 477 LLEEATEDVETLEEE-TEELVENATLTEQL 505
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1951-2149 |
6.91e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1951 KAAE--KLKEEERRRLAEVEAQLAKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQlr 2028
Cdd:PRK07735 70 KAAAlaKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKR-- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2029 qnsdmEIKSKAKQIEEVEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQELRARAEKAEQQKKA---AQEEAERLRKQV 2105
Cdd:PRK07735 148 -----EGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAaaaAKAKAAALAKQK 222
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1835643837 2106 KDETQKKREAEEELKRKVQAEK----EAAREKQRAVEDLEKFRSQAEE 2149
Cdd:PRK07735 223 ASQGNGDSGDEDAKAKAIAAAKakaaAAARAKTKGAEGKKEEEPKQEE 270
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
2678-2767 |
6.92e-03 |
|
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442818 [Multi-domain] Cd Length: 125 Bit Score: 40.22 E-value: 6.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2678 LDKLKEEAERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEA-QAKAQAQDEAEKLRKEAELEAAKraHAEQ 2756
Cdd:COG3599 29 LDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLVVAQETAeEVKENAEKEAELIIKEAELEAEK--IIEE 106
|
90
....*....|.
gi 1835643837 2757 AALKQKQLADE 2767
Cdd:COG3599 107 AQEKARKIVRE 117
|
|
| PRK05431 |
PRK05431 |
seryl-tRNA synthetase; Provisional |
1936-2027 |
6.98e-03 |
|
seryl-tRNA synthetase; Provisional
Pssm-ID: 235461 [Multi-domain] Cd Length: 425 Bit Score: 43.13 E-value: 6.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1936 IKFITET-------LRRLNDEEKAAEKLKEEERRR--LAEVEAQLAKQTQLAEAHAKAKAQAEkEAEELQRRMQEevSKR 2006
Cdd:PRK05431 4 IKLIRENpeavkeaLAKRGFPLDVDELLELDEERRelQTELEELQAERNALSKEIGQAKRKGE-DAEALIAEVKE--LKE 80
|
90 100
....*....|....*....|.
gi 1835643837 2007 EVVAVDAEQQKqtIQQELQQL 2027
Cdd:PRK05431 81 EIKALEAELDE--LEAELEEL 99
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2247-2496 |
6.99e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 6.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2247 RLQAEEVAHKKTLAQE-EAEKQKEDAEREARKRAKTEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAETE 2325
Cdd:pfam13868 33 RIKAEEKEEERRLDEMmEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2326 NSEQQRLLLEEELFRLKNEVNEAI---------QKRKEMEEELAKVRAEMEILLQSKSRAEEESRSNTEKskqmlEVEAS 2396
Cdd:pfam13868 113 EDQAEAEEKLEKQRQLREEIDEFNeeqaewkelEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEK-----EREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2397 KLRELAEEAAKLRAVSEEAKRQRqiAEDEAARQRAEAERILKEKLAAINDATRLKTEAEIALKEKEAENERlrrlAEDEA 2476
Cdd:pfam13868 188 RLRAQQEKAQDEKAERDELRAKL--YQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEA----EREEE 261
|
250 260
....*....|....*....|
gi 1835643837 2477 YQRKLLEEQATQHKQDIEEK 2496
Cdd:pfam13868 262 EFERMLRKQAEDEEIEQEEA 281
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
3106-3205 |
7.06e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 43.31 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3106 EREKYIEEEKAKLENLyEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEaeenVRRKQDELQQLDKKRQEQ 3185
Cdd:COG2433 410 EEEEEIRRLEEQVERL-EAEVEELEAELEEKDERIERLERELSEARSEERREIRKDRE----ISRLDREIERLERELEEE 484
|
90 100
....*....|....*....|
gi 1835643837 3186 EKlladENRKLREKLEQMEE 3205
Cdd:COG2433 485 RE----RIEELKRKLERLKE 500
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2600-2695 |
7.18e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.40 E-value: 7.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2600 KEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQlaQEAALKKIDAEekaHTAIVQQKEQEMLQTRKQEQSild 2679
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQ--ELVALEGLAAE---LEEKQQELEAQLEQLQEKAAE--- 209
|
90
....*....|....*.
gi 1835643837 2680 KLKEEAERAKRAAEDA 2695
Cdd:PRK11448 210 TSQERKQKRKEITDQA 225
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2611-2757 |
8.20e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 8.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2611 EEVERLKAKAEEAKRQKELAEKEAErqiQLAQEAalkkidaeEKAHTAIVQQKEQemlqTRKQEQSILDKLKEEAERAKR 2690
Cdd:PRK00409 516 EKLNELIASLEELERELEQKAEEAE---ALLKEA--------EKLKEELEEKKEK----LQEEEDKLLEEAEKEAQQAIK 580
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835643837 2691 AAedadfartRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQA 2757
Cdd:PRK00409 581 EA--------KKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEELKV 639
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2869-3296 |
8.23e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2869 VEEAEKMRQvAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKM--LKEKMQAIQEASRLKAEAEmlQKQKELAQEQAR 2946
Cdd:COG3064 1 AQEALEEKA-AEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLaeLEAKRQAEEEAREAKAEAE--QRAAELAAEAAK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2947 KFQEDKEQIEQQlaketegfQKSLEAERRQQLEiTAEAERLKLQVLEMSRAQAKAEEdaskfKKKAEEIGNKLHQTELAT 3026
Cdd:COG3064 78 KLAEAEKAAAEA--------EKKAAAEKAKAAK-EAEAAAAAEKAAAAAEKEKAEEA-----KRKAEEEAKRKAEEERKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3027 KERMAVVQTLEIQRQQSGKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMQVAQQEQLRQETQVLQTTFLSEKQLLLE 3106
Cdd:COG3064 144 AEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3107 REKYIEEEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAE------ENVRRKQDELQQLDK 3180
Cdd:COG3064 224 RAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAaalaglAAAAAGLVLDDSAAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3181 KRQEQEKLLADENRKLREKLEQMEEEHRIALAQTREMRTQTDDLAGNLPLTPTVVTQTKAMPNGRDALDGLTQNGMTEQG 3260
Cdd:COG3064 304 AAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADV 383
|
410 420 430
....*....|....*....|....*....|....*.
gi 1835643837 3261 FDGLRQKVTAEKLSIAGILTKETLEKLKRGQLTVEE 3296
Cdd:COG3064 384 EEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVE 419
|
|
| BicD |
pfam09730 |
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled ... |
2575-2987 |
8.26e-03 |
|
Microtubule-associated protein Bicaudal-D; BicD proteins consist of three coiled-coiled domains and are involved in dynein-mediated minus end-directed transport from the Golgi apparatus to the endoplasmic reticulum (ER). For full functioning they bind with GSK-3beta pfam05350 to maintain the anchoring of microtubules to the centromere. It appears that amino-acid residues 437-617 of BicD and the kinase activity of GSK-3 are necessary for the formation of a complex between BicD and GSK-3beta in intact cells.
Pssm-ID: 462863 [Multi-domain] Cd Length: 717 Bit Score: 42.92 E-value: 8.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2575 RQLALEEEQRRKEA--EEKVRKILADEKEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKI--- 2649
Cdd:pfam09730 17 REESLLQESASKEAyyAQRILELQNELKQARAVLSNTQAENERLASLSQELKEECECVELQRGRMRDEIKEYKVREArll 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2650 -DAEEKAHTAIVQQKEQEMLqtrKQEQSILDKLKEEAerakraaedadfarTRAEQEAALSRQQVEEAERLKQRAEEeaq 2728
Cdd:pfam09730 97 qDYSELEEENISLQKQVSVL---KQNQVEFEGLKHEI--------------TRKEEETELLNSQLEEAIRLREIAER--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2729 akaQAQDEAEKLRKEAELEAAKRA--------------------------HAEQAALKQKQLADEEMDKH----KKFAEK 2778
Cdd:pfam09730 157 ---QLDEALETLKTEREQKNSLRKelshymtlndfdyvshlsisldglkfSEDEGAGTEPNNDGEAMDGGenggGGLKNS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2779 TLRQKSQVEQ----------------------ELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVK 2836
Cdd:pfam09730 234 GLDNRTSTPRksevfppapslvsdllselnisEIQKLKQQLIQVEREKVSLLSTLQESQKQLEQAKGALSEQQEKVNRLT 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2837 IQMEELIKLKLRIEEENKMLIMKDKDSTQKLLVEEAE-KMRQVAEeaARLSIEAQEAARMRklaeddlANQRALAEKMLK 2915
Cdd:pfam09730 314 ENLEAMRGLQASKERQDALDSEKDRDSHEDGDYYEVDiNGPEILE--CKYRVAVEEAGELR-------EELKALKARYNT 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835643837 2916 EKMQAIQEASRLKAEAEMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERL 2987
Cdd:pfam09730 385 LEERYKEEKTRWEAEAQDLAEKIRQLEKASHQDQERIAHLEKELGKTRKVAGESEGSLSVAQDELVTFSEEL 456
|
|
| ATP_synt_b |
TIGR01144 |
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria ... |
2045-2142 |
8.59e-03 |
|
ATP synthase, F0 subunit b; This model describes the F1/F0 ATP synthase b subunit in bacteria only. Scoring just below the trusted cutoff are the N-terminal domains of Mycobacterial b/delta fusion proteins and a subunit from an archaeon, Methanosarcina barkeri, in which the ATP synthase homolog differs in architecture and is not experimentally confirmed. This model helps resolve b from the related b' subunit. Within the family is an example from a sodium-translocating rather than proton-translocating ATP synthase. [Energy metabolism, ATP-proton motive force interconversion]
Pssm-ID: 130214 [Multi-domain] Cd Length: 147 Bit Score: 40.46 E-value: 8.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2045 VEYNRRKIEEEIHIVRLQLETMQKHKANAEDELQElrARAEKAEqqkkaAQEEAERLRKQVKDETQKKREAEEElKRKVQ 2124
Cdd:TIGR01144 24 IETRQKKIADGLASAERAKKEAALAQKKAQVILKE--AKDEAQE-----IIENANKRGSEILEEAKAEAREERE-KIKAQ 95
|
90
....*....|....*...
gi 1835643837 2125 AEKEAAREKQRAVEDLEK 2142
Cdd:TIGR01144 96 ARAEIEAEKEQAREELRK 113
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
3051-3206 |
8.80e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.55 E-value: 8.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3051 RRAIAELEHEKEKLKREAEllqKNSQkMQVAQQEQLRQETQVLQTTFLSEKQLLlEREKYIEEEKAKLEnlyedevRKAQ 3130
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAE---RETE-IAIAQANREAEEAELEQEREIETARIA-EAEAELAKKKAEER-------REAE 258
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835643837 3131 KLKQEQEhQMKHLEEEKDQLKVsmddamkkQKEAEENVRRKQDELQQLDKKRQEQEKLLADENRKLREKLEQMEEE 3206
Cdd:COG2268 259 TARAEAE-AAYEIAEANAEREV--------QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEA 325
|
|
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
2580-2746 |
8.92e-03 |
|
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 42.71 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2580 EEEQRRKEAEEKVRKILADEK--EAARQRK---AALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKiDAEEK 2654
Cdd:COG5269 191 EERDRKRYSEAKNREKRAKLKnqDNARLKRlvqIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAALKG-KAEAK 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2655 AHTAIVQQKEQEMLQTRKQEQSILDKLKEEAERA-KRAAEDADF-----ARTRAEQEAALSRQQVEEAErLKQRAeeeAQ 2728
Cdd:COG5269 270 NKAEIEAEALASATAVKKKAKEVMKKALKMEKKAiKNAAKDADYfgdadKAEHIDEDVDLIMDKLGDEE-LGQLA---AD 345
|
170
....*....|....*...
gi 1835643837 2729 AKAQAQDEAEKLRKEAEL 2746
Cdd:COG5269 346 IKAEAAGAAAVFDEFAKM 363
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2672-2751 |
9.08e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.02 E-value: 9.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2672 KQEQSILDKLKEEAERAKRAAEDAD-FARTRAEQEAALSRQQVEEAERLKQRAE--EEAQAKAQAQDEAEKL-RKEAELE 2747
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQaLAEAQQQELVALEGLAAELEEKQQELEAqlEQLQEKAAETSQERKQkRKEITDQ 224
|
....
gi 1835643837 2748 AAKR 2751
Cdd:PRK11448 225 AAKR 228
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2373-2771 |
9.28e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 42.72 E-value: 9.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2373 KSRAEEESRSNTEKSKQMLEVEASKLRELAEEAAKLRAVSEEAKRQrqiAEDEAARQRAEAERILKEKLA-AINDATRLK 2451
Cdd:COG3064 7 EKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQ---AEEEAREAKAEAEQRAAELAAeAAKKLAEAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2452 TEAEIALKEKEAENERLRRLAEDEAYQRKLL----EEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEE 2527
Cdd:COG3064 84 KAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAaaaeKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2528 EIRILKVNFEKASVGKSDLELELNQLKNIAEETQRSKEKAEQEAEKQRQLALEEEQ---RRKEAEEKVRKILADEKEAAR 2604
Cdd:COG3064 164 AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALavaARAAAASREAALAAVEATEEA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2605 QRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAALKKIDAEEKAHTAIVQQKEQEMLQTRKQEQSILDKLKEE 2684
Cdd:COG3064 244 ALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2685 AERAKRAAEDADFARTRAEQEAALSRQQVEEAERLKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQL 2764
Cdd:COG3064 324 AGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGL 403
|
....*..
gi 1835643837 2765 ADEEMDK 2771
Cdd:COG3064 404 RLDLGAA 410
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2778-3122 |
9.39e-03 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 42.25 E-value: 9.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2778 KTLRQKSQVEQELTKVKLQLEETDHQKTLLDEELQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLi 2857
Cdd:pfam09728 8 QLLNKLDSPEEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQKQNKKL- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2858 mkdKDSTQKLLVEEAEKMRQVAE--EAARLSIEAQEAARmrklaeDDLANQRALAEKMLKEKMQAIQEASRLKAEA-EML 2934
Cdd:pfam09728 87 ---KEESKKLAKEEEEKRKELSEkfQSTLKDIQDKMEEK------SEKNNKLREENEELREKLKSLIEQYELRELHfEKL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2935 QKQKELaqeqarkfqedkeqiEQQLAkETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSRAQAKAEEDASKFKKKAEE 3014
Cdd:pfam09728 158 LKTKEL---------------EVQLA-EAKLQQATEEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3015 IGNKLHQT-ELATKERmavvqtleiqrqqsgKEAEELRRAIAELEHEKEKLKREAELLQKNSQKMqvaqqeqlrqetqvl 3093
Cdd:pfam09728 222 FQDTLNKSnEVFTTFK---------------KEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEM--------------- 271
|
330 340
....*....|....*....|....*....
gi 1835643837 3094 qttfLSEKQLLLEREKYIEEEKAKLENLY 3122
Cdd:pfam09728 272 ----AEERQKLKEELEKLQKKLEKLENLC 296
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
3034-3220 |
9.47e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3034 QTLEIQRQQSGKEAEELR-RAIAELEHEKEKLKREAELLQKNSQKMQvaQQEQLRQETQVLQTTFLSEKQlllEREKYIE 3112
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRlDEMMEEERERALEEEEEKEEERKEERKR--YRQELEEQIEEREQKRQEEYE---EKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 3113 EEKAKLENLYEDEVRKAQKLKQEQEHQMKHLEEEKDQLKVSMDDAMKKQKEAEENVRRKQDELQQLDKKRQEQEKLLADE 3192
Cdd:pfam13868 102 QMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEE 181
|
170 180
....*....|....*....|....*...
gi 1835643837 3193 NRKLREKLEQMEEEHRIALAQTREMRTQ 3220
Cdd:pfam13868 182 KEREIARLRAQQEKAQDEKAERDELRAK 209
|
|
| CAF-1_p150 |
pfam11600 |
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide ... |
2064-2170 |
9.47e-03 |
|
Chromatin assembly factor 1 complex p150 subunit, N-terminal; CAF-1_p150 is a polypeptide subunit of CAF-1, which functions in depositing newly synthesized and acetylated histones H3/H4 into chromatin during DNA replication and repair. CAF-1_p150 includes the HP1 interaction site, the PEST, KER and ED interacting sites. CAF-1_p150 interacts directly with newly synthesized and acetylated histones through the acidic KER and ED domains. The PEST domain is associated with proteins that undergo rapid proteolysis.
Pssm-ID: 402959 [Multi-domain] Cd Length: 164 Bit Score: 40.83 E-value: 9.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2064 ETMQKHKANAEDELQELRARAEKAEQQKKAAQEEAERLRKQVKDETQKKREAEEELKRKVQAEKEAAREKQRAvedlEKF 2143
Cdd:pfam11600 11 EEKEKQRLEKDKERLRRQLKLEAEKEEKERLKEEAKAEKERAKEEARRKKEEEKELKEKERREKKEKDEKEKA----EKL 86
|
90 100
....*....|....*....|....*..
gi 1835643837 2144 RSQAEEAERRMKQAEVEKERQIKVAQE 2170
Cdd:pfam11600 87 RLKEEKRKEKQEALEAKLEEKRKKEEE 113
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1977-2121 |
9.48e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.41 E-value: 9.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 1977 LAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKQIEEVEYNRRKIEEEi 2056
Cdd:pfam05672 16 LAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQE- 94
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835643837 2057 hivrlQLETMQKHKANAEDELQElRARAEKAEQQKKAAQEEAERLrkqvkdetQKKREAEEELKR 2121
Cdd:pfam05672 95 -----EQERLQKQKEEAEAKARE-EAERQRQEREKIMQQEEQERL--------ERKKRIEEIMKR 145
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2734-3011 |
9.56e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2734 QDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKSQVEQ---ELTKVKLQLEETDHQKTLLDEE 2810
Cdd:COG1340 14 EEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDElneKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2811 LQRLKEEvtdaMRQKAQVEEELFKVKIQMEELIK----LKLRIEEENKmLIMKDKDSTQKLlvEEAEKMRQVAEEAARLS 2886
Cdd:COG1340 94 LDELRKE----LAELNKAGGSIDKLRKEIERLEWrqqtEVLSPEEEKE-LVEKIKELEKEL--EKAKKALEKNEKLKELR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2887 IEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEASRLKAEAEMLQKQKELAQEQARkfQEDKEQIEQQlaKETEGF 2966
Cdd:COG1340 167 AELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKAD--ELHEEIIELQ--KELREL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1835643837 2967 QKSLEAERRQQLEITAEAERlklqvlemSRAQAKAEEDASKFKKK 3011
Cdd:COG1340 243 RKELKKLRKKQRALKREKEK--------EELEEKAEEIFEKLKKG 279
|
|
| EFh_PEF_Group_I |
cd16180 |
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds ... |
6878-6937 |
9.64e-03 |
|
Penta-EF hand, calcium binding motifs, found in Group I PEF proteins; The family corresponds to Group I PEF proteins that have been found not only in higher animals but also in lower animals, plants, fungi and protists. Group I PEF proteins include apoptosis-linked gene 2 protein (ALG-2), peflin and similar proteins. ALG-2, also termed programmed cell death protein 6 (PDCD6), is a widely expressed calcium-binding modulator protein associated with cell proliferation and death, as well as cell survival. It forms a homodimer in the cell or a heterodimer with its closest paralog peflin. Among the PEF proteins, ALG-2 can bind three Ca2+ ions through its EF1, EF3, and EF5 hands, where it is unique in that its EF5 hand binds Ca2+ ion in a canonical coordination. Peflin is a ubiquitously expressed 30-kD PEF protein containing five EF-hand motifs in its C-terminal domain and a longer N-terminal hydrophobic domain (NHB domain) than any other member of the PEF family. The NHB domain harbors nine repeats of a nonapeptide (A/PPGGPYGGP). Peflin may modulate the function of ALG-2 in Ca2+ signaling. It exists only as a heterodimer with ALG-2, and binds two Ca2+ ions through its EF1 and EF3 hands. Its additional EF5 hand is unpaired and does not bind Ca2+ ion but mediates the heterodimerization with ALG-2. The dissociation of heterodimer occurs in the presence of Ca2+.
Pssm-ID: 320055 [Multi-domain] Cd Length: 164 Bit Score: 40.59 E-value: 9.64e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835643837 6878 RILDIFRSIDRDQDGRISQQEFIESVLSSKFPTNSLE-MNAVASIFDYNGDGFIDYYEFVS 6937
Cdd:cd16180 1 ELRRIFQAVDRDRSGRISAKELQRALSNGDWTPFSIEtVRLMINMFDRDRSGTINFDEFVG 61
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2591-2694 |
9.97e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 39.73 E-value: 9.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835643837 2591 KVRKILADEKEAARQrkaALEEVERLKAKAEEAKrqkelaeKEAERQIQLAQEAALKKIdaeEKAHTAIVQQKEQEMLQT 2670
Cdd:cd06503 23 PILKALDEREEKIAE---SLEEAEKAKEEAEELL-------AEYEEKLAEARAEAQEII---EEARKEAEKIKEEILAEA 89
|
90 100
....*....|....*....|....
gi 1835643837 2671 RKQEQSILDKLKEEAERAKRAAED 2694
Cdd:cd06503 90 KEEAERILEQAKAEIEQEKEKALA 113
|
|
| |
