|
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 ... |
632-736 |
3.92e-75 |
|
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: 245.77 E-value: 3.92e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 632 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLKHRQVKLVNI 711
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1717010358 712 RNDDIADGNPKLTLGLIWTIILHFQ 736
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
629-747 |
2.14e-73 |
|
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: 241.08 E-value: 2.14e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 629 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLKHRQVKL 708
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1717010358 709 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 747
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
627-745 |
9.98e-71 |
|
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: 234.11 E-value: 9.98e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 627 AEDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLKHRQV 706
Cdd:cd21236 10 YKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQV 89
|
90 100 110
....*....|....*....|....*....|....*....
gi 1717010358 707 KLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 745
Cdd:cd21236 90 KLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
749-854 |
4.74e-69 |
|
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: 228.37 E-value: 4.74e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 749 MTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 828
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1717010358 829 PEDVDVPQPDEKSIITYVSSLYDAMP 854
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
750-854 |
1.61e-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: 218.03 E-value: 1.61e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 829
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1717010358 830 EDVDVPQPDEKSIITYVSSLYDAMP 854
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
629-746 |
1.11e-61 |
|
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: 207.58 E-value: 1.11e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 629 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLKHRQVKL 708
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1717010358 709 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 746
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
750-854 |
2.02e-57 |
|
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: 194.82 E-value: 2.02e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDP 829
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1717010358 830 EDVDVPQPDEKSIITYVSSLYDAMP 854
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
634-737 |
1.89e-50 |
|
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: 175.26 E-value: 1.89e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 634 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLKHRQVKLVNIR 712
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1717010358 713 NDDIADGNPKLTLGLIWTIILHFQI 737
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
748-854 |
2.12e-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: 174.85 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 748 DMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLL 827
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1717010358 828 DPEDVDVPQPDEKSIITYVSSLYDAMP 854
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
629-733 |
3.11e-47 |
|
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: 166.39 E-value: 3.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 629 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLKHRQVK 707
Cdd:cd21246 11 DEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKEQRVH 90
|
90 100
....*....|....*....|....*.
gi 1717010358 708 LVNIRNDDIADGNPKLTLGLIWTIIL 733
Cdd:cd21246 91 LENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
750-850 |
9.02e-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: 164.51 E-value: 9.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 829
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1717010358 830 EDVDVPQPDEKSIITYVSSLY 850
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
750-850 |
2.33e-45 |
|
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: 160.64 E-value: 2.33e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 829
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1717010358 830 EDVDVPQPDEKSIITYVSSLY 850
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| S10_plectin |
pfam03501 |
Plectin/S10 domain; This presumed domain is found at the N-terminus of some isoforms of the ... |
7-99 |
2.44e-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: 156.91 E-value: 2.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 7 MPLDQLRAIYELLFREGVMIAKKDkRPQSLHPEIkGVSNLQVIRAMGSLKSRGYVRETFVWRHFYWYLSNEGIVYLRQYL 86
Cdd:pfam03501 1 IPKENRKAIYEYLFKEGVLVAKKD-FNLPKHPEL-NVPNLQVIKAMQSLKSRGYVKEQFAWRHYYWYLTNEGIEYLREYL 78
|
90
....*....|...
gi 1717010358 87 HLPPEIVPGSLQR 99
Cdd:pfam03501 79 HLPAEIVPATLKR 91
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
628-850 |
5.83e-44 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 172.43 E-value: 5.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 628 EDERDRVQKKTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLKHR 704
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 705 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMTESYQ-GLRCDNFTTSWRDGRL 783
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 784 FNAIIHRHKPLLIDMNKVYRQTNLE--NLDQAFNVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLY 850
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
630-737 |
1.94e-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: 155.23 E-value: 1.94e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 630 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLKHRQ 705
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1717010358 706 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 737
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
628-733 |
5.36e-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: 5.36e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 628 EDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLkHRQV 706
Cdd:cd21193 10 QEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKV 88
|
90 100
....*....|....*....|....*..
gi 1717010358 707 KLVNIRNDDIADGNPKLTLGLIWTIIL 733
Cdd:cd21193 89 RLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1938-3169 |
6.72e-43 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 174.63 E-value: 6.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1938 AEKLKEEERRRLAEVEAQLEKQTQlAEAHAKAKAQAEKEAEELQRRMQ--EEVSKR---------EVVAVdAEQQKQTIQ 2006
Cdd:NF041483 85 ADQLRADAERELRDARAQTQRILQ-EHAEHQARLQAELHTEAVQRRQQldQELAERrqtveshvnENVAW-AEQLRARTE 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2007 QELQQLRQNSDMEI-KSKAKKIEEAEynrrkieeeihivRLQLETMQKQKASAEDelqelrARAEeAERQKKAAQEEAER 2085
Cdd:NF041483 163 SQARRLLDESRAEAeQALAAARAEAE-------------RLAEEARQRLGSEAES------ARAE-AEAILRRARKDAER 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2086 LRRQVKDESQKKREAEEELKRKVQAEKDAARekQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAqqsaaael 2165
Cdd:NF041483 223 LLNAASTQAQEATDHAEQLRSSTAAESDQAR--RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAKEAA-------- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2166 nSKRMSFAEKTAQLELSLKQEHIT--VTHLQEEAERLKKQHEEAEKAREEaekelekwhqkanEALRLRLQAEEVAhkKT 2243
Cdd:NF041483 293 -AKQLASAESANEQRTRTAKEEIArlVGEATKEAEALKAEAEQALADARA-------------EAEKLVAEAAEKA--RT 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2244 LAQEEAEKQKEDAEREARK-RAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELirlkADTESGEQqrllleee 2322
Cdd:NF041483 357 VAAEDTAAQLAKAARTAEEvLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ----AEQLKGAA-------- 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2323 lfrlKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRElaEEAARLRALSEEAkr 2402
Cdd:NF041483 425 ----KDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARTAE--ELLTKAKADADEL-- 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2403 qRQIAEGEAARQRAEAerilkeklaaINEATRLKTEAEIALKEKEAENERLRRLAEDEA-YQRKLLEEQATQHKQDIEEK 2481
Cdd:NF041483 497 -RSTATAESERVRTEA----------IERATTLRRQAEETLERTRAEAERLRAEAEEQAeEVRAAAERAARELREETERA 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2482 IILLKKSSDNELERQKNIVEDTLrqrriiEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRS-KEKAEQEAEKQR 2560
Cdd:NF041483 566 IAARQAEAAEELTRLHTEAEERL------TAAEEALADARAEAERIRREAAEETERLRTEAAERIRTlQAQAEQEAERLR 639
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2561 -QLALEEEQRRKEAEEKvrkiladeqeAARQRKAALEEVERLKAKAEE-AKRQKELAEKEAERQIQLAQE--------AA 2630
Cdd:NF041483 640 tEAAADASAARAEGENV----------AVRLRSEAAAEAERLKSEAQEsADRVRAEAAAAAERVGTEAAEalaaaqeeAA 709
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2631 FKKIEAEEKAHAAiVQQKEQEMLQTRKQEKSIL----DKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEA-ERMK 2705
Cdd:NF041483 710 RRRREAEETLGSA-RAEADQERERAREQSEELLasarKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSvAGLQ 788
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2706 QRAEEE-AQAKAQAQDEAEKLRKEAELEA--------AKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQkAQVEQElt 2776
Cdd:NF041483 789 EQAEEEiAGLRSAAEHAAERTRTEAQEEAdrvrsdayAERERASEDANRLRREAQEETEAAKALAERTVSE-AIAEAE-- 865
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2777 kvKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVK----IQMEELIKLKLRIEEENKMLIMKDKDSTQKF 2852
Cdd:NF041483 866 --RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDE 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2853 LAEEAEKMR-QVAEEAARLSIEAQ-EAARMRKLAEDDLANQRALAEKMLKE----KMQAIQEATRLKAEADMLQKQ--KE 2924
Cdd:NF041483 944 ARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTEaervKAEAAAEAERLRTEAREEADRtlDE 1023
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2925 LAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERlklQVLEMSKAqakAEEDAKKFKKQAEDFGNKL 3004
Cdd:NF041483 1024 ARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEA---QADTMVGA---ARKEAERIVAEATVEGNSL 1097
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3005 HQTELATKERMVVvqslEIQRQQSG--KEAEELR-RAIAELEHEKEKLKQEAELLQKNSQE-----MQVAQQEQLRQETQ 3076
Cdd:NF041483 1098 VEKARTDADELLV----GARRDATAirERAEELRdRITGEIEELHERARRESAEQMKSAGErcdalVKAAEEQLAEAEAK 1173
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3077 VlqttflteKHLLLEKEKYIEKEKAklenlyeDEVRKAQKLKQEQEHQLKQLEEEKQQLKAsmgeamKKQKEAEESVRHK 3156
Cdd:NF041483 1174 A--------KELVSDANSEASKVRI-------AAVKKAEGLLKEAEQKKAELVREAEKIKA------EAEAEAKRTVEEG 1232
|
1290
....*....|...
gi 1717010358 3157 QDELHQLDKRRQE 3169
Cdd:NF041483 1233 KRELDVLVRRRED 1245
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
630-737 |
2.30e-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: 149.26 E-value: 2.30e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 630 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLKHRQ 705
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1717010358 706 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 737
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1935-2724 |
3.69e-41 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 169.55 E-value: 3.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1935 EKAAEKLKEEERRRLAEvEAQlEKQTQLAEAHAKAKaQAEKEAEELQR----RMQEEVSKREVVAVDAEQQKQTIQQELQ 2010
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAE-EAK-KTETGKAEEARKAE-EAKKKAEDARKaeeaRKAEDARKAEEARKAEDAKRVEIARKAE 1161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2011 QLRQNSDMEIKSKAKKIEEAeynRRKIEeeihiVRLQLETmqkQKASAEDELQELRaRAEEAERQKKAAQEEAERLRRQV 2090
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAA---RKAEE-----VRKAEEL---RKAEDARKAEAAR-KAEEERKAEEARKAEDAKKAEAV 1229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2091 KDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEV--AQQSAAAELNSK 2168
Cdd:PTZ00121 1230 KKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAkkAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2169 RMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKAnealrlrlqaeEVAHKKTlaqEE 2248
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKA-----------EAAEKKK---EE 1375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2249 AEKQKEDAEREARKRAKAEESalrqKELAEDELEKQRKLADATAQQKFSAEqelirLKADTESGEQQRLLLEEELFRLKN 2328
Cdd:PTZ00121 1376 AKKKADAAKKKAEEKKKADEA----KKKAEEDKKKADELKKAAAAKKKADE-----AKKKAEEKKKADEAKKKAEEAKKA 1446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2329 EVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSK-HMLEVEASKLRELAEEAARLRAL--SEEAKRQRQ 2405
Cdd:PTZ00121 1447 DEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKaEEAKKKADEAKKAAEAKKKADEAkkAEEAKKADE 1526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2406 IAEGEAARQRAEAERILKEKLA-AINEATRLKT-----EAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIE 2479
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKAdELKKAEELKKaeekkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2480 EKIILLKKSSDNELE-RQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEK 2558
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKaEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2559 QRQlalEEEQRRKEAEEK-----VRKILADEQEAARQRKAALEE----VERLKAKAEEAKRQKELAEKEAE--RQIQLAQ 2627
Cdd:PTZ00121 1687 EKK---AAEALKKEAEEAkkaeeLKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEekKKIAHLK 1763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2628 EAAFKKIEAEEKAHAAIVQQ--KEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMK 2705
Cdd:PTZ00121 1764 KEEEKKAEEIRKEKEAVIEEelDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQL 1843
|
810
....*....|....*....
gi 1717010358 2706 QRAEEEAQAKAQAQDEAEK 2724
Cdd:PTZ00121 1844 EEADAFEKHKFNKNNENGE 1862
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
737-852 |
8.14e-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: 147.89 E-value: 8.14e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 737 ISDIQVsgqsEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNV 816
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 817 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 852
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
611-733 |
1.46e-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: 148.25 E-value: 1.46e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 611 ETVPAVGVSEMEDPTPAEDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFH 689
Cdd:cd21318 15 EPAATAKLFECSRIKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIH 94
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1717010358 690 KLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 733
Cdd:cd21318 95 SLENVDKALQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
749-854 |
3.27e-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: 3.27e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 749 MTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 828
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1717010358 829 PEDVDVPQPDEKSIITYVSSLYDAMP 854
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
628-733 |
8.67e-40 |
|
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: 145.58 E-value: 8.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 628 EDERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLKHRQV 706
Cdd:cd21317 25 ADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLKEQKV 104
|
90 100
....*....|....*....|....*..
gi 1717010358 707 KLVNIRNDDIADGNPKLTLGLIWTIIL 733
Cdd:cd21317 105 HLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2446-3191 |
6.00e-39 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 162.23 E-value: 6.00e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2446 KEAENERLRRLAEDEAYQ--RKLLEEQATQHKQDIEE---KIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLN 2520
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEeaFGKAEEAKKTETGKAEEarkAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEI 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2521 FEKASSGKSDLELELNQLKNIAEETHRSKE-KAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEaarQRKAALEEVE 2599
Cdd:PTZ00121 1157 ARKAEDARKAEEARKAEDAKKAEAARKAEEvRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDA---KKAEAVKKAE 1233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2600 RLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKK----IEAEEKAHAAIVQQKEQ----------------EMLQTRKQE 2659
Cdd:PTZ00121 1234 EAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARrqaaIKAEEARKADELKKAEEkkkadeakkaeekkkaDEAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2660 KSILDKLKEEAERAKRAAED----ADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAElEAAK 2735
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADAakkkAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAE-EKKK 1392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2736 RAHAEQAALKQKQLADE--EMDKHKKFAEKtLRQKAQVEQELTKVKLQLEETDHQktlldDESQRLKEEVTDAMRQKAQV 2813
Cdd:PTZ00121 1393 ADEAKKKAEEDKKKADElkKAAAAKKKADE-AKKKAEEKKKADEAKKKAEEAKKA-----DEAKKKAEEAKKAEEAKKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2814 EEelfkvKIQMEElikLKLRIEEENKMLIMKDKDSTQKFLAEEAEKmrqvAEEAARLSIEAQEAARMRKLAEDDLANQRA 2893
Cdd:PTZ00121 1467 EE-----AKKADE---AKKKAEEAKKADEAKKKAEEAKKKADEAKK----AAEAKKKADEAKKAEEAKKADEAKKAEEAK 1534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2894 LAEKMlkEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQlaketegfqksleAERRQQLEitaEAERLK 2973
Cdd:PTZ00121 1535 KADEA--KKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRK-------------AEEAKKAE---EARIEE 1596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2974 LQVLEMSKAQAKAEEdakkfKKQAEDFGNKLHQTELATKERMVVVQsLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEA 3053
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEE-----AKKAEEAKIKAEELKKAEEEKKKVEQ-LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKA 1670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3054 ELLQKNSQEMQVAQQEQLRQETQvlqttfltekhllLEKEKYIEKEKAKLENLYEDEVRKAQKLKQEQE---HQLKQLEE 3130
Cdd:PTZ00121 1671 EEDKKKAEEAKKAEEDEKKAAEA-------------LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEenkIKAEEAKK 1737
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 3131 EKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRKLREKLEQLEEE 3191
Cdd:PTZ00121 1738 EAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2007-2777 |
9.45e-39 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 161.46 E-value: 9.45e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2007 QELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQ--------LETMQKQKASAEDELQELRARAEEAERQKKA 2078
Cdd:PTZ00121 1030 EELTEYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEglkpsykdFDFDAKEDNRADEATEEAFGKAEEAKKTETG 1109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2079 AQEEaERLRRQVKDESQKKREAEE----ELKRKVQ----AEKDAAREKQRAMEDLQKFR-----SQAEEAERRMKQAEVE 2145
Cdd:PTZ00121 1110 KAEE-ARKAEEAKKKAEDARKAEEarkaEDARKAEearkAEDAKRVEIARKAEDARKAEearkaEDAKKAEAARKAEEVR 1188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2146 KERQIKVAQEVAQQSAAAELNSKRMsfAEKTAQLELSLKQEHI----TVTHLQEEAERLKKQHEEAEKAREEAEKELEKW 2221
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERK--AEEARKAEDAKKAEAVkkaeEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFA 1266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2222 HQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESalRQKELAEDELEKQRKLADATAQQKFSAEQE 2301
Cdd:PTZ00121 1267 RRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADAAKKKAEEAKKA 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2302 LIRLKADTESGEQQRLLLEEELFRLKNEVNEAiqkrKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHmlEVEAS 2381
Cdd:PTZ00121 1345 AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEA----KKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKA--AAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2382 KLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERilkeklaainEATRLKTEAEIALKEKEAENErlrrlaEDEA 2461
Cdd:PTZ00121 1419 KADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAK----------KAEEAKKKAEEAKKADEAKKK------AEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2462 YQRKLLEEQATQHKQDIEEkiilLKKSSDnelERQKnivEDTLRQRRIIEEEIRIlklnfEKASSGKSDLELELNQLKNI 2541
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADE----AKKAAE---AKKK---ADEAKKAEEAKKADEA-----KKAEEAKKADEAKKAEEKKK 1547
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2542 AEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKA----KAEEAKRQKELAEK 2617
Cdd:PTZ00121 1548 ADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAeeakKAEEAKIKAEELKK 1627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2618 EAERQIQLAQeaaFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAED---ADYARMRAEQEAALS 2694
Cdd:PTZ00121 1628 AEEEKKKVEQ---LKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDekkAAEALKKEAEEAKKA 1704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2695 RQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQE 2774
Cdd:PTZ00121 1705 EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE 1784
|
...
gi 1717010358 2775 LTK 2777
Cdd:PTZ00121 1785 LDE 1787
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
746-850 |
2.00e-38 |
|
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: 140.91 E-value: 2.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 746 SEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTR 825
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 1717010358 826 LLDPEDVDVPQPDEKSIITYVSSLY 850
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
634-735 |
2.59e-38 |
|
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: 140.23 E-value: 2.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 634 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLKHRQVKLVNI 711
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1717010358 712 RNDDIADGNPKLTLGLIWTIILHF 735
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
746-850 |
5.77e-38 |
|
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: 139.81 E-value: 5.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 746 SEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTR 825
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1717010358 826 LLDPEDVDVPQPDEKSIITYVSSLY 850
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
749-850 |
1.48e-37 |
|
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: 138.46 E-value: 1.48e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 749 MTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 828
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1717010358 829 PEDVDVPQPDEKSIITYVSSLY 850
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
630-737 |
3.86e-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: 3.86e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 630 ERDRVQKKTFTKWVNKHLIKAQ--RHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLKHRQVK 707
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1717010358 708 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 737
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1936-2978 |
7.36e-37 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 154.60 E-value: 7.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1936 KAAEKLKEEERRRLAEVEAQLEK-QTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKrevVAVDAEQQKQTIQQELQQLRQ 2014
Cdd:NF041483 261 RAAEQRMQEAEEALREARAEAEKvVAEAKEAAAKQLASAESANEQRTRTAKEEIAR---LVGEATKEAEALKAEAEQALA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2015 NSdmeiKSKAKKI--EEAEYNRRKIEEEI-----HIVRLQLETMQKqkaSAEDELQELRARAEEAERQKKAAQEEAERLR 2087
Cdd:NF041483 338 DA----RAEAEKLvaEAAEKARTVAAEDTaaqlaKAARTAEEVLTK---ASEDAKATTRAAAEEAERIRREAEAEADRLR 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2088 RQVKDES-QKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQA-EEAERRMKQAEVEKERQIKVAqevaqQSAAAEL 2165
Cdd:NF041483 411 GEAADQAeQLKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAvAEGERIRGEARREAVQQIEEA-----ARTAEEL 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2166 NSKRMSFAEktaqlELSlkqehitvTHLQEEAERLKKqheeaekareeaekelekwhQKANEALRLRLQAEEVAHKktlA 2245
Cdd:NF041483 486 LTKAKADAD-----ELR--------STATAESERVRT--------------------EAIERATTLRRQAEETLER---T 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2246 QEEAEKQKEDAEREARK-RAKAEESALRQKELAEdelekqrklaDATAQQKFSAEQELIRLKAdtesgeqqrllleeelf 2324
Cdd:NF041483 530 RAEAERLRAEAEEQAEEvRAAAERAARELREETE----------RAIAARQAEAAEELTRLHT----------------- 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2325 rlknevnEAIQKRKKMEEELAKVRAEMEILleSKSRAEEESRSNTEKS------KHMLEVEASKLR-ELAEEAARLRALS 2397
Cdd:NF041483 583 -------EAEERLTAAEEALADARAEAERI--RREAAEETERLRTEAAerirtlQAQAEQEAERLRtEAAADASAARAEG 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2398 EE-AKRQRQIAEGEAARQRAE----AERILKEKLAAineATRLKTEAEIALKEKEAENERLRRLAEDE-AYQRKLLEEQA 2471
Cdd:NF041483 654 ENvAVRLRSEAAAEAERLKSEaqesADRVRAEAAAA---AERVGTEAAEALAAAQEEAARRRREAEETlGSARAEADQER 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2472 TQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSD-LELELNQLKNIAEET-HRSK 2549
Cdd:NF041483 731 ERAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEqAEEEIAGLRSAAEHAaERTR 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2550 EKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAA-----RQRKAALEEVERLKAKAEEAKRQkelAEKEAERQIQ 2624
Cdd:NF041483 811 TEAQEEADRVRSDAYAERERASEDANRLRREAQEETEAAkalaeRTVSEAIAEAERLRSDASEYAQR---VRTEASDTLA 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2625 LA-QEAAFKKIEAEEKAH---AAIVQQKEQEMLQTRKQEKSILDKLKEEAERAK-RAAEDADYARMRA-EQEAALSRQQV 2698
Cdd:NF041483 888 SAeQDAARTRADAREDANrirSDAAAQADRLIGEATSEAERLTAEARAEAERLRdEARAEAERVRADAaAQAEQLIAEAT 967
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2699 EEAERMKQRAeeeAQAKAQAQDEAEKLRKEAE-LEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKtlRQKAQVEQELTK 2777
Cdd:NF041483 968 GEAERLRAEA---AETVGSAQQHAERIRTEAErVKAEAAAEAERLRTEAREEADRTLDEARKDANK--RRSEAAEQADTL 1042
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2778 VKLQLEETDHQKTLLDDESQRLK---EEVTDAMRQKAQVEEElfkvKIQMEELIKLKLRIE----EENKMLIMKDKDSTQ 2850
Cdd:NF041483 1043 ITEAAAEADQLTAKAQEEALRTTteaEAQADTMVGAARKEAE----RIVAEATVEGNSLVEkartDADELLVGARRDATA 1118
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2851 kfLAEEAEKMR--------QVAEEAARLSIEAQEAARMR-----KLAEDDLANQRALAEKMLKE--------KMQAIQEA 2909
Cdd:NF041483 1119 --IRERAEELRdritgeieELHERARRESAEQMKSAGERcdalvKAAEEQLAEAEAKAKELVSDanseaskvRIAAVKKA 1196
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2910 TRLKAEADmlQKQKELAQEqARKFQEDKEQIEQQLAKETegfQKSLEAERRQQLEITAEAERLKlQVLE 2978
Cdd:NF041483 1197 EGLLKEAE--QKKAELVRE-AEKIKAEAEAEAKRTVEEG---KRELDVLVRRREDINAEISRVQ-DVLE 1258
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
632-733 |
1.04e-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: 135.59 E-value: 1.04e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 632 DRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLKHRQVKLVN 710
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1717010358 711 IRNDDIADGNPKLTLGLIWTIIL 733
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1936-2480 |
7.77e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 150.86 E-value: 7.77e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1936 KAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMqEEVSKREVVAVDAEQQKQTIQQELQQLRQN 2015
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL-EEAQAEEYELLAELARLEQDIARLEERRRE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2016 SDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQ 2095
Cdd:COG1196 314 LEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALR 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2096 KKREAEEELKRKVQAEKDAAREKQRAmedlqkfrsQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEK 2175
Cdd:COG1196 394 AAAELAAQLEELEEAEEALLERLERL---------EEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLEL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2176 TAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAE-------EVAHKKTLAQEE 2248
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligvEAAYEAALEAAL 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2249 AEKQKEDAEREARKRAKAEESALRQKE-----LAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEEL 2323
Cdd:COG1196 545 AAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2324 FRLKNEVNE-AIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKskhmLEVEASKLRELAEEAARLRALSEEAKR 2402
Cdd:COG1196 625 RTLVAARLEaALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA----LLEAEAELEELAERLAEEELELEEALL 700
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2403 QRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEE 2480
Cdd:COG1196 701 AEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
753-854 |
1.54e-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: 132.55 E-value: 1.54e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 753 EKLLL-WSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 831
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1717010358 832 VDVPQPDEKSIITYVSSLYDAMP 854
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
629-737 |
1.97e-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: 132.35 E-value: 1.97e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 629 DERDRVQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLKHRQVK 707
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1717010358 708 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 737
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
734-850 |
4.15e-35 |
|
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: 132.10 E-value: 4.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 734 HFQISDIQVSGQSEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQA 813
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 814 FNVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 850
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2027-2656 |
1.35e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.54 E-value: 1.35e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2027 IEEA----EYNRRKIEEEihivrLQLETMQKQKASAEDELQELRARAEEAERQKKAA------QEEAERLRRQVKdeSQK 2096
Cdd:COG1196 161 IEEAagisKYKERKEEAE-----RKLEATEENLERLEDILGELERQLEPLERQAEKAeryrelKEELKELEAELL--LLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2097 KREAEEELKRKVQAEKDAAREKQRAMEDLQKfrSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKT 2176
Cdd:COG1196 234 LRELEAELEELEAELEELEAELEELEAELAE--LEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2177 AQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDA 2256
Cdd:COG1196 312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2257 EREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESgeqqrllLEEELFRLKNEVNEAIQK 2336
Cdd:COG1196 392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-------AAEEEAELEEEEEALLEL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2337 RKKMEEELAKVRAEMEILLESKSRAeeesrsnteKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQ---IAEGEAAR 2413
Cdd:COG1196 465 LAELLEEAALLEAALAELLEELAEA---------AARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGavaVLIGVEAA 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2414 QRAEAERILKEKLAAINEATRLKTEAEIALkEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKII--LLKKSSDN 2491
Cdd:COG1196 536 YEAALEAALAAALQNIVVEDDEVAAAAIEY-LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVasDLREADAR 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2492 ELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASsgksdLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRK 2571
Cdd:COG1196 615 YYVLGDTLLGRTLVAARLEAALRRAVTLAGRLRE-----VTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLA 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2572 EAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAI-VQQKEQ 2650
Cdd:COG1196 690 EEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLeELEREL 769
|
....*.
gi 1717010358 2651 EMLQTR 2656
Cdd:COG1196 770 ERLERE 775
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1942-2613 |
1.45e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.54 E-value: 1.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1942 KEEERRRLAEVEAQL--------EKQTQLaeahAKAKAQAEKeAEELqRRMQEEVSKREVVAvdAEQQKQTIQQELQQLR 2013
Cdd:COG1196 174 KEEAERKLEATEENLerledilgELERQL----EPLERQAEK-AERY-RELKEELKELEAEL--LLLKLRELEAELEELE 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2014 QnsdmEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDE 2093
Cdd:COG1196 246 A----ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2094 SQKKREAEEELKRKVQAEKDAAREKQRAmedlqkfrsQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFA 2173
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEA---------EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEAL 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2174 EKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQK 2253
Cdd:COG1196 393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEA 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2254 EDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELF---RLKNEV 2330
Cdd:COG1196 473 ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAAlaaALQNIV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2331 NEAIQKRKKMEEELAKVRAE-MEILLESKSRAEEESRSNTEKSKHMLEVE--ASKLRELAEEAARLRALSEEAKRQRQIA 2407
Cdd:COG1196 553 VEDDEVAAAAIEYLKAAKAGrATFLPLDKIRARAALAAALARGAIGAAVDlvASDLREADARYYVLGDTLLGRTLVAARL 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2408 EGEAARQRAEAERILKEKLAA--INEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILL 2485
Cdd:COG1196 633 EAALRRAVTLAGRLREVTLEGegGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2486 KKSSDNELERQknivedtlrqrriieeeirilklnfekassgksdlELELNQLKNIAEETHRSKEKAEQEAEKQRQLALE 2565
Cdd:COG1196 713 EEERLEEELEE-----------------------------------EALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2566 EEQRRKEAEEKVRKIladeqEAARQRK-----AALEEVERLKAKAEEAKRQKE 2613
Cdd:COG1196 758 EPPDLEELERELERL-----EREIEALgpvnlLAIEEYEELEERYDFLSEQRE 805
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2383-3043 |
1.68e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.15 E-value: 1.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2383 LRELAEEAA---RLRALSEEAKRQRqiaegEAARQR-AEAERILKEKLAAINeatRLKTEAEIALKEKEAENERLRRLAE 2458
Cdd:COG1196 157 RRAIIEEAAgisKYKERKEEAERKL-----EATEENlERLEDILGELERQLE---PLERQAEKAERYRELKEELKELEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2459 DEAYQRKLLEEQATQHKQDIEEKIILLKkssdnELERQKNIVEDTLRQrriieeeiriLKLNFEkassgksDLELELNQL 2538
Cdd:COG1196 229 LLLLKLRELEAELEELEAELEELEAELE-----ELEAELAELEAELEE----------LRLELE-------ELELELEEA 286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2539 KNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKE 2618
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEA 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2619 AERQIQLAQEAAFKKIEAEEKAHAAivQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQV 2698
Cdd:COG1196 367 LLEAEAELAEAEEELEELAEELLEA--LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEAL 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2699 EEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKV 2778
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2779 KLQLE---ETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIqmEELIKLKLRIEEENKMLIMKDKDSTQKFLAE 2855
Cdd:COG1196 525 AVAVLigvEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA--GRATFLPLDKIRARAALAAALARGAIGAAVD 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2856 EAEKMRQVAEEAARLsieAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQE 2935
Cdd:COG1196 603 LVASDLREADARYYV---LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2936 DKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERM 3015
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
650 660
....*....|....*....|....*...
gi 1717010358 3016 VVVQSLEiqrqqsgKEAEELRRAIAELE 3043
Cdd:COG1196 760 PDLEELE-------RELERLEREIEALG 780
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2247-2924 |
5.36e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 141.61 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2247 EEAEKQKEDAEREARKrakaeesALRQKELAEDELEKQRKLAdatAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRL 2326
Cdd:COG1196 196 GELERQLEPLERQAEK-------AERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2327 KNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHmlevEASKLRELAEEAARLRALSEEAKRQRQi 2406
Cdd:COG1196 266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE----LEERLEELEEELAELEEELEELEEELE- 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2407 aegEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLK 2486
Cdd:COG1196 341 ---ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2487 KSSDNELERQKNIVEdtlrqrriieeeirilklnfekassgksdLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEE 2566
Cdd:COG1196 418 RLEEELEELEEALAE-----------------------------LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2567 EQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEA-ERQIQLAQEAAFKKIEAEEKAHAAIV 2645
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGlAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2646 QQkeqemlqtrkqeksildKLKEEAERAKRAAEDAdyarmraeQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKL 2725
Cdd:COG1196 549 QN-----------------IVVEDDEVAAAAIEYL--------KAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2726 RKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTD 2805
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2806 AMRQKAQVEEELFKVKIQMEELiKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAE 2885
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEE-ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 1717010358 2886 DDLANQRALAEKMLKEK----MQAIQEATRLKAEADMLQKQKE 2924
Cdd:COG1196 763 EELERELERLEREIEALgpvnLLAIEEYEELEERYDFLSEQRE 805
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2116-3074 |
6.45e-33 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 141.89 E-value: 6.45e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2116 REKQRAMEDLQKFRSQAEeaerrMKQAEVEKERQIKVAQEVAQQSAA--AELNSKRMSFAEKTA--------QLELSLKQ 2185
Cdd:NF041483 6 RQESHRADDDHLSRFEAE-----MDRLKTEREKAVQHAEDLGYQVEVlrAKLHEARRSLASRPAydgadigyQAEQLLRN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2186 EHITVTHLQEEAERLKKQheeaekaREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQK-------EDAER 2258
Cdd:NF041483 81 AQIQADQLRADAERELRD-------ARAQTQRILQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQtveshvnENVAW 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2259 EARKRAKAEESALRQkeLAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGeqqrllleeelfrlknevneaiqkRK 2338
Cdd:NF041483 154 AEQLRARTESQARRL--LDESRAEAEQALAAARAEAERLAEEARQRLGSEAESA------------------------RA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2339 KMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAAR------------LRALSEEAKRQRQI 2406
Cdd:NF041483 208 EAEAILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRaaeqrmqeaeeaLREARAEAEKVVAE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2407 AEGEAARQRAEAE-------RILKEKLA-----AINEATRLKTEAEIALKEKEAENERLRRLAEDEAyQRKLLEEQATQH 2474
Cdd:NF041483 288 AKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAEALKAEAEQALADARAEAEKLVAEAAEKA-RTVAAEDTAAQL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2475 KQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKAS-----SGKSDLELELNQLKNIAEETHRSK 2549
Cdd:NF041483 367 AKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAeqlkgAAKDDTKEYRAKTVELQEEARRLR 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2550 EKAEQ-------EAEKQRQLALEE-----EQRRKEAEEKVRKILADEQE--------AARQRKAALEEVERLKAKAEEAK 2609
Cdd:NF041483 447 GEAEQlraeavaEGERIRGEARREavqqiEEAARTAEELLTKAKADADElrstataeSERVRTEAIERATTLRRQAEETL 526
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2610 rqkELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDAdYARMRAEQ 2689
Cdd:NF041483 527 ---ERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEA-LADARAEA 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2690 EAaLSRQQVEEAERMKQRAEEEAQA-KAQAQDEAEKLRKEAELEA-AKRAHAEQAALKQKQLADEEMDKHKKFAEKT--- 2764
Cdd:NF041483 603 ER-IRREAAEETERLRTEAAERIRTlQAQAEQEAERLRTEAAADAsAARAEGENVAVRLRSEAAAEAERLKSEAQESadr 681
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2765 LRQKAQVEQEltKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEElfKVKIQMEELI-KLKLRIEEENkmlim 2843
Cdd:NF041483 682 VRAEAAAAAE--RVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERE--RAREQSEELLaSARKRVEEAQ----- 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2844 kdkdSTQKFLAEEAEK----MRQVAEEAARLSIEAqeAARMRKLAEDDLANQRALAEKML-KEKMQAIQEATRLKAEAdm 2918
Cdd:NF041483 753 ----AEAQRLVEEADRrateLVSAAEQTAQQVRDS--VAGLQEQAEEEIAGLRSAAEHAAeRTRTEAQEEADRVRSDA-- 824
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2919 lQKQKELAQEQARKfqedkeqIEQQLAKETEGFQKSLEaerRQQLEITAEAERLKLQV--------LEMSKAQAKAEEDA 2990
Cdd:NF041483 825 -YAERERASEDANR-------LRREAQEETEAAKALAE---RTVSEAIAEAERLRSDAseyaqrvrTEASDTLASAEQDA 893
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2991 KKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEElRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQ 3070
Cdd:NF041483 894 ARTRADAREDANRIRSDAAAQADRLIGEATSEAERLTAEARAEA-ERLRDEARAEAERVRADAAAQAEQLIAEATGEAER 972
|
....
gi 1717010358 3071 LRQE 3074
Cdd:NF041483 973 LRAE 976
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
750-850 |
7.40e-33 |
|
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: 124.83 E-value: 7.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 829
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1717010358 830 EDVDVPQPDEKSIITYVSSLY 850
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2532-3135 |
7.42e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 141.23 E-value: 7.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2532 ELE--LNQLKNIAEETHRSKEKAEQEAEKQRQLALeeeQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAK 2609
Cdd:COG1196 197 ELErqLEPLERQAEKAERYRELKEELKELEAELLL---LKLRELEAELEELEAELEELEAELEELEAELAELEAELEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2610 RQKELAEKEAERQIQLAQEAAfKKIEAEEKAHAAiVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQ 2689
Cdd:COG1196 274 LELEELELELEEAQAEEYELL-AELARLEQDIAR-LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2690 EAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKA 2769
Cdd:COG1196 352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALA 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2770 QVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDST 2849
Cdd:COG1196 432 ELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2850 QKFLAEEAEKMRQV------AEEAARLSIEAQEAARMRKLAEDDLANQRALAEKmlkEKMQAIQEATRLkaEADMLQKQK 2923
Cdd:COG1196 512 AALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY---LKAAKAGRATFL--PLDKIRARA 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2924 ELAQEQARKFQEDKEQIEQQLAKEtegfqkslEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNK 3003
Cdd:COG1196 587 ALAAALARGAIGAAVDLVASDLRE--------ADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSA 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3004 LHQTELATKErmvvvQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQTTFL 3083
Cdd:COG1196 659 GGSLTGGSRR-----ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAE 733
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 3084 TEKHLLLEKEKYIEKEKAKLENLYEDEVRkaqklkQEQEHQLKQLEEEKQQL 3135
Cdd:COG1196 734 REELLEELLEEEELLEEEALEELPEPPDL------EELERELERLEREIEAL 779
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
753-854 |
1.76e-32 |
|
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: 123.53 E-value: 1.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 753 EKLLL-WSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 831
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1717010358 832 VDVPQPDEKSIITYVSSLYDAMP 854
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
629-733 |
2.03e-32 |
|
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: 125.54 E-value: 2.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 629 DERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLKHRQVK 707
Cdd:cd21316 48 DEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLKEQRVH 127
|
90 100
....*....|....*....|....*.
gi 1717010358 708 LVNIRNDDIADGNPKLTLGLIWTIIL 733
Cdd:cd21316 128 LENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2382-3205 |
2.85e-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: 139.42 E-value: 2.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2382 KLRELAEEAARLRALSEEAKR-QRQIAEGEAARQRAEAERILKEKLAA---INEATRLKTEAEIALKEKEAENERLRRLA 2457
Cdd:TIGR02168 204 SLERQAEKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAeeeLEELTAELQELEEKLEELRLEVSELEEEI 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2458 EDeaYQRKLLEeqATQHKQDIEEKIILLKKSSDNeLERQKNIVEDTLrqrriieeeirilklnfEKASSGKSDLELELNQ 2537
Cdd:TIGR02168 284 EE--LQKELYA--LANEISRLEQQKQILRERLAN-LERQLEELEAQL-----------------EELESKLDELAEELAE 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2538 LKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVrkiladeQEAARQRKAALEEVERLKAKAEEAKRQKELAEK 2617
Cdd:TIGR02168 342 LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL-------ETLRSKVAQLELQIASLNNEIERLEARLERLED 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2618 EAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQeksiLDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQ 2697
Cdd:TIGR02168 415 RRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE----LERLEEALEELREELEEAEQALDAAERELAQLQAR 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2698 VEEAERMKQRAEEEAQAKAQAQDEAEKL---------------RKEAELEAAKRAHAEQAALKQKQLADEEMDkhkkfae 2762
Cdd:TIGR02168 491 LDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlselisvdeGYEAAIEAALGGRLQAVVVENLNAAKKAIA------- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2763 ktlrqkAQVEQELTKVKLqLEETDhqktLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLrieeeNKMLI 2842
Cdd:TIGR02168 564 ------FLKQNELGRVTF-LPLDS----IKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLL-----GGVLV 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2843 MKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEkmLKEKMQAIQEATR-LKAEADMLQK 2921
Cdd:TIGR02168 628 VDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEE--LEEKIEELEEKIAeLEKALAELRK 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2922 QKELAQEQARKFQEDKEQIEQQLAketeGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEdakkfkkqaedfg 3001
Cdd:TIGR02168 706 ELEELEEELEQLRKELEELSRQIS----ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE------------- 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3002 nKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAeLLQKNSQEMQVAQQEQLRQETQVLQTT 3081
Cdd:TIGR02168 769 -RLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA-ANLRERLESLERRIAATERRLEDLEEQ 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3082 FLTEKHLLLEKEKYIEKEKAKLENLyEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELH 3161
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
810 820 830 840
....*....|....*....|....*....|....*....|....
gi 1717010358 3162 QLDKRRQEQEKLLADENRKLREKlEQLEEEHRIALAQTREMMIQ 3205
Cdd:TIGR02168 926 QLELRLEGLEVRIDNLQERLSEE-YSLTLEEAEALENKIEDDEE 968
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
627-738 |
3.60e-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: 3.60e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 627 AED-ERDRVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLKH 703
Cdd:cd21311 7 AEDaQWKRIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEE 86
|
90 100 110
....*....|....*....|....*....|....*.
gi 1717010358 704 RQ-VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 738
Cdd:cd21311 87 DEgIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1901-2724 |
4.99e-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: 138.65 E-value: 4.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1901 QEYVDLRTRYSELT-TLTSQYIKFITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEkqtqlaeAHAKAKAQAEKEAEE 1979
Cdd:TIGR02168 213 ERYKELKAELRELElALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1980 LQRRMQEEVSKREvvavDAEQQKQTIQQELQQLRQNsdmeIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAE 2059
Cdd:TIGR02168 286 LQKELYALANEIS----RLEQQKQILRERLANLERQ----LEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2060 DELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRM 2139
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2140 KQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLeLSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKEL- 2218
Cdd:TIGR02168 438 LQAELEELEEELEELQEELERLEEALEELREELEEAEQAL-DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQs 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2219 ----------------EKWHQKANEALRLRLQAEEVahkktlaqEEAEKQKED----AEREARKRAKAEESALRQKELAE 2278
Cdd:TIGR02168 517 glsgilgvlselisvdEGYEAAIEAALGGRLQAVVV--------ENLNAAKKAiaflKQNELGRVTFLPLDSIKGTEIQG 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2279 DELEkqrkladATAQQKFSAEQELIRLKADTEsgEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESK 2358
Cdd:TIGR02168 589 NDRE-------ILKNIEGFLGVAKDLVKFDPK--LRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGG 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2359 SRAEEESRSNTEkskhMLEVEaSKLRELAEEAARLRALSEEAKRQRQiaegEAARQRAEAERILKEKLAAINEATRLKTE 2438
Cdd:TIGR02168 660 VITGGSAKTNSS----ILERR-REIEELEEKIEELEEKIAELEKALA----ELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2439 AEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKkssdnELERQKNIVEDTLRQrriieeeiriLK 2518
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA-----EAEAEIEELEAQIEQ----------LK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2519 LNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKI---LADEQEAARQRKAAL 2595
Cdd:TIGR02168 796 EELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLaaeIEELEELIEELESEL 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2596 EEVERLKAKAEEAKRQKELAEKEAERQIQlAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEE----AE 2671
Cdd:TIGR02168 876 EALLNERASLEEALALLRSELEELSEELR-ELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEysltLE 954
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2672 RAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEK 2724
Cdd:TIGR02168 955 EAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTA 1007
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
737-852 |
5.70e-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: 122.64 E-value: 5.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 737 ISDIQvsgqSEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNV 816
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 817 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 852
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
634-737 |
6.27e-32 |
|
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: 122.40 E-value: 6.27e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 634 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLKHRQVKLVNI 711
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1717010358 712 RNDDIADGNPKLTLGLIWTIILHFQI 737
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
749-847 |
6.84e-32 |
|
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: 122.15 E-value: 6.84e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 749 MTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 828
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1717010358 829 PEDVDVPQPDEKSIITYVS 847
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| PTZ00034 |
PTZ00034 |
40S ribosomal protein S10; Provisional |
5-94 |
9.92e-32 |
|
40S ribosomal protein S10; Provisional
Pssm-ID: 173331 Cd Length: 124 Bit Score: 122.44 E-value: 9.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 5 MLMPLDQLRAIYELLFREGVMIAKKDkRPQSLHPEIkGVSNLQVIRAMGSLKSRGYVRETFVWRHFYWYLSNEGIVYLRQ 84
Cdd:PTZ00034 2 VYVPKANRKAIYRYLFKEGVIVCKKD-PKGPWHPEL-NVPNLHVMMLMRSLKSRGLVKEQFAWQHYYYYLTDEGIEYLRT 79
|
90
....*....|
gi 1717010358 85 YLHLPPEIVP 94
Cdd:PTZ00034 80 YLHLPPDVFP 89
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1481-1558 |
1.01e-31 |
|
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: 120.40 E-value: 1.01e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 1481 LSWQYLIRDIQQIQSWSLIMFRTMKPEDYKQALRNLETHYQEFMRDLPGLRELPADDRMQMEREYNNCIQKYEQLLRT 1558
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
634-737 |
1.19e-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: 121.27 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 634 VQKKTFTKWVNKHLIKAQR-HVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLKHRQVKLVNIR 712
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1717010358 713 NDDIADGNPKLTLGLIWTIILHFQI 737
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
753-855 |
2.21e-31 |
|
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: 120.80 E-value: 2.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 753 EKLLL-WSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN-LENLDQAFNVAERDLGVTRLLDPE 830
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1717010358 831 DVDVPQPDEKSIITYVSSLYDAMPR 855
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2027-2911 |
4.06e-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: 132.49 E-value: 4.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2027 IEEA----EYNRRKIEEEihivrLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAErLRRQVKDES-----QKK 2097
Cdd:TIGR02168 161 FEEAagisKYKERRKETE-----RKLERTRENLDRLEDILNELERQLKSLERQAEKAERYKE-LKAELRELElallvLRL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2098 REAEEELKRKVQAEKDAAREKQRAMEDLQKfrSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTA 2177
Cdd:TIGR02168 235 EELREELEELQEELKEAEEELEELTAELQE--LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2178 QLELSLKQehitvthLQEEAERLKKQheeaekaREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAE 2257
Cdd:TIGR02168 313 NLERQLEE-------LEAQLEELESK-------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2258 REARKRAKAEESALRQKELAEDELEKQRKladataqQKFSAEQELIRLKADTESgeqqrlLLEEELFRLKNEVNEAIQKR 2337
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEA-------RLERLEDRRERLQQEIEE------LLKKLEEAELKELQAELEEL 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2338 KKMEEELAKVRAEMEILLESKSRAEEESRsntekskhmlEVEASKLRELAEEAARLRALseEAKRQRQIAEGEAARQRAE 2417
Cdd:TIGR02168 446 EEELEELQEELERLEEALEELREELEEAE----------QALDAAERELAQLQARLDSL--ERLQENLEGFSEGVKALLK 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2418 AERILKEKLAAINEATRLKTEAEIALkekeaenerlrrlaedEAYQRKLLEEQATQHKQDIEEKIILLKKssdNELERQK 2497
Cdd:TIGR02168 514 NQSGLSGILGVLSELISVDEGYEAAI----------------EAALGGRLQAVVVENLNAAKKAIAFLKQ---NELGRVT 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2498 NIVEDTLRQRRIIEEEIRILKlNFEKASSGKSDLELELNQLK--------------NIAEETHRSKEKAEQE-------- 2555
Cdd:TIGR02168 575 FLPLDSIKGTEIQGNDREILK-NIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdDLDNALELAKKLRPGYrivtldgd 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2556 -----------AEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKElaekEAERQIQ 2624
Cdd:TIGR02168 654 lvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE----ELSRQIS 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2625 lAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQ---EAALSRQQVEEA 2701
Cdd:TIGR02168 730 -ALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQlkeELKALREALDEL 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2702 ERMKQRAEEEAQAKAQAQDEAEKLRKEAE-----LEAAKRAHAEQAALKQKQLADEE--MDKHKKFAEKTLRQKAQVEQE 2774
Cdd:TIGR02168 809 RAELTLLNEEAANLRERLESLERRIAATErrledLEEQIEELSEDIESLAAEIEELEelIEELESELEALLNERASLEEA 888
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2775 LTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKlklRIEEENKMLIMKDKDSTQKFLA 2854
Cdd:TIGR02168 889 LALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQE---RLSEEYSLTLEEAEALENKIED 965
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2855 EEAEKMRQVAE---EAARL------SIEAQEAARMRKlaeDDLANQRALAEKMLKEKMQAIQEATR 2911
Cdd:TIGR02168 966 DEEEARRRLKRlenKIKELgpvnlaAIEEYEELKERY---DFLTAQKEDLTEAKETLEEAIEEIDR 1028
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
630-739 |
4.25e-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: 117.30 E-value: 4.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 630 ERDRVQKKTFTKWVNKHLIKAQR--HVTDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLKHRQ 705
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1717010358 706 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 739
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
755-850 |
6.97e-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: 116.29 E-value: 6.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 755 LLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED-VD 833
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1717010358 834 VPQPDEKSIITYVSSLY 850
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2025-2836 |
7.60e-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: 131.72 E-value: 7.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2025 KKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEdELQELRARAEEAER-----QKKAAQEEAERLRRQVKDESQKKRE 2099
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAE-RYKELKAELRELELallvlRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2100 AEEELKR---KVQAEKDAAREKQRAMEDLQK-FRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAA-AELNSKRMSFAE 2174
Cdd:TIGR02168 258 LTAELQEleeKLEELRLEVSELEEEIEELQKeLYALANEISRLEQQKQILRERLANLERQLEELEAQlEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2175 KTAQLELSLKQehitvthLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKE 2254
Cdd:TIGR02168 338 ELAELEEKLEE-------LKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLE 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2255 DAEREaRKRAKAEESALRqKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESgeqqrllleeelfrLKNEVNEAI 2334
Cdd:TIGR02168 411 RLEDR-RERLQQEIEELL-KKLEEAELKELQAELEELEEELEELQEELERLEEALEE--------------LREELEEAE 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2335 QKRKKMEEELAKVRAEMEILLESKSRAEEESRS--NTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQR-QIAEGEA 2411
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRlQAVVVEN 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2412 ARQRAEAERILKEklaaiNEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLeeqatqhkqDIEEKIILLKKSSDN 2491
Cdd:TIGR02168 555 LNAAKKAIAFLKQ-----NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAK---------DLVKFDPKLRKALSY 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2492 ELERQKnIVED---TLRQRRIIEEEIRILKLNFEKASSG----KSDLELELNQL---KNIAEETHRSKEKAEQEAEKQRQ 2561
Cdd:TIGR02168 621 LLGGVL-VVDDldnALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTNSSILerrREIEELEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2562 LAlEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAH 2641
Cdd:TIGR02168 700 LA-ELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2642 AAIVQQKEQE-----MLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEE----AERMKQRAEEEA 2712
Cdd:TIGR02168 779 EAEAEIEELEaqieqLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDleeqIEELSEDIESLA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2713 QAKAQAQDEAEKLRKEAELEAAKRAHAEQA---ALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETdhqK 2789
Cdd:TIGR02168 859 AEIEELEELIEELESELEALLNERASLEEAlalLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGL---E 935
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1717010358 2790 TLLDDESQRLKEEVTDAMR-QKAQVEEELFKVKIQMEELIKLKLRIEE 2836
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKRLENKIKE 983
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
749-847 |
8.52e-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: 116.09 E-value: 8.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 749 MTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 828
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1717010358 829 PEDVDVPQPDEKSIITYVS 847
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2369-3203 |
1.36e-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: 130.86 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2369 TEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEA 2448
Cdd:pfam02463 144 IEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEE 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2449 ENERLRRLAEDEAYQRKLLEEQAT----------QHKQDIEEKIILLKKSSDNELERQKNIVEDtlrqrriieeeIRILK 2518
Cdd:pfam02463 224 EYLLYLDYLKLNEERIDLLQELLRdeqeeiesskQEIEKEEEKLAQVLKENKEEEKEKKLQEEE-----------LKLLA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2519 LNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQlalEEEQRRKEAEEKVRKILADEQEAARQRKAALEEV 2598
Cdd:pfam02463 293 KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKE---EIEELEKELKELEIKREAEEEEEEELEKLQEKLE 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2599 ERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAivQQKEQEMLQTRKQEKSILDKLKEEAERAKR-AA 2677
Cdd:pfam02463 370 QLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELA--RQLEDLLKEEKKEELEILEEEEESIELKQGkLT 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2678 EDADYARmraEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKH 2757
Cdd:pfam02463 448 EEKEELE---KQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2758 KKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLK--LRIE 2835
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEidPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2836 EENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAE 2915
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2916 ADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEdaKKFKK 2995
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRL--KKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2996 QAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQET 3075
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALEL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3076 QVLQTTFLTEKHLLLEKEKYIEKEKAKLENLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRH 3155
Cdd:pfam02463 843 KEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEER 922
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 3156 KQDELHQLDKRRQEQEKLL---ADENRKLREKLEQLEEEHRIALAQTREMM 3203
Cdd:pfam02463 923 IKEEAEILLKYEEEPEELLleeADEKEKEENNKEEEEERNKRLLLAKEELG 973
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1930-2806 |
1.76e-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: 130.48 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAE----KLKEEERRRLAEVEAQLEKQ----TQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQ 2001
Cdd:pfam02463 155 RLEIEEEAAGsrlkRKKKEALKKLIEETENLAELiidlEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2002 KQTIQQELQQLRQNSDMEIKSKAKKIEeaeynrrKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQE 2081
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIE-------KEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLER 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2082 EAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEvaqqsa 2161
Cdd:pfam02463 308 RKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKL------ 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2162 AAELNSKRMSFAEKTAQLELSLKQEhitVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHK 2241
Cdd:pfam02463 382 ESERLSSAAKLKEEELELKSEEEKE---AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQEL 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2242 KTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEE 2321
Cdd:pfam02463 459 KLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAV 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2322 ELFRLKNEVN---EAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSE 2398
Cdd:pfam02463 539 ENYKVAISTAvivEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADED 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2399 EAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDI 2478
Cdd:pfam02463 619 DKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQ 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2479 EEKIillKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEEThRSKEKAEQEAEK 2558
Cdd:pfam02463 699 LEIK---KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK-EEEKSELSLKEK 774
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2559 QRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEE 2638
Cdd:pfam02463 775 ELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEE 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2639 KAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADyARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQA 2718
Cdd:pfam02463 855 ELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKE-EKKELEEESQKLNLLEEKENEIEERIKEEAEILLKY 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2719 QDEAEKLRKEAELEAAK-RAHAEQAALKQKQLADEEMDKHKK----FAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLD 2793
Cdd:pfam02463 934 EEEPEELLLEEADEKEKeENNKEEEEERNKRLLLAKEELGKVnlmaIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE 1013
|
890
....*....|...
gi 1717010358 2794 DESQRLKEEVTDA 2806
Cdd:pfam02463 1014 ETCQRLKEFLELF 1026
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
735-852 |
4.58e-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: 114.80 E-value: 4.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 735 FQISDIQVsgqsEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAF 814
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1717010358 815 NVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 852
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
633-735 |
9.29e-29 |
|
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: 113.34 E-value: 9.29e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 633 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLKHRQVKLV 709
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1717010358 710 NIRNDDIADGNPKLTLGLIWTIILHF 735
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
737-852 |
6.27e-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: 111.33 E-value: 6.27e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 737 ISDIQVsgqsEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNV 816
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 817 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 852
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
753-852 |
7.03e-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: 110.45 E-value: 7.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 753 EKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED- 831
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1717010358 832 VDVPQPDEKSIITYVSSLYDA 852
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2017-2951 |
2.32e-27 |
|
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: 123.54 E-value: 2.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2017 DMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELraraeeaerQKKAAQEEAERLRRQVKDESQK 2096
Cdd:pfam02463 168 KRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLK---------EKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2097 KREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKT 2176
Cdd:pfam02463 239 IDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2177 AQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREeaekeLEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDA 2256
Cdd:pfam02463 319 SEKEKKKAEKELKKEKEEIEELEKELKELEIKREAE-----EEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLK 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2257 EREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKfSAEQELIRLKadtesgeqqrllleeelFRLKNEVNEAIQK 2336
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEIL-EEEEESIELK-----------------QGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2337 RKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIaeGEAARQRA 2416
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRII--SAHGRLGD 533
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2417 EAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQ 2496
Cdd:pfam02463 534 LGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATL 613
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2497 KNIVEDTLRQRRIIEEEIRILKLNFEKAssgKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEK 2576
Cdd:pfam02463 614 EADEDDKRAKVVEGILKDTELTKLKESA---KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELA 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2577 VRKILADEQEAARQRKAALEEVERLKakaEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKahaaivqqkeqemlqtr 2656
Cdd:pfam02463 691 KEEILRRQLEIKKKEQREKEELKKLK---LEAEELLADRVQEAQDKINEELKLLKQKIDEEEE----------------- 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2657 KQEKSILDKLKEEAERAKRAAEDADYARMRAEQEaaLSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKR 2736
Cdd:pfam02463 751 EEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE--KLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEE 828
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2737 AHAEQAALKQKQLADEEMDKHKKFAEKTLRqkaqvEQELTKVKLQLEETDHQKTLLDDESQRLKEEvtdamrQKAQVEEE 2816
Cdd:pfam02463 829 KIKEEELEELALELKEEQKLEKLAEEELER-----LEEEITKEELLQELLLKEEELEEQKLKDELE------SKEEKEKE 897
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2817 LFKVKIQmEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEddlanQRALAE 2896
Cdd:pfam02463 898 EKKELEE-ESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRL-----LLAKEE 971
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2897 KMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGF 2951
Cdd:pfam02463 972 LGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELF 1026
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2590-3201 |
3.25e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.33 E-value: 3.25e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2590 QRKAALEEVERLKAKAEE---AKRQKELAEKEAERQIQLAQEA---AFKKIEAEEKAHAAIVQQKEqemlqTRKQEKSIL 2663
Cdd:PTZ00121 1061 EAKAHVGQDEGLKPSYKDfdfDAKEDNRADEATEEAFGKAEEAkktETGKAEEARKAEEAKKKAED-----ARKAEEARK 1135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2664 DKLKEEAERAKRAAEDADYARMRAEQEA--ALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKeaeLEAAKRAHAEQ 2741
Cdd:PTZ00121 1136 AEDARKAEEARKAEDAKRVEIARKAEDArkAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARK---AEAARKAEEER 1212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2742 AALKQKQLADEEMDKHKKFAEKTlRQKAQVEQELTKVKLQLEETDHQKTLLDD----------ESQRLKEEVTDAMRQKA 2811
Cdd:PTZ00121 1213 KAEEARKAEDAKKAEAVKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHfarrqaaikaEEARKADELKKAEEKKK 1291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2812 QVEEELFKVKIQMEElikLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAArlsiEAQEAARMRKLAEDDLANQ 2891
Cdd:PTZ00121 1292 ADEAKKAEEKKKADE---AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAA----EAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2892 RALAEKMLKEKMQAIQEATRLKAE----ADMLQKQKELAQEQA---RKFQEDKEQIE------QQLAKETEGFQKSLEAE 2958
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADAAKKKAEekkkADEAKKKAEEDKKKAdelKKAAAAKKKADeakkkaEEKKKADEAKKKAEEAK 1444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2959 RRQQLEITAE----AERLKLQVLEMSKA---QAKAEE--DAKKFKKQAEDFGNKLHQTELATKERMvvvQSLEIQRQQSG 3029
Cdd:PTZ00121 1445 KADEAKKKAEeakkAEEAKKKAEEAKKAdeaKKKAEEakKADEAKKKAEEAKKKADEAKKAAEAKK---KADEAKKAEEA 1521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3030 KEAEELRRAIAEL---EHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEKAKLENL 3106
Cdd:PTZ00121 1522 KKADEAKKAEEAKkadEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLY 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3107 YEDEVRKAQKLKQEQE-----HQLKQLEEEKQQLKASMGEAMKKQKEAEEsVRHKQDElhqlDKRRQEQEKLLADENRKL 3181
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEakikaEELKKAEEEKKKVEQLKKKEAEEKKKAEE-LKKAEEE----NKIKAAEEAKKAEEDKKK 1676
|
650 660
....*....|....*....|
gi 1717010358 3182 REKLEQLEEEHRIALAQTRE 3201
Cdd:PTZ00121 1677 AEEAKKAEEDEKKAAEALKK 1696
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1975-3064 |
4.33e-27 |
|
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: 122.59 E-value: 4.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1975 KEAEELQRRmQEEVSKREVVAVDAEQQKQTIQQELQQLrqnsdMEIKSKAKKIEEAEYNRRKIEEEIhivRLQLETmqkQ 2054
Cdd:pfam01576 2 RQEEEMQAK-EEELQKVKERQQKAESELKELEKKHQQL-----CEEKNALQEQLQAETELCAEAEEM---RARLAA---R 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2055 KASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQkKREAEEELKRKVQAEKDAAREKQRAMED---------- 2124
Cdd:pfam01576 70 KQELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE-QLDEEEAARQKLQLEKVTTEAKIKKLEEdillledqns 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2125 -LQKFRSQAEEAERRMKQAEVEKERQIKVAQEV--AQQSAAAELnSKRMSFAEKTAQLELSLKQEhitvthLQEEAERLK 2201
Cdd:pfam01576 149 kLSKERKLLEERISEFTSNLAEEEEKAKSLSKLknKHEAMISDL-EERLKKEEKGRQELEKAKRK------LEGESTDLQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2202 KQHEEAEKAREEAEKELEKwhqKANEALRLRLQAEEVAHKKTLAQE---EAEKQ----KEDAEREARKRAKAEesalRQK 2274
Cdd:pfam01576 222 EQIAELQAQIAELRAQLAK---KEEELQAALARLEEETAQKNNALKkirELEAQiselQEDLESERAARNKAE----KQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2275 ELAEDELEKQR-----KLADATAQQKFSA--EQELIRLKADTESgeqqrllleeELFRLKNEVNEAIQKRKKMEEELAkv 2347
Cdd:pfam01576 295 RDLGEELEALKteledTLDTTAAQQELRSkrEQEVTELKKALEE----------ETRSHEAQLQEMRQKHTQALEELT-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2348 raemEILLESKsraeeESRSNTEKSKHMLEVEASKLrelaeeAARLRALSEeakrqrqiAEGEAARQRAEAERILKEKLA 2427
Cdd:pfam01576 363 ----EQLEQAK-----RNKANLEKAKQALESENAEL------QAELRTLQQ--------AKQDSEHKRKKLEGQLQELQA 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2428 AINEATRLKTEAEIALKEKEAENERLRR-LAEDEAYQRKLLEEQAT--QHKQDIEEKIillkkssdNELERQKNIVEDTL 2504
Cdd:pfam01576 420 RLSESERQRAELAEKLSKLQSELESVSSlLNEAEGKNIKLSKDVSSleSQLQDTQELL--------QEETRQKLNLSTRL 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2505 RQrriieeeirilklnfekassgksdLELELNQLKNIAEETHRSKEKAEQEAEK-QRQLA-----LEEEQRRKEAEEKVR 2578
Cdd:pfam01576 492 RQ------------------------LEDERNSLQEQLEEEEEAKRNVERQLSTlQAQLSdmkkkLEEDAGTLEALEEGK 547
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2579 KILADEQEAARQRkaaLEEVERLKAKAEEAKR--QKEL----AEKEAERQIQLAQEAAFKKIE---AEEKAHAA-IVQQK 2648
Cdd:pfam01576 548 KRLQRELEALTQQ---LEEKAAAYDKLEKTKNrlQQELddllVDLDHQRQLVSNLEKKQKKFDqmlAEEKAISArYAEER 624
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2649 EQEMLQTRKQEKSILdKLKEEAERAKRAAEDADYAR--MRAEQEAALSRQ-----QVEEAERMKQRAEEEAQA-KAQAQD 2720
Cdd:pfam01576 625 DRAEAEAREKETRAL-SLARALEEALEAKEELERTNkqLRAEMEDLVSSKddvgkNVHELERSKRALEQQVEEmKTQLEE 703
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2721 --------EAEKLRKEAELEAAKRAHAeqaalKQKQLADEEMDKHKKFAEKTLRqkaQVEQELTKVKLQLEETDHQKTLL 2792
Cdd:pfam01576 704 ledelqatEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRRQLVKQVR---ELEAELEDERKQRAQAVAAKKKL 775
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2793 DDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMrQVAEEAARLSI 2872
Cdd:pfam01576 776 ELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKNLEAELL-QLQEDLAASER 854
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2873 EAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQ 2952
Cdd:pfam01576 855 ARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQ 934
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2953 KSLEAerRQQLEITAEAERLKLQVLE----------MSKAQAK---AEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQ 3019
Cdd:pfam01576 935 KSESA--RQQLERQNKELKAKLQEMEgtvkskfkssIAALEAKiaqLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVE 1012
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*
gi 1717010358 3020 SLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQ 3064
Cdd:pfam01576 1013 DERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANAARRKLQ 1057
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1930-2783 |
4.67e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 122.63 E-value: 4.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEEERRRlaeVEAQLEKQTQLAEAHAKAK---AQAEKEAEELQRRMQEEVSKREVVAVD-AEQQKQTI 2005
Cdd:NF041483 446 RGEAEQLRAEAVAEGERIR---GEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERVRTEAIErATTLRRQA 522
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2006 QQELQQLRQNSDmeiKSKAKKIEEAEYNRRKIEEEIHIVRLQLE-TMQKQKASAEDELQELRARAEE----AERQKKAAQ 2080
Cdd:NF041483 523 EETLERTRAEAE---RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErltaAEEALADAR 599
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2081 EEAERLRRQVKDESQKKR-EAEEELKR-KVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMK-QAEVEKERQIKVAQEVA 2157
Cdd:NF041483 600 AEAERIRREAAEETERLRtEAAERIRTlQAQAEQEAERLRTEAAADASAARAEGENVAVRLRsEAAAEAERLKSEAQESA 679
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2158 QQSAaaelnskrmsfAEKTAQLELSLKQEHITVTHLQEEAERLKKQheeaekareeAEKELEKWHQKAN-EALRLRLQAE 2236
Cdd:NF041483 680 DRVR-----------AEAAAAAERVGTEAAEALAAAQEEAARRRRE----------AEETLGSARAEADqERERAREQSE 738
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2237 EVahkktLAQeeAEKQKEDAEREARKRakAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTEsgeqqr 2316
Cdd:NF041483 739 EL-----LAS--ARKRVEEAQAEAQRL--VEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAE------ 803
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2317 llleeelfrlknevNEAIQKRKKMEEELAKVR----AEMEILLESKSRAEEESRSNTEKSKHMLE-------VEASKLR- 2384
Cdd:NF041483 804 --------------HAAERTRTEAQEEADRVRsdayAERERASEDANRLRREAQEETEAAKALAErtvseaiAEAERLRs 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2385 ELAEEAARLRAlseEAKRQRQIAEGEAARQRAEAE----RILKEklaAINEATRLKTEAeialkekEAENERLRRLAEDE 2460
Cdd:NF041483 870 DASEYAQRVRT---EASDTLASAEQDAARTRADARedanRIRSD---AAAQADRLIGEA-------TSEAERLTAEARAE 936
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2461 AYQ-RKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRilklnfEKASSGKSDLELELNQLK 2539
Cdd:NF041483 937 AERlRDEARAEAERVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIR------TEAERVKAEAAAEAERLR 1010
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2540 NIA-EETHRSKEKAEQEAEKQRQLALEE-EQRRKEAEEKVRKILADEQEAARQRKAALEeverlkakaEEAKRQKELAEK 2617
Cdd:NF041483 1011 TEArEEADRTLDEARKDANKRRSEAAEQaDTLITEAAAEADQLTAKAQEEALRTTTEAE---------AQADTMVGAARK 1081
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2618 EAERqiqLAQEAAFKKIEAEEKAHA------------AIVQQKEQEMLQTRkqeksILDKLKEEAERAKR-AAEDADYAR 2684
Cdd:NF041483 1082 EAER---IVAEATVEGNSLVEKARTdadellvgarrdATAIRERAEELRDR-----ITGEIEELHERARReSAEQMKSAG 1153
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2685 MRAEQEAALSRQQVEEAERMKQRAEEEAQAKA-----QAQDEAEKLRKEAELeaaKRAHAEQAALKQKQLADEE----MD 2755
Cdd:NF041483 1154 ERCDALVKAAEEQLAEAEAKAKELVSDANSEAskvriAAVKKAEGLLKEAEQ---KKAELVREAEKIKAEAEAEakrtVE 1230
|
890 900
....*....|....*....|....*...
gi 1717010358 2756 KHKKFAEKTLRQKAQVEQELTKVKLQLE 2783
Cdd:NF041483 1231 EGKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
737-852 |
5.74e-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: 108.66 E-value: 5.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 737 ISDIQVsgqsEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNV 816
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 817 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 852
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| COG5045 |
COG5045 |
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis]; |
5-112 |
1.66e-26 |
|
Ribosomal protein S10E [Translation, ribosomal structure and biogenesis];
Pssm-ID: 227378 Cd Length: 105 Bit Score: 106.55 E-value: 1.66e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 5 MLMPLDQLRAIYELLFREGVMIAKKDKRpQSLHPEIkGVSNLQVIRAMGSLKSRGYVRETFVWRHFYWYLSNEGIVYLRQ 84
Cdd:COG5045 1 MLVPKENRYKIHQRLFQKGVAVAKKDFN-LGKHREL-EIPNLHVIKAMQSLISYGYVKTIHVWRHSYYTLTPEGVEYLRE 78
|
90 100
....*....|....*....|....*...
gi 1717010358 85 YLHLPPEIVPGSLQRVRRPVAMviPARR 112
Cdd:COG5045 79 YLVLPDEGVPSTEAPAVSPTQR--PQRR 104
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
633-735 |
1.79e-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: 106.80 E-value: 1.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 633 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLKHRQVKLV 709
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1717010358 710 NIRNDDIADGNPKLTLGLIWTIILHF 735
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2663-3202 |
4.88e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 118.89 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2663 LDKLKEEAERAKRAAEDADYARmRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEqa 2742
Cdd:COG1196 202 LEPLERQAEKAERYRELKEELK-ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE-- 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2743 alkqkqladeemdkhkkfAEKTLRQKAQVEQELTKvklQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKI 2822
Cdd:COG1196 279 ------------------LELELEEAQAEEYELLA---ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2823 QMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEK 2902
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2903 MQAIQEATRLKAEADMLQKQKEL--AQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMS 2980
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEeeALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2981 KAQAKAEEDAKKFKKQAEDFGNKLHQTELA------TKERMVVVQSLEIQRQQSGkeAEELRRAIAELEHEKEKLKQEAE 3054
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAvligveAAYEAALEAALAAALQNIV--VEDDEVAAAAIEYLKAAKAGRAT 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3055 LLQKNSQEMQVAQQEQLRQETQ------------------------VLQTTFLTEKHLLLEKEKYIEKEKAKLENLYEDE 3110
Cdd:COG1196 576 FLPLDKIRARAALAAALARGAIgaavdlvasdlreadaryyvlgdtLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEG 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3111 VRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRKLREKLEQLEE 3190
Cdd:COG1196 656 GSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAERE 735
|
570
....*....|..
gi 1717010358 3191 EHRIALAQTREM 3202
Cdd:COG1196 736 ELLEELLEEEEL 747
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
1380-1446 |
9.84e-26 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 103.11 E-value: 9.84e-26
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 1380 QLKPRSaaHPVRGRMPLQAVCDYKQMEITVHKGDECVLLNNSQPYKWKVLNASGSESVVPSVCFLIP 1446
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
633-738 |
1.09e-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: 105.11 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 633 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLKHRQVKLV 709
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1717010358 710 NIRNDDIADGNPKLTLGLIWTIILHFQIS 738
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
737-852 |
1.45e-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: 1.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 737 ISDIQVsgqsEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNV 816
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 817 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 852
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
628-737 |
2.90e-25 |
|
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: 103.68 E-value: 2.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 628 EDERDRVQKKTFTKWVNKHLIKAQRHV--TDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLKHR 704
Cdd:cd21247 14 QEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTK 93
|
90 100 110
....*....|....*....|....*....|....
gi 1717010358 705 -QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 737
Cdd:cd21247 94 vPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
755-850 |
4.00e-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: 102.62 E-value: 4.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 755 LLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED-VD 833
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1717010358 834 VPQPDEKSIITYVSSLY 850
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2174-3195 |
5.58e-25 |
|
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: 115.66 E-value: 5.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2174 EKTAQLELSLKQEHITVTHLQEEAERLKKQheeaekareeAEKELEKWHQKanEALRLRLQA-----EEVAHKKTLAQEE 2248
Cdd:pfam01576 19 ERQQKAESELKELEKKHQQLCEEKNALQEQ----------LQAETELCAEA--EEMRARLAArkqelEEILHELESRLEE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2249 AEKQKEDAEREaRKRAKAEESALRQkELAEDELEKQR-KLADATAQQKFSAEQELIRLKADTESgeqQRLLLEEELFRLK 2327
Cdd:pfam01576 87 EEERSQQLQNE-KKKMQQHIQDLEE-QLDEEEAARQKlQLEKVTTEAKIKKLEEDILLLEDQNS---KLSKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2328 NEVNEAIQKRKKMEEELAKVRAEMEIL---LESKSRAEEESRSNTEKSKHMLEVEASKLRElaeeaarlralsEEAKRQR 2404
Cdd:pfam01576 162 SEFTSNLAEEEEKAKSLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQE------------QIAELQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2405 QIAEGEAARQRAEAEriLKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRklleEQATQHKQDIEEkiil 2484
Cdd:pfam01576 230 QIAELRAQLAKKEEE--LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGE---- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2485 lkkssdnELERQKNIVEDTLRQRRIIEEEirilklnfekassgKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLAL 2564
Cdd:pfam01576 300 -------ELEALKTELEDTLDTTAAQQEL--------------RSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2565 EE----------------------EQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQK-ELAEKEAER 2621
Cdd:pfam01576 359 EElteqleqakrnkanlekakqalESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRaELAEKLSKL 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2622 QIQLAQEAAFKKiEAEEKAHAAivqQKEQEMLQTRKQEKSildKLKEEAERAKRAAEdadyARMRA-EQEAALSRQQVEE 2700
Cdd:pfam01576 439 QSELESVSSLLN-EAEGKNIKL---SKDVSSLESQLQDTQ---ELLQEETRQKLNLS----TRLRQlEDERNSLQEQLEE 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2701 AERMKQRAEEEAQ-AKAQAQDEAEKLRKEAE----LEAAKRAHAEQAALKQKQLADEEMDKhkkfaEKTLRQKAQVEQEL 2775
Cdd:pfam01576 508 EEEAKRNVERQLStLQAQLSDMKKKLEEDAGtleaLEEGKKRLQRELEALTQQLEEKAAAY-----DKLEKTKNRLQQEL 582
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2776 TKVKLQLeetDHQKTL--------------LDDE---SQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEEN 2838
Cdd:pfam01576 583 DDLLVDL---DHQRQLvsnlekkqkkfdqmLAEEkaiSARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTN 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2839 KML------IMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDdlanqralAEKMLKEKMQAiqeatrL 2912
Cdd:pfam01576 660 KQLraemedLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATED--------AKLRLEVNMQA------L 725
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2913 KAEADM-LQKQKELAQEQARKFQEDKEQIEQQLakETEGFQKSLEAERRQQLEItaEAERLKLQVLEMSKAQAKAEEDAK 2991
Cdd:pfam01576 726 KAQFERdLQARDEQGEEKRRQLVKQVRELEAEL--EDERKQRAQAVAAKKKLEL--DLKELEAQIDAANKGREEAVKQLK 801
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2992 KFKKQAEDFGNKLHQTELATKErmVVVQSLEIQRQQSGKEAE--ELRRAIAELEHEKEKLKQE----AELLQKNSQEMQV 3065
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRDE--ILAQSKESEKKLKNLEAEllQLQEDLAASERARRQAQQErdelADEIASGASGKSA 879
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3066 AQQEQLRQETQVLQ-TTFLTEKHLLLEKEKYIEKEKAKLENLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGE--- 3141
Cdd:pfam01576 880 LQDEKRRLEARIAQlEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEmeg 959
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 3142 -AMKKQKEA----EESVRHKQDELHQLDKRRQEQEKLLADENRKLREKLEQLEEEHRIA 3195
Cdd:pfam01576 960 tVKSKFKSSiaalEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHA 1018
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
637-734 |
6.64e-25 |
|
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: 102.01 E-value: 6.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 637 KTFTKWVNKHLIKA-QRHVTDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLKHRQVKLVNIR 712
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1717010358 713 NDDIADGnPKLTLGLIWTIILH 734
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
753-853 |
3.52e-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: 99.85 E-value: 3.52e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 753 EKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPEDV 832
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1717010358 833 DVPQPDEKSIITYVSSLYDAM 853
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
750-850 |
4.04e-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: 99.81 E-value: 4.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDP 829
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 1717010358 830 EDVDVPQ-PDEKSIITYVSSLY 850
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
749-855 |
5.81e-24 |
|
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: 99.67 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 749 MTAKEKLLLWSQRMTESY-QGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVY--RQTNLENLDQAFNVAERDLGVTR 825
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1717010358 826 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 855
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2092-3000 |
5.81e-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: 112.37 E-value: 5.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2092 DESQKKREAEEELKRKVQAEK---DAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSK 2168
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAeliIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2169 RMSFAEKTA---QLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKAnEALRLRLQAEEVAHKKTLA 2245
Cdd:pfam02463 246 LRDEQEEIEsskQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2246 QEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQEliRLKADTESGEQQRLLLEEELFR 2325
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKK--LESERLSSAAKLKEEELELKSE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2326 LKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKrqrq 2405
Cdd:pfam02463 403 EEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQ---- 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2406 iaegEAARQRAEAERILKEKLAAINEATRLKTEaEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILL 2485
Cdd:pfam02463 479 ----LVKLQEQLELLLSRQKLEERSQKESKARS-GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEV 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2486 KKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQlkniaeethRSKEKAEQEAEKQRQLALE 2565
Cdd:pfam02463 554 SATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNL---------AQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2566 EEQRRKEAEEKVRKILADEQEAARQRKAALEE--VERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKahaa 2643
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEglAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE---- 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2644 ivqQKEQEMLQTRKQEKSILDKLKEEAERakraaedadyarmraeqeaalsrqQVEEAERMKQRAEEEAQAKAQAQDEAE 2723
Cdd:pfam02463 701 ---IKKKEQREKEELKKLKLEAEELLADR------------------------VQEAQDKINEELKLLKQKIDEEEEEEE 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2724 KLRKEAELEAAKRAHAEQaalKQKQLADEEMDKHKKFAEKTLRQ--KAQVEQELTKVKLQLEETDHQKTLLDDESQRLKE 2801
Cdd:pfam02463 754 KSRLKKEEKEEEKSELSL---KEKELAEEREKTEKLKVEEEKEEklKAQEEELRALEEELKEEAELLEEEQLLIEQEEKI 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2802 EVTDAMRQKAQVEEElfkvKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMR 2881
Cdd:pfam02463 831 KEEELEELALELKEE----QKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEES 906
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2882 KLAEddlanqrALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQ-----QLAKETEGFQKSLE 2956
Cdd:pfam02463 907 QKLN-------LLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEErnkrlLLAKEELGKVNLMA 979
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 1717010358 2957 AERRQQLEITAEAERLKLQVLEMSKA---QAKAEEDAKKFKKQAEDF 3000
Cdd:pfam02463 980 IEEFEEKEERYNKDELEKERLEEEKKkliRAIIEETCQRLKEFLELF 1026
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
750-854 |
8.87e-24 |
|
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: 98.71 E-value: 8.87e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYqGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 829
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1717010358 830 EDVDVPQPDEKSIITYVSSLYDAMP 854
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
634-737 |
1.28e-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: 98.51 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 634 VQKKTFTKWVNKHLIKAQRH--VTDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLKHRQ-VKLV 709
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1717010358 710 NIRNDDIADGNPKLTLGLIWTIILHFQI 737
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
751-850 |
1.57e-23 |
|
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: 98.40 E-value: 1.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 751 AKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPE 830
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1717010358 831 D-VDVPQPDEKSIITYVSSLY 850
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1942-2836 |
2.68e-23 |
|
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: 110.15 E-value: 2.68e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1942 KEEERRRLAEVEA----------QLEKQTQLAEAHAKaKAQAEKEAEELQRRMQEEVSKREVVAVDAE-QQKQTIQQELQ 2010
Cdd:TIGR02168 174 RKETERKLERTREnldrledilnELERQLKSLERQAE-KAERYKELKAELRELELALLVLRLEELREElEELQEELKEAE 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2011 QLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQ- 2089
Cdd:TIGR02168 253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKl 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2090 ------VKDESQKKREAEEELKRKVqaekdaarekqramEDLQKFRSQAEEAERRMKQAEVEKERQikvAQEVAQQSAAA 2163
Cdd:TIGR02168 333 delaeeLAELEEKLEELKEELESLE--------------AELEELEAELEELESRLEELEEQLETL---RSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2164 ELNSKRMSFAEKT-AQLELSLKQEHitvthlQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKK 2242
Cdd:TIGR02168 396 ASLNNEIERLEARlERLEDRRERLQ------QEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2243 TLAQEEAEKQKEDAEREARKRAKAEESALRQKElAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEE 2322
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLE-GFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQ 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2323 LFRLKNEvneaiQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKR 2402
Cdd:TIGR02168 549 AVVVENL-----NAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLG 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2403 QRQIAEgeaarQRAEAERILKEKLAAINEAT----RLKTEAEIALKEKEAENERLRRlaedeayQRKLleEQATQHKQDI 2478
Cdd:TIGR02168 624 GVLVVD-----DLDNALELAKKLRPGYRIVTldgdLVRPGGVITGGSAKTNSSILER-------RREI--EELEEKIEEL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2479 EEKIillkkssdNELERQKNIVEDTLRQrriieeeiriLKLNFEKASSGKSDLELELNQLKNiaeethrSKEKAEQEAEK 2558
Cdd:TIGR02168 690 EEKI--------AELEKALAELRKELEE----------LEEELEQLRKELEELSRQISALRK-------DLARLEAEVEQ 744
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2559 QRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEK---EAERQIQLAQEAAFKKIE 2635
Cdd:TIGR02168 745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREaldELRAELTLLNEEAANLRE 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2636 AEEKAHAAIVqQKEQEMLQTRKQeksiLDKLKEEAERAKRAAEDADYAR--MRAEQEAALSRQQVEEAERMKQRAEEEAQ 2713
Cdd:TIGR02168 825 RLESLERRIA-ATERRLEDLEEQ----IEELSEDIESLAAEIEELEELIeeLESELEALLNERASLEEALALLRSELEEL 899
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2714 AKAQAQDEAEKLRKEAELEAAkRAHAEQAALKQKQLADEEMDKHKKFAEktlrqKAQVEQELTKVKLQLEETDHQKtlLD 2793
Cdd:TIGR02168 900 SEELRELESKRSELRRELEEL-REKLAQLELRLEGLEVRIDNLQERLSE-----EYSLTLEEAEALENKIEDDEEE--AR 971
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2794 DESQRLKEEVT-------DAMRQKAQVEEELFKVKIQMEELIKLKLRIEE 2836
Cdd:TIGR02168 972 RRLKRLENKIKelgpvnlAAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1921-2733 |
1.34e-22 |
|
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: 107.85 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1921 IKFITETLCRLNVEEKAAEKLKEEeRRRLAEVEAQLEKQTQlaEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQ 2000
Cdd:TIGR02169 193 IDEKRQQLERLRREREKAERYQAL-LKEKREYEGYELLKEK--EALERQKEAIERQLASLEEELEKLTEEISELEKRLEE 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2001 QKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQkkaaQ 2080
Cdd:TIGR02169 270 IEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELERE----I 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2081 EEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKfrsQAEEAERRMKQAEVEKERQIKVAQEVAQQs 2160
Cdd:TIGR02169 346 EEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYRE---KLEKLKREINELKRELDRLQEELQRLSEE- 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2161 aAAELNSKRMSFAEKTAQLElslkqehitvTHLQEEAERLKKQheeaekareeaekeleKWHQKANEALRLRLQAEEVAH 2240
Cdd:TIGR02169 422 -LADLNAAIAGIEAKINELE----------EEKEDKALEIKKQ----------------EWKLEQLAADLSKYEQELYDL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2241 KKTLAQEEAE---KQKEDAEREARKRAKAEESalRQKELAEDELEKQRKLADATAQQkfsaeqeLIRLKADTESGEQQRL 2317
Cdd:TIGR02169 475 KEEYDRVEKElskLQRELAEAEAQARASEERV--RGGRAVEEVLKASIQGVHGTVAQ-------LGSVGERYATAIEVAA 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2318 LLEEELFRLKNEV--NEAIQ--KRKKMEE----ELAKVRAEMEIL----------------------------------- 2354
Cdd:TIGR02169 546 GNRLNNVVVEDDAvaKEAIEllKRRKAGRatflPLNKMRDERRDLsilsedgvigfavdlvefdpkyepafkyvfgdtlv 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2355 ---LESKSRAEEESRSNT------EKSKHM------LEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEaarqRAEAE 2419
Cdd:TIGR02169 626 vedIEAARRLMGKYRMVTlegelfEKSGAMtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSE----LRRIE 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2420 RILKEKLAAINEATR----LKTEAEIALKEKEAENERLRRLAED-EAYQRKLLEEQAtqhKQDIEEKIILLKKSSDNELE 2494
Cdd:TIGR02169 702 NRLDELSQELSDASRkigeIEKEIEQLEQEEEKLKERLEELEEDlSSLEQEIENVKS---ELKELEARIEELEEDLHKLE 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2495 RQKNIVEDTLRQRRIIEEEIRILKLNFEkassgKSDLELELNQLKNIAEETHRSKEKAEQE-AEKQRQLALEEEQR--RK 2571
Cdd:TIGR02169 779 EALNDLEARLSHSRIPEIQAELSKLEEE-----VSRIEARLREIEQKLNRLTLEKEYLEKEiQELQEQRIDLKEQIksIE 853
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2572 EAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKK--IEAEEKAHAAIVQQKE 2649
Cdd:TIGR02169 854 KEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKrkRLSELKAKLEALEEEL 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2650 QEMLQTRKQEKSI------LDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAE 2723
Cdd:TIGR02169 934 SEIEDPKGEDEEIpeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYE 1013
|
890
....*....|
gi 1717010358 2724 KLRKEAELEA 2733
Cdd:TIGR02169 1014 KKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2220-3063 |
1.65e-22 |
|
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: 107.45 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2220 KWHQKANEALRLRLQAEEVAHK-KTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAE-----DELEKQRKLADATAQ 2293
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEElEELTAELQELEEKLEELRLEVSELEEEIEELQKELYAlaneiSRLEQQKQILRERLA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2294 QkfsAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEillESKSRAEEesrsnteksk 2373
Cdd:TIGR02168 313 N---LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE---ELESRLEE---------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2374 hmleveaskLRELAEEAARLRAlseEAKRQRQIAEGEAARQRAEAERIlkeklaainEATRLKTEAEIALKEKEAENERL 2453
Cdd:TIGR02168 377 ---------LEEQLETLRSKVA---QLELQIASLNNEIERLEARLERL---------EDRRERLQQEIEELLKKLEEAEL 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2454 RRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKniVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLEL 2533
Cdd:TIGR02168 436 KELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDA--AERELAQLQARLDSLERLQENLEGFSEGVKALLK 513
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2534 ELNQLKNIaeeTHRSKEKAeqEAEKQRQLALEeeqrrKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKE 2613
Cdd:TIGR02168 514 NQSGLSGI---LGVLSELI--SVDEGYEAAIE-----AALGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKG 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2614 lAEKEAERQIQLAQEAAFKK-----IEAEEKAHAAIvqqkeQEMLQTRKQEKSI---LDKLKEEAERAKRAAED-----A 2680
Cdd:TIGR02168 584 -TEIQGNDREILKNIEGFLGvakdlVKFDPKLRKAL-----SYLLGGVLVVDDLdnaLELAKKLRPGYRIVTLDgdlvrP 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2681 DYARMRAEQEAALS----RQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDK 2756
Cdd:TIGR02168 658 GGVITGGSAKTNSSilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2757 HKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELiKLKLRIEE 2836
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTLLN 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2837 ENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEA 2916
Cdd:TIGR02168 817 EEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSEL 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2917 DMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKsLEAERRQQLEITAEAERLKLQVLEMSKA-----QAKAEEDAK 2991
Cdd:TIGR02168 897 EELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEEAEALENkieddEEEARRRLK 975
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2992 KFKKQAEDFG--NKLHQTEL-ATKERMvvvQSLEIQRQQSGKEAEELRRAIAELEHE-KEKLKQEAELLQKNSQEM 3063
Cdd:TIGR02168 976 RLENKIKELGpvNLAAIEEYeELKERY---DFLTAQKEDLTEAKETLEEAIEEIDREaRERFKDTFDQVNENFQRV 1048
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
750-848 |
1.74e-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: 92.30 E-value: 1.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYqglRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVY-RQTNLENLDQAFNVAERDLGVTRLLD 828
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1717010358 829 PEDVDVPQPDEKSIITYVSS 848
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 ... |
633-738 |
2.81e-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: 92.84 E-value: 2.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 633 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLKHRQVKLV 709
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1717010358 710 NIRNDDIADGNPKLTLGLIWTIILHFQIS 738
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2218-2976 |
3.03e-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: 103.22 E-value: 3.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2218 LEKWHQKANEALRLRLQAEEVAHKKTLAQ-EEAEKQKEDAERE-ARKRAKAEESALRQKELAEDELEKQRKLADATAQQK 2295
Cdd:TIGR02169 203 LRREREKAERYQALLKEKREYEGYELLKEkEALERQKEAIERQlASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2296 FSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHM 2375
Cdd:TIGR02169 283 DLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAEL 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2376 LEVEASKLRELAEEAARLRALSEEAKRQRQIAE----------------GEAARQRAEAERILKEKLAAINEA-TRLKTE 2438
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKDYREKLEklkreinelkreldrlQEELQRLSEELADLNAAIAGIEAKiNELEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2439 AEIALKEKEAENERLRRLAED-EAYQRKLLEEQATQhkQDIEEKIillkkssdNELERQKNIVEDTLRQRRIIEEEIRIL 2517
Cdd:TIGR02169 443 KEDKALEIKKQEWKLEQLAADlSKYEQELYDLKEEY--DRVEKEL--------SKLQRELAEAEAQARASEERVRGGRAV 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2518 KLNFEKASSGKSDLELEL----------------NQLKNIAEETHRSKEKAEQEAeKQRQLA---------LEEEQR--R 2570
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQLgsvgeryataievaagNRLNNVVVEDDAVAKEAIELL-KRRKAGratflplnkMRDERRdlS 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2571 KEAEEKVRKILADEQEAARQRKAA-------------LEEVERLKAKAEEAKRQKELAEKE------AERQIQLAQEAAF 2631
Cdd:TIGR02169 592 ILSEDGVIGFAVDLVEFDPKYEPAfkyvfgdtlvvedIEAARRLMGKYRMVTLEGELFEKSgamtggSRAPRGGILFSRS 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2632 KKIEAEEKAHAAIVQQKEQEMLQTRKQE-KSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEE 2710
Cdd:TIGR02169 672 EPAELQRLRERLEGLKRELSSLQSELRRiENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ 751
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2711 EAQAKAQAQD--EAEKLRKEAELEAAKrahAEQAALKQKqLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQ 2788
Cdd:TIGR02169 752 EIENVKSELKelEARIEELEEDLHKLE---EALNDLEAR-LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2789 KTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKlklriEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAA 2868
Cdd:TIGR02169 828 KEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEE-----ELEELEAALRDLESRLGDLKKERDELEAQLRELE 902
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2869 RLSIEAQEAARMRKLAEDDLANQRALAEKMLKE---KMQAIQEATRLKAEADMLQKQKELAQEQARKFQ-------EDKE 2938
Cdd:TIGR02169 903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEiedPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYE 982
|
810 820 830
....*....|....*....|....*....|....*...
gi 1717010358 2939 QIEQQLaKETEGFQKSLEAERRQQLEITAEAERLKLQV 2976
Cdd:TIGR02169 983 EVLKRL-DELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
633-738 |
3.24e-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: 92.46 E-value: 3.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 633 RVQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLKHRQVKLV 709
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1717010358 710 NIRNDDIADGNPKLTLGLIWTIILHFQIS 738
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1913-2816 |
1.93e-20 |
|
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: 100.63 E-value: 1.93e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1913 LTTLTSQYIKFITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQ---RRMQEEVS 1989
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQaalARLEEETA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1990 KREvvavDAEQQKQTIQQELQQLRQNSDMEIKSKAKkieeAEYNRRKIEEEIHIVRLQLETMQKQKASAedelQELRARA 2069
Cdd:pfam01576 258 QKN----NALKKIRELEAQISELQEDLESERAARNK----AEKQRRDLGEELEALKTELEDTLDTTAAQ----QELRSKR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2070 E-EAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKER 2148
Cdd:pfam01576 326 EqEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEH 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2149 QIKVAQEVAQ--QSAAAELNSKRMSFAEKTAQLELSLKqehiTVTHLQEEAE----RLKKQHEEAEKAREEAEKEL-EKW 2221
Cdd:pfam01576 406 KRKKLEGQLQelQARLSESERQRAELAEKLSKLQSELE----SVSSLLNEAEgkniKLSKDVSSLESQLQDTQELLqEET 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2222 HQKANEALRLRlQAEEVAHKKTLAQEEAEKQKEDAERE--------ARKRAKAEESALRQKELAEDELEKQRKLaDATAQ 2293
Cdd:pfam01576 482 RQKLNLSTRLR-QLEDERNSLQEQLEEEEEAKRNVERQlstlqaqlSDMKKKLEEDAGTLEALEEGKKRLQREL-EALTQ 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2294 QKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKS- 2372
Cdd:pfam01576 560 QLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRAl 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2373 --KHMLEvEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAaineatRLKTEAEIALKE-KEAE 2449
Cdd:pfam01576 640 slARALE-EALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRALEQQVE------EMKTQLEELEDElQATE 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2450 NERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERqknivEDTLRQRRIieeeirilklnfekASSGKS 2529
Cdd:pfam01576 713 DAKLRLEVNMQALKAQFERDLQARDEQGEEKRRQLVKQVRELEAEL-----EDERKQRAQ--------------AVAAKK 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2530 DLELELNQLKNIAEETHRSKEKAEQEAEKQrQLALEEEQRRKEAEEKVRK-ILADEQEAARQRKAALEEVERLKAKAEEA 2608
Cdd:pfam01576 774 KLELDLKELEAQIDAANKGREEAVKQLKKL-QAQMKDLQRELEEARASRDeILAQSKESEKKLKNLEAELLQLQEDLAAS 852
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2609 KRQKELAEKEA-ERQIQLAQEAAFKKIEAEEKAH-AAIVQQKEQEMlqtrKQEKSILDKLKEEAERAKRAAEDADyARMR 2686
Cdd:pfam01576 853 ERARRQAQQERdELADEIASGASGKSALQDEKRRlEARIAQLEEEL----EEEQSNTELLNDRLRKSTLQVEQLT-TELA 927
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2687 AEQEAAlsrQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEA--AKRAHAEQaalkqkQLADEEmdKHKKFAEKT 2764
Cdd:pfam01576 928 AERSTS---QKSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIAAleAKIAQLEE------QLEQES--RERQAANKL 996
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2765 LRQKaqvEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEE 2816
Cdd:pfam01576 997 VRRT---EKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEE 1045
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
754-851 |
2.02e-20 |
|
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: 89.33 E-value: 2.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 754 KLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD-PEDV 832
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1717010358 833 DVPQPDEKSIITYVSSLYD 851
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1940-2665 |
2.51e-20 |
|
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: 100.43 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1940 KLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQeevskreVVAVDAEQQKQTIQQELQQLrqnsdme 2019
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ-------LLTLCTPCMPDTYHERKQVL------- 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2020 iKSKAKKIEEAEYNRRKIEEEIHivrlQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQvkdesQKKRE 2099
Cdd:TIGR00618 225 -EKELKHLREALQQTQQSHAYLT----QKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRA-----RKAAP 294
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2100 AEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ- 2178
Cdd:TIGR00618 295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQq 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2179 --LELSLKQEHITVTHLQEEAERLKK--------QHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEe 2248
Cdd:TIGR00618 375 htLTQHIHTLQQQKTTLTQKLQSLCKeldilqreQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQC- 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2249 aEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQkfsaEQELIRLKADTESGEQQRLLLEEELFRLKN 2328
Cdd:TIGR00618 454 -EKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLE----LQEEPCPLCGSCIHPNPARQDIDNPGPLTR 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2329 EVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESrsntEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQiAE 2408
Cdd:TIGR00618 529 RMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM----QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE-KL 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2409 GEAARQRAEAERILKEKLA-AIN-----------------EATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQ 2470
Cdd:TIGR00618 604 SEAEDMLACEQHALLRKLQpEQDlqdvrlhlqqcsqelalKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2471 ATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEirilklnfekASSGKSDLELE---LNQLKNIAEETHR 2547
Cdd:TIGR00618 684 KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENA----------SSSLGSDLAARedaLNQSLKELMHQAR 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2548 SKEKAEQEAEKQRQLALEEEQRRKEAEEKVrkiladEQEAARQRKAALEEVERLKAKAEE--AKRQKELAEKEAErQIQL 2625
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHL------AAEIQFFNRLREEDTHLLKTLEAEigQEIPSDEDILNLQ-CETL 826
|
730 740 750 760
....*....|....*....|....*....|....*....|
gi 1717010358 2626 AQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDK 2665
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQ 866
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
750-849 |
3.27e-20 |
|
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: 88.69 E-value: 3.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDP 829
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1717010358 830 ED-VDVPQPDEKSIITYVSSL 849
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2528-3218 |
9.00e-20 |
|
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: 98.50 E-value: 9.00e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2528 KSDLELELNQLKNIAEETHRSKEKAEQEAEKQ-----RQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLK 2602
Cdd:TIGR00618 221 KQVLEKELKHLREALQQTQQSHAYLTQKREAQeeqlkKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2603 AKAE-EAKRQK---ELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKsildklKEEAERAKRAAE 2678
Cdd:TIGR00618 301 AVTQiEQQAQRihtELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHE------VATSIREISCQQ 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2679 DADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHK 2758
Cdd:TIGR00618 375 HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCE 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2759 KFAEKTLRQKAQ----VEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIqMEELIKLKLRI 2834
Cdd:TIGR00618 455 KLEKIHLQESAQslkeREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDN-PGPLTRRMQRG 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2835 EEENKMLIMKDKDsTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEkMQAIQEATRLKA 2914
Cdd:TIGR00618 534 EQTYAQLETSEED-VYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDL-TEKLSEAEDMLA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2915 EAdmLQKQKELAQEQARKFQedKEQIEQQLAKEtegFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFK 2994
Cdd:TIGR00618 612 CE--QHALLRKLQPEQDLQD--VRLHLQQCSQE---LALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQK 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2995 KQaedfgnklHQTELATKERMVVVQSLEIQRQQSGKEaEELRRAIAELEH----EKEKLKQEAELLQKNSQEMQVAQQEQ 3070
Cdd:TIGR00618 685 MQ--------SEKEQLTYWKEMLAQCQTLLRELETHI-EEYDREFNEIENasssLGSDLAAREDALNQSLKELMHQARTV 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3071 LRQETQVLQTTFLTEKHLLlekekyieKEKAKLENLyEDEVRKAQKLKQEQEHQLKQLEEEKQQlkasmgEAMKKQKEAE 3150
Cdd:TIGR00618 756 LKARTEAHFNNNEEVTAAL--------QTGAELSHL-AAEIQFFNRLREEDTHLLKTLEAEIGQ------EIPSDEDILN 820
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 3151 ESVRHKQDELHQLDKRRQEQEKLLAdENRKLREKLEQLEEEHRIALAQTREMMIQTDDLAGSSQTKAM 3218
Cdd:TIGR00618 821 LQCETLVQEEEQFLSRLEEKSATLG-EITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQ 887
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1933-2487 |
3.43e-19 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 97.13 E-value: 3.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1933 VEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKA-----KAQAEKEAEELQRRmQEEVSKREVVAVDAEQQKQTiqq 2007
Cdd:PTZ00121 1410 LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKAdeakkKAEEAKKAEEAKKK-AEEAKKADEAKKKAEEAKKA--- 1485
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2008 elQQLRQNSDmEIKSKAKKIEEAEYNRRKIEEeihivrlqLETMQKQKASAEDELQELRARAEEAER--QKKAAQE--EA 2083
Cdd:PTZ00121 1486 --DEAKKKAE-EAKKKADEAKKAAEAKKKADE--------AKKAEEAKKADEAKKAEEAKKADEAKKaeEKKKADElkKA 1554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2084 ERLRR--QVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSA 2161
Cdd:PTZ00121 1555 EELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKK 1634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2162 AAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHK 2241
Cdd:PTZ00121 1635 VEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEE 1714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2242 KTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRkladaTAQQKFSAEQELIRLKADTESgeqqrlllee 2321
Cdd:PTZ00121 1715 KKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEA---------- 1779
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2322 elfRLKNEVNEAIQKRKKMEEELAK-VRAEMEILLESksraeeeSRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEA 2400
Cdd:PTZ00121 1780 ---VIEEELDEEDEKRRMEVDKKIKdIFDNFANIIEG-------GKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAF 1849
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2401 KRQRQIAEGEAARQ-----RAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHK 2475
Cdd:PTZ00121 1850 EKHKFNKNNENGEDgnkeaDFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIPNNNMAGKNNDIIDDKLDKDEYIKRDA 1929
|
570
....*....|..
gi 1717010358 2476 QDIEEKIILLKK 2487
Cdd:PTZ00121 1930 EETREEIIKISK 1941
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2017-2870 |
3.69e-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: 3.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2017 DMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEdELQELRARAEEAERQKKAAQ-EEAERLRRQVKDESQ 2095
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGYELLKEkEALERQKEAIERQLA 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2096 KKREAEEELKRKVQAEKDAAREKQRAMEDL-QKFRSQAEEAERRMK------QAEVEK-ERQIKVAQEVAQQSAA--AEL 2165
Cdd:TIGR02169 248 SLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKekigelEAEIASlERSIAEKERELEDAEErlAKL 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2166 NSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHeeaekareeaekelekwhqkanEALRLRLQAEEVAHKKTLA 2245
Cdd:TIGR02169 328 EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL----------------------EDLRAELEEVDKEFAETRD 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2246 QEEAEKQKEDAEREARkrakaEESALRQKELAEDELEKQRKLADATAQQKfSAEQELIRLKADTESGEQqrllleeelfr 2325
Cdd:TIGR02169 386 ELKDYREKLEKLKREI-----NELKRELDRLQEELQRLSEELADLNAAIA-GIEAKINELEEEKEDKAL----------- 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2326 lknEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRsntEKSKHMLEVEASKlRELAEEAARLRALSEEAKRQRQ 2405
Cdd:TIGR02169 449 ---EIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELS---KLQRELAEAEAQA-RASEERVRGGRAVEEVLKASIQ 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2406 -----IAE-GEAARQRAEA-ERILKEKLAAINEATRLKTEAEIA-LKEKEAENER---LRRLAEDEAYQRKLLEEQATQH 2474
Cdd:TIGR02169 522 gvhgtVAQlGSVGERYATAiEVAAGNRLNNVVVEDDAVAKEAIElLKRRKAGRATflpLNKMRDERRDLSILSEDGVIGF 601
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2475 KQDIEEkiillkksSDNELERQ-KNIVEDTLRQRRIIEEEIRILKLN--------FEK-------------ASSGKSDLE 2532
Cdd:TIGR02169 602 AVDLVE--------FDPKYEPAfKYVFGDTLVVEDIEAARRLMGKYRmvtlegelFEKsgamtggsraprgGILFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2533 LELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAaleEVERLKAKAEEAKR-Q 2611
Cdd:TIGR02169 674 AELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEK---LKERLEELEEDLSSlE 750
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2612 KELAEKEAERQiQLAQEAAFK--KIEAEEKAHAAIVQQKEQEMLQTRKQEksiLDKLKEEAERAKRAAEDADYARMRAEQ 2689
Cdd:TIGR02169 751 QEIENVKSELK-ELEARIEELeeDLHKLEEALNDLEARLSHSRIPEIQAE---LSKLEEEVSRIEARLREIEQKLNRLTL 826
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2690 EAALSRQQVEEAERmkQRAEEEAQAKAQAQdeaeklrKEAELEAAKRAHAEQAALKQKQLADEEmDKHKKFAEKTLRQKA 2769
Cdd:TIGR02169 827 EKEYLEKEIQELQE--QRIDLKEQIKSIEK-------EIENLNGKKEELEEELEELEAALRDLE-SRLGDLKKERDELEA 896
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2770 Q---VEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIqMEELIKLKLRIEEENK------M 2840
Cdd:TIGR02169 897 QlreLERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELS-LEDVQAELQRVEEEIRalepvnM 975
|
890 900 910
....*....|....*....|....*....|
gi 1717010358 2841 LIMKDKDSTQKFLAEEAEKMRQVAEEAARL 2870
Cdd:TIGR02169 976 LAIQEYEEVLKRLDELKEKRAKLEEERKAI 1005
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
750-850 |
3.74e-19 |
|
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: 85.86 E-value: 3.74e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDP 829
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1717010358 830 EDVDV--PQPDEKSIITYVSSLY 850
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1756-2613 |
5.07e-19 |
|
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: 96.28 E-value: 5.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1756 ERDVDLDRYRERVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYDWLIKWIKDAKQRQEQIQSvpitdsktmkeql 1835
Cdd:TIGR02168 222 LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQK------------- 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1836 lqlkklleEIESNRTKVDECQKYAKQYIDAIKDYELQLVTYKAQVEpvvspakkpKVQSTSDSIIQEYVDLRTRYSELtt 1915
Cdd:TIGR02168 289 --------ELYALANEISRLEQQKQILRERLANLERQLEELEAQLE---------ELESKLDELAEELAELEEKLEEL-- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1916 ltsqyikfiTETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEkqtQLAEAHAKAKAQAEKEAEELQRrmqeevskrevva 1995
Cdd:TIGR02168 350 ---------KEELESLEAELEELEAELEELESRLEELEEQLE---TLRSKVAQLELQIASLNNEIER------------- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1996 vdAEQQKQTIQQELQQLRQnsdmEIKSKAKKIEEAEynRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQ 2075
Cdd:TIGR02168 405 --LEARLERLEDRRERLQQ----EIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2076 KKAAQEEAERLrRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAER--------RMKQAEVEKE 2147
Cdd:TIGR02168 477 LDAAERELAQL-QARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAaieaalggRLQAVVVENL 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2148 RQIKVAQEvaqqsAAAELNSKRMSFAEKTaqlelSLKQEHITVTHLqeeaERLKKQheeaeKAREEAEKELEKWHQKANE 2227
Cdd:TIGR02168 556 NAAKKAIA-----FLKQNELGRVTFLPLD-----SIKGTEIQGNDR----EILKNI-----EGFLGVAKDLVKFDPKLRK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2228 ALRLRLQAEEVAHKKTLAQEEAEKQKEDAE-------------REARKRAKAEESAL-RQKELAedELEKQRKLADATAQ 2293
Cdd:TIGR02168 617 ALSYLLGGVLVVDDLDNALELAKKLRPGYRivtldgdlvrpggVITGGSAKTNSSILeRRREIE--ELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2294 QkfsAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKsk 2373
Cdd:TIGR02168 695 E---LEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEER-- 769
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2374 hmLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERiLKEKLAaineatrlktEAEIALKEKEAENERL 2453
Cdd:TIGR02168 770 --LEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL-LNEEAA----------NLRERLESLERRIAAT 836
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2454 RRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDnELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLEL 2533
Cdd:TIGR02168 837 ERRLEDLEEQIEELSEDIESLAAEIEELEELIEELES-ELEALLNERASLEEALALLRSELEELSEELRELESKRSELRR 915
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2534 ELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKE-AEEKVRKILADEQEAARQRK--------------AALEEV 2598
Cdd:TIGR02168 916 ELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEeAEALENKIEDDEEEARRRLKrlenkikelgpvnlAAIEEY 995
|
890
....*....|....*
gi 1717010358 2599 ERLKAKAEEAKRQKE 2613
Cdd:TIGR02168 996 EELKERYDFLTAQKE 1010
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1616-2458 |
1.49e-18 |
|
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: 94.74 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1616 IHFELEGIKKNLDKVSEKTQKVLAQKEQststpllRTEHEITLQKMDQvyslsTIYLEKLKTINLVIRSthgAEEVVKTY 1695
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKAERYKELKAE-------LRELELALLVLRL-----EELREELEELQEELKE---AEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1696 EDQLKEVHAvpsdskELEATKAELKKLRSQVEGHQPLFNTLEADLNKAkdvnEQMLRSHSERDVDLDRYRERVQQLLERW 1775
Cdd:TIGR02168 259 TAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRL----EQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1776 QAilvQIDLRQRELDQLGRQLRYYRETYDWLIKWIKDAKQRQEQIQSVPITDSKTMKEQLLQLKKLLEEIESNRTKVdec 1855
Cdd:TIGR02168 329 ES---KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEI--- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1856 qKYAKQYIDAIKDYELQLVTYKAQVEPVVSPAKKPKVQSTSDSIIQEYVDLRTRYSELTTLTSQyikfITETLCRLNVEE 1935
Cdd:TIGR02168 403 -ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREELEEAEQAL 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1936 KAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEK------------EAEE---------LQRRMQEEVSKREVV 1994
Cdd:TIGR02168 478 DAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEgyeaaieaaLGGRLQAVVVENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1995 AVDA-EQQKQ-----------------TIQQELQQLRQNSD---------MEIKSKAKK--------------IEEAEYN 2033
Cdd:TIGR02168 558 AKKAiAFLKQnelgrvtflpldsikgtEIQGNDREILKNIEgflgvakdlVKFDPKLRKalsyllggvlvvddLDNALEL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2034 RRKIEEEIHIVRLQLET------MQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRK 2107
Cdd:TIGR02168 638 AKKLRPGYRIVTLDGDLvrpggvITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2108 VQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIkvAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQeh 2187
Cdd:TIGR02168 718 RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELE--AEIEELEERLEEAEEELAEAEAEIEELEAQIEQ-- 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2188 itvthLQEEAERLKKQHeeaekareeaekelekwhqkanEALRLRLQAEEV-AHKKTLAQEEAEKQKEDAEREARKRAKA 2266
Cdd:TIGR02168 794 -----LKEELKALREAL----------------------DELRAELTLLNEeAANLRERLESLERRIAATERRLEDLEEQ 846
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2267 EESALRQKELAEDELEKQRKLADAtaqqkfsAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAK 2346
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEE-------LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2347 VRAEMEILLESKSRAEEESRSNTEKskhmLEVEASKLRELAEEAARLRALSEEAkrqrqiAEGEAARQRAEAERILKEKL 2426
Cdd:TIGR02168 920 LREKLAQLELRLEGLEVRIDNLQER----LSEEYSLTLEEAEALENKIEDDEEE------ARRRLKRLENKIKELGPVNL 989
|
890 900 910
....*....|....*....|....*....|..
gi 1717010358 2427 AAINEATRLKTEAEIALKEKEAENERLRRLAE 2458
Cdd:TIGR02168 990 AAIEEYEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
746-851 |
1.50e-18 |
|
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: 84.23 E-value: 1.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 746 SEDMTAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTR 825
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 1717010358 826 LLDPEDV-DVPQPDEKSIITYVSSLYD 851
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2382-3193 |
2.04e-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: 2.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2382 KLRELAEEAARLRALSEEAKRQRQIAEGEaaRQRAEAERILKEKLAAInEATRLKTEAEIALKEK---EAENERLRRLAE 2458
Cdd:TIGR02169 178 ELEEVEENIERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKeaiERQLASLEEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2459 DEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASsgksdlelelNQL 2538
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE----------ERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2539 KNIAEETHRSKEKAEQEAEKQRQLALEEEQ---RRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELA 2615
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEELEREIEEERKRRDKlteEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2616 EKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSR 2695
Cdd:TIGR02169 405 KRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2696 QqvEEAERMKQRAEEEAQAKAQAQDE---AEKLRKE---------AELEAAKRAHA---EQAALKQKQLADEEMDKHKKF 2760
Cdd:TIGR02169 485 L--SKLQRELAEAEAQARASEERVRGgraVEEVLKAsiqgvhgtvAQLGSVGERYAtaiEVAAGNRLNNVVVEDDAVAKE 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2761 AEKTLRQ-KAQVEQELTKVKLQLEETDHQKTLLD----------DESQRLKEEVTDAMRQKAQVeEELFKVKIQMEELIK 2829
Cdd:TIGR02169 563 AIELLKRrKAGRATFLPLNKMRDERRDLSILSEDgvigfavdlvEFDPKYEPAFKYVFGDTLVV-EDIEAARRLMGKYRM 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2830 LKLRIEEENKMLIM----KDKDSTQKFLAEEAEKMRQVAEEAARLSIEaqeaarmrklaEDDLANQRALAEKMLKEKMQA 2905
Cdd:TIGR02169 642 VTLEGELFEKSGAMtggsRAPRGGILFSRSEPAELQRLRERLEGLKRE-----------LSSLQSELRRIENRLDELSQE 710
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2906 IQEATR----LKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAkETEGFQKSLEAeRRQQLEITAEAERLKLQVLEMSK 2981
Cdd:TIGR02169 711 LSDASRkigeIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIE-NVKSELKELEA-RIEELEEDLHKLEEALNDLEARL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2982 AQAKAEEDAKKFKKQAEDfgnkLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQ 3061
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEE----VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3062 EMqvaQQEQLRQETQVLQttfltekhlllekekyiekekaklenlYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGE 3141
Cdd:TIGR02169 865 EL---EEELEELEAALRD---------------------------LESRLGDLKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 3142 AMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADEN--RKLREKLEQLEEEHR 3193
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELslEDVQAELQRVEEEIR 968
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2536-2772 |
2.55e-18 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 90.64 E-value: 2.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2536 NQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKvrKILADEQeaarqrkaaleeverlKAKAEEAKRQKELA 2615
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKE--RLAAQEQ----------------KKQAEEAAKQAALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2616 EKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMlqtrkqeksildKLKEEAERAKRAAEDAdyarmRAEQEAALSR 2695
Cdd:PRK09510 131 QKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEA------------KKKAEAEAAKKAAAEA-----KKKAEAEAAA 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2696 QQVEEAermKQRAEEEAQAKAQAQDEaeklrKEAELEAAKRahAEQAALKQKQLADEEmdKHKKFAEKTLRQKAQVE 2772
Cdd:PRK09510 194 KAAAEA---KKKAEAEAKKKAAAEAK-----KKAAAEAKAA--AAKAAAEAKAAAEKA--AAAKAAEKAAAAKAAAE 258
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
635-735 |
2.58e-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: 83.40 E-value: 2.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 635 QKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLKHRQVKLVN 710
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1717010358 711 IRNDDIADGNPKLTLGLIWTIILHF 735
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1919-2469 |
2.82e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.18 E-value: 2.82e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1919 QYIKFITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAK---AKAQAEKEAEELQRRMQeevskrevva 1995
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEDlreTIAETEREREELAEEVR---------- 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1996 vDAEQQKQTIQQELQQLRQNSDMEikskakkieeaeynrrkiEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAErq 2075
Cdd:PRK02224 283 -DLRERLEELEEERDDLLAEAGLD------------------DADAEAVEARREELEDRDEELRDRLEECRVAAQAHN-- 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2076 kkaaqEEAERLRRQVKD---ESQKKREAEEELKRKVQAEKDAAREKQRAMEDLqkfRSQAEEAERRMKQAEVEKERqikv 2152
Cdd:PRK02224 342 -----EEAESLREDADDleeRAEELREEAAELESELEEAREAVEDRREEIEEL---EEEIEELRERFGDAPVDLGN---- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2153 aqevaQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVthlqEEAERLKK--------QHEEAEKAREEAEKELEKWHQK 2224
Cdd:PRK02224 410 -----AEDFLEELREERDELREREAELEATLRTARERV----EEAEALLEagkcpecgQPVEGSPHVETIEEDRERVEEL 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2225 ANEALRLRLQAEEVAHKKTLAQE--EAEKQKED--------AEREARKRAKAEESALRQKELAE--DELEKQRKLADATA 2292
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDlvEAEDRIERleerredlEELIAERRETIEEKRERAEELREraAELEAEAEEKREAA 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2293 QQKFSAEQELIRLKADTESgeqqrllleeelfrLKNEVNEAIQKRKKMEEELAKVRAemeillesksrAEEESRSNTEKS 2372
Cdd:PRK02224 561 AEAEEEAEEAREEVAELNS--------------KLAELKERIESLERIRTLLAAIAD-----------AEDEIERLREKR 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2373 KHMLEVEASKLRELAEEAARLRALSEEAKRQRqIAEGEAARQRAEA--ERIlKEKLAAINEA-TRLKTE---AEIALKEK 2446
Cdd:PRK02224 616 EALAELNDERRERLAEKRERKRELEAEFDEAR-IEEAREDKERAEEylEQV-EEKLDELREErDDLQAEigaVENELEEL 693
|
570 580
....*....|....*....|...
gi 1717010358 2447 EAENERLRRLAEDEAYQRKLLEE 2469
Cdd:PRK02224 694 EELRERREALENRVEALEALYDE 716
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
753-849 |
3.14e-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: 82.75 E-value: 3.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 753 EKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN----LENLDQAFNVAERDLGVTRLLD 828
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1717010358 829 PEDVDVPQPDEKSIITYVSSL 849
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1931-2949 |
3.31e-18 |
|
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: 93.32 E-value: 3.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1931 LNVEEKAAEKLKEEErrrlAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKrevVAVDAEQQKQTIQQELQ 2010
Cdd:pfam01576 112 LDEEEAARQKLQLEK----VTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEFTSN---LAEEEEKAKSLSKLKNK 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2011 QLRQNSDME--IKSKAKKIEEAEYNRRKIE-------EEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQE 2081
Cdd:pfam01576 185 HEAMISDLEerLKKEEKGRQELEKAKRKLEgestdlqEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALK 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2082 EAERLRRQVKdesqkkrEAEEELKRKVQAEKDAAREKQRAMEDLQKFRSqaeEAERRMKQAEVEKERQIKVAQEVAQQSA 2161
Cdd:pfam01576 265 KIRELEAQIS-------ELQEDLESERAARNKAEKQRRDLGEELEALKT---ELEDTLDTTAAQQELRSKREQEVTELKK 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2162 AAELNSKRMSfaektAQLElSLKQEHIT-VTHLQEEAERLKKqheeaekareeAEKELEKWHQkANEALRLRLQAEevah 2240
Cdd:pfam01576 335 ALEEETRSHE-----AQLQ-EMRQKHTQaLEELTEQLEQAKR-----------NKANLEKAKQ-ALESENAELQAE---- 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2241 KKTLAQ--EEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLL 2318
Cdd:pfam01576 393 LRTLQQakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQD 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2319 LEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEillesksrAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSE 2398
Cdd:pfam01576 473 TQELLQEETRQKLNLSTRLRQLEDERNSLQEQLE--------EEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALE 544
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2399 EAKRQRQiAEGEAARQRAEAERILKEKLAAINeaTRLKTEAEIALKEKEAENERL-----------RRLAEDEAYQRKLL 2467
Cdd:pfam01576 545 EGKKRLQ-RELEALTQQLEEKAAAYDKLEKTK--NRLQQELDDLLVDLDHQRQLVsnlekkqkkfdQMLAEEKAISARYA 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2468 EE--QATQHKQDIEEKIILLKKSSDNELErQKNIVEDTLRQrriieeeiriLKLNFEKASSGKSDLElelnqlKNIaEET 2545
Cdd:pfam01576 622 EErdRAEAEAREKETRALSLARALEEALE-AKEELERTNKQ----------LRAEMEDLVSSKDDVG------KNV-HEL 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2546 HRSKEKAEQEAEKQRQlALEEeqrrkeaeekvrkiLADEQEAARQRKAALE-EVERLKAKAEEAKRQKELAEKEAERQI- 2623
Cdd:pfam01576 684 ERSKRALEQQVEEMKT-QLEE--------------LEDELQATEDAKLRLEvNMQALKAQFERDLQARDEQGEEKRRQLv 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2624 -QLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVeeae 2702
Cdd:pfam01576 749 kQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI---- 824
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2703 rMKQRAEEEAQAKAQaqdEAEKLRKEAELEAAKRAHaEQAALKQKQLADEEMDKHKKFAeKTLRQKAQVEQELTKVKLQL 2782
Cdd:pfam01576 825 -LAQSKESEKKLKNL---EAELLQLQEDLAASERAR-RQAQQERDELADEIASGASGKS-ALQDEKRRLEARIAQLEEEL 898
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2783 EETDHQKTLLDDESQRLKEEVTD------AMRQKAQVEEelfKVKIQMEELIK-LKLRIEEENKMLIMKDKDStqkfLAE 2855
Cdd:pfam01576 899 EEEQSNTELLNDRLRKSTLQVEQlttelaAERSTSQKSE---SARQQLERQNKeLKAKLQEMEGTVKSKFKSS----IAA 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2856 EAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQE 2935
Cdd:pfam01576 972 LEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEASRANA 1051
|
1050
....*....|....
gi 1717010358 2936 DKEQIEQQLAKETE 2949
Cdd:pfam01576 1052 ARRKLQRELDDATE 1065
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
750-849 |
3.49e-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: 82.98 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDP 829
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1717010358 830 ED-VDVPQPDEKSIITYVSSL 849
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
636-733 |
2.29e-17 |
|
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: 80.46 E-value: 2.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 636 KKTFTKWVNKHL-IKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLKHRQV-KLVNI 711
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1717010358 712 RNDDI-ADGNPKLTLGLIWTIIL 733
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2536-2768 |
4.19e-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: 86.44 E-value: 4.19e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2536 NQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVR--KILADEQEAARQRKAALEEVERLKAKAEEAKRQKe 2613
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAaeKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAK- 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2614 lAEKEAERQiqlAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKsilDKLKEEAErAKRAAEDAdyarmRAEQEAAL 2693
Cdd:TIGR02794 136 -AEAEAERK---AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE---AKAKAEAE-AKAKAEEA-----KAKAEAAK 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2694 SRQQVEEAErmKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQK 2768
Cdd:TIGR02794 203 AKAAAEAAA--KAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1969-2715 |
4.65e-17 |
|
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: 89.51 E-value: 4.65e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1969 AKAQAEKEA--EELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSD-MEIKSKAKKIEEAEYNRRKIEEEIHIVR 2045
Cdd:pfam12128 185 AKAMHSKEGkfRDVKSMIVAILEDDGVVPPKSRLNRQQVEHWIRDIQAIAGiMKIRPEFTKLQQEFNTLESAELRLSHLH 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2046 LQLETMQKQKASAEDELQELRARAEEAERQKKAA-QEEAERLRRQVK--DESQKKREAEEEL--KRKVQAEKDAAREKQR 2120
Cdd:pfam12128 265 FGYKSDETLIASRQEERQETSAELNQLLRTLDDQwKEKRDELNGELSaaDAAVAKDRSELEAleDQHGAFLDADIETAAA 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2121 AMEDLQKFRSQAEEAERRMKqAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTA-QLELSLKQEHITVTHLQEEAER 2199
Cdd:pfam12128 345 DQEQLPSWQSELENLEERLK-ALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAkIREARDRQLAVAEDDLQALESE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2200 LKKQHEEAEKAREEAEKELEKwhqkANEALRLRL--------------QAEEVAHKKTLAQEEAEKQKEDAEREARKRAK 2265
Cdd:pfam12128 424 LREQLEAGKLEFNEEEYRLKS----RLGELKLRLnqatatpelllqleNFDERIERAREEQEAANAEVERLQSELRQARK 499
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2266 AEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLkadtesgeqqrllleeelfrLKNEVNEaiqkrkkMEEELA 2345
Cdd:pfam12128 500 RRDQASEALRQASRRLEERQSALDELELQLFPQAGTLLHF--------------------LRKEAPD-------WEQSIG 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2346 KVrAEMEILLesksRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEK 2425
Cdd:pfam12128 553 KV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQL 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2426 LAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLR 2505
Cdd:pfam12128 628 VQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKE 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2506 QRRIIEEEIRILKLNFEKASSGKSDLeleLNQLKNIAEETHRSKEKAEQEaEKQRQLA---------LEEEQRRKEAEEK 2576
Cdd:pfam12128 708 QKREARTEKQAYWQVVEGALDAQLAL---LKAAIAARRSGAKAELKALET-WYKRDLAslgvdpdviAKLKREIRTLERK 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2577 VRKILADEQEAAR----QRKAALEEVERLKAKAEEAKR-----QKELAEKEAERQIQLAqeaafkKIEAEEKAhaaivqq 2647
Cdd:pfam12128 784 IERIAVRRQEVLRyfdwYQETWLQRRPRLATQLSNIERaiselQQQLARLIADTKLRRA------KLEMERKA------- 850
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2648 keQEMLQTRKQEKsiLDKLKEEAERAKRAAEDADYArmRAEQEAALSRQQVEEAERMKQRAEEEAQAK 2715
Cdd:pfam12128 851 --SEKQQVRLSEN--LRGLRCEMSKLATLKEDANSE--QAQGSIGERLAQLEDLKLKRDYLSESVKKY 912
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1998-2867 |
4.79e-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: 89.74 E-value: 4.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1998 AEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELraraeeaERQKK 2077
Cdd:TIGR02169 182 VEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASL-------EEELE 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2078 AAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAME-DLQKFRSQAEEAERRMKQAEveKERQIKVAQEV 2156
Cdd:TIGR02169 255 KLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEaEIASLERSIAEKERELEDAE--ERLAKLEAEID 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2157 AQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAE 2236
Cdd:TIGR02169 333 KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQ 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2237 EVAHKKTLAQEEAEKQKEDAErearkrAKAEESALRQKELAEdELEKQRKLADATAQQKFSAEQELIRLKAdtesgeqqr 2316
Cdd:TIGR02169 413 EELQRLSEELADLNAAIAGIE------AKINELEEEKEDKAL-EIKKQEWKLEQLAADLSKYEQELYDLKE--------- 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2317 llleeelfrlknEVNEAIQKRKKMEEELAKVRAEMEILleskSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRAL 2396
Cdd:TIGR02169 477 ------------EYDRVEKELSKLQRELAEAEAQARAS----EERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2397 SEEAKRQRQIA-----EGEAArqraEAERILKEKlaAINEATRLkteaeiALKEKEAENERLRRLAED------------ 2459
Cdd:TIGR02169 541 IEVAAGNRLNNvvvedDAVAK----EAIELLKRR--KAGRATFL------PLNKMRDERRDLSILSEDgvigfavdlvef 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2460 ---------------------EAYQRKLLEEQATQHKQDIEEK-------------IILLKKSSDNELERQKNIVEDTLR 2505
Cdd:TIGR02169 609 dpkyepafkyvfgdtlvvediEAARRLMGKYRMVTLEGELFEKsgamtggsraprgGILFSRSEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2506 QRRIIEEEIRILKLNFEKASSGKSDLELEL----NQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEkVRKIL 2581
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIgeieKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKE-LEARI 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2582 ADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQiqlAQEAAFKKIEAEekahaaivqqkeqemLQTRKQEKS 2661
Cdd:TIGR02169 768 EELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVS---RIEARLREIEQK---------------LNRLTLEKE 829
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2662 ILDKLKEEAERAKRAAEDADYARmraEQEAALSRQQVEEaerMKQRAEEEAQAKAQAQDEAEKLRKEAEleaakRAHAEQ 2741
Cdd:TIGR02169 830 YLEKEIQELQEQRIDLKEQIKSI---EKEIENLNGKKEE---LEEELEELEAALRDLESRLGDLKKERD-----ELEAQL 898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2742 AALKQK-QLADEEMDKHKKFAEKTLRQKAQVEQELTkvklqlEETDHQKTLLDDESQRLKEEVTDAMRQKAQVE----EE 2816
Cdd:TIGR02169 899 RELERKiEELEAQIEKKRKRLSELKAKLEALEEELS------EIEDPKGEDEEIPEEELSLEDVQAELQRVEEEiralEP 972
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2817 LFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEA 2867
Cdd:TIGR02169 973 VNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1845-2600 |
8.76e-17 |
|
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: 88.58 E-value: 8.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1845 IESNRTKVDECQKYAKQYIDAIKDYELQLVTYKAQVEPVVSpaKKPKVQSTSDSIIQEYVDLRTRYSELTtltsQYIKFI 1924
Cdd:TIGR02168 234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL--EVSELEEEIEELQKELYALANEISRLE----QQKQIL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1925 TETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQT 2004
Cdd:TIGR02168 308 RERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2005 IQQELQQLRQNSDmEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEdeLQELRARAEEAERQKKAAQEEAE 2084
Cdd:TIGR02168 388 VAQLELQIASLNN-EIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE--LEELEEELEELQEELERLEEALE 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2085 RLRRQVKDESQKKREAEEELKRKvQAEKDAAREKQRAMEDLQ------------------------KFRSQAEEA----- 2135
Cdd:TIGR02168 465 ELREELEEAEQALDAAERELAQL-QARLDSLERLQENLEGFSegvkallknqsglsgilgvlseliSVDEGYEAAieaal 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2136 ERRMKQAEVEKERQIKVAQEVAQQSAA-------------AELNSKRMSFAeKTAQLELSLKQEHIT------------- 2189
Cdd:TIGR02168 544 GGRLQAVVVENLNAAKKAIAFLKQNELgrvtflpldsikgTEIQGNDREIL-KNIEGFLGVAKDLVKfdpklrkalsyll 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2190 -----VTHLQEEAERLKK-----------------------QHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHK 2241
Cdd:TIGR02168 623 ggvlvVDDLDNALELAKKlrpgyrivtldgdlvrpggvitgGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAE 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2242 KTLAQEEAEKQKEDAEReaRKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRlllee 2321
Cdd:TIGR02168 703 LRKELEELEEELEQLRK--ELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE----- 775
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2322 elfrlknEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAK 2401
Cdd:TIGR02168 776 -------ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIE 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2402 RQRQIAEgEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRR-LAEDEAYQRKLLEE--QATQHKQDI 2478
Cdd:TIGR02168 849 ELSEDIE-SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEeLRELESKRSELRREleELREKLAQL 927
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2479 EEKIILLKKSSDNELERQKNIVEDTLRqrrIIEEEIRILKLNFEKASSGKSDLELELNQLKNI---AEEthrskekaEQE 2555
Cdd:TIGR02168 928 ELRLEGLEVRIDNLQERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRLENKIKELGPVnlaAIE--------EYE 996
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 1717010358 2556 AEKQRQLALEEEQRR-KEAEEKVRKILADEQEAARQR-KAALEEVER 2600
Cdd:TIGR02168 997 ELKERYDFLTAQKEDlTEAKETLEEAIEEIDREARERfKDTFDQVNE 1043
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2268-3003 |
9.11e-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: 88.49 E-value: 9.11e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2268 ESALRQKELAED--ELEKQRKLADATAQQKFSAEQELIRLKADTEsGEQQRLLLEEELFRLKNEVNEAIQKrkKMEEELA 2345
Cdd:TIGR00618 160 AKSKEKKELLMNlfPLDQYTQLALMEFAKKKSLHGKAELLTLRSQ-LLTLCTPCMPDTYHERKQVLEKELK--HLREALQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2346 KVRAEMEILLESKSRAEEESRSNTEkskhmLEVEASKLRELAEEAARLRALSEEAKRQRQIAEgeaarqraeaeriLKEK 2425
Cdd:TIGR00618 237 QTQQSHAYLTQKREAQEEQLKKQQL-----LKQLRARIEELRAQEAVLEETQERINRARKAAP-------------LAAH 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2426 LAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLR 2505
Cdd:TIGR00618 299 IKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2506 QRRIIEEEIRILKLNFEKASSGKSDLELEL------NQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRK 2579
Cdd:TIGR00618 379 QHIHTLQQQKTTLTQKLQSLCKELDILQREqatidtRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEK 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2580 ILADE-QEAARQRKAALEEVERL-----KAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEML 2653
Cdd:TIGR00618 459 IHLQEsAQSLKEREQQLQTKEQIhlqetRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYA 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2654 QTRKQEKSILDKLKEEAERAKRAAEDADYARmRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEaELEA 2733
Cdd:TIGR00618 539 QLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLAC-EQHA 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2734 AKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQ------KAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAM 2807
Cdd:TIGR00618 617 LLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAlqltltQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWK 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2808 RQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKdkdstqkfLAEEAEKMRQVAEEAARLSIEAQEAARMrklaEDD 2887
Cdd:TIGR00618 697 EMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSD--------LAAREDALNQSLKELMHQARTVLKARTE----AHF 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2888 LANQRALAEKMLKEKMQ----AIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQ-QLAKETEGFQKSLEAERRQQ 2962
Cdd:TIGR00618 765 NNNEEVTAALQTGAELShlaaEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCeTLVQEEEQFLSRLEEKSATL 844
|
730 740 750 760
....*....|....*....|....*....|....*....|.
gi 1717010358 2963 LEITaeaeRLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNK 3003
Cdd:TIGR00618 845 GEIT----HQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGI 881
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
754-851 |
1.08e-16 |
|
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: 78.77 E-value: 1.08e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 754 KLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD-PEDV 832
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 1717010358 833 DVPQPDEKSIITYVSSLYD 851
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1902-2888 |
1.21e-16 |
|
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: 88.18 E-value: 1.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1902 EYVDLRTRYSELTTLTSQYIKFITETLCRLNV--------------------EEKAAEKLKEEERRRLAEVEAQLEKQTQ 1961
Cdd:TIGR00606 114 EGVITRYKHGEKVSLSSKCAEIDREMISHLGVskavlnnvifchqedsnwplSEGKALKQKFDEIFSATRYIKALETLRQ 193
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1962 LAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAvdAEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEI 2041
Cdd:TIGR00606 194 VRQTQGQKVQEHQMELKYLKQYKEKACEIRDQIT--SKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEI 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2042 HIVRLQLETMQKQKASAE--------------DELQELRAR-AEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKR 2106
Cdd:TIGR00606 272 KALKSRKKQMEKDNSELElkmekvfqgtdeqlNDLYHNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTELLVEQGR 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2107 kVQAEKDAAREKQRAMEDL-QKFRSQAE--------EAERRMKQA-EVEKERQIKVAQEVAQQsaAAELNSKRMSFAEKT 2176
Cdd:TIGR00606 352 -LQLQADRHQEHIRARDSLiQSLATRLEldgfergpFSERQIKNFhTLVIERQEDEAKTAAQL--CADLQSKERLKQEQA 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2177 AQLELSLKQEHITVTH----LQEEAERLKKQHEEAEKAREEAEKELEKwHQKANEALRLRLQAEEVAHKKTLAQEEAEKQ 2252
Cdd:TIGR00606 429 DEIRDEKKGLGRTIELkkeiLEKKQEELKFVIKELQQLEGSSDRILEL-DQELRKAERELSKAEKNSLTETLKKEVKSLQ 507
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2253 KEDAEREARKRAKAEESALRQKElaedelEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNE 2332
Cdd:TIGR00606 508 NEKADLDRKLRKLDQEMEQLNHH------TTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHS 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2333 AIQKRKKMEEELAKVRAEMEILLESKS--RAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGE 2410
Cdd:TIGR00606 582 KSKEINQTRDRLAKLNKELASLEQNKNhiNNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGA 661
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2411 AARQRAEAERILKEKLAAINEATR-LKTEAEIalKEKEAENERLRRLAEDEayqRKLLEEQATQHKQDIEEkIILLKKSS 2489
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRvFQTEAEL--QEFISDLQSKLRLAPDK---LKSTESELKKKEKRRDE-MLGLAPGR 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2490 DNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASS----------GKSDLELELNQLKNIAEETHRSKEKAEQEAEKQ 2559
Cdd:TIGR00606 736 QSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETllgtimpeeeSAKVCLTDVTIMERFQMELKDVERKIAQQAAKL 815
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2560 RQLAL-----EEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKI 2634
Cdd:TIGR00606 816 QGSDLdrtvqQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELST 895
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2635 EAEEkAHAAIVQQKEQEMlqtrkqeksildklkeeaerakraaedadyarmraEQEAALSRQQVEEAERMKQRAEEEAQA 2714
Cdd:TIGR00606 896 EVQS-LIREIKDAKEQDS-----------------------------------PLETFLEKDQQEKEELISSKETSNKKA 939
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2715 KAQAQDEAEKLrkeaeleaakrahaeqaalkqKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDD 2794
Cdd:TIGR00606 940 QDKVNDIKEKV---------------------KNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINE 998
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2795 ESQRLKEEVTDAMRQKAQVEEELFKVKI--QMEELIK-LKLRIEEENKMLIMKDKDSTQKFlaeeAEKMRQVAEEAARLS 2871
Cdd:TIGR00606 999 DMRLMRQDIDTQKIQERWLQDNLTLRKRenELKEVEEeLKQHLKEMGQMQVLQMKQEHQKL----EENIDLIKRNHVLAL 1074
|
1050
....*....|....*..
gi 1717010358 2872 IEAQEAARMRKLAEDDL 2888
Cdd:TIGR00606 1075 GRQKGYEKEIKHFKKEL 1091
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1940-2398 |
1.80e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 87.13 E-value: 1.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1940 KLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEevSKREVVAVDAEQQKQTIQQELQQLRQNSDmE 2019
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK--LEKLLQLLPLYQELEALEAELAELPERLE-E 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2020 IKSKAKKIEEAEYNRRKIEEEIHIVRLQLET-MQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKR 2098
Cdd:COG4717 151 LEERLEELRELEEELEELEAELAELQEELEElLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELE 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2099 EAEEELkrkvqaEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAA--ELNSKRMSFAEKT 2176
Cdd:COG4717 231 QLENEL------EAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLflLLAREKASLGKEA 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2177 AQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDA 2256
Cdd:COG4717 305 EELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDE 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2257 E--REARKRAKAEESALRQKELAEDELEKQRK--LADATAQQKFSAEQELIRLKAdtesgeqqrllleeelfrlknEVNE 2332
Cdd:COG4717 385 EelRAALEQAEEYQELKEELEELEEQLEELLGelEELLEALDEEELEEELEELEE---------------------ELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2333 AIQKRKKMEEELAKVRAEMEILLESKSRAEEEsrsntekskHMLEVEASKLRELAEEAARLRALSE 2398
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALE 500
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2458-3208 |
3.32e-16 |
|
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: 86.77 E-value: 3.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2458 EDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLnfeKASSGKSDLELELNQ 2537
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRA---RLAARKQELEEILHE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2538 LKN-IAEETHRSKEKAEQEAEKQRQLALEEEQRrkEAEEKVRKILADEQEAARQRKAALEEvERLKAKAEEAKRQKE--- 2613
Cdd:pfam01576 80 LESrLEEEEERSQQLQNEKKKMQQHIQDLEEQL--DEEEAARQKLQLEKVTTEAKIKKLEE-DILLLEDQNSKLSKErkl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2614 LAEKEAERQIQLAQEaafkkieaEEKAHAAIVQQKEQEMLQTRKQEK-SILDKLKEEAERAKRAAeDADYARMRaEQEAA 2692
Cdd:pfam01576 157 LEERISEFTSNLAEE--------EEKAKSLSKLKNKHEAMISDLEERlKKEEKGRQELEKAKRKL-EGESTDLQ-EQIAE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2693 LsRQQVEEAERMKQRAEEEAQAkAQAQDEAEKLRKEAELEAAKRAHAEQAALKqkqladEEMDKHKKFAEKTLRQKAQVE 2772
Cdd:pfam01576 227 L-QAQIAELRAQLAKKEEELQA-ALARLEEETAQKNNALKKIRELEAQISELQ------EDLESERAARNKAEKQRRDLG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2773 QELTKVKLQLEET------------------DHQKTLLDDESQRLKEEVTDaMRQK-AQVEEELfkvkiqMEELIKLKlr 2833
Cdd:pfam01576 299 EELEALKTELEDTldttaaqqelrskreqevTELKKALEEETRSHEAQLQE-MRQKhTQALEEL------TEQLEQAK-- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2834 ieeENKMLIMKDKDSTQKFLAEEAEKMRQvaeeaarLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLK 2913
Cdd:pfam01576 370 ---RNKANLEKAKQALESENAELQAELRT-------LQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2914 AEADMLQKQKELAQEQARKFQEDKEQIEQQLaketEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKF 2993
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQL----QDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNV 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2994 KKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQlRQ 3073
Cdd:pfam01576 516 ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQ-RQ 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3074 ETQVLQTTFLTEKHLLLEKEKYIEKEKAKLENLYED-------------EVRKAQKLKQEQEHQLKQLEEEKQQLKASMG 3140
Cdd:pfam01576 595 LVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEareketralslarALEEALEAKEELERTNKQLRAEMEDLVSSKD 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3141 EAMKKQKEAEESVRHKQDELHQLDKRRQEQE-KLLADENRKLR-----------------EKLEQLEEEHRIALAQTREM 3202
Cdd:pfam01576 675 DVGKNVHELERSKRALEQQVEEMKTQLEELEdELQATEDAKLRlevnmqalkaqferdlqARDEQGEEKRRQLVKQVREL 754
|
....*.
gi 1717010358 3203 MIQTDD 3208
Cdd:pfam01576 755 EAELED 760
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2351-2692 |
3.53e-16 |
|
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: 86.33 E-value: 3.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2351 MEILLESKSRAEEESRSNTEKskhmleVEASKLRELAEEAARlralseEAKRQRQIAEGEAARQrAEAERilkeKLAAIN 2430
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEK------MEQERLRQEKEEKAR------EVERRRKLEEAEKARQ-AEMDR----QAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2431 EATRLKTEAE-----IALKEKEAENERLRR--LAEDEAYQRKL--LEEQATQHKQDIEEKIILLKKSSDNELERQKNIVE 2501
Cdd:pfam17380 338 EQERMAMERErelerIRQEERKRELERIRQeeIAMEISRMRELerLQMERQQKNERVRQELEAARKVKILEEERQRKIQQ 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2502 -----DTLRQRRIIEEEIRILKLNFEKASsgksdlELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQR-RKEAEE 2575
Cdd:pfam17380 418 qkvemEQIRAEQEEARQREVRRLEEERAR------EMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRdRKRAEE 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2576 KVRKILADEQEaARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQiqlAQEAAFKKIEAEEKahaaivqQKEQEMLQT 2655
Cdd:pfam17380 492 QRRKILEKELE-ERKQAMIEEERKRKLLEKEMEERQKAIYEEERRRE---AEEERRKQQEMEER-------RRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|....*..
gi 1717010358 2656 RKQEKSILDKLKEEAERAKRAAEDadyARMRAEQEAA 2692
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVES---EKARAEYEAT 594
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2522-3188 |
3.79e-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: 86.82 E-value: 3.79e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2522 EKASSGKSDLELELNQLKnIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAE--EKVRKILADEQEAARQRKAALEEVE 2599
Cdd:pfam12128 247 QQEFNTLESAELRLSHLH-FGYKSDETLIASRQEERQETSAELNQLLRTLDDQwkEKRDELNGELSAADAAVAKDRSELE 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2600 RLKAKA---EEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAiVQQKEQEMLQTRKQE--------KSILDKLKE 2668
Cdd:pfam12128 326 ALEDQHgafLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQD-VTAKYNRRRSKIKEQnnrdiagiKDKLAKIRE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2669 EAERAKRAAED---ADYARMRAEQEAALSRQQvEEAERMKQRAEEEAQAKAQAQDEAE-KLRKEAELEAAKRAHAEQ-AA 2743
Cdd:pfam12128 405 ARDRQLAVAEDdlqALESELREQLEAGKLEFN-EEEYRLKSRLGELKLRLNQATATPElLLQLENFDERIERAREEQeAA 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2744 LKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQ-----KTL---LDDESQRLKEEVT----------- 2804
Cdd:pfam12128 484 NAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqaGTLlhfLRKEAPDWEQSIGkvispellhrt 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2805 --DAMRQKAQVEEE--LFKVKI-----------QMEELIKLKLRIEEEnkmlimkDKDSTQKFLAEEAEKMRQVAEEAAR 2869
Cdd:pfam12128 564 dlDPEVWDGSVGGElnLYGVKLdlkridvpewaASEEELRERLDKAEE-------ALQSAREKQAAAEEQLVQANGELEK 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2870 LSIEAQEAARMRKLAEDDL--------ANQRALAEKMLKEKMQAIQEATRLKAEADML-QKQKELAQEQARKFQEDKEQi 2940
Cdd:pfam12128 637 ASREETFARTALKNARLDLrrlfdekqSEKDKKNKALAERKDSANERLNSLEAQLKQLdKKHQAWLEEQKEQKREARTE- 715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2941 EQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKA-----EEDAKKFKKQAEDFGNKLHQTEL----AT 3011
Cdd:pfam12128 716 KQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLAslgvdPDVIAKLKREIRTLERKIERIAVrrqeVL 795
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3012 KERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQlrqetQVLQTTFLTEKHLLLe 3091
Cdd:pfam12128 796 RYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQ-----QVRLSENLRGLRCEM- 869
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3092 kekyiekekAKLENLYEDEvrKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMK---------KQKEAEESVRHKQDelHQ 3162
Cdd:pfam12128 870 ---------SKLATLKEDA--NSEQAQGSIGERLAQLEDLKLKRDYLSESVKKyvehfknviADHSGSGLAETWES--LR 936
|
730 740
....*....|....*....|....*.
gi 1717010358 3163 LDKRRQEQEKLLADENRKLREKLEQL 3188
Cdd:pfam12128 937 EEDHYQNDKGIRLLDYRKLVPYLEQW 962
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4632-4670 |
6.40e-16 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 74.29 E-value: 6.40e-16
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 4632 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4670
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2762-3131 |
6.58e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.76 E-value: 6.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2762 EKTLRQKAQVEQELTKVKLQLEETDHQKtllddesQRLKEEVTDAMR-QKAQVEEELFKVkiqmeELIKLKLRieeenkm 2840
Cdd:COG1196 175 EEAERKLEATEENLERLEDILGELERQL-------EPLERQAEKAERyRELKEELKELEA-----ELLLLKLR------- 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2841 limkdkdstqkflaEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQ 2920
Cdd:COG1196 236 --------------ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2921 KQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDF 3000
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3001 GNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQt 3080
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEA- 460
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 3081 tfltekhlLLEKEKYIEKEKAKLENLYEDEVRKAQKLKQEQEHQLKQLEEE 3131
Cdd:COG1196 461 --------LLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2551-2748 |
7.25e-16 |
|
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: 82.59 E-value: 7.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2551 KAEQEAEKQRQ----LALEEEQRRKEAEEKVRKiLADEQEAARQRKAALEEverlKAKAEEAKRQKELAEKEAERQIQLA 2626
Cdd:TIGR02794 47 AVAQQANRIQQqkkpAAKKEQERQKKLEQQAEE-AEKQRAAEQARQKELEQ----RAAAEKAAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2627 QEAAfKKIEAEEKAHA-AIVQQKEQEMLQTRKQEksilDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEE----- 2700
Cdd:TIGR02794 122 EEAK-AKQAAEAKAKAeAEAERKAKEEAAKQAEE----EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAeeaka 196
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2701 -AERMKQRAEEEAQAKAQA----QDEAEKLRKEAELEAAKRAHAEQAALKQKQ 2748
Cdd:TIGR02794 197 kAEAAKAKAAAEAAAKAEAeaaaAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1693-2288 |
8.49e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 85.37 E-value: 8.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1693 KTYEDQLKEVHAVpSDSKELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRSHSERDVDLDRYRERVQQLL 1772
Cdd:COG1196 216 RELKEELKELEAE-LLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1773 ERWQAILVQIDLRQRELDQLGRQLRYYRETydwLIKWIKDAKQRQEQiqsvpitdsktmkeqllqlkklleeIESNRTKV 1852
Cdd:COG1196 295 AELARLEQDIARLEERRRELEERLEELEEE---LAELEEELEELEEE-------------------------LEELEEEL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1853 DECQKYAKQYIDAIKDYELQLVTYKAQVEpvvspakkpKVQSTSDSIIQEYVDLRTRYSELTTLTSQYIKFITETLCRLN 1932
Cdd:COG1196 347 EEAEEELEEAEAELAEAEEALLEAEAELA---------EAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1933 VEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQL 2012
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2013 RQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAA---QEEAERLRRQ 2089
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEylkAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2090 VKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKR 2169
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2170 MSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEA 2249
Cdd:COG1196 658 AGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREEL 737
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1717010358 2250 EKQKEDAEREARKRAKAEESALRQKELAEDELEK-QRKLA 2288
Cdd:COG1196 738 LEELLEEEELLEEEALEELPEPPDLEELERELERlEREIE 777
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
752-863 |
1.72e-15 |
|
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: 75.41 E-value: 1.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 752 KEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 831
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 1717010358 832 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 863
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2530-3089 |
1.83e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 84.35 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2530 DLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKI---------LADEQEAARQRKaalEEVER 2600
Cdd:PRK03918 159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREIneisselpeLREELEKLEKEV---KELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2601 LKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDA 2680
Cdd:PRK03918 236 LKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKR 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2681 dyaRMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKF 2760
Cdd:PRK03918 316 ---LSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2761 AEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKE----------EVTDAMRQ--KAQVEEELFKVKIQMEELI 2828
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKakgkcpvcgrELTEEHRKelLEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2829 KLKLRIEEENKMLIMK-DKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAA--RMRKLAE--DDLANQRALAEKMLKEKM 2903
Cdd:PRK03918 473 EKERKLRKELRELEKVlKKESELIKLKELAEQLKELEEKLKKYNLEELEKKaeEYEKLKEklIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2904 QAIQEATRLKAEADMLQKQK-ELAQEQARKFQEDKEQIEQQLaKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKA 2982
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELaELLKELEELGFESVEELEERL-KELEPFYNEYLELKDAEKELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2983 Q---AKAEEDAKKFKKQAEDFGNKLHQTELATKERmvvvQSLEIQRQQSGKEA--EELRRAIAELEHEKEKLKQEAELLQ 3057
Cdd:PRK03918 632 FeelAETEKRLEELRKELEELEKKYSEEEYEELRE----EYLELSRELAGLRAelEELEKRREEIKKTLEKLKEELEERE 707
|
570 580 590
....*....|....*....|....*....|..
gi 1717010358 3058 KNSQEMQVAqqEQLRQETQVLQTTFLTEKHLL 3089
Cdd:PRK03918 708 KAKKELEKL--EKALERVEELREKVKKYKALL 737
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2451-3202 |
2.27e-15 |
|
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: 84.01 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2451 ERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDN------ELERQKNIVEDTLRqrriieeeirilklnfeKA 2524
Cdd:pfam15921 74 EHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDlqtklqEMQMERDAMADIRR-----------------RE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2525 SSGKSDLElelNQLKNIAEETHRSK-------EKAEQEAEKQRQLALEEEQRRKEaeekVRKILADEQEAA--------- 2588
Cdd:pfam15921 137 SQSQEDLR---NQLQNTVHELEAAKclkedmlEDSNTQIEQLRKMMLSHEGVLQE----IRSILVDFEEASgkkiyehds 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2589 ------RQRKAALEEVER--------LKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQ 2654
Cdd:pfam15921 210 mstmhfRSLGSAISKILReldteisyLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2655 TRKQEKSILDKLKEEAERAKRaaEDADYARMRAEQEAALS--RQQVEEAERM-KQRAEEEAQAKAQAQDEAEKLRKEAEL 2731
Cdd:pfam15921 290 ARSQANSIQSQLEIIQEQARN--QNSMYMRQLSDLESTVSqlRSELREAKRMyEDKIEELEKQLVLANSELTEARTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2732 EAAKRAHAEQAAlkQKQLADeemdKHKKFAEKTLrQKAQVEQELTKVKLQLEETDHQKTLLDD---ESQRLkEEVTDAMR 2808
Cdd:pfam15921 368 FSQESGNLDDQL--QKLLAD----LHKREKELSL-EKEQNKRLWDRDTGNSITIDHLRRELDDrnmEVQRL-EALLKAMK 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2809 Q--KAQVEEELFKVKIQMEELIKLKlrieeenkmlimkdkdSTQKFLAEEAEKMRQVAEE--AARLSIEAQEaarmRKLA 2884
Cdd:pfam15921 440 SecQGQMERQMAAIQGKNESLEKVS----------------SLTAQLESTKEMLRKVVEEltAKKMTLESSE----RTVS 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2885 edDLANQralaekmLKEKMQAIQ----EATRLKAEADM-LQKQKELAQE--QARKFQEDKEQIEQQLAKEtegfQKSLEA 2957
Cdd:pfam15921 500 --DLTAS-------LQEKERAIEatnaEITKLRSRVDLkLQELQHLKNEgdHLRNVQTECEALKLQMAEK----DKVIEI 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2958 ERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRR 3037
Cdd:pfam15921 567 LRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLR 646
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3038 AIAELEHEKEKLKQEAellqKNSQEmqvaQQEQLRQETQVLQTTFltekhlllekekyiekekaklENLYEDEVRKAQKL 3117
Cdd:pfam15921 647 AVKDIKQERDQLLNEV----KTSRN----ELNSLSEDYEVLKRNF---------------------RNKSEEMETTTNKL 697
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3118 KQEQEHQLKQLEEEKQQLKA---SMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRK---LREKLEQLEEE 3191
Cdd:pfam15921 698 KMQLKSAQSELEQTRNTLKSmegSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEAMTNANKEkhfLKEEKNKLSQE 777
|
810
....*....|.
gi 1717010358 3192 HRIALAQTREM 3202
Cdd:pfam15921 778 LSTVATEKNKM 788
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2559-2973 |
2.57e-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: 83.63 E-value: 2.57e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2559 QRQLALEEEQRrkeaEEKVRKIladEQEAARQRKaaleeverlKAKAEEAKRQKELAEKEAERQIQLAQEAAfkkIEAEe 2638
Cdd:pfam17380 279 QHQKAVSERQQ----QEKFEKM---EQERLRQEK---------EEKAREVERRRKLEEAEKARQAEMDRQAA---IYAE- 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2639 kaHAAIVQQKEQEMLQTRKQEKsildklKEEAERAKRAAEDADYARMRAEQEAALSRQQveEAERMKQRAEEEAQAKAQA 2718
Cdd:pfam17380 339 --QERMAMERERELERIRQEER------KRELERIRQEEIAMEISRMRELERLQMERQQ--KNERVRQELEAARKVKILE 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2719 QDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMdkhkkfaektlrqkaqvEQELTKVKLQLEETDHQktllddesqr 2798
Cdd:pfam17380 409 EERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEER-----------------AREMERVRLEEQERQQQ---------- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2799 lkeevtdaMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKmrqvaeeaarlsieaqeaa 2878
Cdd:pfam17380 462 --------VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERK------------------- 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2879 rmrklaeddlanqRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELA-----QEQARKFQEDKEQIEqQLAKETEGFQK 2953
Cdd:pfam17380 515 -------------RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEerrriQEQMRKATEERSRLE-AMEREREMMRQ 580
|
410 420
....*....|....*....|.
gi 1717010358 2954 SLEAER-RQQLEITAEAERLK 2973
Cdd:pfam17380 581 IVESEKaRAEYEATTPITTIK 601
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
755-850 |
4.08e-15 |
|
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: 74.32 E-value: 4.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 755 LLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAErDLGVTRLLDPED-VD 833
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1717010358 834 VPQPDEKSIITYVSSLY 850
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
752-855 |
9.23e-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: 73.54 E-value: 9.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 752 KEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 831
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1717010358 832 VDV--PQPDEKSIITYVSSLYDAMPR 855
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2341-3223 |
9.55e-15 |
|
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: 82.15 E-value: 9.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2341 EEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEvEASKLRELAEEAARLRALSEEAKrqrqiaeGEAARQRAEAER 2420
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCE-EKNALQEQLQAETELCAEAEEMR-------ARLAARKQELEE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2421 ILKEKLAAINEATRLKTEAEIALKEKEAENERL-RRLAEDEAYQRKL-LEEQATQHKQDIEEKIILLKKSSDNELERQKN 2498
Cdd:pfam01576 76 ILHELESRLEEEEERSQQLQNEKKKMQQHIQDLeEQLDEEEAARQKLqLEKVTTEAKIKKLEEDILLLEDQNSKLSKERK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2499 IVEDTLRQRRIIEEEIRilklnfEKASSgksdleleLNQLKNIAEETHRSKEKAEQEAEKQRQlALEEEQRRKEAEekvr 2578
Cdd:pfam01576 156 LLEERISEFTSNLAEEE------EKAKS--------LSKLKNKHEAMISDLEERLKKEEKGRQ-ELEKAKRKLEGE---- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2579 kiLADEQEAARQRKAALEEverlkAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQK-EQEMLQTRK 2657
Cdd:pfam01576 217 --STDLQEQIAELQAQIAE-----LRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDlESERAARNK 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2658 QEKSILDkLKEEAERAKRAAEDAdYARMRAEQEAALSRQQveEAERMKQRAEEEAQA-KAQAQDEAEKLRKEAE-----L 2731
Cdd:pfam01576 290 AEKQRRD-LGEELEALKTELEDT-LDTTAAQQELRSKREQ--EVTELKKALEEETRShEAQLQEMRQKHTQALEelteqL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2732 EAAKRAHAEqaalkqkqladeeMDKHKKFAEKtlrQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKA 2811
Cdd:pfam01576 366 EQAKRNKAN-------------LEKAKQALES---ENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRA 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2812 QVEEELFKVKIQMEELIKLKLRIEEENKMLiMKDKDS-------TQKFLAEEAekmRQVAEEAARLSIEAQEAARMRKLA 2884
Cdd:pfam01576 430 ELAEKLSKLQSELESVSSLLNEAEGKNIKL-SKDVSSlesqlqdTQELLQEET---RQKLNLSTRLRQLEDERNSLQEQL 505
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2885 EDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLqkqkELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLE 2964
Cdd:pfam01576 506 EEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL----EALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQE 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2965 I---TAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAE 3041
Cdd:pfam01576 582 LddlLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQ 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3042 LEHEKEKLKQEAELLQKNSQEMQVAQQeQLRQETQVLQTTFltekhlllekekyiekekaklenlyedevrkaqklkQEQ 3121
Cdd:pfam01576 662 LRAEMEDLVSSKDDVGKNVHELERSKR-ALEQQVEEMKTQL------------------------------------EEL 704
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3122 EHQLKQLEEEKQQLKASMgEAMKKQKEAEESVRHKQDElhqldkrrqEQEKLLADENRKLREKLEQLEEEHRIALAQTRE 3201
Cdd:pfam01576 705 EDELQATEDAKLRLEVNM-QALKAQFERDLQARDEQGE---------EKRRQLVKQVRELEAELEDERKQRAQAVAAKKK 774
|
890 900
....*....|....*....|..
gi 1717010358 3202 MMIQTDDLagSSQTKAMPNGRD 3223
Cdd:pfam01576 775 LELDLKEL--EAQIDAANKGRE 794
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4055-4093 |
1.29e-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: 1.29e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 4055 ILEAQIATGGIIDPVHSHRVPIDIAYKRGYFDEEMNKIL 4093
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
752-851 |
1.33e-14 |
|
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: 72.69 E-value: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 752 KEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 831
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1717010358 832 VDV--PQPDEKSIITYVSSLYD 851
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2584-2774 |
1.38e-14 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 79.47 E-value: 1.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2584 EQEAARQRKAalEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFK-KIEAEEKAHAAIVQQKEQEMLQTRKQEKSi 2662
Cdd:PRK09510 69 QQQKSAKRAE--EQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEqKKQAEEAAKQAALKQKQAEEAAAKAAAAA- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2663 ldKLKEEAErAKRAAEDADYARMRAEQEAALSRQQVEEAErMKQRAEEEAQAKA--QAQDEAEKLRKE-AELEAAKRAHA 2739
Cdd:PRK09510 146 --KAKAEAE-AKRAAAAAKKAAAEAKKKAEAEAAKKAAAE-AKKKAEAEAAAKAaaEAKKKAEAEAKKkAAAEAKKKAAA 221
|
170 180 190
....*....|....*....|....*....|....*
gi 1717010358 2740 EQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQE 2774
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
653-732 |
1.52e-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: 72.62 E-value: 1.52e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 653 HVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLKHRQV----KLVNIRNDDIADGNPKLT 724
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1717010358 725 LGLIWTII 732
Cdd:cd21223 105 LALLWRII 112
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2032-2418 |
1.55e-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: 1.55e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2032 YNRRKIEEEIHIVRLqLETMQKQKASAEDELQELRARAEEaERQKKAAQEEAERLRRQVK-DESQKKREAEEELKRKVQA 2110
Cdd:pfam17380 260 YNGQTMTENEFLNQL-LHIVQHQKAVSERQQQEKFEKMEQ-ERLRQEKEEKAREVERRRKlEEAEKARQAEMDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2111 EKD-AAREKQRAMEdlqkfRSQAEEAERrmkqaEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ-LELSLK---Q 2185
Cdd:pfam17380 338 EQErMAMERERELE-----RIRQEERKR-----ELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeLEAARKvkiL 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2186 EHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKwhQKANEALRLRLQAEEVAHK-KTLAQEEAEKQKEDAEREARKRA 2264
Cdd:pfam17380 408 EEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEE--ERAREMERVRLEEQERQQQvERLRQQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2265 KAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESgeqqrllleeelfrlknevneaiQKRKKMEEEL 2344
Cdd:pfam17380 486 RKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-----------------------ERRREAEEER 542
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2345 AKvraemEILLESKSRAEEEsrsntekskhmleveaskLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEA 2418
Cdd:pfam17380 543 RK-----QQEMEERRRIQEQ------------------MRKATEERSRLEAMEREREMMRQIVESEKARAEYEA 593
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
632-731 |
1.62e-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: 72.56 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 632 DRVQKKTFTKWVNKHLIKAQ-RHVTDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYL-KHRQV 706
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1717010358 707 KLVNIRNDDIADGNPKLTLGLIWTI 731
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
628-734 |
2.06e-14 |
|
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: 72.31 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 628 EDERDrvqKKTFTKWVNKHLIKAQRHvtDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIA 697
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYA 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 698 LDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 734
Cdd:cd21219 71 VDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2592-2775 |
2.39e-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: 77.96 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2592 KAALEEVERLKAKAEEAKRQKELAEKEAERQiqlaQEAAFKKIEAEEKAHAAIVQQK--EQEMLQTRKQEKSILDKLKEE 2669
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQ----AEEAEKQRAAEQARQKELEQRAaaEKAAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2670 AERAKRAAEDAdyarmRAEQEAALSRQQVEEAERmkqRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQL 2749
Cdd:TIGR02794 122 EEAKAKQAAEA-----KAKAEAEAERKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEE 193
|
170 180
....*....|....*....|....*.
gi 1717010358 2750 ADEEMDKHKKFAEKTLRQKAQVEQEL 2775
Cdd:TIGR02794 194 AKAKAEAAKAKAAAEAAAKAEAEAAA 219
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3397-3435 |
2.90e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.28 E-value: 2.90e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 3397 LLEAQIATGGIIDPVDSHRVPLEVAYKRNYFDEEMNEVL 3435
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3724-3762 |
3.10e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 69.28 E-value: 3.10e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 3724 LLDAQLATGGIIDPVNSHRVPLDVACKRGYLDEETNNSL 3762
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2415-3054 |
5.14e-14 |
|
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: 79.38 E-value: 5.14e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2415 RAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLL--EEQATQHKQDIEEKIIL--LKKSSD 2490
Cdd:pfam05483 94 KVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLikENNATRHLCNLLKETCArsAEKTKK 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2491 NELERqknivEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELN-QLKNIAEETHRSKEKAEQEA-EKQRQLAL---- 2564
Cdd:pfam05483 174 YEYER-----EETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfKLKEDHEKIQHLEEEYKKEInDKEKQVSLlliq 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2565 --EEEQRRK-------EAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAK---RQKELAEKEAERQIQLA------ 2626
Cdd:pfam05483 249 itEKENKMKdltflleESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKmslQRSMSTQKALEEDLQIAtkticq 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2627 ----QEAAFKKIEAEEKAHAAIVQQKE------QEMLQTRKQE-KSILDKLKE-EAERAKRAAEDADYARMRAEQEAALs 2694
Cdd:pfam05483 329 lteeKEAQMEELNKAKAAHSFVVTEFEattcslEELLRTEQQRlEKNEDQLKIiTMELQKKSSELEEMTKFKNNKEVEL- 407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2695 rqqvEEAERMKQRAEEEAQAKAQAQDEAEKLR-KEAELEAAKRAhaeqaalKQKQLADEEMD--KHKKFAEKTLRQKAQV 2771
Cdd:pfam05483 408 ----EELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFLLQA-------REKEIHDLEIQltAIKTSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2772 EQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKlKLRIEEENKMLIMKDKDSTQK 2851
Cdd:pfam05483 477 KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLK-QIENLEEKEMNLRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2852 FLAEEAE----KMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQ 2927
Cdd:pfam05483 556 EFIQKGDevkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2928 EQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQ---------------AKAEEDAKK 2992
Cdd:pfam05483 636 IKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQkeidkrcqhkiaemvALMEKHKHQ 715
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2993 FKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAE 3054
Cdd:pfam05483 716 YDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2522-3196 |
6.46e-14 |
|
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: 79.00 E-value: 6.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2522 EKASSGKSDLELELNQLKNIAEETHRSKEkAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERL 2601
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIE-AQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCAR 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2602 KAKaeeaKRQKELAEKEAERQIQLAQEAAFKKIeaeekahaaiVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDAD 2681
Cdd:pfam05483 167 SAE----KTKKYEYEREETRQVYMDLNNNIEKM----------ILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYK 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2682 YARMRAEQEAALSRQQVEEAE-RMKQRA--EEEAQAKAQAQDEAEKLRKEAELEAAKRAHAeqaalKQKQLADEEMDKHK 2758
Cdd:pfam05483 233 KEINDKEKQVSLLLIQITEKEnKMKDLTflLEESRDKANQLEEKTKLQDENLKELIEKKDH-----LTKELEDIKMSLQR 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2759 KFA-EKTLRQKAQVEqelTKVKLQLEEtdhqktllddESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELiklkLRIEEE 2837
Cdd:pfam05483 308 SMStQKALEEDLQIA---TKTICQLTE----------EKEAQMEELNKAKAAHSFVVTEFEATTCSLEEL----LRTEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2838 NkmliMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQ-EAARMRKLAEDDlanqralaEKMLKEKMQAIQEATRLKAEA 2916
Cdd:pfam05483 371 R----LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEvELEELKKILAED--------EKLLDEKKQFEKIAEELKGKE 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2917 dmlQKQKELAQEQARKFQEDKEQI------EQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQA------ 2984
Cdd:pfam05483 439 ---QELIFLLQAREKEIHDLEIQLtaiktsEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASdmtlel 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2985 -KAEEDAKKFKKQAEDFGNK---LHQTELATKERMVVVQSLEIQRQQSGK----EAEELRRAIAELEHEKEKLKQEAELL 3056
Cdd:pfam05483 516 kKHQEDIINCKKQEERMLKQienLEEKEMNLRDELESVREEFIQKGDEVKckldKSEENARSIEYEVLKKEKQMKILENK 595
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3057 QKNSQ---EMQVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEKAKLENL---YEDEVRKAQKLKQEQEHQLKQLEE 3130
Cdd:pfam05483 596 CNNLKkqiENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAkqkFEEIIDNYQKEIEDKKISEEKLLE 675
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 3131 EKQQLKASMGEAMKKQKEAEESVRHKQDELHQL-DKRRQEQEKLLADENRK--LREKLEQLEEEHRIAL 3196
Cdd:pfam05483 676 EVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALmEKHKHQYDKIIEERDSElgLYKNKEQEQSSAKAAL 744
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2571-2790 |
9.62e-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: 76.42 E-value: 9.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2571 KEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAafkkIEAEEKAHAAIVQQKEQ 2650
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAA----KQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2651 EMLQtRKQEKSilDKLKEEAERAKRAAEDAdyaRMRAEQEAALSRQqvEEAermkQRAEEEAQAKAQAQDEAEKLRKE-A 2729
Cdd:TIGR02794 122 EEAK-AKQAAE--AKAKAEAEAERKAKEEA---AKQAEEEAKAKAA--AEA----KKKAEEAKKKAEAEAKAKAEAEAkA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2730 ELEAAKrAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKT 2790
Cdd:TIGR02794 190 KAEEAK-AKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2532-3004 |
1.10e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 77.89 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2532 ELELNQLKNIAEETHRSKEKAEQEAEKQRQLA-LEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKR 2610
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEeLEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2611 QKELAEKEAERQIQLAQEaafkkIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQE 2690
Cdd:COG4717 147 RLEELEERLEELRELEEE-----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2691 AALSRQQVEEAERMKQRAEEEAQAKAQAQ-------------------DEAEKLRKEAELEAAKRAHAEQAALKQKQLAD 2751
Cdd:COG4717 222 LEELEEELEQLENELEAAALEERLKEARLllliaaallallglggsllSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2752 EEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEevtdAMRQKAQVEEELfkvkiqmeeliKLK 2831
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQE----LLREAEELEEEL-----------QLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2832 LRIEEENKMLIMKDKDSTQKF--LAEEAEKMRQVAEEAARLSieaqeaARMRKLAEDDLANQRALAEKMLKEKMQaiqea 2909
Cdd:COG4717 367 ELEQEIAALLAEAGVEDEEELraALEQAEEYQELKEELEELE------EQLEELLGELEELLEALDEEELEEELE----- 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2910 tRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKaEED 2989
Cdd:COG4717 436 -ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYR-EER 513
|
490
....*....|....*
gi 1717010358 2990 AKKFKKQAEDFGNKL 3004
Cdd:COG4717 514 LPPVLERASEYFSRL 528
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2567-3266 |
1.43e-13 |
|
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: 78.17 E-value: 1.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2567 EQRRKEAEEK--VRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERqiqlAQEAAFKKIEAEEKAHAAI 2644
Cdd:TIGR02168 155 EERRAIFEEAagISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEK----AERYKELKAELRELELALL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2645 VQQKEQemlqtrkqeksildkLKEEAERAkraaedadyarmraeqeaalsRQQVEEAERMKQRAEEEAQAKAQAQDEAEK 2724
Cdd:TIGR02168 231 VLRLEE---------------LREELEEL---------------------QEELKEAEEELEELTAELQELEEKLEELRL 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2725 LRKEAEleaaKRAHAEQAALKQKQLADEEMDKHKKFAEKtlrQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVT 2804
Cdd:TIGR02168 275 EVSELE----EEIEELQKELYALANEISRLEQQKQILRE---RLANLERQLEELEAQLEELESKLDELAEELAELEEKLE 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2805 DAMRQKAQVEEELFKVKIQMEELiklKLRIEEENKMLimkdkdstQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLA 2884
Cdd:TIGR02168 348 ELKEELESLEAELEELEAELEEL---ESRLEELEEQL--------ETLRSKVAQLELQIASLNNEIERLEARLERLEDRR 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2885 EDDLANQRALAEKMLKEKMQAIQEA-TRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKEtegfqKSLEAERRQQL 2963
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAA-----ERELAQLQARL 491
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2964 EITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAED---FGNKLHQT-ELATKERM--VVVQSLEIQRQ--QSGKEAEEL 3035
Cdd:TIGR02168 492 DSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSElisVDEGYEAAiEAALGGRLqaVVVENLNAAKKaiAFLKQNELG 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3036 RRAIAELEHEKEKLKQEAELLQKNSQEMQV----------------------------------AQQEQLRQETQ--VLQ 3079
Cdd:TIGR02168 572 RVTFLPLDSIKGTEIQGNDREILKNIEGFLgvakdlvkfdpklrkalsyllggvlvvddldnalELAKKLRPGYRivTLD 651
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3080 TTFLT-----------EKHLLLEKEKYIEKEKAKLENLyEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKE 3148
Cdd:TIGR02168 652 GDLVRpggvitggsakTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3149 AEESVRHKQDELHQLDKRRQEQEKLLADENRKLREKLEQLEEEHRIALAQTREMMIQTDDLAGSSQtkAMPNGRDAVDGL 3228
Cdd:TIGR02168 731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE--ELKALREALDEL 808
|
730 740 750
....*....|....*....|....*....|....*...
gi 1717010358 3229 aQNGMTELGFDGLRQKVTAEKLSNAGILNKDTLEKLKR 3266
Cdd:TIGR02168 809 -RAELTLLNEEAANLRERLESLERRIAATERRLEDLEE 845
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1205-1394 |
1.51e-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: 72.86 E-value: 1.51e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1205 LHTFVSAATKELMWLNDKEEEEVNFDWSDRNTNMAAKKENYSGLMRELELKEKKIKEIQSSGDRLLREDHPGRQTVEAFQ 1284
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1285 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDMKDTEEYLNKMQETMRKKYQCDrsiTVTRLEDLLQDSIDEKEQLTEY 1364
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|
gi 1717010358 1365 KGQLSALAKRAKTIVQLKPRSAAHPVRGRM 1394
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
635-735 |
1.64e-13 |
|
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: 69.63 E-value: 1.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 635 QKKTFTKWVNKHLIK--AQRHVTDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLKHRQV 706
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1717010358 707 KLVNIRNDDIADGNPKLTLGLIWTIILHF 735
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
750-847 |
1.78e-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: 69.33 E-value: 1.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQrmtESYQGLRCDNFTTSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 828
Cdd:cd21230 1 TPKQRLLGWIQ---NKIPQLPITNFTTDWNDGRALGALVDSCAPgLCPDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1717010358 829 PEDVDVPQPDEKSIITYVS 847
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2693-3201 |
2.27e-13 |
|
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: 77.57 E-value: 2.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2693 LSRQQVEeaermkqRAEEEAQAKAQAQDEAEKLRK-EAELEAAKRAHAEQAALKQKQLADE--EMDKHKKFAEKTLRQKA 2769
Cdd:pfam12128 218 LNRQQVE-------HWIRDIQAIAGIMKIRPEFTKlQQEFNTLESAELRLSHLHFGYKSDEtlIASRQEERQETSAELNQ 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2770 QVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEE---ELFKVKIQMEELIKLKLR-IEEENKMLIMKD 2845
Cdd:pfam12128 291 LLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDadiETAAADQEQLPSWQSELEnLEERLKALTGKH 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2846 KDSTQKFLAEEAEKMRQVAEEAARLSIEA----QEAARMRKLAEDDLANQralaEKMLKEKMQAiqeatrLKAEADMLQK 2921
Cdd:pfam12128 371 QDVTAKYNRRRSKIKEQNNRDIAGIKDKLakirEARDRQLAVAEDDLQAL----ESELREQLEA------GKLEFNEEEY 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2922 QKELAQEQArKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDfg 3001
Cdd:pfam12128 441 RLKSRLGEL-KLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEE-- 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3002 nklHQTELATKERMVVVQS---LEIQRQQSGKEAEELRRAIA-ELEHE--------KEKLKQEAEL------LQKNSQEM 3063
Cdd:pfam12128 518 ---RQSALDELELQLFPQAgtlLHFLRKEAPDWEQSIGKVISpELLHRtdldpevwDGSVGGELNLygvkldLKRIDVPE 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3064 QVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEKAKLENLYEDEVRKAQKLKQEQEhQLKQLEEEKQQLKASMGEAM 3143
Cdd:pfam12128 595 WAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARL-DLRRLFDEKQSEKDKKNKAL 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 3144 K-KQKEAEESVRHKQDELHQLDKRRQ---EQEKLLADENRKLR-EKLEQLEEEHRIALAQTRE 3201
Cdd:pfam12128 674 AeRKDSANERLNSLEAQLKQLDKKHQawlEEQKEQKREARTEKqAYWQVVEGALDAQLALLKA 736
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
750-850 |
2.72e-13 |
|
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: 69.33 E-value: 2.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAErDLGVTRLLDP 829
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1717010358 830 ED-VDVPQPDEKSIITYVSSLY 850
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2843-3193 |
2.73e-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: 76.70 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2843 MKDKDSTQKFLAEEAEKMRQVAEEAARlsieaqEAARMRKLAEDDLANQRALAEkmlkekmqaiQEATRLKAEADMLQKQ 2922
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDR----------QAAIYAEQERMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2923 KELAQEQARKFQEDKEQIEQQ-LAKETEGFqKSLEaerRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFG 3001
Cdd:pfam17380 348 RELERIRQEERKRELERIRQEeIAMEISRM-RELE---RLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3002 NKLHQTELATKERMvvvQSLEIQRQqsgKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQ---VL 3078
Cdd:pfam17380 424 QIRAEQEEARQREV---RRLEEERA---REMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQrrkIL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3079 QTTFLTEKHLLLekekyiekekaklenlyeDEVRKAQKLKQEQEHQLKQLEEEKQQLKASmgEAMKKQKEAEESVRHKQd 3158
Cdd:pfam17380 498 EKELEERKQAMI------------------EEERKRKLLEKEMEERQKAIYEEERRREAE--EERRKQQEMEERRRIQE- 556
|
330 340 350
....*....|....*....|....*....|....*
gi 1717010358 3159 elhQLDKRRQEQEKLLADEnrKLREKLEQLEEEHR 3193
Cdd:pfam17380 557 ---QMRKATEERSRLEAME--REREMMRQIVESEK 586
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
752-853 |
2.74e-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: 69.34 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 752 KEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 831
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 1717010358 832 -VDVPQPDEKSIITYVSSLYDAM 853
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2589-2817 |
3.37e-13 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 76.53 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2589 RQRKAALEEVERLKAKAEEAK-----RQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAA---IVQQKEQEMLQTRKQEK 2660
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKarfeaRQARLEREKAAREARHKKAAEARAAKDKDAVAAAlarVKAKKAAATQPIVIKAG 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2661 SILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAK-RAHA 2739
Cdd:PRK05035 512 ARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIaRAKA 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2740 EQAALKQKQLADEEMDkhkkfaEKTLRQKAQVEQELTKV---KLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEE 2816
Cdd:PRK05035 592 KKAAQQAASAEPEEQV------AEVDPKKAAVAAAIARAkakKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQA 665
|
.
gi 1717010358 2817 L 2817
Cdd:PRK05035 666 N 666
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
752-847 |
3.40e-13 |
|
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: 68.57 E-value: 3.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 752 KEKLLLWSQRMTESyqgLRCDNFTTSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPE 830
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPgLCPNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1717010358 831 DVDVPQPDEKSIITYVS 847
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2586-3195 |
3.90e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.88 E-value: 3.90e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2586 EAARQRKAALEEVERLKAKAEEAKRQKEL---AEKEAERQIQLAQEAAfkKIEAEEKAHAAIVQQKEQEMLQTRKQE-KS 2661
Cdd:COG4913 225 EAADALVEHFDDLERAHEALEDAREQIELlepIRELAERYAAARERLA--ELEYLRAALRLWFAQRRLELLEAELEElRA 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2662 ILDKLKEEAERAKRAAEDADYARMRAEQE-AALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAK----- 2735
Cdd:COG4913 303 ELARLEAELERLEARLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeef 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2736 RAHAEQAALKQKQLADEEMDKHKKFAEkTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKeevtDAMRQKAQVEE 2815
Cdd:COG4913 383 AALRAEAAALLEALEEELEALEEALAE-AEAALRDLRRELRELEAEIASLERRKSNIPARLLALR----DALAEALGLDE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2816 -------ELFKVKIQMEE---------------LI------KLKLRIEEENKMlimKDKDSTQKFLAEEAEKMRQVAEE- 2866
Cdd:COG4913 458 aelpfvgELIEVRPEEERwrgaiervlggfaltLLvppehyAAALRWVNRLHL---RGRLVYERVRTGLPDPERPRLDPd 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2867 --AARLSIEAQEAarmRKLAEDDLANQRALA----EKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQED-KEQ 2939
Cdd:COG4913 535 slAGKLDFKPHPF---RAWLEAELGRRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDnRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2940 IEQqLAKETEGFQKSLEAERRQQLEITAEAERL--KLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKErmvv 3017
Cdd:COG4913 612 LAA-LEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD---- 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3018 VQSLEiqrqqsgKEAEELRRAIAELEHEKEKLKQEAELLQKnsqemqvaQQEQLRQETQVLQTTfltekhLLLEKEKYIE 3097
Cdd:COG4913 687 LAALE-------EQLEELEAELEELEEELDELKGEIGRLEK--------ELEQAEEELDELQDR------LEAAEDLARL 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3098 KEKAKLENLYEDEVRKA--QKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEA-----------EESVRHKQDELHQL- 3163
Cdd:COG4913 746 ELRALLEERFAAALGDAveRELRENLEERIDALRARLNRAEEELERAMRAFNREwpaetadldadLESLPEYLALLDRLe 825
|
650 660 670
....*....|....*....|....*....|....*..
gi 1717010358 3164 -----DKRRQEQEKLLADENRKLREKLEQLEEEHRIA 3195
Cdd:COG4913 826 edglpEYEERFKELLNENSIEFVADLLSKLRRAIREI 862
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
637-738 |
4.34e-13 |
|
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: 68.80 E-value: 4.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 637 KTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLKHRQVKLV 709
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1717010358 710 NIRNDDIADGNPKLTLGLIWTIILHFQIS 738
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1943-2806 |
4.45e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.53 E-value: 4.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1943 EEERRRLAEVEAQLEKqtqlaeahakAKAQAEKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQELQQL--RQNSDMEI 2020
Cdd:PRK04863 278 ANERRVHLEEALELRR----------ELYTSRRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAAsdHLNLVQTA 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2021 KSKAKKIEEAEYNRRKIEEeihivrlQLEtmqkqkaSAEDELQELRARAEEAERQKKAAQEEAERLRRQVKD-----ESQ 2095
Cdd:PRK04863 344 LRQQEKIERYQADLEELEE-------RLE-------EQNEVVEEADEQQEENEARAEAAEEEVDELKSQLADyqqalDVQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2096 KKR-----EAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEA-------ERRMKQAEVEKERQIKVAQEVaqQSAAA 2163
Cdd:PRK04863 410 QTRaiqyqQAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEAteellslEQKLSVAQAAHSQFEQAYQLV--RKIAG 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2164 ELNSKRmsfAEKTAQlelSLKQEHITVTHLQEEAERLKKQHEEaekareeaekeLEKWHQKANEALRLRLQAEEVAHKKT 2243
Cdd:PRK04863 488 EVSRSE---AWDVAR---ELLRRLREQRHLAEQLQQLRMRLSE-----------LEQRLRQQQRAERLLAEFCKRLGKNL 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2244 LAQEEAEKqkEDAEREARKrakaeesalrqkELAEDELEKQRkladataQQKFSAEQELIRLKADtesgeqqrllleeel 2323
Cdd:PRK04863 551 DDEDELEQ--LQEELEARL------------ESLSESVSEAR-------ERRMALRQQLEQLQAR--------------- 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2324 frlknevneaIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQ 2403
Cdd:PRK04863 595 ----------IQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2404 RQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIalkekEAENERLRR---LAEDEAYQRKLLEEQatqhkqDIEE 2480
Cdd:PRK04863 665 SQPGGSEDPRLNALAERFGGVLLSEIYDDVSLEDAPYF-----SALYGPARHaivVPDLSDAAEQLAGLE------DCPE 733
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2481 KIILLKKSSD---------NELERQKnIVEDTLRQrriieeeirilkLNFEKASS----GKSDLELELNQLKNIAEETHR 2547
Cdd:PRK04863 734 DLYLIEGDPDsfddsvfsvEELEKAV-VVKIADRQ------------WRYSRFPEvplfGRAAREKRIEQLRAEREELAE 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2548 SKEKAEQEAEK-QR-------------QLALEEE---------QRRKEAEEKVRKILADEQEAARQRKAALEEV------ 2598
Cdd:PRK04863 801 RYATLSFDVQKlQRlhqafsrfigshlAVAFEADpeaelrqlnRRRVELERALADHESQEQQQRSQLEQAKEGLsalnrl 880
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2599 ---------ERLKAKAEEAKRQKELAEkEAERQIQlAQEAAFKKIEA------EEKAHAAIVQQKEQEMLQTRKQEKSIL 2663
Cdd:PRK04863 881 lprlnlladETLADRVEEIREQLDEAE-EAKRFVQ-QHGNALAQLEPivsvlqSDPEQFEQLKQDYQQAQQTQRDAKQQA 958
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2664 DKLKE-EAERAKRAAEDAdyARMRAEqEAALS---RQQVEEAERMKQRAEEEA-QAKAQAQDEAEKLrkeAELEAAKRAH 2738
Cdd:PRK04863 959 FALTEvVQRRAHFSYEDA--AEMLAK-NSDLNeklRQRLEQAEQERTRAREQLrQAQAQLAQYNQVL---ASLKSSYDAK 1032
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2739 AEQ-AALKQ--KQL---ADEEMDKHKKFAEKTLRQ--------KAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVT 2804
Cdd:PRK04863 1033 RQMlQELKQelQDLgvpADSGAEERARARRDELHArlsanrsrRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
..
gi 1717010358 2805 DA 2806
Cdd:PRK04863 1113 NA 1114
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3321-3358 |
4.82e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.81 E-value: 4.82e-13
10 20 30
....*....|....*....|....*....|....*...
gi 1717010358 3321 LLEAQAASGFIIDPVKNERLSVNEAVKENVIGPELHNK 3358
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQK 38
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2244-3204 |
5.41e-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: 76.24 E-value: 5.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2244 LAQEEAEKQKEDAEREARKRAKAEESaLRQ------KELAEDELEKQrkLADATAQQKFSAEQELIRLKADTESgeqqrl 2317
Cdd:TIGR00606 165 LSEGKALKQKFDEIFSATRYIKALET-LRQvrqtqgQKVQEHQMELK--YLKQYKEKACEIRDQITSKEAQLES------ 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2318 lLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALS 2397
Cdd:TIGR00606 236 -SREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTV 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2398 EEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDeayqrklLEEQATQHKQD 2477
Cdd:TIGR00606 315 REKERELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATR-------LELDGFERGPF 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2478 IEEKIILLKKSSDNELERQKNIVEDTLR--QRRIIEEEIRILKLNFEKASSGKSdLELELNQL-KNIAEETHRSKEKAEQ 2554
Cdd:TIGR00606 388 SERQIKNFHTLVIERQEDEAKTAAQLCAdlQSKERLKQEQADEIRDEKKGLGRT-IELKKEILeKKQEELKFVIKELQQL 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2555 EAEKQRQLALEEEQRRKEAE-EKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKEL-AEKEAERQIQLAqeaAFK 2632
Cdd:TIGR00606 467 EGSSDRILELDQELRKAERElSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLnHHTTTRTQMEML---TKD 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2633 KIEAEEKAHAAIVQQKEQEMLQT-----RKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQR 2707
Cdd:TIGR00606 544 KMDKDEQIRKIKSRHSDELTSLLgyfpnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2708 AEEEAQAKAQAQDEA---EKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQkAQVEQELTKVKLQLEe 2784
Cdd:TIGR00606 624 YEDKLFDVCGSQDEEsdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV-FQTEAELQEFISDLQ- 701
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2785 tdHQKTLLDDESQRLKEEVTDAMRQKaqvEEELFKVKIQMEELiklklrieeenkmlimkdkDSTQKFLAEEAEKMRQVA 2864
Cdd:TIGR00606 702 --SKLRLAPDKLKSTESELKKKEKRR---DEMLGLAPGRQSII-------------------DLKEKEIPELRNKLQKVN 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2865 EEAARLsieaqeaarmrklaEDDLANQralaEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQedkeqieqQL 2944
Cdd:TIGR00606 758 RDIQRL--------------KNDIEEQ----ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIA--------QQ 811
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2945 AKETEGFQKSLEAERRQQlEITAEAERLKLQVLEMSKAQaKAEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQ 3024
Cdd:TIGR00606 812 AAKLQGSDLDRTVQQVNQ-EKQEKQHELDTVVSKIELNR-KLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3025 RQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQttfltekhlllekekyieKEKAKLE 3104
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVN------------------DIKEKVK 951
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3105 NLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQldkrRQEQEKLLADE--NRKLR 3182
Cdd:TIGR00606 952 NIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDT----QKIQERWLQDNltLRKRE 1027
|
970 980
....*....|....*....|..
gi 1717010358 3183 EKLEQLEEEHRIALAQTREMMI 3204
Cdd:TIGR00606 1028 NELKEVEEELKQHLKEMGQMQV 1049
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4313-4351 |
7.26e-13 |
|
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: 7.26e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 4313 LLDAQAATGFIIDPVKNEMLTVDEAVRKGVVGPELHDRL 4351
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2649-3201 |
7.85e-13 |
|
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: 7.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2649 EQEMLQTRKQEKsILDKLKEEAERAKRAAEDADYAR--------MRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQD 2720
Cdd:COG4913 241 HEALEDAREQIE-LLEPIRELAERYAAARERLAELEylraalrlWFAQRRLELLEAELEELRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2721 EAeklrkEAELEAAKRAHAeQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQktlLDDESQRLK 2800
Cdd:COG4913 320 AL-----REELDELEAQIR-GNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE---FAALRAEAA 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2801 EEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLimKDKDSTqkfLAEEAEKMRQVAEEAARLSIEA------ 2874
Cdd:COG4913 391 ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASL--ERRKSN---IPARLLALRDALAEALGLDEAElpfvge 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2875 -----QEAARMRKLAEDDLANQR---ALAEKMLKEKMQAIqEATRLKAEADMLQKQKELAQEQARKFQEDkeQIEQQLAK 2946
Cdd:COG4913 466 lievrPEEERWRGAIERVLGGFAltlLVPPEHYAAALRWV-NRLHLRGRLVYERVRTGLPDPERPRLDPD--SLAGKLDF 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2947 ETEGFQKSLEAE--RRQQLEITAEAERLKLQVLEMSKA-QAKAEEDAkkFKKQAEDFGNKLHQTELATKERmvvVQSLEI 3023
Cdd:COG4913 543 KPHPFRAWLEAElgRRFDYVCVDSPEELRRHPRAITRAgQVKGNGTR--HEKDDRRRIRSRYVLGFDNRAK---LAALEA 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3024 QRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQK----NSQEMQVAQ-QEQLRQETQVLQttfltekHLLLEKekyiek 3098
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRlaeySWDEIDVASaEREIAELEAELE-------RLDASS------ 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3099 ekaklenlyeDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADEn 3178
Cdd:COG4913 685 ----------DDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE- 753
|
570 580
....*....|....*....|...
gi 1717010358 3179 RKLREKLEQLEEEHRIALAQTRE 3201
Cdd:COG4913 754 RFAAALGDAVERELRENLEERID 776
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2279-2721 |
1.11e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.80 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2279 DELEKQRKLADATAQQKFSAEQELIRLKAdtesgeqqrllleeelfrlknEVNEAIQKRKKMEEELAKVRAEMEI--LLE 2356
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEE---------------------ELEELEAELEELREELEKLEKLLQLlpLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2357 SKSRAEEESRSNTEKSKHMLEveasKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLK 2436
Cdd:COG4717 133 ELEALEAELAELPERLEELEE----RLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2437 TEAEIALKEKEAENERLRRlaEDEAYQRKLLEEQATQHKQDIEEKIIL-------------LKKSSDNELERQKNIVEDT 2503
Cdd:COG4717 209 AELEEELEEAQEELEELEE--ELEQLENELEAAALEERLKEARLLLLIaaallallglggsLLSLILTIAGVLFLVLGLL 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2504 LRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILAD 2583
Cdd:COG4717 287 ALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2584 EQEAARQR---KAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAI---VQQKEQEMLQTRK 2657
Cdd:COG4717 367 ELEQEIAAllaEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELeeeLEELEEELEELEE 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2658 QEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEA--QAKAQAQDE 2721
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELleEAREEYREE 512
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2547-3244 |
1.43e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 74.99 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2547 RSKEKAEQEAEKQRqlaLEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAkrQKELAEKE--AERQIQ 2624
Cdd:PRK04863 295 LYTSRRQLAAEQYR---LVEMARELAELNEAESDLEQDYQAASDHLNLVQTALRQQEKIERY--QADLEELEerLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2625 LAQEAAFKKIEAEEKAHAAivqqkEQEMLQTRKQ---EKSILDKLKEEA---ERAKRAAEdadyarmRAEQEAALSRQQV 2698
Cdd:PRK04863 370 VVEEADEQQEENEARAEAA-----EEEVDELKSQladYQQALDVQQTRAiqyQQAVQALE-------RAKQLCGLPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2699 EEAERMKQRAEEEAQAKAQAQDEAEklRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLR----QKAQVEQ- 2773
Cdd:PRK04863 438 DNAEDWLEEFQAKEQEATEELLSLE--QKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLRrlreQRHLAEQl 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2774 -----ELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAM---RQKAQVEEELFKVKIQMEELIKLKLRIEEEnkmlimkd 2845
Cdd:PRK04863 516 qqlrmRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDeleQLQEELEARLESLSESVSEARERRMALRQQ-------- 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2846 kdstQKFLAEEAEKMRQVAEEAarlsIEAQEA-ARMRKLAEDDLANQRALaekmlkekMQAIQeatrlkaeaDMLQKQKE 2924
Cdd:PRK04863 588 ----LEQLQARIQRLAARAPAW----LAAQDAlARLREQSGEEFEDSQDV--------TEYMQ---------QLLERERE 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2925 LAQE----QARKFQEDkEQIEQQLAKETEgfqkslEAERRQQLeitaeAERL---------------------------- 2972
Cdd:PRK04863 643 LTVErdelAARKQALD-EEIERLSQPGGS------EDPRLNAL-----AERFggvllseiyddvsledapyfsalygpar 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2973 -KLQVLEMSKAQAKAE------EDAKKFKKQAEDFGNKLHQTELAtkERMVVVQSLEIQRQQS--------GKEAEELRr 3037
Cdd:PRK04863 711 hAIVVPDLSDAAEQLAgledcpEDLYLIEGDPDSFDDSVFSVEEL--EKAVVVKIADRQWRYSrfpevplfGRAAREKR- 787
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3038 aIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEKA-KLENLYEDEVRKAQK 3116
Cdd:PRK04863 788 -IEQLRAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQLNRRRVELErALADHESQEQQQRSQ 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3117 LKQEQEH---------QLKQLEEEK-QQLKASMGEAMKKQKEAEESVRHKQDELHQLDkrrQEQEKLLADEnrklrEKLE 3186
Cdd:PRK04863 867 LEQAKEGlsalnrllpRLNLLADETlADRVEEIREQLDEAEEAKRFVQQHGNALAQLE---PIVSVLQSDP-----EQFE 938
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 3187 QLEEEHRIALAQTREMMIQTDDLAGSSQTKAMPNGRDAVDGLAQN-GMTELgfdgLRQK 3244
Cdd:PRK04863 939 QLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNsDLNEK----LRQR 993
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2193-2767 |
1.54e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.57 E-value: 1.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2193 LQEEAERLKKQHEEAEKAREEAEKELEKWHQKA-NEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEEsal 2271
Cdd:COG4913 240 AHEALEDAREQIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEA--- 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2272 RQKELAEDELEKQRKLADATAQQKFSAEQELIRLKAdtesgeqqrllleeelfrlknEVNEAIQKRKKMEEELAKVRAEM 2351
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGDRLEQLEREIERLER---------------------ELEERERRRARLEALLAALGLPL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2352 EillesksRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERI---LKEKLAA 2428
Cdd:COG4913 376 P-------ASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2429 INEATRLKTE-----AE-IALKEKEAE----------NERLRRLAEDEAYQR-----------------KLLEEQATQHK 2475
Cdd:COG4913 449 LAEALGLDEAelpfvGElIEVRPEEERwrgaiervlgGFALTLLVPPEHYAAalrwvnrlhlrgrlvyeRVRTGLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2476 QDIEEKIILLK---KSS------DNELERQKNIV----EDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQL--KN 2540
Cdd:COG4913 529 PRLDPDSLAGKldfKPHpfrawlEAELGRRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLgfDN 608
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2541 iaeethrskekAEQEAEKQRQLAlEEEQRRKEAEEKVRKiLADEQEAARQRKAALEEVERLKAKAEEAKR-QKELAEKEA 2619
Cdd:COG4913 609 -----------RAKLAALEAELA-ELEEELAEAEERLEA-LEAELDALQERREALQRLAEYSWDEIDVASaEREIAELEA 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2620 ERqiqlaqeaafkkiEAEEKAHAAIVQQKEQemlqtrkqeksiLDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVE 2699
Cdd:COG4913 676 EL-------------ERLDASSDDLAALEEQ------------LEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2700 EAERMKQRAEEEAQakAQAQDEAEKLRKEAELEAAKRAHAEQAAlKQKQLADEEMDKHKKFAEKTLRQ 2767
Cdd:COG4913 731 ELQDRLEAAEDLAR--LELRALLEERFAAALGDAVERELRENLE-ERIDALRARLNRAEEELERAMRA 795
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
750-850 |
1.88e-12 |
|
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: 66.98 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAErDLGVTRLLDP 829
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1717010358 830 ED-VDVPQPDEKSIITYVSSLY 850
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
627-729 |
2.22e-12 |
|
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: 66.68 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 627 AEDERD-RVqkktFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIA 697
Cdd:cd21300 3 AEGEREaRV----FTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYA 76
|
90 100 110
....*....|....*....|....*....|..
gi 1717010358 698 LDYLKHRQVKLVNIRNDDIADGNPKLTLGLIW 729
Cdd:cd21300 77 VELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1943-2307 |
2.53e-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: 73.62 E-value: 2.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1943 EEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRM-----QEEVSKREvvavdaeQQKQTIQQELQQLRQNSD 2017
Cdd:pfam17380 234 EKMERRKESFNLAEDVTTMTPEYTVRYNGQTMTENEFLNQLLhivqhQKAVSERQ-------QQEKFEKMEQERLRQEKE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2018 MEIKS--KAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKasaEDELQelRARAEEAERqkkaaqeEAERLRRQ-VKDES 2094
Cdd:pfam17380 307 EKAREveRRRKLEEAEKARQAEMDRQAAIYAEQERMAMER---ERELE--RIRQEERKR-------ELERIRQEeIAMEI 374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2095 QKKREAEeelkrKVQAEKDAAREKQRA-MEDLQKFRSQAEEAERRMKQAEVEKErQIKVAQEVAQQSAAAELNSKRMSFA 2173
Cdd:pfam17380 375 SRMRELE-----RLQMERQQKNERVRQeLEAARKVKILEEERQRKIQQQKVEME-QIRAEQEEARQREVRRLEEERAREM 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2174 EKTAQLELSlKQEHITVTHLQEEAERLKKQHEEAEkareeaekelEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQK 2253
Cdd:pfam17380 449 ERVRLEEQE-RQQQVERLRQQEEERKRKKLELEKE----------KRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2254 EDAEREARKRAKAEEsalRQKELAEDELEKQRKLAD--ATAQQKFSAEQELIRLKA 2307
Cdd:pfam17380 518 LEKEMEERQKAIYEE---ERRREAEEERRKQQEMEErrRIQEQMRKATEERSRLEA 570
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1933-2179 |
2.62e-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: 73.62 E-value: 2.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1933 VEEKAAEKLKEEERRR-LAEVE----AQLEKQTQLAEAHAKAKAQAEKEAE---------ELQRRMQEEVS-------KR 1991
Cdd:pfam17380 301 LRQEKEEKAREVERRRkLEEAEkarqAEMDRQAAIYAEQERMAMERERELErirqeerkrELERIRQEEIAmeisrmrEL 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1992 EVVAVDAEQQKQTIQQELQQLRQNSDMEiKSKAKKIEEAEYNRRKIEEE------IHIVRLQLETMQKQKASAEDEL--- 2062
Cdd:pfam17380 381 ERLQMERQQKNERVRQELEAARKVKILE-EERQRKIQQQKVEMEQIRAEqeearqREVRRLEEERAREMERVRLEEQerq 459
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2063 -QELRARAEEAERQKKAAQEEAERLRRQVKDESQKK--REAEEELKRKVQAEKDAAREKQRAMEDLQKfrSQAEEAERRM 2139
Cdd:pfam17380 460 qQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKilEKELEERKQAMIEEERKRKLLEKEMEERQK--AIYEEERRRE 537
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1717010358 2140 KQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQL 2179
Cdd:pfam17380 538 AEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREM 577
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1963-2186 |
3.04e-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: 3.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1963 AEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQELQQLRQnsdmEIKSKAKKIEEAEYNRRKIEEEIH 2042
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELA----ALKKEEKALLKQLAALER----RIAALARRIRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2043 IVRLQLETMQKQKASAEDELQELRARAEEAERQKKAA-------QEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAA 2115
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAlllspedFLDAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2116 REKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKV--AQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQE 2186
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARleKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
752-851 |
3.30e-12 |
|
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: 65.82 E-value: 3.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 752 KEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTN---LENLDQAFNVAER-DLGVTRLL 827
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1717010358 828 DPEDVdVPQPDEKSIITYVSSLYD 851
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2593-2794 |
3.73e-12 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 71.76 E-value: 3.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2593 AALEEVERLKAKAEEAKRQKELAEKEAERQI------QLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKL 2666
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQAeelqqkQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2667 KEEAERAKRAAEDAdyarmrAEQEAALSRQQVEEAermKQRAEEEAQAK----AQAQDEAEKLRKEAElEAAKRAHAE-- 2740
Cdd:PRK09510 139 AKAAAAAKAKAEAE------AKRAAAAAKKAAAEA---KKKAEAEAAKKaaaeAKKKAEAEAAAKAAA-EAKKKAEAEak 208
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2741 -QAALKQKQLADEEMDKHKKFAEKtlRQKAQVEQELTKVKLQLEETDHQKTLLDD 2794
Cdd:PRK09510 209 kKAAAEAKKKAAAEAKAAAAKAAA--EAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1937-2131 |
7.34e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 72.64 E-value: 7.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1937 AAEKLkEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRmqEEVSKREVVAVDAEQQKQTIQQELQQLRQNS 2016
Cdd:COG4913 608 NRAKL-AALEAELAELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS 684
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2017 DmEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEE--AERLRRQVKDES 2094
Cdd:COG4913 685 D-DLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAllEERFAAALGDAV 763
|
170 180 190
....*....|....*....|....*....|....*...
gi 1717010358 2095 QkkREAEEELKRKVQAEKDAAREKQRAMEDL-QKFRSQ 2131
Cdd:COG4913 764 E--RELRENLEERIDALRARLNRAEEELERAmRAFNRE 799
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1900-2389 |
1.05e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.02 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1900 IQEYVDLRTRYSELTTLTSQYIKfITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEKqtqlAEAHAKAKAQAEKEAEE 1979
Cdd:PRK03918 275 IEELEEKVKELKELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEERIKE----LEEKEERLEELKKKLKE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1980 LQRRMqEEVSKREVVAVDAEQqkqtIQQELQQLRQN-SDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASA 2058
Cdd:PRK03918 350 LEKRL-EELEERHELYEEAKA----KKEELERLKKRlTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKEL 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2059 EDELQELRA--------RAEEAERQKKaaqEEAERLRRQVKDESQKKREAEEELK--RKVQAEKDAAREKQRAMEDLQKF 2128
Cdd:PRK03918 425 KKAIEELKKakgkcpvcGRELTEEHRK---ELLEEYTAELKRIEKELKEIEEKERklRKELRELEKVLKKESELIKLKEL 501
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2129 RSQAEEAERRMKQAEVEK-ERQIKVAQEVAQQSAAAElnsKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQheea 2207
Cdd:PRK03918 502 AEQLKELEEKLKKYNLEElEKKAEEYEKLKEKLIKLK---GEIKSLKKELEKLEELKKKLAELEKKLDELEEELAE---- 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2208 ekareeAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKL 2287
Cdd:PRK03918 575 ------LLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKE 648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2288 ADAtAQQKFSaEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVR-AEMEILLESKSRAE-EES 2365
Cdd:PRK03918 649 LEE-LEKKYS-EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREkAKKELEKLEKALERvEEL 726
|
490 500
....*....|....*....|....*
gi 1717010358 2366 RSNTEKSKHMLEVEA-SKLRELAEE 2389
Cdd:PRK03918 727 REKVKKYKALLKERAlSKVGEIASE 751
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3648-3686 |
1.10e-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: 1.10e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 3648 LLEAQAGTGYIIDPVKNEKFPVEEAVKASVVGPEFNEKL 3686
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1907-2149 |
1.56e-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: 71.31 E-value: 1.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1907 RTRYSELTTLTSQYIKFITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRmqE 1986
Cdd:pfam17380 364 RIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRL--E 441
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1987 EVSKREVVAVDAEQQKQtiQQELQQLRQNSDmEIKSKAKKIEEAEYNRRKIEEEihivrlqletmqkQKASAEDELQELR 2066
Cdd:pfam17380 442 EERAREMERVRLEEQER--QQQVERLRQQEE-ERKRKKLELEKEKRDRKRAEEQ-------------RRKILEKELEERK 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2067 ARAEEAERQKKAAQEEAERlRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEK 2146
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEE-RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVES 584
|
...
gi 1717010358 2147 ERQ 2149
Cdd:pfam17380 585 EKA 587
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
752-852 |
1.65e-11 |
|
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: 63.91 E-value: 1.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 752 KEKLLLWSQRMTESYQGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLDPED 831
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 1717010358 832 VdVPQPDEKSIITYVSSLYDA 852
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1889-2482 |
1.90e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1889 KPKVQSTSDSIIQEYVDLRTRYSELTTLTSQYikfitETLCRLnveEKAAEKLkEEERRRLAEVEAQLEKQTqlAEAHAK 1968
Cdd:COG4913 220 EPDTFEAADALVEHFDDLERAHEALEDAREQI-----ELLEPI---RELAERY-AAARERLAELEYLRAALR--LWFAQR 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1969 AKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQL 2048
Cdd:COG4913 289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2049 ETMQKQKASAEDELQELRARA----EEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKR----------KVQAEKDA 2114
Cdd:COG4913 369 AALGLPLPASAEEFAALRAEAaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIASlerrksnipaRLLALRDA 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2115 AREK------------------------QRAMEDL---QKFR--------SQAEEAERRMKQA------EVEKERQIKVA 2153
Cdd:COG4913 449 LAEAlgldeaelpfvgelievrpeeerwRGAIERVlggFALTllvppehyAAALRWVNRLHLRgrlvyeRVRTGLPDPER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2154 QEVAQQSAAAELNSKRMSFAEkTAQLELSLKQEHITVTHLQE--------EAERLKKQheeaekareeAEKELEKWHQKA 2225
Cdd:COG4913 529 PRLDPDSLAGKLDFKPHPFRA-WLEAELGRRFDYVCVDSPEElrrhpraiTRAGQVKG----------NGTRHEKDDRRR 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2226 ----------NEALRLRLQAEEVAHKKTLAqeEAEKQKEDAEREARKRAKAEESALRQKELAEDEL---EKQRKLAData 2292
Cdd:COG4913 598 irsryvlgfdNRAKLAALEAELAELEEELA--EAEERLEALEAELDALQERREALQRLAEYSWDEIdvaSAEREIAE--- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2293 qqkfsAEQELIRLkadtESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKS 2372
Cdd:COG4913 673 -----LEAELERL----DASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2373 KHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKE-KLAAINEATRLKTEAEiALKEKEAENE 2451
Cdd:COG4913 744 RLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLD 822
|
650 660 670
....*....|....*....|....*....|...
gi 1717010358 2452 RLR--RLAEDEAYQRKLLEEQATQHKQDIEEKI 2482
Cdd:COG4913 823 RLEedGLPEYEERFKELLNENSIEFVADLLSKL 855
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2449-2804 |
1.95e-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: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2449 ENERLRRLAEDEAYQRKLLEEQATQHKQDIE-EKIILLKKSSDNELERQKNIVE-DTLRQRRIIEEEIRilklnFEKASS 2526
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKAVSERQQQEKFEKMEqERLRQEKEEKAREVERRRKLEEaEKARQAEMDRQAAI-----YAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2527 GKSDLELELNQLKNiaEETHRSKEKAEQE---AEKQRQLALEEEQ-RRKEAEEKVRKiladEQEAARQRKAALEEVERlK 2602
Cdd:pfam17380 342 MAMERERELERIRQ--EERKRELERIRQEeiaMEISRMRELERLQmERQQKNERVRQ----ELEAARKVKILEEERQR-K 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2603 AKAEEAKRQKELAEKEAERQIQLaqeaafKKIEAEEKAHAAIVQQKEQEmlqtRKQEKSILDKLKEEAERAKraaedady 2682
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREV------RRLEEERAREMERVRLEEQE----RQQQVERLRQQEEERKRKK-------- 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2683 ARMRAEQEaalSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQaalKQKQLADEEMDKHKKFAE 2762
Cdd:pfam17380 477 LELEKEKR---DRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE---ERRREAEEERRKQQEMEE 550
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1717010358 2763 K--TLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVT 2804
Cdd:pfam17380 551 RrrIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2236-3044 |
2.01e-11 |
|
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: 71.02 E-value: 2.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2236 EEVAHKKTLAQEEAEKqkedaereaRKRAKAEESALrQKELAEDELekqrklADATAQQKFSAEQELIRLKADTesgeqq 2315
Cdd:pfam12128 237 MKIRPEFTKLQQEFNT---------LESAELRLSHL-HFGYKSDET------LIASRQEERQETSAELNQLLRT------ 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2316 rllleeELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEEsrsNTEKSKHMLEVEASKLRELAEEAARLRA 2395
Cdd:pfam12128 295 ------LDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDA---DIETAAADQEQLPSWQSELENLEERLKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2396 LSEEAkrqrQIAEGEAARQRAEAERILKEKLAAINEatRLKTEAEIALKEKEAENERLRRLaedEAYQRKLLEEQATQHK 2475
Cdd:pfam12128 366 LTGKH----QDVTAKYNRRRSKIKEQNNRDIAGIKD--KLAKIREARDRQLAVAEDDLQAL---ESELREQLEAGKLEFN 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2476 qdIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQE 2555
Cdd:pfam12128 437 --EEEYRLKSRLGELKLRLNQATATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRR 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2556 AEKQRQlALEEEQR-------------RKEA---EEKVRKILADEQ-----------EAARQRKAALEEVeRLKAKAEEA 2608
Cdd:pfam12128 515 LEERQS-ALDELELqlfpqagtllhflRKEApdwEQSIGKVISPELlhrtdldpevwDGSVGGELNLYGV-KLDLKRIDV 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2609 KRQKELaEKEAERQIQLAQEAafkkIEAEEKAHAAIvqqkEQEMLQTRKQeksiLDKLKEEAERAKRAAEDADYARMRae 2688
Cdd:pfam12128 593 PEWAAS-EEELRERLDKAEEA----LQSAREKQAAA----EEQLVQANGE----LEKASREETFARTALKNARLDLRR-- 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2689 qeaaLSRQQVEEAERMKQRAEEEaqaKAQAQDEAEKLRKEAeleaakrahaeQAALKQKQLADEEMDKHKKFAEKTLRQK 2768
Cdd:pfam12128 658 ----LFDEKQSEKDKKNKALAER---KDSANERLNSLEAQL-----------KQLDKKHQAWLEEQKEQKREARTEKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2769 AQVEQELTKVKLQL--EETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDK 2846
Cdd:pfam12128 720 WQVVEGALDAQLALlkAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFD 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2847 DSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLAN---QRALAEKMLKE------KMQAIQEA-TRLKAEA 2916
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKlemERKASEKQQVRlsenlrGLRCEMSKlATLKEDA 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2917 DMLQKQKELAQ--EQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQvlEMSKAQAKAEEDAKKFK 2994
Cdd:pfam12128 880 NSEQAQGSIGErlAQLEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDH--YQNDKGIRLLDYRKLVP 957
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2995 KQAEDFGNKLHQTELATKERMVV--------VQSLEIQRQQSGKEAEELRRAIAELEH 3044
Cdd:pfam12128 958 YLEQWFDVRVPQSIMVLREQVSIlgvdltefYDVLADFDRRIASFSRELQREVGEEAF 1015
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4389-4427 |
2.37e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.19 E-value: 2.37e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 4389 LLDAQLATGGIIDPRFGFHLSLEISYQRGYLNRETYDRL 4427
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2340-2975 |
2.42e-11 |
|
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: 70.92 E-value: 2.42e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2340 MEEELAKVRAE----MEILLEsksraEEESRSNTEKSKHMLEVEAsklreLAEEAARLRALSEEAKRQRQIAEGEAARQR 2415
Cdd:pfam15921 243 VEDQLEALKSEsqnkIELLLQ-----QHQDRIEQLISEHEVEITG-----LTEKASSARSQANSIQSQLEIIQEQARNQN 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2416 AEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILL-----KKSSD 2490
Cdd:pfam15921 313 SMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLladlhKREKE 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2491 NELERQKN-----------IVEDTLRQRRiieeeirilklnfekassgkSDLELELNQLKNIAEEThrskeKAEQEAEKQ 2559
Cdd:pfam15921 393 LSLEKEQNkrlwdrdtgnsITIDHLRREL--------------------DDRNMEVQRLEALLKAM-----KSECQGQME 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2560 RQLAleEEQRRKEAEEKVRKIladeqeaarqrKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEK 2639
Cdd:pfam15921 448 RQMA--AIQGKNESLEKVSSL-----------TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEA 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2640 AHAAIVQQKEQEMLQTRKqeksiLDKLKEEAERAKRAAEDADYARMR-AEQEAALS--RQQVEEAERMKQRAEEEAQA-- 2714
Cdd:pfam15921 515 TNAEITKLRSRVDLKLQE-----LQHLKNEGDHLRNVQTECEALKLQmAEKDKVIEilRQQIENMTQLVGQHGRTAGAmq 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2715 --KAQAQDEAEKLRKE-AELEAAKRAHAEQAALKQKQLADEEMDKHK--KFAEKTLRQKAQVEQELTKVKLQLEETDHQK 2789
Cdd:pfam15921 590 veKAQLEKEINDRRLElQEFKILKDKKDAKIRELEARVSDLELEKVKlvNAGSERLRAVKDIKQERDQLLNEVKTSRNEL 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2790 TLLDDESQRLKEEvtdaMRQKAQvEEELFKVKIQMeELIKLKLRIEE-ENKMLIMKDKDSTQKFLAEEAEKmrQVAeeAA 2868
Cdd:pfam15921 670 NSLSEDYEVLKRN----FRNKSE-EMETTTNKLKM-QLKSAQSELEQtRNTLKSMEGSDGHAMKVAMGMQK--QIT--AK 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2869 RLSIEAQEAArmRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKET 2948
Cdd:pfam15921 740 RGQIDALQSK--IQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKAS 817
|
650 660
....*....|....*....|....*..
gi 1717010358 2949 EGFQKSLEAERRQQleitAEAERLKLQ 2975
Cdd:pfam15921 818 LQFAECQDIIQRQE----QESVRLKLQ 840
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2563-3206 |
2.91e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.45 E-value: 2.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2563 ALEE-EQRRKEAEEKVRKILADEQEAARQRKAALEEVErlkakaeeakrQKELAEKEAERQIQLAQ-EAAFKKIEaEEKA 2640
Cdd:PRK02224 163 KLEEyRERASDARLGVERVLSDQRGSLDQLKAQIEEKE-----------EKDLHERLNGLESELAElDEEIERYE-EQRE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2641 HAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEE--AERMKQRAEEE-----AQ 2713
Cdd:PRK02224 231 QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleEERDDLLAEAGlddadAE 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2714 AKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLD 2793
Cdd:PRK02224 311 AVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2794 DESQRLKEEVTDAMRQKAQVEEELfkvkiqmEELIKLKLRIEEEnkmliMKDKDSTQKFLAEEAEKMRQVAEEAA--RLS 2871
Cdd:PRK02224 391 EEIEELRERFGDAPVDLGNAEDFL-------EELREERDELRER-----EAELEATLRTARERVEEAEALLEAGKcpECG 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2872 IEAQEAARMRKLAEDdlanqRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEqARKFQEDKEQIEQQLAKETEGf 2951
Cdd:PRK02224 459 QPVEGSPHVETIEED-----RERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDR-IERLEERREDLEELIAERRET- 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2952 qksLEAERRQQLEITAEAERLKlqvlemSKAQAKaEEDAKKFKKQAEdfgnklhqtelatkERMVVVQSLEIQRQQSGKE 3031
Cdd:PRK02224 532 ---IEEKRERAEELRERAAELE------AEAEEK-REAAAEAEEEAE--------------EAREEVAELNSKLAELKER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3032 AEELRRaIAELEHEKEKLKQEAELLqkNSQEMQVAQQEQLRQETqvlqttfLTEKhlllekekyIEKEKAKLENLYEDEV 3111
Cdd:PRK02224 588 IESLER-IRTLLAAIADAEDEIERL--REKREALAELNDERRER-------LAEK---------RERKRELEAEFDEARI 648
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3112 RKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVrhkqDELHQLDKRRQE-QEKLLADENrkLREKLEQLEE 3190
Cdd:PRK02224 649 EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENEL----EELEELRERREAlENRVEALEA--LYDEAEELES 722
|
650
....*....|....*.
gi 1717010358 3191 EHRIALAQTREMMIQT 3206
Cdd:PRK02224 723 MYGDLRAELRQRNVET 738
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1580-2451 |
3.28e-11 |
|
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: 70.39 E-value: 3.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1580 RLQLEGCESRTIHKIRSPMEKDPIKECSQRISEQQQIHFELEGIKKNLDKVSEKTQKVLAQKEQSTSTPLLRTEHEITLQ 1659
Cdd:pfam02463 155 RLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1660 KMDQVYSLSTIYLEKLKTINLVIR---------STHGAEEVVKTYEDQLKEVHAVPSDSKELEATKAELKKLRSQVEGHQ 1730
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQeiekeeeklAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1731 PLfNTLEADLNKAKDVNEQMLRSHSERDVDLDRYRERVQQLLErwqAILVQIDLRQRELDQLGRQLRYYRETYDWLIKWI 1810
Cdd:pfam02463 315 KL-KESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEE---EEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1811 KDAKQRQEQIQSVPITDSKTMKEQLLQLKKLLEEIESNRTKVDECQKY-----AKQYIDAIKDYELQLVTYKAQVEPVVS 1885
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESielkqGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1886 PAKKPKVQSTSDSIIQEYVDLRTRYSELTTLtSQYIKFITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEK---QTQL 1962
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQK-ESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKvaiSTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1963 AEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIH 2042
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2043 IVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAM 2122
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2123 EDLQKFRSQAEEAERRMKQAEVEK-ERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHI------TVTHLQE 2195
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDKiNEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELaeerekTEKLKVE 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2196 EAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVA---HKKTLAQEEAEKQKEDAEREARKRAKAEESALR 2272
Cdd:pfam02463 790 EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEeleELALELKEEQKLEKLAEEELERLEEEITKEELL 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2273 QKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEME 2352
Cdd:pfam02463 870 QELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKE 949
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2353 ILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAE-EAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINE 2431
Cdd:pfam02463 950 KEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEkEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSI 1029
|
890 900
....*....|....*....|
gi 1717010358 2432 ATRLKTEAEIALKEKEAENE 2451
Cdd:pfam02463 1030 NKGWNKVFFYLELGGSAELR 1049
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1109-1298 |
4.07e-11 |
|
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: 65.93 E-value: 4.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1109 LRYLQELLSWVEENQRRINSAEWGVDLPSVESHLGSHRGLHQSIDEFRAKIERARADEAQI---SPGSRSSYRDYLGKLD 1185
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1186 LQYAKLLNSSKSRLRHLE---SLHTFVSAATKELMWLNDKEEEEVNFDWSDRNTNMAAKKENYSGLMRELELKEKKIKEI 1262
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1717010358 1263 QSSGDRLLREDHP-GRQTVEAFQAALQTQWSWMLQLC 1298
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
3021-3217 |
4.25e-11 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.97 E-value: 4.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3021 LEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEmQVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEK 3100
Cdd:COG1196 216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEE-LEAELAELEAELEELRLELEELELELEEAQAEEYELL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3101 AKLENLYEDEVRKAQKLKQEQEhQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRK 3180
Cdd:COG1196 295 AELARLEQDIARLEERRRELEE-RLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
|
170 180 190
....*....|....*....|....*....|....*..
gi 1717010358 3181 LREKLEQLEEEHRIALAQTREMMIQTDDLAGSSQTKA 3217
Cdd:COG1196 374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEE 410
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2332-2939 |
5.25e-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: 69.37 E-value: 5.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2332 EAIQKRK-KMEEELAKVRAEME---ILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIA 2407
Cdd:pfam05483 88 EKIKKWKvSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2408 EGEAARQRAEAERILK---------EKLAAINEATRLKTE---AEIALKEKEaENERLRRLAE-------DEAYQRKLLE 2468
Cdd:pfam05483 168 AEKTKKYEYEREETRQvymdlnnniEKMILAFEELRVQAEnarLEMHFKLKE-DHEKIQHLEEeykkeinDKEKQVSLLL 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2469 EQATQHKQDIEEKIILLKKSSD--NELERQKNIVEDTLRQRRIIE----EEIRILKLNFEKASSGKSDLELELNQLKNIA 2542
Cdd:pfam05483 247 IQITEKENKMKDLTFLLEESRDkaNQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQIATKTI 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2543 EETHRSKEKAEQEAEKQRQ-------------LALEE----EQRRKEAEEKVRKILADEQEaarQRKAALEEVERLKAKA 2605
Cdd:pfam05483 327 CQLTEEKEAQMEELNKAKAahsfvvtefeattCSLEEllrtEQQRLEKNEDQLKIITMELQ---KKSSELEEMTKFKNNK 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2606 EeaKRQKELAEKEAERQIQLAQEAAFKKIEAEekahaaiVQQKEQEM---LQTRKQEKSILD------------------ 2664
Cdd:pfam05483 404 E--VELEELKKILAEDEKLLDEKKQFEKIAEE-------LKGKEQELiflLQAREKEIHDLEiqltaiktseehylkeve 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2665 KLKEEAERAK-RAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAA 2743
Cdd:pfam05483 475 DLKTELEKEKlKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2744 LKQKQLADE---EMDKHKKFAE-------KTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQV 2813
Cdd:pfam05483 555 EEFIQKGDEvkcKLDKSEENARsieyevlKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2814 EEELFKVKIQMEElIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIE-----AQEAARMRKLAE--- 2885
Cdd:pfam05483 635 EIKVNKLELELAS-AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEidkrcQHKIAEMVALMEkhk 713
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2886 ---DDLANQRALAEKMLKEKMQAIQ--------EATRLKAEADMLQKQKELAQEQARKFQEDKEQ 2939
Cdd:pfam05483 714 hqyDKIIEERDSELGLYKNKEQEQSsakaaleiELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3979-4017 |
5.49e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.03 E-value: 5.49e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 3979 LLEAQAATGFITDAVKNQKLYVNEAVKAGLVGPELHEKL 4017
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2806-3234 |
5.99e-11 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 68.87 E-value: 5.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2806 AMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAE 2885
Cdd:COG5281 8 AALAAAAAAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAAALAED 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2886 DDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEI 2965
Cdd:COG5281 88 AAAAAAAAEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2966 TAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERmvvvqsLEIQRQQSGKEAEELRRAIAELEHE 3045
Cdd:COG5281 168 AAAAAAAAAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAA------EAAAAEAQALAAAALAEQAALAAAS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3046 KEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEKAKLENLYEDEVRKAQKLKQEQEHQL 3125
Cdd:COG5281 242 AAAQALAALAAAAAAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3126 KQLEEEKQQLKAsmgEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRKLREKLEQLEEEHRIALAQTREMMIQ 3205
Cdd:COG5281 322 QALRAAAQALAA---LAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATN 398
|
410 420
....*....|....*....|....*....
gi 1717010358 3206 TDDLAGSSQTKAMPNGRDAVDGLAQNGMT 3234
Cdd:COG5281 399 VAAQVAQAATSAFSGLTDALAGAVTTGKL 427
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2236-2779 |
6.84e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 6.84e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2236 EEVAHKKTLAQEEAEKQKEDAEREARKRAKAE-----ESALRQKELAEDELEKQRKLADATaQQKFSAEQELIRLKADTE 2310
Cdd:PRK03918 228 KEVKELEELKEEIEELEKELESLEGSKRKLEEkirelEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2311 SGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEA 2390
Cdd:PRK03918 307 DELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2391 ARLRALSEEAKRQRQIAEgeaarqraEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEayqrklleeq 2470
Cdd:PRK03918 387 EKLEKELEELEKAKEEIE--------EEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEE---------- 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2471 atqHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQrriieeeirilKLNFEKASSGKSDLELE---LNQLKNIAEETHR 2547
Cdd:PRK03918 449 ---HRKELLEEYTAELKRIEKELKEIEEKERKLRKE-----------LRELEKVLKKESELIKLkelAEQLKELEEKLKK 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2548 -SKEKAEQEAEKQRQlaLEEEQRRKEAEEKVRKILADEQEAARQRKAALEEverlkaKAEEAKRQKELAEKEAERQIQLA 2626
Cdd:PRK03918 515 yNLEELEKKAEEYEK--LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEK------KLDELEEELAELLKELEELGFES 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2627 QEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKsiLDKLKEEAE--RAKRAAEDADYARMRAEQEAALSRQQVEEAERM 2704
Cdd:PRK03918 587 VEELEERLKELEPFYNEYLELKDAEKELEREEKE--LKKLEEELDkaFEELAETEKRLEELRKELEELEKKYSEEEYEEL 664
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2705 KQRAEEEaqakaqaqdEAEKLRKEAELEAAKRAHAEQAALKQKQLAD-EEMDKHKKFAEKTLRQKAQVEQELTKVK 2779
Cdd:PRK03918 665 REEYLEL---------SRELAGLRAELEELEKRREEIKKTLEKLKEElEEREKAKKELEKLEKALERVEELREKVK 731
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4901-4939 |
6.88e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 60.03 E-value: 6.88e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 4901 LLEAQACTGGIIDINTGQKFSVTDAVNKGLVDKIMVDRI 4939
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1936-2142 |
8.36e-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: 67.48 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1936 KAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQE---EVSKREVVAVDAEQQKQTIQQELQQL 2012
Cdd:COG4942 23 AEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRAleqELAALEAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2013 R--------------QNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKAsaedELQELRARAEEAERQKKA 2078
Cdd:COG4942 103 KeelaellralyrlgRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2079 AQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQA 2142
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2570-3208 |
9.83e-11 |
|
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: 68.83 E-value: 9.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2570 RKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKrQKELAEKEAERQIQLAQEaafkkieaeekaHAAIVQQ-- 2647
Cdd:COG3096 277 ANERRELSERALELRRELFGARRQLAEEQYRLVEMARELE-ELSARESDLEQDYQAASD------------HLNLVQTal 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2648 KEQEMLQTRKQEksiLDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERM---KQRAEEEAQAKA-------Q 2717
Cdd:COG3096 344 RQQEKIERYQED---LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladYQQALDVQQTRAiqyqqavQ 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2718 AQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMdkhkkfaeKTLRQK--------AQVEQELTKVKLQLEETDHQk 2789
Cdd:COG3096 421 ALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEV--------LELEQKlsvadaarRQFEKAYELVCKIAGEVERS- 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2790 tlldDESQRLKEEVTDAMRQKAQVEEElfkVKIQMEeLIKLKLRIEEENKmlimkdkdsTQKFLAEEAEKMRQVAEEAAR 2869
Cdd:COG3096 492 ----QAWQTARELLRRYRSQQALAQRL---QQLRAQ-LAELEQRLRQQQN---------AERLLEEFCQRIGQQLDAAEE 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2870 LSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEA-------DMLQKQKELAQEQARKFQEDKEQIEQ 2942
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARApawlaaqDALERLREQSGEALADSQEVTAAMQQ 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2943 QLAKETE-GFQKSLEAERRQQLEITAE----------------AERL-----------------------------KLQV 2976
Cdd:COG3096 635 LLEREREaTVERDELAARKQALESQIErlsqpggaedprllalAERLggvllseiyddvtledapyfsalygparhAIVV 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2977 LEMSKAQAKAE------EDAKKFKKQAEDF-GNKLHQTELatkERMVVVQSLEIQRQQS--------GK----------- 3030
Cdd:COG3096 715 PDLSAVKEQLAgledcpEDLYLIEGDPDSFdDSVFDAEEL---EDAVVVKLSDRQWRYSrfpevplfGRaarekrleelr 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3031 -EAEELRRAIAELEHEKEKLKQ-----------------------------------EAELLQKNSQEMQVAQQ-EQLRQ 3073
Cdd:COG3096 792 aERDELAEQYAKASFDVQKLQRlhqafsqfvgghlavafapdpeaelaalrqrrselERELAQHRAQEQQLRQQlDQLKE 871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3074 ETQVLQTtFLTEKHLLLEKEKYIEkekakLENLYE--DEVRKAQKLKQEQEHQLKQLEEEKQQLKA--SMGEAMKKQ--- 3146
Cdd:COG3096 872 QLQLLNK-LLPQANLLADETLADR-----LEELREelDAAQEAQAFIQQHGKALAQLEPLVAVLQSdpEQFEQLQADylq 945
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 3147 -KEAEESVRHKQDELHQLDKRR-----QEQEKLLA---DENRKLREKLEQLEEEHRialaQTREMMIQTDD 3208
Cdd:COG3096 946 aKEQQRRLKQQIFALSEVVQRRphfsyEDAVGLLGensDLNEKLRARLEQAEEARR----EAREQLRQAQA 1012
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2348-3205 |
1.28e-10 |
|
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: 68.44 E-value: 1.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2348 RAEMEILLESKSRAEEESRsnteKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEG------EAARQRAEAERi 2421
Cdd:COG3096 277 ANERRELSERALELRRELF----GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnlvqTALRQQEKIER- 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2422 LKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEA---------YQRKLLEEQ--ATQHKQDIeekiillkkssd 2490
Cdd:COG3096 352 YQEDLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslksqladYQQALDVQQtrAIQYQQAV------------ 419
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2491 NELERQKNIvedtlrqrriieeeirilklnfekasSGKSDLELElnqlkNIAEETHRSKEKAEQEAEKQRQLaleeEQRr 2570
Cdd:COG3096 420 QALEKARAL--------------------------CGLPDLTPE-----NAEDYLAAFRAKEQQATEEVLEL----EQK- 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2571 keaeekvrkiLADEQEAARQRKAALE-------EVERLKA--KAEEAKRQKELAEKEAERQIQLAQEAAfkkiEAEEKAH 2641
Cdd:COG3096 464 ----------LSVADAARRQFEKAYElvckiagEVERSQAwqTARELLRRYRSQQALAQRLQQLRAQLA----ELEQRLR 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2642 aaivQQKEQEMLQTR-----KQEKSILDKLKEEAERAKRAAEDA-DYARMRAEQEAALsRQQVEEAERMKQRAEEEAQAK 2715
Cdd:COG3096 530 ----QQQNAERLLEEfcqriGQQLDAAEELEELLAELEAQLEELeEQAAEAVEQRSEL-RQQLEQLRARIKELAARAPAW 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2716 AQAQDEAEKLRKEAElEAAKRAHAEQAALkQKQLADEemdkhkkfaektlRQKAQVEQELTKVKLQLEETDHQKTLLD-D 2794
Cdd:COG3096 605 LAAQDALERLREQSG-EALADSQEVTAAM-QQLLERE-------------REATVERDELAARKQALESQIERLSQPGgA 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2795 ESQRLK---------------EEVT--DA---------MRQkAQVEEELFKVKIQMEELIKLK----------------- 2831
Cdd:COG3096 670 EDPRLLalaerlggvllseiyDDVTleDApyfsalygpARH-AIVVPDLSAVKEQLAGLEDCPedlyliegdpdsfddsv 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2832 LRIEEENKMLIMKDKD-----------------STQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRAL 2894
Cdd:COG3096 749 FDAEELEDAVVVKLSDrqwrysrfpevplfgraAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAV 828
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2895 A-----EKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQE------------DKEQIEQQLAKETEGFQKSLEA 2957
Cdd:COG3096 829 AfapdpEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpqanllADETLADRLEELREELDAAQEA 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2958 ER--RQQLEITAEAERLkLQVLEMSKAQakaEEDAKKFKKQAEDFGNKLHQTELATKErmvVVQSLEiqrQQSGKEAEEL 3035
Cdd:COG3096 909 QAfiQQHGKALAQLEPL-VAVLQSDPEQ---FEQLQADYLQAKEQQRRLKQQIFALSE---VVQRRP---HFSYEDAVGL 978
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3036 RRAIAEL-EHEKEKLKQeAELLQKNSQEMQVAQQEQLRQETQVLQttfltekhlllekekyiekekaklenlyedEVRKA 3114
Cdd:COG3096 979 LGENSDLnEKLRARLEQ-AEEARREAREQLRQAQAQYSQYNQVLA------------------------------SLKSS 1027
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3115 QKLKQEqehQLKQLEEEKQQLkasmgeAMKKQKEAEESVRHKQDELHQ----LDKRRQEQEKLLA---DENRKLREKLEQ 3187
Cdd:COG3096 1028 RDAKQQ---TLQELEQELEEL------GVQADAEAEERARIRRDELHEelsqNRSRRSQLEKQLTrceAEMDSLQKRLRK 1098
|
970
....*....|....*...
gi 1717010358 3188 LEEEHRialaQTREMMIQ 3205
Cdd:COG3096 1099 AERDYK----QEREQVVQ 1112
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
628-735 |
1.35e-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: 61.83 E-value: 1.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 628 EDERDRVQ--KKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDYL 701
Cdd:cd21222 8 DEAPEKLAevKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELM 87
|
90 100 110
....*....|....*....|....*....|....
gi 1717010358 702 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 735
Cdd:cd21222 88 EDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1934-2136 |
1.47e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 66.75 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavdAEQQKQTiqqELQQLR 2013
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQKQA---EEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2014 QNSDMEIKSKAKKIEEAEYnRRKIEEEIHiVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERlrrqVKDE 2093
Cdd:PRK09510 141 AAAAAKAKAEAEAKRAAAA-AKKAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1717010358 2094 SQKKREAE-EELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAE 2136
Cdd:PRK09510 215 AKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2568-2949 |
1.49e-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: 67.23 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2568 QRRKEAEEKVRKILADEQEAARQRKAalEEVERLKAKAEEAKRQ-KELAEKEAERQIQLAQ-----EAAFKKIEAEEKAH 2641
Cdd:pfam07888 33 QNRLEECLQERAELLQAQEAANRQRE--KEKERYKRDREQWERQrRELESRVAELKEELRQsrekhEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2642 AAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAE-DADYARMRAEQEAALSRQQVEEAERmkqraeEEAQAKAQaQD 2720
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLErETELERMKERAKKAGAQRKEEEAER------KQLQAKLQ-QT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2721 EAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKkfaektLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLK 2800
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQK------LTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2801 EEVTDAMRQKAQVEEELFKVKIQMEEL------IKLKLRieeENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEA 2874
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQLtlqladASLALR---EGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERL 334
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2875 QEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEatrLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETE 2949
Cdd:pfam07888 335 QEERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2538-2730 |
1.59e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 67.21 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2538 LKNIAEEThRSKEKAEQEAEKQRQLALEEEQRRKEAEEkvrkiLADEQEAARQRKAAlEEVERLKAKAEEaKRQKELAEK 2617
Cdd:COG2268 191 RRKIAEII-RDARIAEAEAERETEIAIAQANREAEEAE-----LEQEREIETARIAE-AEAELAKKKAEE-RREAETARA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2618 EAERQIQLAQEAAfkkieaeekahaaivQQKEQEMLQTRKQEKSIldKLkEEAERAKRaaedadyarmRAEQEAALSRQQ 2697
Cdd:COG2268 263 EAEAAYEIAEANA---------------EREVQRQLEIAEREREI--EL-QEKEAERE----------EAELEADVRKPA 314
|
170 180 190
....*....|....*....|....*....|....
gi 1717010358 2698 VEEAERMKQRAEEEAQA-KAQAQDEAEKLRKEAE 2730
Cdd:COG2268 315 EAEKQAAEAEAEAEAEAiRAKGLAEAEGKRALAE 348
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2546-3120 |
1.59e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 68.02 E-value: 1.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2546 HRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEkEAERQIQL 2625
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLE-AELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2626 AQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAED---------ADYARMRAEQEAALSRQ 2696
Cdd:COG4913 317 RLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAAlglplpasaEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2697 QvEEAERMKQRAEEEAQAKAQAQDEAEKLRKE------------AELEAAKRAHAEQAALKQKQL--ADEEMD---KHKK 2759
Cdd:COG4913 397 E-EELEALEEALAEAEAALRDLRRELRELEAEiaslerrksnipARLLALRDALAEALGLDEAELpfVGELIEvrpEEER 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2760 F---AEKTLRQKAQveqeltkvklqleetdhqkTLLDDEsqRLKEEVTDAMRQkaqveeelfkvkiqmeelIKLKLRIee 2836
Cdd:COG4913 476 WrgaIERVLGGFAL-------------------TLLVPP--EHYAAALRWVNR------------------LHLRGRL-- 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2837 enkmlimkdkdSTQKFLAEEAEKMRQVAEE---AARLSIEAQEAarmRKLAEDDLANQRALA----EKMLKEKMQAIQEA 2909
Cdd:COG4913 515 -----------VYERVRTGLPDPERPRLDPdslAGKLDFKPHPF---RAWLEAELGRRFDYVcvdsPEELRRHPRAITRA 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2910 TRLKAEADMLQKQKELAQEQARKFQED-KEQIEqQLAKETEGFQKSLEAERRQQLEITAEAERL--KLQVLEMSKAQAKA 2986
Cdd:COG4913 581 GQVKGNGTRHEKDDRRRIRSRYVLGFDnRAKLA-ALEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2987 EEDAKKFKKQAEDFGNKLHQTELATKErmvvVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQvA 3066
Cdd:COG4913 660 EIDVASAEREIAELEAELERLDASSDD----LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQ-D 734
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 3067 QQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEKAKLENLYEDEVRKAQKLKQE 3120
Cdd:COG4913 735 RLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2673-2879 |
1.70e-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: 67.28 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2673 AKRAAEDADYARMRAEQeaalSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAhaEQAALKQKQLADE 2752
Cdd:pfam15709 326 EKREQEKASRDRLRAER----AEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRF--EEIRLRKQRLEEE 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2753 EMDKhkkfAEKTLRQKAQVEQELTKVKLQLEEtdHQKTLLDDESQRLKEEVTDAMRQKAQVEEElfkvKIQMEELIKLKL 2832
Cdd:pfam15709 400 RQRQ----EEEERKQRLQLQAAQERARQQQEE--FRRKLQELQRKKQQEEAERAEAEKQRQKEL----EMQLAEEQKRLM 469
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2833 RIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIE-----AQEAAR 2879
Cdd:pfam15709 470 EMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEeamkqAQEQAR 521
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1937-2806 |
1.82e-10 |
|
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: 68.06 E-value: 1.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1937 AAEKLKEEERRRLAEVEAQLEKQTQlAEAHAKAKAQAekeAEELQRRMQEevskrevvAVDAEQQKQTIQQELQQLrqNS 2016
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSA-RESDLEQDYQA---ASDHLNLVQT--------ALRQQEKIERYQEDLEEL--TE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2017 DMEIKSKAkkIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAeEAERQKKAAQEEAERLRR-------Q 2089
Cdd:COG3096 362 RLEEQEEV--VEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRA-IQYQQAVQALEKARALCGlpdltpeN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2090 VKDESQKKREAEE-------ELKRKVQAEKDAAREKQRAMEDLQKFrsqaeeaerrmkQAEVEKERQIKVAQEV-----A 2157
Cdd:COG3096 439 AEDYLAAFRAKEQqateevlELEQKLSVADAARRQFEKAYELVCKI------------AGEVERSQAWQTARELlrryrS 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2158 QQSAAAELNSKRMSFAEktaqLELSLKQehitvthlQEEAERLkkqheeaekareeaekeLEKWHQKANEALRLRLQAEE 2237
Cdd:COG3096 507 QQALAQRLQQLRAQLAE----LEQRLRQ--------QQNAERL-----------------LEEFCQRIGQQLDAAEELEE 557
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2238 VahkktlaQEEAEKQKEDAEREARkRAKAEESALRQKelaEDELEKQRKLADATAQQKFSAEQELIRLKAdtesgeqqrl 2317
Cdd:COG3096 558 L-------LAELEAQLEELEEQAA-EAVEQRSELRQQ---LEQLRARIKELAARAPAWLAAQDALERLRE---------- 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2318 lleeelfrlknEVNEAIqkrkkmeEELAKVRAEMEILLEsKSRAEEESRSNTEKSKHMLEVEASKLRELA-EEAARLRAL 2396
Cdd:COG3096 617 -----------QSGEAL-------ADSQEVTAAMQQLLE-REREATVERDELAARKQALESQIERLSQPGgAEDPRLLAL 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2397 SEE------AKRQRQIAEGEA---------ARQR---AEAERIlKEKLA-----------------AINEATRLKTEAEI 2441
Cdd:COG3096 678 AERlggvllSEIYDDVTLEDApyfsalygpARHAivvPDLSAV-KEQLAgledcpedlyliegdpdSFDDSVFDAEELED 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2442 ALKEKEAENE-RLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDN--ELERQKNIVEDTLRQrriieeeirILK 2518
Cdd:COG3096 757 AVVVKLSDRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFDvqKLQRLHQAFSQFVGG---------HLA 827
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2519 LNFE--------KASSGKSDLELELNQLkniAEETHRSKEKAEQEAEKQRQLA--------LEEE---QRRKEAEEKVRK 2579
Cdd:COG3096 828 VAFApdpeaelaALRQRRSELERELAQH---RAQEQQLRQQLDQLKEQLQLLNkllpqanlLADEtlaDRLEELREELDA 904
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2580 ILADEQEAARQRKaALEEVERLKA-----KAEEAKRQKELAEKEAERQIQLAQEAAFKKIeAEEKAHAAivQQKEQEMLQ 2654
Cdd:COG3096 905 AQEAQAFIQQHGK-ALAQLEPLVAvlqsdPEQFEQLQADYLQAKEQQRRLKQQIFALSEV-VQRRPHFS--YEDAVGLLG 980
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2655 trkQEKSILDKLKEEAERAKRAAEDadyARMRAEQeaalSRQQVEEAERMKQRAEEEAQAKAQAQDEAEklRKEAELEAA 2734
Cdd:COG3096 981 ---ENSDLNEKLRARLEQAEEARRE---AREQLRQ----AQAQYSQYNQVLASLKSSRDAKQQTLQELE--QELEELGVQ 1048
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2735 KRAHAEQAALKQKQLADEEMDKHKKfaektlrQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDA 2806
Cdd:COG3096 1049 ADAEAEERARIRRDELHEELSQNRS-------RRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQA 1113
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2570-3057 |
1.97e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.06 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2570 RKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKElAEKEAERQIQLAqeaafkkieaeeKAHAAIVQQKe 2649
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNE-AESDLEQDYQAA------------SDHLNLVQTA- 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2650 qeMLQTRKQEKSI--LDKLKEEAERAKRAAEDADyarmraeqeaalsrQQVEEAERMKQRAEEEA-QAKAQAQDEAEKLr 2726
Cdd:PRK04863 344 --LRQQEKIERYQadLEELEERLEEQNEVVEEAD--------------EQQEENEARAEAAEEEVdELKSQLADYQQAL- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2727 KEAELEAAKRAHAEQAALKQKQLADEeMDKHKKFAEKTLRQKAQVEQELTKVKLQLEetdhqktllddesQRLKeeVTDA 2806
Cdd:PRK04863 407 DVQQTRAIQYQQAVQALERAKQLCGL-PDLTADNAEDWLEEFQAKEQEATEELLSLE-------------QKLS--VAQA 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2807 MRQkaqveeelfkvkiQMEELIKLKLRIeeenkmlimkdkdstqkflAEEAEkmRQVAEEAARLSIEAQEAARMrkLAED 2886
Cdd:PRK04863 471 AHS-------------QFEQAYQLVRKI-------------------AGEVS--RSEAWDVARELLRRLREQRH--LAEQ 514
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2887 DLANQRALAEkmLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEIT 2966
Cdd:PRK04863 515 LQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQ 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2967 AEAERLKLQVLEMSKAQAKAEedakkfkKQAEDFGNklhqtELATKermvvvQSLEIQRQQSGKEAEELRRAIAELEHEK 3046
Cdd:PRK04863 593 ARIQRLAARAPAWLAAQDALA-------RLREQSGE-----EFEDS------QDVTEYMQQLLERERELTVERDELAARK 654
|
490
....*....|.
gi 1717010358 3047 EKLKQEAELLQ 3057
Cdd:PRK04863 655 QALDEEIERLS 665
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2537-2769 |
2.13e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 67.28 E-value: 2.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2537 QLKNIAEETHRSkEKAEQEAEkQRQLALEEEQ-----RRKEAEEKVRKILADEQEAARQR---KAALEEVERLKAKAEEA 2608
Cdd:PRK05035 437 EIRAIEQEKKKA-EEAKARFE-ARQARLEREKaareaRHKKAAEARAAKDKDAVAAALARvkaKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2609 KRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIV--------QQKEQEMLQTRKQEKSILDKLKEEAE----RAKRA 2676
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAaaiarakaKKAAQQAANAEAEEEVDPKKAAVAAAiaraKAKKA 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2677 AEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDK 2756
Cdd:PRK05035 595 AQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAED 674
|
250
....*....|....*
gi 1717010358 2757 HKK--FAEKTLRQKA 2769
Cdd:PRK05035 675 PKKaaVAAAIARAKA 689
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2374-2961 |
2.31e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 67.63 E-value: 2.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2374 HMLE-----VEASKLRELAEEAARLRALSEEAKRQRQIAEG-EAARQRAEAERILKEKLAAINEATRLKTeAEIALKEKE 2447
Cdd:COG4913 216 YMLEepdtfEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2448 AENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKlnfEKASSG 2527
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAAL 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2528 KSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKiLADEQEAARQRKAAL-EEVERLKAKAE 2606
Cdd:COG4913 372 GLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-LEAEIASLERRKSNIpARLLALRDALA 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2607 EAKRQKE-----LAE----KEAERQIQLA-----------------QEAAFKKIEAEEKAHAAI----VQQKEQEMLQTR 2656
Cdd:COG4913 451 EALGLDEaelpfVGElievRPEEERWRGAiervlggfaltllvppeHYAAALRWVNRLHLRGRLvyerVRTGLPDPERPR 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2657 KQEKSILDKLK--------------------------EEAERAKRAA---------------EDADYARMR--------- 2686
Cdd:COG4913 531 LDPDSLAGKLDfkphpfrawleaelgrrfdyvcvdspEELRRHPRAItragqvkgngtrhekDDRRRIRSRyvlgfdnra 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2687 ----AEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADeemdkhkkfAE 2762
Cdd:COG4913 611 klaaLEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELER---------LD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2763 KTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELfkvkiqmEELIKLKlrieeenkmli 2842
Cdd:COG4913 682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRL-------EAAEDLA----------- 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2843 mkdkdstQKFLAEEAEKMRqvaeeaARLSIEAQEAARMRKLAE--DDLANQRALAEKMLKEKMQAIQEA---------TR 2911
Cdd:COG4913 744 -------RLELRALLEERF------AAALGDAVERELRENLEEriDALRARLNRAEEELERAMRAFNREwpaetadldAD 810
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2912 LKAEADMLQKQKELAQEQARKFQED-KEQIEQQLAKETEGFQKSLEAERRQ 2961
Cdd:COG4913 811 LESLPEYLALLDRLEEDGLPEYEERfKELLNENSIEFVADLLSKLRRAIRE 861
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
636-732 |
2.37e-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: 60.67 E-value: 2.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 636 KKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 701
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1717010358 702 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 732
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2168-2717 |
2.51e-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: 67.07 E-value: 2.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2168 KRMSFAEKTAQLELsLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKAnEALRLRLQAEEVAHKKtlaQE 2247
Cdd:pfam05557 19 KQMELEHKRARIEL-EKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQA-ELNRLKKKYLEALNKK---LN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2248 EAEKQKEDAE----------REARKRAKAEESALRQKELAEDELEKQRKLADATAQQkfsAEQELIRLKADTEsgeqqrl 2317
Cdd:pfam05557 94 EKESQLADARevisclknelSELRRQIQRAELELQSTNSELEELQERLDLLKAKASE---AEQLRQNLEKQQS------- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2318 lleeelfrlknEVNEAIQKRKKMEEELAKVRAEMEILleSKSRAEEESRSNTEKSKHMLEVEASKLRE-------LAEEA 2390
Cdd:pfam05557 164 -----------SLAEAEQRIKELEFEIQSQEQDSEIV--KNSKSELARIPELEKELERLREHNKHLNEnienkllLKEEV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2391 ARLRA-LSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAeIALKEKEAENERLRRLAEDEAYQRKLLEE 2469
Cdd:pfam05557 231 EDLKRkLEREEKYREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPED-LSRRIEQLQQREIVLKEENSSLTSSARQL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2470 QATQhKQDIEEKIILLKKSSD--NELERQKNIVEDTLRQRRIIEEEIRILK---------LNFEKASSGKSDLELELNQL 2538
Cdd:pfam05557 310 EKAR-RELEQELAQYLKKIEDlnKKLKRHKALVRRLQRRVLLLTKERDGYRailesydkeLTMSNYSPQLLERIEEAEDM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2539 ----KNIAEETHRSKEKAEQEAEKQRQLA----LEEEQRRKEAEEKVRKILADEQEAARQrkaaleEVERLKAKAEEAKR 2610
Cdd:pfam05557 389 tqkmQAHNEEMEAQLSVAEEELGGYKQQAqtleRELQALRQQESLADPSYSKEEVDSLRR------KLETLELERQRLRE 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2611 QKELAEKEAERQiQLAQEAAFKKIEaeekahaaIVQQKEQEMLQTRKQEKSILDKLKEEAERAKR-------AAEDADYA 2683
Cdd:pfam05557 463 QKNELEMELERR-CLQGDYDPKKTK--------VLHLSMNPAAEAYQQRKNQLEKLQAEIERLKRllkkledDLEQVLRL 533
|
570 580 590
....*....|....*....|....*....|....*...
gi 1717010358 2684 RM----RAEQEAALSRQQVEEAERMKQRAEEEAQAKAQ 2717
Cdd:pfam05557 534 PEttstMNFKEVLDLRKELESAELKNQRLKEVFQAKIQ 571
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1710-2141 |
2.57e-10 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 67.27 E-value: 2.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1710 KELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRSHSERDVDLDRYRERVQQLLERWQAILVQIDLRQREL 1789
Cdd:COG1196 344 EELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1790 DQLGRQLRYYRETYDWLIKWIKDAKQRQEQIQSVPITDSKTMKEQLLQLKKLLEEIESNRTKVDECQKYAKQYIDAIKDY 1869
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1870 ELQLVTYKAQVEPVVSPAKKPKVqstsdsIIQEYVDLRTRYSELTTLTSQYIKFITETlcrLNVEEKAAEKLKEEERRRL 1949
Cdd:COG1196 504 EGFLEGVKAALLLAGLRGLAGAV------AVLIGVEAAYEAALEAALAAALQNIVVED---DEVAAAAIEYLKAAKAGRA 574
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1950 AEVEAQLEKQTQLAEAHAK---------AKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNS-DME 2019
Cdd:COG1196 575 TFLPLDKIRARAALAAALArgaigaavdLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTlEGE 654
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2020 IKSKAKKIEEAEynRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKRE 2099
Cdd:COG1196 655 GGSAGGSLTGGS--RRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEA 732
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1717010358 2100 AEEELKRKVQAEK----DAAREKQRAMEDLQKFRSQAEEAERRMKQ 2141
Cdd:COG1196 733 EREELLEELLEEEelleEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1944-2830 |
2.93e-10 |
|
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: 67.28 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1944 EERRRLAEVEAQLEK-----QTQLAEAHAKAKAQAeKEAEELQRRmQEEVSKREVVAVD-------AEQQKQTI---QQE 2008
Cdd:COG3096 278 NERRELSERALELRRelfgaRRQLAEEQYRLVEMA-RELEELSAR-ESDLEQDYQAASDhlnlvqtALRQQEKIeryQED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2009 LQQLrqNSDMEIKSKAkkIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEeAERQKKAAQEEAERLRR 2088
Cdd:COG3096 356 LEEL--TERLEEQEEV--VEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAI-QYQQAVQALEKARALCG 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2089 -------QVKDESQKKREAEE-------ELKRKVQAEKDAAREKQRAMEDLQKFrsqaeeaerrmkQAEVEKERQIKVAQ 2154
Cdd:COG3096 431 lpdltpeNAEDYLAAFRAKEQqateevlELEQKLSVADAARRQFEKAYELVCKI------------AGEVERSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2155 EV-----AQQSAAAELNSKRMSFAEktaqLELSLKQehitvthlQEEAERLkkqheeaekareeaekeLEKWHQKANEAL 2229
Cdd:COG3096 499 ELlrryrSQQALAQRLQQLRAQLAE----LEQRLRQ--------QQNAERL-----------------LEEFCQRIGQQL 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2230 RLRLQAEEVahkktlaQEEAEKQKEDAEREARkRAKAEESALRQKElaeDELEKQRKLADATAQQKFSAEQELIRLKAdt 2309
Cdd:COG3096 550 DAAEELEEL-------LAELEAQLEELEEQAA-EAVEQRSELRQQL---EQLRARIKELAARAPAWLAAQDALERLRE-- 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2310 esgeqqrllleeelfrlknEVNEAIqkrkkmeEELAKVRAEMEILLEsKSRAEEESRSNTEKSKHMLEVEASKLRELA-E 2388
Cdd:COG3096 617 -------------------QSGEAL-------ADSQEVTAAMQQLLE-REREATVERDELAARKQALESQIERLSQPGgA 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2389 EAARLRALSEE------AKRQRQIAEGEA---------ARQR---AEAERIlKEKLA-----------------AINEAT 2433
Cdd:COG3096 670 EDPRLLALAERlggvllSEIYDDVTLEDApyfsalygpARHAivvPDLSAV-KEQLAgledcpedlyliegdpdSFDDSV 748
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2434 RLKTEAEIALKEKEAENE-RLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDN--ELERQKNIVEDTLRQRrii 2510
Cdd:COG3096 749 FDAEELEDAVVVKLSDRQwRYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFDvqKLQRLHQAFSQFVGGH--- 825
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2511 eeeiriLKLNFE--------KASSGKSDLELELNQLkniAEETHRSKEKAEQEAEKQRQLA--------LEEE---QRRK 2571
Cdd:COG3096 826 ------LAVAFApdpeaelaALRQRRSELERELAQH---RAQEQQLRQQLDQLKEQLQLLNkllpqanlLADEtlaDRLE 896
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2572 EAEEKVRKILADEQEAARQRKAaLEEVERLKA-----KAEEAKRQKELAEKEAERQIQLAQEAAFKKIeAEEKAHAAivQ 2646
Cdd:COG3096 897 ELREELDAAQEAQAFIQQHGKA-LAQLEPLVAvlqsdPEQFEQLQADYLQAKEQQRRLKQQIFALSEV-VQRRPHFS--Y 972
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2647 QKEQEMLQtrkQEKSILDKLKEEAERAKRAAEDAdyaRMRAEQeaalSRQQVEEAERMKQRAEEEAQAKAQAQDEAEklR 2726
Cdd:COG3096 973 EDAVGLLG---ENSDLNEKLRARLEQAEEARREA---REQLRQ----AQAQYSQYNQVLASLKSSRDAKQQTLQELE--Q 1040
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2727 KEAELEAAKRAHAEQAALKQKQladeemdkhkkfaektlrqkaQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDA 2806
Cdd:COG3096 1041 ELEELGVQADAEAEERARIRRD---------------------ELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
|
970 980
....*....|....*....|....
gi 1717010358 2807 MRQKAQVEEELFKVKIQMEELIKL 2830
Cdd:COG3096 1100 ERDYKQEREQVVQAKAGWCAVLRL 1123
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2538-3202 |
3.35e-10 |
|
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: 67.28 E-value: 3.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2538 LKNIAEETHRSKEKAEQEAE---KQRQLALEEEQR---RKEAEEKV--RKILADEQEAARQRKAALEEVERLKAKAEeaK 2609
Cdd:COG3096 274 MRHANERRELSERALELRRElfgARRQLAEEQYRLvemARELEELSarESDLEQDYQAASDHLNLVQTALRQQEKIE--R 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2610 RQKELAEKE--AERQIQLAQEAAFKKIEAEEKAHAAivqqkeqemlqtrkqeksildklKEEAERAKraAEDADYAR-MR 2686
Cdd:COG3096 352 YQEDLEELTerLEEQEEVVEEAAEQLAEAEARLEAA-----------------------EEEVDSLK--SQLADYQQaLD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2687 AEQEAALSRQQV----EEAERM--------KQRAEEEAQAKAQAQDEAEKLR----KEAELEAAKRAHAEQAALKQKQLA 2750
Cdd:COG3096 407 VQQTRAIQYQQAvqalEKARALcglpdltpENAEDYLAAFRAKEQQATEEVLeleqKLSVADAARRQFEKAYELVCKIAG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2751 DEEMDKHKKFAEKTLR----QKAQVEQ------ELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMrqkaQVEEELFKV 2820
Cdd:COG3096 487 EVERSQAWQTARELLRryrsQQALAQRlqqlraQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAE----ELEELLAEL 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2821 KIQMEELiKLKLRIEEENKMlimkdkdSTQKFLAEEAEKMRQVAEEAARLsIEAQEAA-RMRKLAEDDLANQRALAEKMl 2899
Cdd:COG3096 563 EAQLEEL-EEQAAEAVEQRS-------ELRQQLEQLRARIKELAARAPAW-LAAQDALeRLREQSGEALADSQEVTAAM- 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2900 keKMQAIQEaTRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAE--------R 2971
Cdd:COG3096 633 --QQLLERE-REATVERDELAARKQALESQIERLSQPGGAEDPRLLALAERLGGVLLSEIYDDVTLEDAPYfsalygpaR 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2972 LKLQVLEMSKAQAKAE------EDAKKFKKQAEDF-GNKLHQTELatkERMVVVQSLEIQRQQS--------GKEAEELR 3036
Cdd:COG3096 710 HAIVVPDLSAVKEQLAgledcpEDLYLIEGDPDSFdDSVFDAEEL---EDAVVVKLSDRQWRYSrfpevplfGRAAREKR 786
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3037 raIAELEHEKEKLKQEAELLQKNSQEMQVAQQeQLRQetqvlqttFLTEkHLLLekekyiekekaKLENLYEDEVRKAQK 3116
Cdd:COG3096 787 --LEELRAERDELAEQYAKASFDVQKLQRLHQ-AFSQ--------FVGG-HLAV-----------AFAPDPEAELAALRQ 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3117 LKQEQEHQLKQLEEEKQQlkasmgeamkkQKEAEESVRHKQDELHQLdkrrQEQEKLLADENrkLREKLEQLEEEHRIAL 3196
Cdd:COG3096 844 RRSELERELAQHRAQEQQ-----------LRQQLDQLKEQLQLLNKL----LPQANLLADET--LADRLEELREELDAAQ 906
|
....*.
gi 1717010358 3197 AQTREM 3202
Cdd:COG3096 907 EAQAFI 912
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2541-2840 |
3.36e-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: 65.33 E-value: 3.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2541 IAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEA--ARQRKAALEEVERLKAKAEEAKRQKELAEKE 2618
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEqiEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2619 AERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAER---------AKRAAEDADYARMRAEQ 2689
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEReeereaereEIEEEKEREIARLRAQQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2690 EAALSRQqvEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAA-KRAHAEQAALKQKQLAdEEMDKHKKFAEKTLRQK 2768
Cdd:pfam13868 194 EKAQDEK--AERDELRAKLYQEEQERKERQKEREEAEKKARQRQElQQAREEQIELKERRLA-EEAEREEEEFERMLRKQ 270
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2769 AQVEQeltKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKM 2840
Cdd:pfam13868 271 AEDEE---IEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1930-2620 |
4.11e-10 |
|
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: 66.68 E-value: 4.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQEL 2009
Cdd:pfam15921 93 RLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQI 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2010 QQLR------QNSDMEIKSKAKKIEEAeyNRRKIEEEIHIVRLQLETM----QKQKASAEDELQELRARAEEAERQ---- 2075
Cdd:pfam15921 173 EQLRkmmlshEGVLQEIRSILVDFEEA--SGKKIYEHDSMSTMHFRSLgsaiSKILRELDTEISYLKGRIFPVEDQleal 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2076 KKAAQEEAERLRRQVKDE-SQKKREAEEE---LKRKVQAEKDAAREKQRAMEDLQ----------------------KFR 2129
Cdd:pfam15921 251 KSESQNKIELLLQQHQDRiEQLISEHEVEitgLTEKASSARSQANSIQSQLEIIQeqarnqnsmymrqlsdlestvsQLR 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2130 SQAEEAERRMKQAEVEKERQIKVAqevaqQSAAAELNSKRMSFAEKTAQLELSLkQEHITVTHLQEEAERLKKQHEEAEK 2209
Cdd:pfam15921 331 SELREAKRMYEDKIEELEKQLVLA-----NSELTEARTERDQFSQESGNLDDQL-QKLLADLHKREKELSLEKEQNKRLW 404
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2210 AREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKelAEDELEKQRKLAD 2289
Cdd:pfam15921 405 DRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQ--LESTKEMLRKVVE 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2290 ATAQQKF---SAEQELIRLKADTESGEQQRLLLEEELFRLKNEVN---EAIQKRKKMEEELAKVRAEMEIL---LESKSR 2360
Cdd:pfam15921 483 ELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDlklQELQHLKNEGDHLRNVQTECEALklqMAEKDK 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2361 AEEESRSNTEKSKHM----------LEVEASKL-RELAEEAARLRALS-EEAKRQRQIAEGEAARQRAEAERIL-----K 2423
Cdd:pfam15921 563 VIEILRQQIENMTQLvgqhgrtagaMQVEKAQLeKEINDRRLELQEFKiLKDKKDAKIRELEARVSDLELEKVKlvnagS 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2424 EKLAAINEatrLKTEAEIALKEKEAENERLRRLAED-EAYQRKLleEQATQHKQDIEEKIILLKKSSDNELERQKNived 2502
Cdd:pfam15921 643 ERLRAVKD---IKQERDQLLNEVKTSRNELNSLSEDyEVLKRNF--RNKSEEMETTTNKLKMQLKSAQSELEQTRN---- 713
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2503 TLRQRRIIEEEIRILKLNFEKASSGK--------SDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAE 2574
Cdd:pfam15921 714 TLKSMEGSDGHAMKVAMGMQKQITAKrgqidalqSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELE 793
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1717010358 2575 ekvrkiLADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAE 2620
Cdd:pfam15921 794 ------VLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2051-2301 |
4.32e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.21 E-value: 4.32e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2051 MQKQKASAedelqelrARAEEaERQKKAAQEEaerlrrqvkDESQKKREAEEELKRKVQAEKDAAREKQRamedlqkfrs 2130
Cdd:PRK09510 67 QQQQQKSA--------KRAEE-QRKKKEQQQA---------EELQQKQAAEQERLKQLEKERLAAQEQKK---------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2131 QAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAElnSKRMSFAEKTAQLELSLKqehitvthlqEEAERLKKQHEEAeka 2210
Cdd:PRK09510 119 QAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKK----------AEAEAAKKAAAEA--- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2211 reeaekelekwhqKANEALRLRLQAEEVAHKKtlAQEEAEKQkedAEREARKRAKAEESALRQKELAEDELEKQRKLADA 2290
Cdd:PRK09510 184 -------------KKKAEAEAAAKAAAEAKKK--AEAEAKKK---AAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAK 245
|
250
....*....|.
gi 1717010358 2291 TAQQKFSAEQE 2301
Cdd:PRK09510 246 AAEKAAAAKAA 256
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2529-2803 |
5.29e-10 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 65.39 E-value: 5.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2529 SDLELELNQLKNIAEEthRSKEKAEQE-AEKQR--QLALEEEQRRKE-AEEKvrkilADEQEAARQRKAALEEVerlKAK 2604
Cdd:PRK07735 1 MDPEKDLEDLKKEAAR--RAKEEARKRlVAKHGaeISKLEEENREKEkALPK-----NDDMTIEEAKRRAAAAA---KAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2605 AEEAKRQKELAEKEAERQiqlAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYAR 2684
Cdd:PRK07735 71 AAALAKQKREGTEEVTEE---EKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2685 MRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAEL-----------EAAKRAHAEQAAL-KQKQ---- 2748
Cdd:PRK07735 148 EGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEvteeekakakaKAAAAAKAKAAALaKQKAsqgn 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2749 -LADEEMDKHKKF------AEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEV 2803
Cdd:PRK07735 228 gDSGDEDAKAKAIaaakakAAAAARAKTKGAEGKKEEEPKQEEPSVNQPYLNKYVEVIKEKL 289
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1710-2134 |
5.45e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 5.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1710 KELEATKAELKKLRSQVEGHQPLFNTLEAdLNKAKDVNEQmLRSHSERDVDLDRYRERVQQLLERWQAILVQIDLRQREL 1789
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEA-ELEELREELEKLEKLLQLLPLYQELEALEAELAELPERL 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1790 DQLGRQLRYYRETYDWLIKWIKDAKQRQEQIQsvpitdsktmKEQLLQLKKLLEEIESNRTKVDECQKYAKQYIDAIKDY 1869
Cdd:COG4717 149 EELEERLEELRELEEELEELEAELAELQEELE----------ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1870 ELQLVTYKAQVEPVVSPAKKPKVQSTSDSIIQEY------VDLRTRYSELTTLTSQYIKFITETLC-------RLNVEEK 1936
Cdd:COG4717 219 QEELEELEEELEQLENELEAAALEERLKEARLLLliaaalLALLGLGGSLLSLILTIAGVLFLVLGllallflLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1937 AAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQ-QKQTIQQELQQLRQN 2015
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2016 SDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETM---------QKQKASAEDELQELRARAEEAERQKKAAQEEAERL 2086
Cdd:COG4717 379 AGVEDEEELRAALEQAEEYQELKEELEELEEQLEELlgeleelleALDEEELEEELEELEEELEELEEELEELREELAEL 458
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2087 RRQVK-----DESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEE 2134
Cdd:COG4717 459 EAELEqleedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2747-3201 |
5.98e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.94 E-value: 5.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2747 KQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDdESQRLKEEVTDAMRQKAQVEEELFKVK--IQM 2824
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQE-ELEELEEELEELEAELEELREELEKLEklLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2825 EELIKLKLRIEEEnkmliMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAarmrklaeddlanQRALAEKMLKEKMQ 2904
Cdd:COG4717 128 LPLYQELEALEAE-----LAELPERLEELEERLEELRELEEELEELEAELAEL-------------QEELEELLEQLSLA 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2905 AIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQA 2984
Cdd:COG4717 190 TEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2985 K-AEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEM 3063
Cdd:COG4717 270 SlILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEEL 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3064 QVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEkekaklenlyEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAM 3143
Cdd:COG4717 350 QELLREAEELEEELQLEELEQEIAALLAEAGVED----------EEELRAALEQAEEYQELKEELEELEEQLEELLGELE 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 3144 KKQKEA-EESVRHKQDELHQLDKRRQEQEKLLADENRKLREKLEQLEEEHRIALAQTRE 3201
Cdd:COG4717 420 ELLEALdEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQEL 478
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2381-2764 |
7.79e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 7.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2381 SKLRELAEEAARLRALSEE-AKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLR-RLAE 2458
Cdd:COG4717 78 EELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEeRLEE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2459 DEAYQRKL--LEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELEL- 2535
Cdd:COG4717 158 LRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELe 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2536 --NQLKNIAEE--------------------------------------------THRSKEKAEQEAEKQRQLALE---E 2566
Cdd:COG4717 238 aaALEERLKEArlllliaaallallglggsllsliltiagvlflvlgllallfllLAREKASLGKEAEELQALPALeelE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2567 EQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQiQLAQEAAFKKIEAEEKAHAAivQ 2646
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIA-ALLAEAGVEDEEELRAALEQ--A 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2647 QKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDE--AEK 2724
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAEL 474
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1717010358 2725 LRKEAELEAAKRAHAEQAALkqKQLADEEMDKHKKFAEKT 2764
Cdd:COG4717 475 LQELEELKAELRELAEEWAA--LKLALELLEEAREEYREE 512
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
628-734 |
7.87e-10 |
|
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: 59.44 E-value: 7.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 628 EDERDrvqKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLK 702
Cdd:cd21299 1 ETSRE---ERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1717010358 703 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 734
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2382-2962 |
8.22e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.83 E-value: 8.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2382 KLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAE-RILKEKLAAInEATRLKTEAEIALKEKEAENERLRRLAED- 2459
Cdd:PRK02224 163 KLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKEeKDLHERLNGL-ESELAELDEEIERYEEQREQARETRDEADe 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2460 --EAYQRKLLE-EQATQHKQDIEEKIILLKKSSDN---ELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLEL 2533
Cdd:PRK02224 242 vlEEHEERREElETLEAEIEDLRETIAETEREREElaeEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELED 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2534 ELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKE 2613
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2614 LAEkeaerqIQLAQEAAFKKIEAEEKAhaaivqqkeqemlQTRKQEKSILDKLKEEAERAKRAaedadyARMRAEQEAAL 2693
Cdd:PRK02224 402 DAP------VDLGNAEDFLEELREERD-------------ELREREAELEATLRTARERVEEA------EALLEAGKCPE 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2694 SRQQVEEAERM------KQRAEEEAQAKAQAQDEAEKLRKEAE-LEAAKRAHAEQAALKQK-QLADEEMDKHKKFAEKTL 2765
Cdd:PRK02224 457 CGQPVEGSPHVetieedRERVEELEAELEDLEEEVEEVEERLErAEDLVEAEDRIERLEERrEDLEELIAERRETIEEKR 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2766 RQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEE---LFKVKIQMEELIKLKLRIEEENKMLI 2842
Cdd:PRK02224 537 ERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERiesLERIRTLLAAIADAEDEIERLREKRE 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2843 MKDKDSTQK--FLAEEAEKMRQVAEEAARLSIEAQEAARMRklAEDDLANqralaekmLKEKMQAIQEA-TRLKAEADM- 2918
Cdd:PRK02224 617 ALAELNDERreRLAEKRERKRELEAEFDEARIEEAREDKER--AEEYLEQ--------VEEKLDELREErDDLQAEIGAv 686
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2919 ---LQKQKELAQEqaRKFQEDKEQIEQQLAKETEGFQKS---LEAERRQQ 2962
Cdd:PRK02224 687 eneLEELEELRER--REALENRVEALEALYDEAEELESMygdLRAELRQR 734
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2647-3080 |
8.41e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.17 E-value: 8.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2647 QKEQEMLQTRKQEKSILDKLK-EEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKL 2725
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2726 RKEAELEA-------------AKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLL 2792
Cdd:COG4717 132 QELEALEAelaelperleeleERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2793 DDESQRLKEEVTDAMRQKAQVEEELFKVKIQmEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEE----AA 2868
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALE-ERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGllalLF 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2869 RLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAI-----QEATRLKAEADMLQKQKELAQEQARKFQE-DKEQIEQ 2942
Cdd:COG4717 291 LLLAREKASLGKEAEELQALPALEELEEEELEELLAALglppdLSPEELLELLDRIEELQELLREAEELEEElQLEELEQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2943 QLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEmskAQAKAEEDAKKFKKQAEDFGNKLHQTELatkermvvvQSLE 3022
Cdd:COG4717 371 EIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE---LEEQLEELLGELEELLEALDEEELEEEL---------EELE 438
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 3023 IQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQ-EMQVAQQEQLRQETQVLQT 3080
Cdd:COG4717 439 EELEELEEELEELREELAELEAELEQLEEDGELAELLQElEELKAELRELAEEWAALKL 497
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1963-2177 |
8.51e-10 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 64.47 E-value: 8.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1963 AEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQnsdmEIKSKAKKIEEAEynrRKIEEEIH 2042
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAE---AEIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2043 IVRLQLETMQKQKASA-----------------------------EDELQELRARAEEAERQKKAAQEEAERLRRQVKDE 2093
Cdd:COG3883 87 ELGERARALYRSGGSVsyldvllgsesfsdfldrlsalskiadadADLLEELKADKAELEAKKAELEAKLAELEALKAEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2094 SQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFA 2173
Cdd:COG3883 167 EAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
....
gi 1717010358 2174 EKTA 2177
Cdd:COG3883 247 AGAG 250
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2590-3187 |
1.00e-09 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 65.59 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2590 QRKAALEEVERLKAKAEEAKrqkeLAEKEAERQIQlaqeAAFKKIEAEEKAHAAIVQQKEQEMLQ-TRKQEksildkLKE 2668
Cdd:PRK10246 192 QHKSARTELEKLQAQASGVA----LLTPEQVQSLT----ASLQVLTDEEKQLLTAQQQQQQSLNWlTRLDE------LQQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2669 EAERAKRAAEDADYARMRAE-QEAALSRQQVEEAER-MKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQ 2746
Cdd:PRK10246 258 EASRRQQALQQALAAEEKAQpQLAALSLAQPARQLRpHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2747 KQLADEEMD-------KHKKFA---------EKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLK-EEVTDAMRQ 2809
Cdd:PRK10246 338 SAELQAQQQslntwlaEHDRFRqwnnelagwRAQFSQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTaDEVAAALAQ 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2810 KAQ---VEEELFKVKIQMEELIKLKLRIEEenkmlimkdkdSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAE- 2885
Cdd:PRK10246 418 HAEqrpLRQRLVALHGQIVPQQKRLAQLQV-----------AIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKTICEq 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2886 ----DDLANQRAL------------AEKMLKEKMQAIqEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETE 2949
Cdd:PRK10246 487 eariKDLEAQRAQlqagqpcplcgsTSHPAVEAYQAL-EPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDES 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2950 GFQKSLEAER--RQQLEITAEAERLKLQVlemskaqakaEEDAKKFKKQAEDFGNKLH--------QTELATKERMVVVQ 3019
Cdd:PRK10246 566 EAQSLRQEEQalTQQWQAVCASLNITLQP----------QDDIQPWLDAQEEHERQLRllsqrhelQGQIAAHNQQIIQY 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3020 SLEIQRQQSGKEAEELRRAIAELEHEKEKL-----KQEAELLQKNsQEMQVAQQEQLRQETQVLQTtfltekhLLLEKEK 3094
Cdd:PRK10246 636 QQQIEQRQQQLLTALAGYALTLPQEDEEASwlatrQQEAQSWQQR-QNELTALQNRIQQLTPLLET-------LPQSDDL 707
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3095 YIEKEKAKLENLYE--DEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQ----KEA------EESVRHKQDELHQ 3162
Cdd:PRK10246 708 PHSEETVALDNWRQvhEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQFDTALQASvfddQQAflaallDEETLTQLEQLKQ 787
|
650 660
....*....|....*....|....*.
gi 1717010358 3163 -LDKRRQEQEKLLADENRKLREKLEQ 3187
Cdd:PRK10246 788 nLENQRQQAQTLVTQTAQALAQHQQH 813
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1582-2306 |
1.35e-09 |
|
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: 65.14 E-value: 1.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1582 QLEGCESRTIHKIRSPMEKDPiKECSQRISEQQqihFELEGIkknldkvsekTQKVLAQKEQSTStplLRTEHEITLQKM 1661
Cdd:pfam15921 246 QLEALKSESQNKIELLLQQHQ-DRIEQLISEHE---VEITGL----------TEKASSARSQANS---IQSQLEIIQEQA 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1662 DQVYSLSTIYLEKLKTINLVIRSThgAEEVVKTYEDQLKEVHavpsdsKELEATKAELKKLRSQVEGHQPLFNTLEADLN 1741
Cdd:pfam15921 309 RNQNSMYMRQLSDLESTVSQLRSE--LREAKRMYEDKIEELE------KQLVLANSELTEARTERDQFSQESGNLDDQLQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1742 KakdvneqMLRSHSERDVDLDRYRERVQQLLERWQAILVQIDLRQRELDQlgRQLRYYRetYDWLIKWIKDAKQRQEQIQ 1821
Cdd:pfam15921 381 K-------LLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRELDD--RNMEVQR--LEALLKAMKSECQGQMERQ 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1822 SVPITDSKtmkeqllqlkklleeiesnrtkvdecqkyakQYIDAIKDYELQLVTYKAQVEPVVS--PAKKPKVQSTSDSI 1899
Cdd:pfam15921 450 MAAIQGKN-------------------------------ESLEKVSSLTAQLESTKEMLRKVVEelTAKKMTLESSERTV 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1900 iqeyvdlrtrySELTTltsqyikfitetlcRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLA-EAHAKAKAQAEKEAE 1978
Cdd:pfam15921 499 -----------SDLTA--------------SLQEKERAIEATNAEITKLRSRVDLKLQELQHLKnEGDHLRNVQTECEAL 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1979 ELQRRMQEEVskrevvavdAEQQKQTIQQELQQLRQNSDMeikSKAKKIEEAEynrrkIEEEIHIVRLQLETMQKQKASA 2058
Cdd:pfam15921 554 KLQMAEKDKV---------IEILRQQIENMTQLVGQHGRT---AGAMQVEKAQ-----LEKEINDRRLELQEFKILKDKK 616
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2059 EDELQELRARAEEAERQK-KAAQEEAERLrRQVKDESQKKREAEEELKRKvQAEKDAAREKQRAMEdlQKFRSQAEEAER 2137
Cdd:pfam15921 617 DAKIRELEARVSDLELEKvKLVNAGSERL-RAVKDIKQERDQLLNEVKTS-RNELNSLSEDYEVLK--RNFRNKSEEMET 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2138 RMKQAEVekerQIKVAQEVAQQSAAaelNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHeeaekareeaeke 2217
Cdd:pfam15921 693 TTNKLKM----QLKSAQSELEQTRN---TLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQF------------- 752
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2218 LEKWHQKANEALRLrLQAEEVAHKKTLAQEEAEKQKEDAEREArkrAKAEESALRQK----ELAEDELEKQRKLADATAQ 2293
Cdd:pfam15921 753 LEEAMTNANKEKHF-LKEEKNKLSQELSTVATEKNKMAGELEV---LRSQERRLKEKvanmEVALDKASLQFAECQDIIQ 828
|
730
....*....|...
gi 1717010358 2294 QKfsaEQELIRLK 2306
Cdd:pfam15921 829 RQ---EQESVRLK 838
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2602-2822 |
1.44e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 64.12 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2602 KAKAEEAKRQKELAEKEAERQIQLAQEAAfKKIEAEEKAHAaivqqkeqemlqtrKQEKSILDKLKEEAERAKRAAE--- 2678
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETEIAIAQA-NREAEEAELEQ--------------EREIETARIAEAEAELAKKKAEerr 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2679 DADYARMRAEQEAALSRQQVE-EAERMKQRAEEEAQAKAQaqdEAEKLRKEAELEAAKRAHAEqaALKQKQLADEEmdkh 2757
Cdd:COG2268 256 EAETARAEAEAAYEIAEANAErEVQRQLEIAEREREIELQ---EKEAEREEAELEADVRKPAE--AEKQAAEAEAE---- 326
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2758 kkfAE-KTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEevtdAMRQKAQVEEELFKVKI 2822
Cdd:COG2268 327 ---AEaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE----IAEAAAKPLEKIDKITI 385
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2528-2821 |
1.62e-09 |
|
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: 63.52 E-value: 1.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2528 KSDLELELNQLKNIA-EETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILAD---EQEAARQRKAALEEVERLKA 2603
Cdd:pfam15558 19 EEQRMRELQQQAALAwEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGreeRRRADRREKQVIEKESRWRE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2604 KAE--EAKRQKELAEKEAE-RQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEML--------------QTRKQEKSILDKL 2666
Cdd:pfam15558 99 QAEdqENQRQEKLERARQEaEQRKQCQEQRLKEKEEELQALREQNSLQLQERLeeachkrqlkereeQKKVQENNLSELL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2667 KEEA---ERAKRAAEDADYARMRAEQEAALS-----RQQVEEAERMKQRAEEEAQAKAQAQDEAEklRKEAELEAAKRAH 2738
Cdd:pfam15558 179 NHQArkvLVDCQAKAEELLRRLSLEQSLQRSqenyeQLVEERHRELREKAQKEEEQFQRAKWRAE--EKEEERQEHKEAL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2739 AEqaalkqkqLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRlkEEVTDAMRQKAQVEEELF 2818
Cdd:pfam15558 257 AE--------LADRKIQQARQVAHKTVQDKAQRARELNLEREKNHHILKLKVEKEEKCHR--EGIKEAIKKKEQRSEQIS 326
|
...
gi 1717010358 2819 KVK 2821
Cdd:pfam15558 327 REK 329
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1937-2179 |
1.71e-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: 1.71e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1937 AAEKLKEEERRRLAEVEAQLEKQtqlaeahAKAKAQAEKEAEELqrrmQEEVSKREVVAVDAEQQKQTIQQELQQLRQns 2016
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAEL-------EKELAALKKEEKAL----LKQLAALERRIAALARRIRALEQELAALEA-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2017 dmEIKSKAKKIEEAeynRRKIEEEIHIVRLQLETMQKQKA--------SAEDELQELR----------ARAEEAERQkKA 2078
Cdd:COG4942 84 --ELAELEKEIAEL---RAELEAQKEELAELLRALYRLGRqpplalllSPEDFLDAVRrlqylkylapARREQAEEL-RA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2079 AQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIkvaQEVAQ 2158
Cdd:COG4942 158 DLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALI---ARLEA 234
|
250 260
....*....|....*....|.
gi 1717010358 2159 QSAAAELNSKRMSFAEKTAQL 2179
Cdd:COG4942 235 EAAAAAERTPAAGFAALKGKL 255
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1943-2614 |
1.96e-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: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1943 EEERRRLAEVEAQ----LEKQTQLAEAHAKAKAQAEKEAEELQRRMqeevSKREVVAVDAEQQKQTIQQELQQLRQNsdm 2018
Cdd:pfam07111 79 EEEVRLLRETSLQqkmrLEAQAMELDALAVAEKAGQAEAEGLRAAL----AGAEMVRKNLEEGSQRELEEIQRLHQE--- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2019 EIKSKAKKIEEAeynrrkieeeihivrlqLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKdesqkkr 2098
Cdd:pfam07111 152 QLSSLTQAHEEA-----------------LSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLS------- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2099 EAEEELKRKVQaekdaarekqrAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ 2178
Cdd:pfam07111 208 KTQEELEAQVT-----------LVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQVRVQSLT 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2179 LELSLKQEHITvthlqeeaERLKKQHEEAEKAREEAEKELEKWHQKANeALRLRLQAEEVAHKKTLAQEEAEKqkedAER 2258
Cdd:pfam07111 277 HMLALQEEELT--------RKIQPSDSLEPEFPKKCRSLLNRWREKVF-ALMVQLKAQDLEHRDSVKQLRGQV----AEL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2259 EARKRAKAEESALRQKELaedelekqrkladataqQKFSAEQELIRLKADTesgeqqrllleeelfrLKNEVNEAIQKRK 2338
Cdd:pfam07111 344 QEQVTSQSQEQAILQRAL-----------------QDKAAEVEVERMSAKG----------------LQMELSRAQEARR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2339 KMEEELAKVRAEMEILLESKSRAEEESRSNTEKskhmleveasklreLAEEAARLRALSEE---AKRQRQIAEGEAARQR 2415
Cdd:pfam07111 391 RQQQQTASAEEQLKFVVNAMSSTQIWLETTMTR--------------VEQAVARIPSLSNRlsyAVRKVHTIKGLMARKV 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2416 AEAERILK-----------------EKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDI 2478
Cdd:pfam07111 457 ALAQLRQEscpppppappvdadlslELEQLREERNRLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRA 536
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2479 EEKIILLKKSSDNELERQKNIVED--TLRQRRIIEEEIRILKLNfEKASSGKSDLELELNQLKNIAEETHRSKEKAeqea 2556
Cdd:pfam07111 537 QESLASVGQQLEVARQGQQESTEEaaSLRQELTQQQEIYGQALQ-EKVAEVETRLREQLSDTKRRLNEARREQAKA---- 611
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2557 ekqrQLALEEEQRRKEAEEKVRKILADEQEAARQrkaalEEVERLKAKAEEAKRQKEL 2614
Cdd:pfam07111 612 ----VVSLRQIQHRATQEKERNQELRRLQDEARK-----EEGQRLARRVQELERDKNL 660
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4556-4594 |
2.34e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.41 E-value: 2.34e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 4556 LLEAQAATGYVIDPIKCLKLAVEDAVRMGIVGTEFKDKL 4594
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2524-2750 |
2.59e-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: 62.86 E-value: 2.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2524 ASSGKSDLELELNQL-KNIAEETHRSKEKAEQEAEKQRQLAlEEEQRRKEAEEKVRKiLADEQEAARQRKAALEEvERLK 2602
Cdd:COG4942 18 QADAAAEAEAELEQLqQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRA-LEQELAALEAELAELEK-EIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2603 AKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAED--A 2680
Cdd:COG4942 95 LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAerA 174
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2681 DYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLA 2750
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1880-2425 |
2.75e-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: 2.75e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1880 VEPVVSPAKKPKVQStSDSIIQEYVDLRTRYSELTTLTSQYIKFITE-----TLCRLNVEEKAAEK-----LKEEERRRL 1949
Cdd:pfam05483 192 IEKMILAFEELRVQA-ENARLEMHFKLKEDHEKIQHLEEEYKKEINDkekqvSLLLIQITEKENKMkdltfLLEESRDKA 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1950 AEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQlrQNSDMEIKSKAKK--- 2026
Cdd:pfam05483 271 NQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEE--KEAQMEELNKAKAahs 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2027 --IEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRR------QVKDESQKKR 2098
Cdd:pfam05483 349 fvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKilaedeKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2099 EAEEELKRKVQAEKDAAREKQRAMEDLQ----KFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSfaE 2174
Cdd:pfam05483 429 KIAEELKGKEQELIFLLQAREKEIHDLEiqltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELT--Q 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2175 KTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELE----KWHQKANEALRLRLQAEEVAHKKTLAQEEAE 2250
Cdd:pfam05483 507 EASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELEsvreEFIQKGDEVKCKLDKSEENARSIEYEVLKKE 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2251 KQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQ--------------- 2315
Cdd:pfam05483 587 KQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfeeiidnyqkeiedk 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2316 ---RLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLES------KSRAEEESRSNTEKSKhmlEVEASKLR-E 2385
Cdd:pfam05483 667 kisEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKhkhqydKIIEERDSELGLYKNK---EQEQSSAKaA 743
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1717010358 2386 LAEEAARLRALSEEAKRQRQIAEGEAARQRAEAER---ILKEK 2425
Cdd:pfam05483 744 LEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKEntaILKDK 786
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2707-3209 |
2.88e-09 |
|
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: 64.04 E-value: 2.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2707 RAEEEAQAKAQ----AQDEAEKL--------RKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTlrqkaQVEQE 2774
Cdd:pfam01576 2 RQEEEMQAKEEelqkVKERQQKAeselkeleKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAARKQ-----ELEEI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2775 LTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAqvEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDStqKFLA 2854
Cdd:pfam01576 77 LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLD--EEEAARQKLQLEKVTTEAKIKKLEEDILLLEDQNS--KLSK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2855 EEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLK-EKMQAIQEATRLKAEADMLQKQKELAQEQARKf 2933
Cdd:pfam01576 153 ERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKeEKGRQELEKAKRKLEGESTDLQEQIAELQAQI- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2934 qedkEQIEQQLAKETEGFQKSL---EAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLH--QTE 3008
Cdd:pfam01576 232 ----AELRAQLAKKEEELQAALarlEEETAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEalKTE 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3009 LA-TKERMVVVQSLEIQRQQsgkEAEELRRAIAELEHEKEKlkQEAELLQKNSQ--EMQVAQQEQLRQETQVLQTTflte 3085
Cdd:pfam01576 308 LEdTLDTTAAQQELRSKREQ---EVTELKKALEEETRSHEA--QLQEMRQKHTQalEELTEQLEQAKRNKANLEKA---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3086 KHLLLEKEKYIEKekaklenlyedEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELH---- 3161
Cdd:pfam01576 379 KQALESENAELQA-----------ELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELEsvss 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3162 -----------------QLDKRRQEQEKLLADENRK-----------------LREKLEQLEEEHRIALAQTREMMIQTD 3207
Cdd:pfam01576 448 llneaegkniklskdvsSLESQLQDTQELLQEETRQklnlstrlrqledernsLQEQLEEEEEAKRNVERQLSTLQAQLS 527
|
..
gi 1717010358 3208 DL 3209
Cdd:pfam01576 528 DM 529
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2049-2282 |
2.89e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.90 E-value: 2.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2049 ETMQKQKASAEDELQElraraEEAERQKKAAQEEAERLRRQvkdesQKKREAEEELKRKVQAEKDAAREKQRAMEDLQ-K 2127
Cdd:PRK09510 79 EQRKKKEQQQAEELQQ-----KQAAEQERLKQLEKERLAAQ-----EQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKaK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2128 FRSQAEEAERRMKQAEVEKERQikvAQEVAQQSAAAElnskrmsfAEKTAQLELSLKQEhitvthlqEEAErlkkqheea 2207
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKKK---AEAEAAKKAAAE--------AKKKAEAEAAAKAA--------AEAK--------- 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2208 ekareeaekelekwhQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELE 2282
Cdd:PRK09510 201 ---------------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2022-2203 |
2.91e-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: 62.86 E-value: 2.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2022 SKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAE 2101
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2102 EELKRK-----------------------------VQAEKDAAREKQRAMEDLQKFRSQAEEAER-RMKQAEVEKERQIK 2151
Cdd:COG4942 97 AELEAQkeelaellralyrlgrqpplalllspedfLDAVRRLQYLKYLAPARREQAEELRADLAElAALRAELEAERAEL 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2152 VAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQ 2203
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2591-3073 |
3.09e-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: 63.51 E-value: 3.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2591 RKAALEEVERLKAKAEEAKRQKELAE-------KEAERQIQLAQE--AAFKKIEAEE---KAHAAIVQQKEQEMLQTRKQ 2658
Cdd:pfam05701 37 RKLVELELEKVQEEIPEYKKQSEAAEaakaqvlEELESTKRLIEElkLNLERAQTEEaqaKQDSELAKLRVEEMEQGIAD 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2659 EKSILDKLKEEAERAKRAAEDADYARMRAEQEaALSRQQ---VEEAERMKQRAEEEAQAKAQAQDEAEKLRKE-----AE 2730
Cdd:pfam05701 117 EASVAAKAQLEVAKARHAAAVAELKSVKEELE-SLRKEYaslVSERDIAIKRAEEAVSASKEIEKTVEELTIEliatkES 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2731 LEAAKRAHAEqaALKQKQLADEEMDKHKKFAEKTLRqkaQVEQELTKVKLQLEETDHQKTLLDDES---QRLKEEVTDAM 2807
Cdd:pfam05701 196 LESAHAAHLE--AEEHRIGAALAREQDKLNWEKELK---QAEEELQRLNQQLLSAKDLKSKLETASallLDLKAELAAYM 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2808 RQKAQVEEELFKVKIQMEELIKLKL---RIE-EENKMLIMKDKDSTQ--KFLAE------EAEK-----MRQvAEEAARL 2870
Cdd:pfam05701 271 ESKLKEEADGEGNEKKTSTSIQAALasaKKElEEVKANIEKAKDEVNclRVAAAslrselEKEKaelasLRQ-REGMASI 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2871 SIEAQEAARMRKLAEDDLANQRALA--EKML---KEKMQAIQEATRLKAEAdmlqkqkELAQEQARKFQEDKEQIEQQLA 2945
Cdd:pfam05701 350 AVSSLEAELNRTKSEIALVQAKEKEarEKMVelpKQLQQAAQEAEEAKSLA-------QAAREELRKAKEEAEQAKAAAS 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2946 KetegFQKSLEAERRqQLEITAEAERLKL---QVLEMSKAQAKAEEDAKKFKK------QAEDFGNKLHQTELATKER-M 3015
Cdd:pfam05701 423 T----VESRLEAVLK-EIEAAKASEKLALaaiKALQESESSAESTNQEDSPRGvtlsleEYYELSKRAHEAEELANKRvA 497
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 3016 VVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLK---QEAEllqkNSQEMQVAQQEQLRQ 3073
Cdd:pfam05701 498 EAVSQIEEAKESELRSLEKLEEVNREMEERKEALKialEKAE----KAKEGKLAAEQELRK 554
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1934-2125 |
3.48e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.52 E-value: 3.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EEKAAEKLKEEERRRLAEVEAQ----------LEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKrevvavdAEQQKQ 2003
Cdd:PRK09510 96 QAAEQERLKQLEKERLAAQEQKkqaeeaakqaALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-------AAAEAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2004 TIQQELQQLRQnsdmeiKSKAKKIEEAEYNRRKIEEEihivrlqletmqKQKASAEDELQELRARAEEAERQKKAAQEEA 2083
Cdd:PRK09510 169 KKAEAEAAKKA------AAEAKKKAEAEAAAKAAAEA------------KKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA 230
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1717010358 2084 erlrrqvkdESQKKREAEEELKRKvQAEKDAAREKQRAMEDL 2125
Cdd:PRK09510 231 ---------AAEAKAAAEKAAAAK-AAEKAAAAKAAAEVDDL 262
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2065-3044 |
3.81e-09 |
|
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: 63.82 E-value: 3.81e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2065 LRARAEEAERQKKAAQEEAERL--RRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRS---QAEEAERRm 2139
Cdd:COG3096 274 MRHANERRELSERALELRRELFgaRRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLVQTalrQQEKIERY- 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2140 kQAEVEkERQIKVAQevaQQSAAAELNSKRmsfAEKTAQLELSlkqehitvthlQEEAERLKKQheeaekaREEAEKELE 2219
Cdd:COG3096 353 -QEDLE-ELTERLEE---QEEVVEEAAEQL---AEAEARLEAA-----------EEEVDSLKSQ-------LADYQQALD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2220 KWHQKA---NEALRLRLQAEEVAHKKTLAQEEAEkqkedaEREARKRAKAEE--SALRqkelaedELEKQRKLADATAQQ 2294
Cdd:COG3096 407 VQQTRAiqyQQAVQALEKARALCGLPDLTPENAE------DYLAAFRAKEQQatEEVL-------ELEQKLSVADAARRQ 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2295 KFSAEQELIRLKADTESGEQQRLLLEEELFRLknEVNEAIQKRKKMEEELAkvraEMEILLESKSRAEEES-----RSNT 2369
Cdd:COG3096 474 FEKAYELVCKIAGEVERSQAWQTARELLRRYR--SQQALAQRLQQLRAQLA----ELEQRLRQQQNAERLLeefcqRIGQ 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2370 E-KSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEA 2448
Cdd:COG3096 548 QlDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQE 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2449 ENERLRRLAEDEAyQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEdtlrqrriieeeirilKLNFEKASSGK 2528
Cdd:COG3096 628 VTAAMQQLLERER-EATVERDELAARKQALESQIERLSQPGGAEDPRLLALAE----------------RLGGVLLSEIY 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2529 SDLELE--------LNQLKN--IAEETHRSKEKAEQEAEKQRQLALEE------EQRRKEAEEKVRKILAdeQEAARQ-R 2591
Cdd:COG3096 691 DDVTLEdapyfsalYGPARHaiVVPDLSAVKEQLAGLEDCPEDLYLIEgdpdsfDDSVFDAEELEDAVVV--KLSDRQwR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2592 KAALEEVERLKAKAeeakRQKELAEKEAERQIqlaqeaafkkiEAEEKAHAAIVQQKEQEMLQTRKQeksILDKLKEEAE 2671
Cdd:COG3096 769 YSRFPEVPLFGRAA----REKRLEELRAERDE-----------LAEQYAKASFDVQKLQRLHQAFSQ---FVGGHLAVAF 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2672 RAKRAAEDADYARMRAEQEAALSRQQVEEaermkQRAEEEAQAKAQAQDEAEKLRKEAEL----EAAKRAHAEQAALKQK 2747
Cdd:COG3096 831 APDPEAELAALRQRRSELERELAQHRAQE-----QQLRQQLDQLKEQLQLLNKLLPQANLladeTLADRLEELREELDAA 905
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2748 QLADEEMDKHKKFAEK------TLR----QKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKE-EVTDAMRQKAQVEEe 2816
Cdd:COG3096 906 QEAQAFIQQHGKALAQleplvaVLQsdpeQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPHfSYEDAVGLLGENSD- 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2817 lfkvkiqMEELIKLKLrieeenkmlimkdkdstqkflaEEAEKMRQVAEEAARlSIEAQEAARMRKLAedDLANQRALAE 2896
Cdd:COG3096 985 -------LNEKLRARL----------------------EQAEEARREAREQLR-QAQAQYSQYNQVLA--SLKSSRDAKQ 1032
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2897 KMLKEKMQAIQEaTRLKAEADmlqkqkelAQEQARkfqEDKEQIEQQLaketegfqkSLEAERRQQLEitAEAERLKLQV 2976
Cdd:COG3096 1033 QTLQELEQELEE-LGVQADAE--------AEERAR---IRRDELHEEL---------SQNRSRRSQLE--KQLTRCEAEM 1089
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2977 LEMSKAQAKAEEDAKKFKKQAE----------------DFGNKLHQTELAtkermvvVQSLEIQRQQSGKEAEELRRAIA 3040
Cdd:COG3096 1090 DSLQKRLRKAERDYKQEREQVVqakagwcavlrlardnDVERRLHRRELA-------YLSADELRSMSDKALGALRLAVA 1162
|
....
gi 1717010358 3041 ELEH 3044
Cdd:COG3096 1163 DNEH 1166
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2671-3075 |
3.95e-09 |
|
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: 63.55 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2671 ERAKRAAEDADYARMRAEQEAALsrqqvEEAERMKQRAEEEAQAKAQAQDEAEKLRKEaeleaakRAHAEQAALKQKQLA 2750
Cdd:TIGR02169 154 ERRKIIDEIAGVAEFDRKKEKAL-----EELEEVEENIERLDLIIDEKRQQLERLRRE-------REKAERYQALLKEKR 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2751 DEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQ-KAQVEEELFKVKIQMEElik 2829
Cdd:TIGR02169 222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGE--- 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2830 LKLRIEeenkmlimkdkdSTQKFLAEEAEKMRQVAEEaarlsiEAQEAARMRKLAEDDLANQRALAEKMlKEKMQAIQEA 2909
Cdd:TIGR02169 299 LEAEIA------------SLERSIAEKERELEDAEER------LAKLEAEIDKLLAEIEELEREIEEER-KRRDKLTEEY 359
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2910 TRLKAEADMLQKQkelAQEQARKFQEDKEQIeQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEED 2989
Cdd:TIGR02169 360 AELKEELEDLRAE---LEEVDKEFAETRDEL-KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAK 435
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2990 AKKFKKQAEDFGNKLHQTElatkermvvvQSLEIQRQQSGKEAEELRR---AIAELEHEKEKLKQEAELLQKNSQEMQVA 3066
Cdd:TIGR02169 436 INELEEEKEDKALEIKKQE----------WKLEQLAADLSKYEQELYDlkeEYDRVEKELSKLQRELAEAEAQARASEER 505
|
....*....
gi 1717010358 3067 QQEQLRQET 3075
Cdd:TIGR02169 506 VRGGRAVEE 514
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1999-2178 |
4.01e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.13 E-value: 4.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1999 EQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNR-RKIEEEihivRLQLETMQKQKASAEDELQELRARAEEA----- 2072
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERlKQLEKE----RLAAQEQKKQAEEAAKQAALKQKQAEEAaakaa 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2073 ERQKKAAQEEAERLR---RQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQ 2149
Cdd:PRK09510 143 AAAKAKAEAEAKRAAaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAE 222
|
170 180
....*....|....*....|....*....
gi 1717010358 2150 IKVAQEVAQQSAAAELNSKRMSFAEKTAQ 2178
Cdd:PRK09510 223 AKAAAAKAAAEAKAAAEKAAAAKAAEKAA 251
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1934-2159 |
4.80e-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: 61.79 E-value: 4.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQELQQLR 2013
Cdd:TIGR02794 78 EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA----EAEAERKAKEEAAKQAE 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2014 QNSDMEIKSKAKKieEAEYNRRKIEEEihivrlqletmQKQKASAEDelqelRARAEEAERQKKAAQEEAERlrrqvkdE 2093
Cdd:TIGR02794 154 EEAKAKAAAEAKK--KAEEAKKKAEAE-----------AKAKAEAEA-----KAKAEEAKAKAEAAKAKAAA-------E 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2094 SQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQ 2159
Cdd:TIGR02794 209 AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQ 274
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1937-2742 |
5.06e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 5.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1937 AAEKLKEEERRRLAEVEAQLEKQT--------------------QLAEAHAKAKAQAEKEAEELQRRMQEEVskrEVVAV 1996
Cdd:PRK04863 297 TSRRQLAAEQYRLVEMARELAELNeaesdleqdyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEQN---EVVEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1997 DAEQQkqtiqQELQQLRQNSDMEIKSKAKKIeeAEYNRRKIEEEIHIVRLQ-----LETMQKQKASAEDELQELRARAEE 2071
Cdd:PRK04863 374 ADEQQ-----EENEARAEAAEEEVDELKSQL--ADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEE 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2072 AERQKKAAQEEAERLRRQVKDESQKKREAEE--ELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAER----RMKQAEVE 2145
Cdd:PRK04863 447 FQAKEQEATEELLSLEQKLSVAQAAHSQFEQayQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2146 KERQikvaQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEK----- 2220
Cdd:PRK04863 527 QRLR----QQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRlaara 602
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2221 --WHQkANEAL-RLRLQAEE--------VAHKKTLAQEEAEKQKEDAEREARKRA-KAEESALRQKELAEDEleKQRKLA 2288
Cdd:PRK04863 603 paWLA-AQDALaRLREQSGEefedsqdvTEYMQQLLERERELTVERDELAARKQAlDEEIERLSQPGGSEDP--RLNALA 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2289 DataqqKFSAEQeLIRLKADT---ESGEQQRLLLEEELFRLKNEVNEAIQKRKKME---EELAKVRAEMEILLESKSRAE 2362
Cdd:PRK04863 680 E-----RFGGVL-LSEIYDDVsleDAPYFSALYGPARHAIVVPDLSDAAEQLAGLEdcpEDLYLIEGDPDSFDDSVFSVE 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2363 EESRSNTEKSKHMlEVEASKLRE--LAEEAARlRALSEEAKRQRQ-IAEG--EAARQRAEAERILK--EKLAAINEATRL 2435
Cdd:PRK04863 754 ELEKAVVVKIADR-QWRYSRFPEvpLFGRAAR-EKRIEQLRAEREeLAERyaTLSFDVQKLQRLHQafSRFIGSHLAVAF 831
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2436 KTEAEIALKEKEAE-NERLRRLAEDEAYqrkllEEQATQHKQDIEEKIILLkkssdNELERQKNIVEDTLRQRRIIEEEI 2514
Cdd:PRK04863 832 EADPEAELRQLNRRrVELERALADHESQ-----EQQQRSQLEQAKEGLSAL-----NRLLPRLNLLADETLADRVEEIRE 901
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2515 RIlklnfEKASSGKSDLELE---LNQLKNIA------EETHRSKEKAEQEAEKQRQL------ALEEEQRRKE--AEEKV 2577
Cdd:PRK04863 902 QL-----DEAEEAKRFVQQHgnaLAQLEPIVsvlqsdPEQFEQLKQDYQQAQQTQRDakqqafALTEVVQRRAhfSYEDA 976
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2578 RKILADEQEAARQRKAALEEVERLKAKAEEAKRQKElaekeaerqiqlAQEAAFKKIEAEEKAHAaivqQKEQEMLQTRK 2657
Cdd:PRK04863 977 AEMLAKNSDLNEKLRQRLEQAEQERTRAREQLRQAQ------------AQLAQYNQVLASLKSSY----DAKRQMLQELK 1040
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2658 QEksiLDKL----KEEAERAKRAAEDADYARMRAeqeaalSRQQVEEAErmKQRAEEEAQAKAQAQdeaeKLRKEAELEA 2733
Cdd:PRK04863 1041 QE---LQDLgvpaDSGAEERARARRDELHARLSA------NRSRRNQLE--KQLTFCEAEMDNLTK----KLRKLERDYH 1105
|
....*....
gi 1717010358 2734 AKRAHAEQA 2742
Cdd:PRK04863 1106 EMREQVVNA 1114
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2387-2760 |
5.18e-09 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 62.58 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2387 AEEAARLRALSEEAKRQRQIAEGEAARQraEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEayQRKL 2466
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQ--VTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERR--QKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2467 LEEQATQHKQD---IEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRilklnfEKASSGKSDLELELNQLKNIAE 2543
Cdd:pfam02029 80 QEALERQKEFDptiADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEE------ETEIREKEYQENKWSTEVRQAE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2544 EthrskekaEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLkaKAEEAKRQKELAEKEAERQI 2623
Cdd:pfam02029 154 E--------EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG--HPEVKSQNGEEEVTKLKVTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2624 QLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQeaalsRQQVEEAER 2703
Cdd:pfam02029 224 KRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKREER-----RKLLEEEEQ 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2704 mkQRAEEEAQAKAQAQDEAEKLRKEAEleaakRAHAEQAALKQKQLADEEMDKHKKF 2760
Cdd:pfam02029 299 --RRKQEEAERKLREEEEKRRMKEEIE-----RRRAEAAEKRQKLPEDSSSEGKKPF 348
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2766-3168 |
5.91e-09 |
|
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: 63.16 E-value: 5.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2766 RQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEvtdamRQKAQVEEELFKVKIQMEELIKLK-LRIEEENKMLIMK 2844
Cdd:TIGR02169 170 RKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE-----REKAERYQALLKEKREYEGYELLKeKEALERQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2845 DKDSTQKFLAEEAEKMRQVAEEAARLSIE-AQEAARMRKLAEDDlanQRALAEKMlkEKMQAIQEATRlKAEADMLQKQK 2923
Cdd:TIGR02169 245 QLASLEEELEKLTEEISELEKRLEEIEQLlEELNKKIKDLGEEE---QLRVKEKI--GELEAEIASLE-RSIAEKERELE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2924 ELAQEQarkfQEDKEQIEQQLAkETEGFQKSLEAERRQQLEITAEAERLKLqvlEMSKAQAKAEEDAKKFKkqaedfgnk 3003
Cdd:TIGR02169 319 DAEERL----AKLEAEIDKLLA-EIEELEREIEEERKRRDKLTEEYAELKE---ELEDLRAELEEVDKEFA--------- 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3004 lhqtelATKERMVvvqsleiqrqqsgkeaeELRRAIAELEHEKEKLKQEAELLQKNSQEMQvAQQEQLRQETQVLQttfl 3083
Cdd:TIGR02169 382 ------ETRDELK-----------------DYREKLEKLKREINELKRELDRLQEELQRLS-EELADLNAAIAGIE---- 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3084 tEKHLLLekekyiekekaklenlyEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQL 3163
Cdd:TIGR02169 434 -AKINEL-----------------EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEA 495
|
....*
gi 1717010358 3164 DKRRQ 3168
Cdd:TIGR02169 496 EAQAR 500
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1952-2178 |
6.05e-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: 61.40 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1952 VEAQLEKQTQLAEAHAKAKAQAEKEAeelqRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQnsDMEIKSKAKKIEEAe 2031
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAA----KKEQERQKKLEQQAEEAEKQRAAEQARQKELEQ--RAAAEKAAKQAEQA- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2032 ynrRKIEEEihivrlqletmqKQKASAEdelqelrARAEEAERQKKAAQEEAERlrrQVKDESQKKREAEEELKRKVQAE 2111
Cdd:TIGR02794 111 ---AKQAEE------------KQKQAEE-------AKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEAKAKAAAEAK 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2112 KDAAREKQRAMEDLQKfrsqAEEAERRMKQ--AEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ 2178
Cdd:TIGR02794 166 KKAEEAKKKAEAEAKA----KAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKAD 230
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2598-3074 |
6.89e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2598 VERLKAKAEEAKRQKELAEKEAERQIQlAQEAAFKKIEAEEKAHAAIVQQkeqemLQTRKQEKSILDKLKEEAERAKRAA 2677
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELK-ELEEELKEAEEKEEEYAELQEE-----LEELEEELEELEAELEELREELEKL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2678 EDADYARMRAEQEAALSRQQVEEAERMkQRAEEEAQAKAQAQDEAEKLRKEAEleaAKRAHAEQAALKQKQLADEEMDKH 2757
Cdd:COG4717 122 EKLLQLLPLYQELEALEAELAELPERL-EELEERLEELRELEEELEELEAELA---ELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2758 KKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLK-EEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEE 2836
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAlEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAG 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2837 ENKM---LIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAE---KMLKEKMQAIQEAT 2910
Cdd:COG4717 278 VLFLvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLellDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2911 RLKAEADMLQKQKELAQ-----------------EQARKFQEDKE---QIEQQLAKETEGFQKSLEAERRQQLEitAEAE 2970
Cdd:COG4717 358 ELEEELQLEELEQEIAAllaeagvedeeelraalEQAEEYQELKEeleELEEQLEELLGELEELLEALDEEELE--EELE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2971 RLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNklhQTELATKERmvvvqsleiqrqqsgkEAEELRRAIAELEHEKEKLK 3050
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEE---DGELAELLQ----------------ELEELKAELRELAEEWAALK 496
|
490 500
....*....|....*....|....
gi 1717010358 3051 QEAELLQKNSQEMQVAQQEQLRQE 3074
Cdd:COG4717 497 LALELLEEAREEYREERLPPVLER 520
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2554-3201 |
7.31e-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: 62.46 E-value: 7.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2554 QEAEKQRQLALEEEQRRKEAEEKVRKIladeQEAARQRKAALE----EVERLkAKAEEAKRqkelAEKEAERQIQLAQEA 2629
Cdd:pfam07111 59 QALSQQAELISRQLQELRRLEEEVRLL----RETSLQQKMRLEaqamELDAL-AVAEKAGQ----AEAEGLRAALAGAEM 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2630 AFKKIEAEEKAHAAIVQQKEQEMLQTRKQ-EKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRA 2708
Cdd:pfam07111 130 VRKNLEEGSQRELEEIQRLHQEQLSSLTQaHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKT 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2709 EEEAQAKAQAqdeAEKLRKEAELEAAKRAHAEQAALKQKQLadeeMDKHKKFAEKtlRQKAQVEQELTKVKLQleETDHQ 2788
Cdd:pfam07111 210 QEELEAQVTL---VESLRKYVGEQVPPEVHSQTWELERQEL----LDTMQHLQED--RADLQATVELLQVRVQ--SLTHM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2789 KTLLDdesqrlkEEVTDAMRQKAQVEEELFK-----VKIQMEELIKLKLRIEEENkmliMKDKDSTQKFLAeeaekmrQV 2863
Cdd:pfam07111 279 LALQE-------EELTRKIQPSDSLEPEFPKkcrslLNRWREKVFALMVQLKAQD----LEHRDSVKQLRG-------QV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2864 AEEAARLSIEAQEAARMrklaeddlanQRALAEKmlkekmQAIQEATRLKAEAdmLQKQKELAQEQARkfqedkeqieqq 2943
Cdd:pfam07111 341 AELQEQVTSQSQEQAIL----------QRALQDK------AAEVEVERMSAKG--LQMELSRAQEARR------------ 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2944 laketegfqksleaerRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKE------RMVV 3017
Cdd:pfam07111 391 ----------------RQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKvhtikgLMAR 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3018 VQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQE-----------AELLQKN---SQEMQVAQQEQLRQETQVLQTTFL 3083
Cdd:pfam07111 455 KVALAQLRQESCPPPPPAPPVDADLSLELEQLREErnrldaelqlsAHLIQQEvgrAREQGEAERQQLSEVAQQLEQELQ 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3084 TEKHLLLEKEKYIEKEKAKLENLYEDEVRKAQKLKQEQEHQLKQLEEE--------KQQL---KASMGEAMKKQKEAEES 3152
Cdd:pfam07111 535 RAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKvaevetrlREQLsdtKRRLNEARREQAKAVVS 614
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 3153 VRHKQDELHQLDKRRQE----QEKLLADENRKLREKLEQLEEEHRIALAQTRE 3201
Cdd:pfam07111 615 LRQIQHRATQEKERNQElrrlQDEARKEEGQRLARRVQELERDKNLMLATLQQ 667
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2077-2497 |
7.76e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.09 E-value: 7.76e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2077 KAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERqikVAQEV 2156
Cdd:COG4717 49 ERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEK---LEKLL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2157 AQQSAAAELNSKRMSFAEKTAQLElSLKQEHITVTHLQEEAERLKKQheeaekareeaekeLEKWHQKANEALRLRLQAE 2236
Cdd:COG4717 126 QLLPLYQELEALEAELAELPERLE-ELEERLEELRELEEELEELEAE--------------LAELQEELEELLEQLSLAT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2237 EVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQK-ELAEDELE---KQRKLADATAQQKFSAEQELIRLKADTESG 2312
Cdd:COG4717 191 EEELQDLAEELEELQQRLAELEEELEEAQEELEELEEElEQLENELEaaaLEERLKEARLLLLIAAALLALLGLGGSLLS 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2313 EQQRLL------------LEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEA 2380
Cdd:COG4717 271 LILTIAgvlflvlgllalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQ 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2381 SKLRELAEEAARLRALSEEAKRQRQIAEG--------EAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENER 2452
Cdd:COG4717 351 ELLREAEELEEELQLEELEQEIAALLAEAgvedeeelRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEEL 430
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1717010358 2453 LRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQK 2497
Cdd:COG4717 431 EEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELL 475
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2753-3190 |
8.69e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.39 E-value: 8.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2753 EMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKaqveEELFKVKIQMEELIKLKL 2832
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2833 RIEEENKMLIMKDKDsTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLaeddlanqRALAEKMLKEKMQAIQEATRL 2912
Cdd:PRK03918 249 SLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEYIKL--------SEFYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2913 KAEADMLQKQKELAQEQARKFQEDKEQIEQqLAKETEGFQKSLEA-ERRQQLEITAEAERLKLQVLEMSKAQAKAEEdAK 2991
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKE-LEKRLEELEERHELyEEAKAKKEELERLKKRLTGLTPEKLEKELEE-LE 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2992 KFKKQAED----FGNKLHQTELATKERMVVVQSL------------EIQRQQSGKEAEELRRAIAELEHEKEKLKQEAEL 3055
Cdd:PRK03918 398 KAKEEIEEeiskITARIGELKKEIKELKKAIEELkkakgkcpvcgrELTEEHRKELLEEYTAELKRIEKELKEIEEKERK 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3056 LQKNSQ--EMQVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEKAKLENLYE-------------DEVRKAQKLKQE 3120
Cdd:PRK03918 478 LRKELRelEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEkliklkgeikslkKELEKLEELKKK 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3121 Q---EHQLKQLEEEKQQLKASMGE------------------AMKKQKEAEESVRHKQDELHQLDKRRQEQEKL---LAD 3176
Cdd:PRK03918 558 LaelEKKLDELEEELAELLKELEElgfesveeleerlkelepFYNEYLELKDAEKELEREEKELKKLEEELDKAfeeLAE 637
|
490
....*....|....
gi 1717010358 3177 ENRKLREKLEQLEE 3190
Cdd:PRK03918 638 TEKRLEELRKELEE 651
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1974-2675 |
8.87e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 62.24 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1974 EKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQELQQLRQnsdmeIKSKAKKIEEAEYNRRKIEEEIHIVRLQLetmqk 2053
Cdd:COG4913 220 EPDTFEAADALVEHFDDLE----RAHEALEDAREQIELLEP-----IRELAERYAAARERLAELEYLRAALRLWF----- 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2054 qkasAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELkrkvqaekdaAREKQRAMEDLQKFRSQAE 2133
Cdd:COG4913 286 ----AQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI----------RGNGGDRLEQLEREIERLE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2134 EAERRMKQaevekerqikvaqevaqqsaaaelnsKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQheeaekaree 2213
Cdd:COG4913 352 RELEERER--------------------------RRARLEALLAALGLPLPASAEEFAALRAEAAALLEA---------- 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2214 aekeLEKWHQKANEALRLRLQAeevahKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDelekqrkLADATAQ 2293
Cdd:COG4913 396 ----LEEELEALEEALAEAEAA-----LRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEA-------LGLDEAE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2294 QKFSAeqELIRLKADTES--------------------GEQqrllleeelfrlkNEVNEAIQkRKKMEEEL--AKVRAEm 2351
Cdd:COG4913 460 LPFVG--ELIEVRPEEERwrgaiervlggfaltllvppEHY-------------AAALRWVN-RLHLRGRLvyERVRTG- 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2352 eilLESKSRAEEESRSNTEKskhmLEVEASKLR-----ELAEEAARLRALSEEA-----------------------KRQ 2403
Cdd:COG4913 523 ---LPDPERPRLDPDSLAGK----LDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgngtrhekDDR 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2404 RQIAE-----GEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLleEQATQHKQDI 2478
Cdd:COG4913 596 RRIRSryvlgFDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDV--ASAEREIAEL 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2479 EEKIILLKKSSD--NELERQKNIVEDTLRQrriieeeiriLKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEA 2556
Cdd:COG4913 674 EAELERLDASSDdlAALEEQLEELEAELEE----------LEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLA 743
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2557 EKQRQLALEE---EQRRKEAEEKVRKILADEQEAARQRKAALEevERLKAKAEEAKRQKELAEKEAERQIQLAQE--AAF 2631
Cdd:COG4913 744 RLELRALLEErfaAALGDAVERELRENLEERIDALRARLNRAE--EELERAMRAFNREWPAETADLDADLESLPEylALL 821
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1717010358 2632 KKIEAEEKAHAaivQQKEQEMLQTRKQEK--SILDKLKEEAERAKR 2675
Cdd:COG4913 822 DRLEEDGLPEY---EERFKELLNENSIEFvaDLLSKLRRAIREIKE 864
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1976-2844 |
9.77e-09 |
|
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: 62.06 E-value: 9.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1976 EAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHivrlqleTMQKQK 2055
Cdd:pfam15921 86 QVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVH-------ELEAAK 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2056 ASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDesqkkreAEEELKRKVQaekdaareKQRAMEDLQkFRSQAEEA 2135
Cdd:pfam15921 159 CLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVD-------FEEASGKKIY--------EHDSMSTMH-FRSLGSAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2136 ERRMKQAEVEKERQIKVAQEVAQQSAAAElnskrmsfAEKTAQLELSLKQEhitvthlQEEAERLKKQHeeaekareeaE 2215
Cdd:pfam15921 223 SKILRELDTEISYLKGRIFPVEDQLEALK--------SESQNKIELLLQQH-------QDRIEQLISEH----------E 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2216 KELEKWHQKANEAlrlRLQAEEVAHKKTLAQEEAEKQK-------EDAEREARKRAKAEESALRQKELAEDELEKQRKLA 2288
Cdd:pfam15921 278 VEITGLTEKASSA---RSQANSIQSQLEIIQEQARNQNsmymrqlSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2289 DATAqqkfsAEQELIRLKADTESGeqqrllleeelfrlknEVNEAIQkrkKMEEELAKVRAEMEILLESKSRAEEESRSN 2368
Cdd:pfam15921 355 NSEL-----TEARTERDQFSQESG----------------NLDDQLQ---KLLADLHKREKELSLEKEQNKRLWDRDTGN 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2369 TEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQ--RQIAEGEAARQRAEAERILKEKLAAINEATRlKTEAEIALKEK 2446
Cdd:pfam15921 411 SITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQmeRQMAAIQGKNESLEKVSSLTAQLESTKEMLR-KVVEELTAKKM 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2447 EAENERLRRLAEDEAYQRKLLEEQATQhkqdieEKIILLKKSSD---NELERQKNiVEDTLRQRRIIEEEirilkLNFEK 2523
Cdd:pfam15921 490 TLESSERTVSDLTASLQEKERAIEATN------AEITKLRSRVDlklQELQHLKN-EGDHLRNVQTECEA-----LKLQM 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2524 ASSGKSdLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEkvRKILADEQEAA-RQRKAALEEVERLK 2602
Cdd:pfam15921 558 AEKDKV-IEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQE--FKILKDKKDAKiRELEARVSDLELEK 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2603 AKAEEAKRQKELAEKEaerqiqlaqeaafkkieaeekahaaiVQQKEQEMLQTRKQEKSILDKLKEEAERAKRaaedaDY 2682
Cdd:pfam15921 635 VKLVNAGSERLRAVKD--------------------------IKQERDQLLNEVKTSRNELNSLSEDYEVLKR-----NF 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2683 ARMRAEQEAALSRQQVE------EAERMKQRAEEEAQAKAQAQDEAEKLRKEAeleAAKRAHAEqaALKQK-QLADEEMD 2755
Cdd:pfam15921 684 RNKSEEMETTTNKLKMQlksaqsELEQTRNTLKSMEGSDGHAMKVAMGMQKQI---TAKRGQID--ALQSKiQFLEEAMT 758
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2756 KHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDamrqkaqVEEELFKVKIQMEELIKLKLRIE 2835
Cdd:pfam15921 759 NANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVAN-------MEVALDKASLQFAECQDIIQRQE 831
|
....*....
gi 1717010358 2836 EENKMLIMK 2844
Cdd:pfam15921 832 QESVRLKLQ 840
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2628-2999 |
9.80e-09 |
|
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: 62.39 E-value: 9.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2628 EAAFKKIEAEEKaHAAIVQQKEQEMLQTrkqeksiLDKLKEEAERAKRAAEDADYARmraEQEAALSRQQVEEAERMKQR 2707
Cdd:TIGR02169 173 EKALEELEEVEE-NIERLDLIIDEKRQQ-------LERLRREREKAERYQALLKEKR---EYEGYELLKEKEALERQKEA 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2708 AEEEAQAKAQAQDEAEKLRKEAELE-AAKRAHAEQAALKQKQLADEEMdkhkkfaektlrqkAQVEQELTKVKLQLEetd 2786
Cdd:TIGR02169 242 IERQLASLEEELEKLTEEISELEKRlEEIEQLLEELNKKIKDLGEEEQ--------------LRVKEKIGELEAEIA--- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2787 hqktLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEElikLKLRIEEENKMLImKDKDSTQKFLAEEAEKMRQVAEE 2866
Cdd:TIGR02169 305 ----SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRD-KLTEEYAELKEELEDLRAELEEV 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2867 AARLSIEAQEAARMRKLAED---DLANQRALAEKMLKEKMQAIQEATRLKAE-ADMLQKQKELAQ--EQARKFQEDKEQI 2940
Cdd:TIGR02169 377 DKEFAETRDELKDYREKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAiAGIEAKINELEEekEDKALEIKKQEWK 456
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2941 EQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQvLEMSKAQAKAEEDAKKFKKQAED 2999
Cdd:TIGR02169 457 LEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRE-LAEAEAQARASEERVRGGRAVEE 514
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4977-5015 |
9.88e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 53.87 E-value: 9.88e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 4977 FLEVQYLTGGLIEPDLPTRVNLDEALRKGTIDARTAQKL 5015
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1935-2163 |
1.09e-08 |
|
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: 60.63 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1935 EKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRmqeevskrevvavdAEQQKQTIQQELQQLRQ 2014
Cdd:TIGR02794 58 QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ--------------AEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2015 NSDMEIKSKAKKiEEAEYNRRKIEEeihiVRLQLETMQKQKASAEDelqelRARAEEAERQKKAAQEEAERLRRQVKDES 2094
Cdd:TIGR02794 124 AKAKQAAEAKAK-AEAEAERKAKEE----AAKQAEEEAKAKAAAEA-----KKKAEEAKKKAEAEAKAKAEAEAKAKAEE 193
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2095 QKKREAEEELKRKVQAEKDAAREKQRAmedlqkfrsQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAA 2163
Cdd:TIGR02794 194 AKAKAEAAKAKAAAEAAAKAEAEAAAA---------AAAEAERKADEAELGDIFGLASGSNAEKQGGAR 253
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1955-2163 |
1.14e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1955 QLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKrevvaVDAEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAeynr 2034
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQER-----LKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2035 rkieeeihivrlQLETMQKQKASAEDELQELRARAEEAERQKKA-AQEEAErlrRQVKDESQKKREAEEELKRKVQAEKD 2113
Cdd:PRK09510 138 ------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKkAEAEAA---KKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2114 AAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAA 2163
Cdd:PRK09510 203 AEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAA 252
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2832-3191 |
1.14e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.28 E-value: 1.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2832 LRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLA---NQRALAEKM------LKEK 2902
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqTALRQQEKIeryqadLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2903 MQAIQEATRLKAEADmlqKQKELAQEQARKFQEDKEQIEQQLAKETEGF--QKSLEAERRQQLEITAEAERL-KLQVLEM 2979
Cdd:PRK04863 361 EERLEEQNEVVEEAD---EQQEENEARAEAAEEEVDELKSQLADYQQALdvQQTRAIQYQQAVQALERAKQLcGLPDLTA 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2980 SKAQAKAEEdakkFKKQAEDFGNKLHQTEL------ATKERMVVVQSL------EIQRQQSGKEAEELRRAIAELEHEKE 3047
Cdd:PRK04863 438 DNAEDWLEE----FQAKEQEATEELLSLEQklsvaqAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3048 KLKQ-EAEL--LQKNSQEMQvAQQEQLRQETQVLQTTFLTEKHLllekEKYIEKEKAKLENLyEDEVRKAQKLKQEQEHQ 3124
Cdd:PRK04863 514 QLQQlRMRLseLEQRLRQQQ-RAERLLAEFCKRLGKNLDDEDEL----EQLQEELEARLESL-SESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 3125 LKQLEEEKQQLKASMGEAMKKQKEAE-------ESVRHKQDeLHQLDKRRQEQEKLLADENRKLREKLEQLEEE 3191
Cdd:PRK04863 588 LEQLQARIQRLAARAPAWLAAQDALArlreqsgEEFEDSQD-VTEYMQQLLERERELTVERDELAARKQALDEE 660
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1946-2121 |
1.20e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 61.04 E-value: 1.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1946 RRRLAEVEAQLEKQTQLAEAHA-KAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQnsdmEIKSKA 2024
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETA----RAEAEA 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2025 kKIEEAEYNRRK-IEEEIHIVRLQLETmQKQKASAEDELQELRA---RAEEAERQKKAAQEEAErlrrqvKDESQKKREA 2100
Cdd:COG2268 267 -AYEIAEANAEReVQRQLEIAEREREI-ELQEKEAEREEAELEAdvrKPAEAEKQAAEAEAEAE------AEAIRAKGLA 338
|
170 180
....*....|....*....|....*
gi 1717010358 2101 EEE-LKRKVQAEK---DAAREKQRA 2121
Cdd:COG2268 339 EAEgKRALAEAWNklgDAAILLMLI 363
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1688-2180 |
1.38e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.59 E-value: 1.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1688 AEEVVKTYEDQLKEVHAVPSDSKELEATKAELKK----LRSQVEGHQPLFNTLEADLNKAKDvneqmlrshserDVDLDR 1763
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERereeLAEEVRDLRERLEELEEERDDLLA------------EAGLDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1764 Y-RERVQQLLERWQAILVQIdlrQRELDQLGRQLRYYRETYDWLIKWIKDAKQRQEQIQSVPITDSKTmkeqllqlkkll 1842
Cdd:PRK02224 307 AdAEAVEARREELEDRDEEL---RDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESE------------ 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1843 eeIESNRTKVDECQkyakqyiDAIKDYELQLVTYKAQVEPvvSPAKKPKVQSTSDSIIQEYVDLRTRYSELTTltsqyik 1922
Cdd:PRK02224 372 --LEEAREAVEDRR-------EEIEELEEEIEELRERFGD--APVDLGNAEDFLEELREERDELREREAELEA------- 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1923 fiteTLcrlnveekaaeklkEEERRRLAEVEAQLEK-------QTQLAEAHAKAKAQAEKEAEELQRRMQeevskrevva 1995
Cdd:PRK02224 434 ----TL--------------RTARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELE---------- 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1996 vDAEQQKQTIQQELQQLRqnsdmEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQ 2075
Cdd:PRK02224 486 -DLEEEVEEVEERLERAE-----DLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA 559
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2076 KKAAQEEAERLRRQVKDESQKKREAEEELKR--KVQAEKDAAREKQRAMEDLQKFRSQAEEA--ERRMKQAEvEKERQIK 2151
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAELKERIESleRIRTLLAAIADAEDEIERLREKREALAELndERRERLAE-KRERKRE 638
|
490 500
....*....|....*....|....*....
gi 1717010358 2152 VAQEVaQQSAAAELNSKRMSFAEKTAQLE 2180
Cdd:PRK02224 639 LEAEF-DEARIEEAREDKERAEEYLEQVE 666
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2336-2748 |
1.43e-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: 1.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2336 KRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQR 2415
Cdd:NF033838 108 KEKSEAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2416 AEAERILKEKLAAINEATRLKTEAEIalKEKEAENERLRRLAEDeayqRKLLEEQAtQHKQDIEEKIILLKKSSDNELER 2495
Cdd:NF033838 188 AELELVKEEAKEPRDEEKIKQAKAKV--ESKKAEATRLEKIKTD----REKAEEEA-KRRADAKLKEAVEKNVATSEQDK 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2496 QKNIVedtlRQRRIIEEEIRILKLNFEKASSgksdlelelnqlKNIAEETHRSKekaeqeaekqrqlALEEEQRRKEAEE 2575
Cdd:NF033838 261 PKRRA----KRGVLGEPATPDKKENDAKSSD------------SSVGEETLPSP-------------SLKPEKKVAEAEK 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2576 KVrkiladeQEAARQRKAALEEVERLKAKAEEAKRQKELAE-----KEAErqIQLAQEAAfKKIEAEEKAHAAIVQQKEQ 2650
Cdd:NF033838 312 KV-------EEAKKKAKDQKEEDRRNYPTNTYKTLELEIAEsdvkvKEAE--LELVKEEA-KEPRNEEKIKQAKAKVESK 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2651 EMLQTRkQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVE-EAERMKQRAEeeaQAKAQAQDEaeklrKEA 2729
Cdd:NF033838 382 KAEATR-LEKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEkPAPKPEKPAE---QPKAEKPAD-----QQA 452
|
410
....*....|....*....
gi 1717010358 2730 ELEAAKRAHAEQAALKQKQ 2748
Cdd:NF033838 453 EEDYARRSEEEYNRLTQQQ 471
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
750-852 |
1.52e-08 |
|
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: 55.85 E-value: 1.52e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 750 TAKEKLLLWSQRMTESyqgLRCDNFTTSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFNVAERDLGVTRLLD 828
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPgLCPDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 1717010358 829 PEDVDVPQPDEKSIITYVSSLYDA 852
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1948-2121 |
1.56e-08 |
|
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: 58.78 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1948 RLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQELQQLRQNsdmeIKSKAKKI 2027
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELE----DLEKEIKRLELEIEEVEAR----IKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2028 EEAEYNRrkieeEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRK 2107
Cdd:COG1579 83 GNVRNNK-----EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAE 157
|
170
....*....|....
gi 1717010358 2108 vQAEKDAAREKQRA 2121
Cdd:COG1579 158 -LEELEAEREELAA 170
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2543-2722 |
1.72e-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: 1.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2543 EETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKilaDEQEAARQRKAALEEVERLKAKAEEAK---RQKELAEKEA 2619
Cdd:pfam15709 357 QEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERKQRLQLQAAQERarqQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2620 ERQIQLAQEAAfKKIEAEEKahaaivQQKEQEMlqtrkqeksildKLKEEAERAKRAAEDADYARMRAEQEAALSRQQve 2699
Cdd:pfam15709 434 ELQRKKQQEEA-ERAEAEKQ------RQKELEM------------QLAEEQKRLMEMAEEERLEYQRQKQEAEEKARL-- 492
|
170 180
....*....|....*....|....*...
gi 1717010358 2700 EAERMKQRAEEEA-----QAKAQAQDEA 2722
Cdd:pfam15709 493 EAEERRQKEEEAArlaleEAMKQAQEQA 520
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1911-2294 |
1.74e-08 |
|
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: 61.52 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1911 SELTTLTSQYIKFITETLCR--LNVEEKAAEKLKEEERRRLAEVEAQLEKQTQ---LAEAHAKAKAQAEKEAEEL----- 1980
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFrdLQGQLAHAKKQQELQQRYAELCAAAITCTAQcekLEKIHLQESAQSLKEREQQlqtke 479
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1981 QRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDM----EIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKA 2056
Cdd:TIGR00618 480 QIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRA 559
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2057 SAEDELQELRARAEEAERQKKAAQEEAERLRrQVKDESQKKREAEEELKRKVQAEKDA-AREKQRAMEDLQKFRSQAEEA 2135
Cdd:TIGR00618 560 SLKEQMQEIQQSFSILTQCDNRSKEDIPNLQ-NITVRLQDLTEKLSEAEDMLACEQHAlLRKLQPEQDLQDVRLHLQQCS 638
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2136 ERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLElSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAE 2215
Cdd:TIGR00618 639 QELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQ-KMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYD 717
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2216 KELEKWhQKANEALRLRLQAEEVAHKKTLAQEEAE-----KQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADA 2290
Cdd:TIGR00618 718 REFNEI-ENASSSLGSDLAAREDALNQSLKELMHQartvlKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREE 796
|
....
gi 1717010358 2291 TAQQ 2294
Cdd:TIGR00618 797 DTHL 800
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2552-2775 |
1.77e-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: 1.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2552 AEQEAEKQRQLALEEEQRRKEAEEKVRkiladeQEAARQRKAALEEVERLKAKAEEAKRQkelaEKEAERQIQLAQEAAF 2631
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKEL------AALKKEEKALLKQLAALERRIAALARR----IRALEQELAALEAELA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2632 KKIEAEEKAHAAIVQQKEQEMLQTRKQEKS-------ILDKLKEEAERAKRAAEDADYARMRAEQEAALsRQQVEEAERM 2704
Cdd:COG4942 87 ELEKEIAELRAELEAQKEELAELLRALYRLgrqpplaLLLSPEDFLDAVRRLQYLKYLAPARREQAEEL-RADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2705 KQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQEL 2775
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1711-2600 |
1.87e-08 |
|
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: 61.24 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1711 ELEATKAELKKLRSQVEghqplfntlEADLnKAKDVNEQMLRSHSERDvDLDRYRE--------RVQQLLERWQAILVQI 1782
Cdd:TIGR02169 171 KKEKALEELEEVEENIE---------RLDL-IIDEKRQQLERLRRERE-KAERYQAllkekreyEGYELLKEKEALERQK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1783 DLRQRELDQLGRQLRYYRETYDWLIKWIKDAKQRQEQI-QSVPITDSKTMKEQLLQLKKLLEEIESNRTKVDECQKYAKQ 1861
Cdd:TIGR02169 240 EAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELnKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1862 YIDAIKDYELQLVTYKAQVEPVVSPAKKPKVQStsDSIIQEYVDLRTRYSELTTLTSQYIKFITETLCRLNVEEKAAEKL 1941
Cdd:TIGR02169 320 AEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1942 KEE------ERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavdaeqqkqtiqQELQQLRQn 2015
Cdd:TIGR02169 398 KREinelkrELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQE--------------WKLEQLAA- 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2016 sDMEIKSKAKKIEEAEYnrRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAE-----------------EAERQKKA 2078
Cdd:TIGR02169 463 -DLSKYEQELYDLKEEY--DRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgtvaqlgSVGERYAT 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2079 AQEEAERLRRQ---VKDESQKKrEAEEELKRK---------VQAEKDAAREKQRAMEDL------------QKFRS---- 2130
Cdd:TIGR02169 540 AIEVAAGNRLNnvvVEDDAVAK-EAIELLKRRkagratflpLNKMRDERRDLSILSEDGvigfavdlvefdPKYEPafky 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2131 ---------QAEEAERRMKQAevekeRQIKVAQEVAQQSAAAELNSKRMSFAEKTAqlelslKQEHITVTHLQEEAERLK 2201
Cdd:TIGR02169 619 vfgdtlvveDIEAARRLMGKY-----RMVTLEGELFEKSGAMTGGSRAPRGGILFS------RSEPAELQRLRERLEGLK 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2202 KQheeaekaREEAEKELEKWHQKANEALRLRlqaeEVAHKKTlaqEEAEKQKEDAEREARKRAKaeesalRQKELAEDEL 2281
Cdd:TIGR02169 688 RE-------LSSLQSELRRIENRLDELSQEL----SDASRKI---GEIEKEIEQLEQEEEKLKE------RLEELEEDLS 747
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2282 EKQRKLADataqqkfsAEQELIRLKADTEsgeqqrllleeELFRLKNEVNEAIQ--KRKKMEEELAKVRAEMEILLESKS 2359
Cdd:TIGR02169 748 SLEQEIEN--------VKSELKELEARIE-----------ELEEDLHKLEEALNdlEARLSHSRIPEIQAELSKLEEEVS 808
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2360 RAEEESRSnTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRqiaegeaaRQRAEAERILKEKLAAINEatrlktEA 2439
Cdd:TIGR02169 809 RIEARLRE-IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSI--------EKEIENLNGKKEELEEELE------EL 873
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2440 EIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEkiillKKSSDNELERQKNIVEDTLRQ---RRIIEEEIRI 2516
Cdd:TIGR02169 874 EAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEK-----KRKRLSELKAKLEALEEELSEiedPKGEDEEIPE 948
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2517 LKLNFEKASSGKSDLELELNQLKNIaeethrsKEKAEQEAEkqrqlalEEEQRRKEAEEKvRKILADEQEAARQRKAALE 2596
Cdd:TIGR02169 949 EELSLEDVQAELQRVEEEIRALEPV-------NMLAIQEYE-------EVLKRLDELKEK-RAKLEEERKAILERIEEYE 1013
|
....
gi 1717010358 2597 EVER 2600
Cdd:TIGR02169 1014 KKKR 1017
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
2521-3151 |
1.92e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 61.35 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2521 FEKASSGKSDLELELNQLKNIA---EETHRSKEKAEQ--EAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAAl 2595
Cdd:PRK10246 190 FEQHKSARTELEKLQAQASGVAlltPEQVQSLTASLQvlTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQQ- 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2596 eeverlkAKAEEAKRQKELAekeaerQIQLAQEAAfkkieaEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKR 2675
Cdd:PRK10246 269 -------ALAAEEKAQPQLA------ALSLAQPAR------QLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRAR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2676 AAEDAdyARMRAEQEAALSR--QQVEEAERMK--------------QRAEEEAQAKAQAQDEAEKLRKEA---------- 2729
Cdd:PRK10246 330 IRHHA--AKQSAELQAQQQSlnTWLAEHDRFRqwnnelagwraqfsQQTSDREQLRQWQQQLTHAEQKLNalpaitltlt 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2730 --ELEAAKRAHAEQAALKQKQLAdeemdKHKKFAEKTLRQK------AQVEQELTKVKLQLEETDHQKTLLDDESQRLK- 2800
Cdd:PRK10246 408 adEVAAALAQHAEQRPLRQRLVA-----LHGQIVPQQKRLAqlqvaiQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKt 482
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2801 -----EEVTDAMRQKAQVEE---------------------ELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLA 2854
Cdd:PRK10246 483 iceqeARIKDLEAQRAQLQAgqpcplcgstshpaveayqalEPGVNQSRLDALEKEVKKLGEEGAALRGQLDALTKQLQR 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2855 EEAEKMRQVAEEAArLSIEAQE---AARMRKLAEDDLANQraLAEKMLKEKmQAIQEATRLkaeadMLQKQKELAQEQAR 2931
Cdd:PRK10246 563 DESEAQSLRQEEQA-LTQQWQAvcaSLNITLQPQDDIQPW--LDAQEEHER-QLRLLSQRH-----ELQGQIAAHNQQII 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2932 KFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLK--------LQVLEMSKAQAKA--------EEDAKKFKK 2995
Cdd:PRK10246 634 QYQQQIEQRQQQLLTALAGYALTLPQEDEEASWLATRQQEAQswqqrqneLTALQNRIQQLTPlletlpqsDDLPHSEET 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2996 QAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEEL----------------------RRAIAELEHEKEKLKQEA 3053
Cdd:PRK10246 714 VALDNWRQVHEQCLSLHSQLQTLQQQDVLEAQRLQKAQAQfdtalqasvfddqqaflaalldEETLTQLEQLKQNLENQR 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3054 ELLQKNSQEMQVAQQEQLRQETQVLQTTfLTEKHLllekekyIEKEKAKLENLYEDEVRKAqklkqEQEHQLKQLEEEKQ 3133
Cdd:PRK10246 794 QQAQTLVTQTAQALAQHQQHRPDGLDLT-VTVEQI-------QQELAQLAQQLRENTTRQG-----EIRQQLKQDADNRQ 860
|
730
....*....|....*...
gi 1717010358 3134 QLKASMGEAMKKQKEAEE 3151
Cdd:PRK10246 861 QQQALMQQIAQATQQVED 878
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2453-2887 |
2.17e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 2.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2453 LRRLAEDEAyQRKLLEEQATQHKQDIEEKiillkkssdNELERQKNIVEDTLRQRRIIEEEIRILKLNFEkASSGKSDLE 2532
Cdd:COG4717 70 LKELKELEE-ELKEAEEKEEEYAELQEEL---------EELEEELEELEAELEELREELEKLEKLLQLLP-LYQELEALE 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2533 LELN-----------QLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERL 2601
Cdd:COG4717 139 AELAelperleeleeRLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2602 KAKAEEAKRQKELAEKEAERQI---QLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSIL------------DKL 2666
Cdd:COG4717 219 QEELEELEEELEQLENELEAAAleeRLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLgllallflllarEKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2667 KEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAE--EEAQAKAQAQDEAEKLRKEAELEaakRAHAEQAAL 2744
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLEllDRIEELQELLREAEELEEELQLE---ELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2745 KQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELfkvKIQM 2824
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL---EELR 452
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2825 EELIKLKLRIEEenkmliMKDKDSTQKFLAEEAE---KMRQVAEEAARLSIEAQEAARMRKLAEDD 2887
Cdd:COG4717 453 EELAELEAELEQ------LEEDGELAELLQELEElkaELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
614-737 |
2.21e-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: 55.78 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 614 PAVGVSEMEDPTPAEDERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRM 686
Cdd:cd21331 2 PALTKPENQDIDWTLLEGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGA 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 687 RFHKLQNVQIALDYLKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 737
Cdd:cd21331 80 NMKKLENCNYAVELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1939-2804 |
2.29e-08 |
|
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: 60.90 E-value: 2.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1939 EKLKEEERRRLAEVEAQLEKQTQLaeaHAKAKAQAEKEAEELQRRMQEEVSKREVVAvDAEQQKQTIQQELQQLRQNSdm 2018
Cdd:pfam15921 77 ERVLEEYSHQVKDLQRRLNESNEL---HEKQKFYLRQSVIDLQTKLQEMQMERDAMA-DIRRRESQSQEDLRNQLQNT-- 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2019 eikskakkIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRA---RAEEAERQKKAAQEEAERLrrqvkdESQ 2095
Cdd:pfam15921 151 --------VHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSilvDFEEASGKKIYEHDSMSTM------HFR 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2096 KKREAEEELKRKVQAEKDAAREKQRAMED-LQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAE 2174
Cdd:pfam15921 217 SLGSAISKILRELDTEISYLKGRIFPVEDqLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANS 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2175 KTAQLELslkqehitvthLQEEAerlKKQHEEAEKAREEAEKELEKWHQKANEALRL-RLQAEEVAHKKTLAQEEAEKQk 2253
Cdd:pfam15921 297 IQSQLEI-----------IQEQA---RNQNSMYMRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSELTEA- 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2254 edaeREARKRAKAEESALrqkelaEDELekQRKLADATAQQK-FSAEQELIRLKADTESGEQQRLLLEeelfrlKNEVNE 2332
Cdd:pfam15921 362 ----RTERDQFSQESGNL------DDQL--QKLLADLHKREKeLSLEKEQNKRLWDRDTGNSITIDHL------RRELDD 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2333 AIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHM---LEVEASKLRELAEEAARLRALSEEAkrQRQIAEG 2409
Cdd:pfam15921 424 RNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLtaqLESTKEMLRKVVEELTAKKMTLESS--ERTVSDL 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2410 EAARQraEAERILKeklAAINEATRLKTEAEIALKEKE---AENERLRRL-AEDEAYQRKLLEEQATQH--KQDIEEKII 2483
Cdd:pfam15921 502 TASLQ--EKERAIE---ATNAEITKLRSRVDLKLQELQhlkNEGDHLRNVqTECEALKLQMAEKDKVIEilRQQIENMTQ 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2484 LLKK--SSDNELERQKNIVEDTLRQRRIIEEEIRILK----LNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAE 2557
Cdd:pfam15921 577 LVGQhgRTAGAMQVEKAQLEKEINDRRLELQEFKILKdkkdAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERD 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2558 kqrQLALEEEQRRKEaeekVRKILADEQEAARQRKAALEEVERLKAKAeeaKRQKELAEKEAERQiqlaqEAAFKKIEAE 2637
Cdd:pfam15921 657 ---QLLNEVKTSRNE----LNSLSEDYEVLKRNFRNKSEEMETTTNKL---KMQLKSAQSELEQT-----RNTLKSMEGS 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2638 EkAHAAIVQQKEQEMLQTRKQEksiLDKLKEEAERAKRAAEDADYARMRAEqeaalsrqqvEEAERMKQRAEEEAQAKAQ 2717
Cdd:pfam15921 722 D-GHAMKVAMGMQKQITAKRGQ---IDALQSKIQFLEEAMTNANKEKHFLK----------EEKNKLSQELSTVATEKNK 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2718 AQDEAEKLRKEaeleaakrahaeqaalkqkqladeemdkhkkfaEKTLRQK-AQVEQELTKVKLQLEETDHQKTLLDDES 2796
Cdd:pfam15921 788 MAGELEVLRSQ---------------------------------ERRLKEKvANMEVALDKASLQFAECQDIIQRQEQES 834
|
....*...
gi 1717010358 2797 QRLKEEVT 2804
Cdd:pfam15921 835 VRLKLQHT 842
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2016-2203 |
2.41e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.84 E-value: 2.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2016 SDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKD--- 2092
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2093 ESQKKREAE------------EELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEaerrmKQAEVEKERQIKVAQEVAQQS 2160
Cdd:COG3883 94 ALYRSGGSVsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEA-----KKAELEAKLAELEALKAELEA 168
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1717010358 2161 AAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQ 2203
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAA 211
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4899-4936 |
2.47e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 52.48 E-value: 2.47e-08
10 20 30
....*....|....*....|....*....|....*...
gi 1717010358 4899 QRLLEAQACTGGIIDINTGQKFSVTDAVNKGLVDKIMV 4936
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2737-2974 |
2.77e-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: 2.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2737 AHAEQAALKQKQLAD--EEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVE 2814
Cdd:COG4942 17 AQADAAAEAEAELEQlqQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2815 EELFKVKIQMEELIKLKLRIEEENK-MLIMKDKDSTQkfLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRA 2893
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPlALLLSPEDFLD--AVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2894 LAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLK 2973
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
.
gi 1717010358 2974 L 2974
Cdd:COG4942 255 L 255
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
745-847 |
3.17e-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: 54.79 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 745 QSEDMTAKEKLLLWSQRMTESyqgLRCDNFTTSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFNVAERDLGV 823
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPgLCPDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 1717010358 824 TRLLDPEDVDVPQPDEKSIITYVS 847
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2597-3183 |
3.28e-08 |
|
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: 60.14 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2597 EVERLKAKAEEAKRQKELAEKEAERQIqlaqeaafkkIEAEEKAHAAIVQQKEqemlqTRKQEKSILDKLKEEAERAKRA 2676
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRAR----------IELEKKASALKRQLDR-----ESDRNQELQKRIRLLEKREAEA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2677 AEdadyaRMRAEQEAALSRQQVEEAerMKQRAEEEAQAKAQAQDEAEKLRKEAElEAAKRAHAEQAALKQKQLADEEMDK 2756
Cdd:pfam05557 68 EE-----ALREQAELNRLKKKYLEA--LNKKLNEKESQLADAREVISCLKNELS-ELRRQIQRAELELQSTNSELEELQE 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2757 HKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDE--SQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKlKLRI 2834
Cdd:pfam05557 140 RLDLLKAKASEAEQLRQNLEKQQSSLAEAEQRIKELEFEiqSQEQDSEIVKNSKSELARIPELEKELERLREHNK-HLNE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2835 EEENKMLIMKDKDSTQKFLaEEAEKMRqvaEEAARLSIE----AQEAARMRKLAEDDLANQR---ALAEK---MLKEKMQ 2904
Cdd:pfam05557 219 NIENKLLLKEEVEDLKRKL-EREEKYR---EEAATLELEkeklEQELQSWVKLAQDTGLNLRspeDLSRRieqLQQREIV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2905 AIQEATRLKAEADMLQK-QKELAQE--QARKFQEDkeqiEQQLAKETEGFQKSLEaerRQQLEITAEAERLKLQVLEMSK 2981
Cdd:pfam05557 295 LKEENSSLTSSARQLEKaRRELEQElaQYLKKIED----LNKKLKRHKALVRRLQ---RRVLLLTKERDGYRAILESYDK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2982 AQAKAEEDAKKFK--KQAEDFGNKLHQTELATKERMVVVQ---------------SLEIQRQQ--------SGKEAEELR 3036
Cdd:pfam05557 368 ELTMSNYSPQLLEriEEAEDMTQKMQAHNEEMEAQLSVAEeelggykqqaqtlerELQALRQQesladpsySKEEVDSLR 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3037 RAIAELEHEKEKLKQeaellQKNSQEMQVAQQEqLRQETQVLQTTFLtekhlllekekyiekekakleNLYEDEVRKAQK 3116
Cdd:pfam05557 448 RKLETLELERQRLRE-----QKNELEMELERRC-LQGDYDPKKTKVL---------------------HLSMNPAAEAYQ 500
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 3117 LKQEQEHQL-KQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKlladENRKLRE 3183
Cdd:pfam05557 501 QRKNQLEKLqAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAEL----KNQRLKE 564
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2052-2292 |
3.28e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 60.35 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2052 QKQKASAED----ELQELRARAEEAERQKKAAQEeAERLRRQVKDESQkkrEAEEELKRKVQAEKDAAREKQRAMEDlqk 2127
Cdd:PRK05035 443 QEKKKAEEAkarfEARQARLEREKAAREARHKKA-AEARAAKDKDAVA---AALARVKAKKAAATQPIVIKAGARPD--- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2128 fRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRmSFAEKTAQLELSLKQEHITVTHLQEEAERL-----KK 2202
Cdd:PRK05035 516 -NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIAR-AKAKKAAQQAANAEAEEEVDPKKAAVAAAIarakaKK 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2203 QHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELE 2282
Cdd:PRK05035 594 AAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAE 673
|
250
....*....|
gi 1717010358 2283 KQRKLADATA 2292
Cdd:PRK05035 674 DPKKAAVAAA 683
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1510-2298 |
3.30e-08 |
|
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: 60.37 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1510 KQALRNLETHYQEFMRDLpglrELPADDRMQMEREYNNCIQKYEQLLRTQEKGEQDEVTCKNYISQLKDIRLQLEGCESR 1589
Cdd:pfam02463 207 KKALEYYQLKEKLELEEE----YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKK 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1590 TIHKIRSPMEKDPIKECSQRISEQQQIHFELEGIKKNLDKVSEKTQKVLAQKEQSTSTPLLRTEHEITLQKMDQVYSLST 1669
Cdd:pfam02463 283 LQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1670 IYLEKLKTINLVIRSTHGAEEVVKTYEDQLKEVHAVPSD-------------SKELEATKAELKKLRSQVEGHQPLFNTL 1736
Cdd:pfam02463 363 KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSeeekeaqlllelaRQLEDLLKEEKKEELEILEEEEESIELK 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1737 EADLNKAKDvNEQMLRSHSERDVDLDRYRERVQQLLERWQAILVQIDLRQR-ELDQLGRQLRYYRETYDWLIKWIKDAKQ 1815
Cdd:pfam02463 443 QGKLTEEKE-ELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRqKLEERSQKESKARSGLKVLLALIKDGVG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1816 RQEQIQSVPITDSKTMKEQLLQLKKLLEEIESNRTKVDECQKYAKQYIDA----------IKDYELQLVTYKAQVEPVVS 1885
Cdd:pfam02463 522 GRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTelplgarklrLLIPKLKLPLKSIAVLEIDP 601
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1886 PAKKPKVQSTSDSIIQEYVD--LRTRYSELTTLTSQYIKFI--------TETLCRLNVEEKAAEKLKEEERRRLAEVEAQ 1955
Cdd:pfam02463 602 ILNLAQLDKATLEADEDDKRakVVEGILKDTELTKLKESAKakesglrkGVSLEEGLAEKSEVKASLSELTKELLEIQEL 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1956 LEKQTQLAEAHAKAKAQAEK----------------EAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDME 2019
Cdd:pfam02463 682 QEKAESELAKEEILRRQLEIkkkeqrekeelkklklEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEE 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2020 IKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKRE 2099
Cdd:pfam02463 762 KEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALE 841
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2100 AEEELKRKVQAEKDAAREKQRAMEDLQKFRS------QAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFA 2173
Cdd:pfam02463 842 LKEEQKLEKLAEEELERLEEEITKEELLQELllkeeeLEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2174 EKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKAN-------------------EALRLRLQ 2234
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKvnlmaieefeekeerynkdELEKERLE 1001
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2235 AEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSA 2298
Cdd:pfam02463 1002 EEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAELRLEDPDDPFSGGIEISA 1065
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1930-2628 |
3.48e-08 |
|
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: 60.12 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavDAEQQKQTIQQEL 2009
Cdd:pfam05483 82 KLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENK----DLIKENNATRHLC 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2010 QQLRQNSdmeiKSKAKKIEEAEYNRrkieEEIHIVRLQLETMQKQKASAedeLQELRARAEEAERQkkaaqeeaerLRRQ 2089
Cdd:pfam05483 158 NLLKETC----ARSAEKTKKYEYER----EETRQVYMDLNNNIEKMILA---FEELRVQAENARLE----------MHFK 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2090 VKDESQKKREAEEELKRKVQAEKDAAR-------EKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEvAQQSAA 2162
Cdd:pfam05483 217 LKEDHEKIQHLEEEYKKEINDKEKQVSllliqitEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIE-KKDHLT 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2163 AELNSKRMSFAEKTAQ---LELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVA 2239
Cdd:pfam05483 296 KELEDIKMSLQRSMSTqkaLEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2240 HK--KTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDE-LEKQRKLADATAQQKFSAEQELIRLKADTEsgeqqr 2316
Cdd:pfam05483 376 EDqlKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEkLLDEKKQFEKIAEELKGKEQELIFLLQARE------ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2317 llleeelfRLKNEVNEAIQKRKKMEEELAKVRAEMeillesKSRAEEESRSNTEKSKH--MLEVEAsklRELAEEAARLr 2394
Cdd:pfam05483 450 --------KEIHDLEIQLTAIKTSEEHYLKEVEDL------KTELEKEKLKNIELTAHcdKLLLEN---KELTQEASDM- 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2395 aLSEEAKRQRQIAEGEAARQR--------AEAERILKEKLAAINEATRLK-TEAEIALKEKEAENERLRRLAEDEAYQRK 2465
Cdd:pfam05483 512 -TLELKKHQEDIINCKKQEERmlkqienlEEKEMNLRDELESVREEFIQKgDEVKCKLDKSEENARSIEYEVLKKEKQMK 590
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2466 LLEEQATQHKQDIEEKIILLKK-SSDNELERQKNIVEDtlRQRRIIEEEIRILKLNFEkasSGKSDLELELNQLKNIAEE 2544
Cdd:pfam05483 591 ILENKCNNLKKQIENKNKNIEElHQENKALKKKGSAEN--KQLNAYEIKVNKLELELA---SAKQKFEEIIDNYQKEIED 665
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2545 THRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILAD-----------------------------EQEAARQRKAAL 2595
Cdd:pfam05483 666 KKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEmvalmekhkhqydkiieerdselglyknkEQEQSSAKAALE 745
|
730 740 750
....*....|....*....|....*....|...
gi 1717010358 2596 EEVERLKAKAEEAKRQKELAEKEAERQIQLAQE 2628
Cdd:pfam05483 746 IELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2385-2613 |
3.80e-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: 59.01 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2385 ELAEEAARLRALSEEAKRQRQIAEgEAARQRAEAERILKEKLAAINEATRL--KTEAEIALKEKEAE--NERLRRLAEDE 2460
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELA-ALKKEEKALLKQLAALERRIAALARRirALEQELAALEAELAelEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2461 AYQRKLLEEQ-ATQHKQDIEEKIILLKKSSD-NELERQKNIVEDTLRQRRiieeeirilklnfEKASSGKSDLElELNQL 2538
Cdd:COG4942 100 EAQKEELAELlRALYRLGRQPPLALLLSPEDfLDAVRRLQYLKYLAPARR-------------EQAEELRADLA-ELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2539 KNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKE 2613
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4630-4666 |
3.92e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 52.10 E-value: 3.92e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1717010358 4630 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4666
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2609-2957 |
4.01e-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: 59.77 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2609 KRQKELAEKEAERQIQLAQEAAFKKIEAEEKA---HAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARM 2685
Cdd:pfam09731 77 GESKEPKEEKKQVKIPRQSGVSSEVAEEEKEAtkdAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2686 RAEQEAALSRQQVEEAERmKQRAEEEAQAKAQAQDEAEKLRKEAELeaakrahaeqAALKQKQLADEEMDKHKKFAEKTL 2765
Cdd:pfam09731 157 QAVKAHTDSLKEASDTAE-ISREKATDSALQKAEALAEKLKEVINL----------AKQSEEEAAPPLLDAAPETPPKLP 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2766 rqkaqveQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKV-----KIQMEEL----IKLKLRIEE 2836
Cdd:pfam09731 226 -------EHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFPDIIPVlkednLLSNDDLnsliAHAHREIDQ 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2837 ENKMLIMKDKDSTQKfLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAE--KMLKEKMQAIQEATRLKA 2914
Cdd:pfam09731 299 LSKKLAELKKREEKH-IERALEKQKEELDKLAEELSARLEEVRAADEAQLRLEFEREREEirESYEEKLRTELERQAEAH 377
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1717010358 2915 EADMLQKQKELAQEQARKFQEDkeqIEQQLAKETEGFQKSLEA 2957
Cdd:pfam09731 378 EEHLKDVLVEQEIELQREFLQD---IKEKVEEERAGRLLKLNE 417
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1709-2139 |
4.63e-08 |
|
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: 60.07 E-value: 4.63e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1709 SKELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMLRSHSERDVDLDRYRERVQQLLERWQAILVQIDLRQRE 1788
Cdd:TIGR02168 683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1789 LDQLGRQLRYYRETYDWLIKWIKDAKQRQEQIQSvpitdsktmkeqllqlkklleEIESNRTKVDECQKyakqyidaikd 1868
Cdd:TIGR02168 763 IEELEERLEEAEEELAEAEAEIEELEAQIEQLKE---------------------ELKALREALDELRA----------- 810
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1869 yELQLVTYKAQvepvvspakkpKVQSTSDSIIQEYVDLRTRyselttltsqyIKFITETLCRLNVEEKAAEKLKEEERRR 1948
Cdd:TIGR02168 811 -ELTLLNEEAA-----------NLRERLESLERRIAATERR-----------LEDLEEQIEELSEDIESLAAEIEELEEL 867
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1949 LAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEevskrevvavdAEQQKQTIQQELQQLRQnsdmeikskakkiE 2028
Cdd:TIGR02168 868 IEELESELEALLNERASLEEALALLRSELEELSEELRE-----------LESKRSELRRELEELRE-------------K 923
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2029 EAEYNRRKIEEEIHIVRLQletmQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELkrkv 2108
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQ----ERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEY---- 995
|
410 420 430
....*....|....*....|....*....|.
gi 1717010358 2109 QAEKDAAREKQRAMEDLQKFRSQAEEAERRM 2139
Cdd:TIGR02168 996 EELKERYDFLTAQKEDLTEAKETLEEAIEEI 1026
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2502-3074 |
4.71e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.93 E-value: 4.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2502 DTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEeeQRRKEAEEKVRKIL 2581
Cdd:COG4913 252 ELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLE--ARLDALREELDELE 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2582 ADEQEAARQRKAALE-EVERLKAKAEEAKRQKELAEKEAeRQIQLAQ---EAAFKKIEAEEKAHAAIVQQKEQEMLQTRK 2657
Cdd:COG4913 330 AQIRGNGGDRLEQLErEIERLERELEERERRRARLEALL-AALGLPLpasAEEFAALRAEAAALLEALEEELEALEEALA 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2658 QEKSILDKLKEEAE---------RAKRAAEDADYARMRAEQEAALSRQ-----------QVEEAERMKQRA--------- 2708
Cdd:COG4913 409 EAEAALRDLRRELReleaeiaslERRKSNIPARLLALRDALAEALGLDeaelpfvgeliEVRPEEERWRGAiervlggfa 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2709 -----EEEAQAKAQAQDEAEKLRKEAELEAAK--RAHAEQAALKQKQLADE---EMDKHKKFAEKTLRQKAQV-----EQ 2773
Cdd:COG4913 489 ltllvPPEHYAAALRWVNRLHLRGRLVYERVRtgLPDPERPRLDPDSLAGKldfKPHPFRAWLEAELGRRFDYvcvdsPE 568
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2774 ELTKVKLQL--------EETDHQKtllDDESQRLKEEVT--DAMRQKAQVEEELfkvkiqmeeliklkLRIEEEnkmlim 2843
Cdd:COG4913 569 ELRRHPRAItragqvkgNGTRHEK---DDRRRIRSRYVLgfDNRAKLAALEAEL--------------AELEEE------ 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2844 kdkdstqkfLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDL---ANQRALAEkmLKEKMQAIQEA----TRLKAEA 2916
Cdd:COG4913 626 ---------LAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvaSAEREIAE--LEAELERLDASsddlAALEEQL 694
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2917 DMLQKQKELAQEQARKFQEDKEQIEQQLaketEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQ 2996
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKEL----EQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2997 AEDFGNKLhQTELATKERMVVVQSLEIQRQQ---------SGKEAEELRRAIAELEHEK--EKLKQEAELLQKNSQEMQV 3065
Cdd:COG4913 771 LEERIDAL-RARLNRAEEELERAMRAFNREWpaetadldaDLESLPEYLALLDRLEEDGlpEYEERFKELLNENSIEFVA 849
|
....*....
gi 1717010358 3066 AQQEQLRQE 3074
Cdd:COG4913 850 DLLSKLRRA 858
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1931-2149 |
4.79e-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: 4.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1931 LNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEvskrevvavdaEQQKQTIQQELQ 2010
Cdd:pfam13868 57 LEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE-----------DQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2011 QLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIhivRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQV 2090
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDER---ILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2091 KDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQ 2149
Cdd:pfam13868 203 RDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEE 261
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1939-2468 |
4.93e-08 |
|
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: 59.75 E-value: 4.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1939 EKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDM 2018
Cdd:pfam05557 64 EAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2019 eiksKAKKIEEAEynrrkieeeihIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKR 2098
Cdd:pfam05557 144 ----LKAKASEAE-----------QLRQNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELARIPELEKELER 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2099 EAEE-----ELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQE--------VAQQSAAAEL 2165
Cdd:pfam05557 209 LREHnkhlnENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSWVKLAQDtglnlrspEDLSRRIEQL 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2166 NSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLR--LQAEEVAHKKT 2243
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgYRAILESYDKE 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2244 LAQEEAEKQKEDAEREARK---RAKAEESALR-QKELAEDELEKQRKLADataqqkfSAEQELIRLKADTESgeqqrlll 2319
Cdd:pfam05557 369 LTMSNYSPQLLERIEEAEDmtqKMQAHNEEMEaQLSVAEEELGGYKQQAQ-------TLERELQALRQQESL-------- 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2320 eEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSK--HMLEVEASKLRE-LAEEAARLRal 2396
Cdd:pfam05557 434 -ADPSYSKEEVDSLRRKLETLELERQRLREQKNELEMELERRCLQGDYDPKKTKvlHLSMNPAAEAYQqRKNQLEKLQ-- 510
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2397 seeakrqrqiAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIA--LKEKEAENERLRRLaeDEAYQRKLLE 2468
Cdd:pfam05557 511 ----------AEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLdlRKELESAELKNQRL--KEVFQAKIQE 572
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1976-2405 |
5.93e-08 |
|
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: 59.45 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1976 EAEELQRRMQEE---VSKREVVAVDAEQQKQTIQQELQQLRQNSDME---IKSKAKKIEEAEYNRRKIEEEIHIVRLQLE 2049
Cdd:pfam10174 346 EVDALRLRLEEKesfLNKKTKQLQDLTEEKSTLAGEIRDLKDMLDVKerkINVLQKKIENLQEQLRDKDKQLAGLKERVK 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2050 TMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQK-- 2127
Cdd:pfam10174 426 SLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELTEKESSLIDLKEha 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2128 --FRSQAEEAERRMKQAEVEKER----------QIKVAQEVAQQSAAAElnskrmSFAEKTAQLELSLKQEHITVTHLQE 2195
Cdd:pfam10174 506 ssLASSGLKKDSKLKSLEIAVEQkkeecsklenQLKKAHNAEEAVRTNP------EINDRIRLLEQEVARYKEESGKAQA 579
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2196 EAERLK---KQHEEAEKAREEAEKELEKWHQKanealRLRLQAEEVAHKKTLAQEEAEKQKEDAErEARKRAKAEESALR 2272
Cdd:pfam10174 580 EVERLLgilREVENEKNDKDKKIAELESLTLR-----QMKEQNKKVANIKHGQQEMKKKGAQLLE-EARRREDNLADNSQ 653
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2273 QKELAE--DELEKQRKLADATAQQKFSAEQELirlkadtesgeqqrllleeeLFRLKNEVNEAIQKRKKMEEelakvrae 2350
Cdd:pfam10174 654 QLQLEElmGALEKTRQELDATKARLSSTQQSL--------------------AEKDGHLTNLRAERRKQLEE-------- 705
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2351 meiLLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLR----ALSEEAKRQRQ 2405
Cdd:pfam10174 706 ---ILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALKrekdRLVHQLKQQTQ 761
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2761-2988 |
6.04e-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: 58.62 E-value: 6.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2761 AEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELfkvKIQMEELIKLKLRIEEenkm 2840
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQEL---AALEAELAELEKEIAE---- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2841 lIMKDKDSTQKFLAE---EAEKMRQVAEEAARLSIE-AQEAARMRKLAEDDLANQRALAEKmLKEKMQAIQE-ATRLKAE 2915
Cdd:COG4942 95 -LRAELEAQKEELAEllrALYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEE-LRADLAELAAlRAELEAE 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2916 ADMLQKQKELAQEQARKFQEDKEQIEQQLAKetegFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEE 2988
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLAR----LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
637-731 |
6.08e-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: 6.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 637 KTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLKHRQVKL 708
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1717010358 709 VNIRNDDIADGNPKLTLGLIWTI 731
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
745-852 |
6.43e-08 |
|
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: 53.94 E-value: 6.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 745 QSEDMTAKEKLLLWSQRMTESyqgLRCDNFTTSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFNVAERDLGV 823
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPgLCPDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 1717010358 824 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 852
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1507-2094 |
6.74e-08 |
|
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: 59.35 E-value: 6.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1507 EDYKQALRNLETHYQEFMRDLPGLRELPADDRMQME---REYNNCIQKYEQLLRTQEKGEQDEVT-----CKNYISQLKD 1578
Cdd:pfam05483 179 EETRQVYMDLNNNIEKMILAFEELRVQAENARLEMHfklKEDHEKIQHLEEEYKKEINDKEKQVSllliqITEKENKMKD 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1579 IRLQLEgcESRTihKIRSPMEKDPIKECSQRISEQQQIHF--ELEGIKKNLDKvSEKTQKVLAQKEQSTSTPL--LRTEH 1654
Cdd:pfam05483 259 LTFLLE--ESRD--KANQLEEKTKLQDENLKELIEKKDHLtkELEDIKMSLQR-SMSTQKALEEDLQIATKTIcqLTEEK 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1655 EITLQKMDQVYSLSTIYLEKLKTinlvirSTHGAEEVVKTYEDQLKEvhavpsDSKELEATKAELKKLRSQVEGHQPLFN 1734
Cdd:pfam05483 334 EAQMEELNKAKAAHSFVVTEFEA------TTCSLEELLRTEQQRLEK------NEDQLKIITMELQKKSSELEEMTKFKN 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1735 TLEADLNKAKDVneqmlRSHSERDVDLDRYRERVQQLLE-RWQAILVQIDLRQRELDQLGRQLRYYRETYDWLIKWIKDA 1813
Cdd:pfam05483 402 NKEVELEELKKI-----LAEDEKLLDEKKQFEKIAEELKgKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDL 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1814 KQR--QEQIQSVPITDSKTMKEQLLQLKKLLE-----EIESNRTKVDECQKYAKQYIDAIKDYELQLVTYKAQVEPVVSP 1886
Cdd:pfam05483 477 KTEleKEKLKNIELTAHCDKLLLENKELTQEAsdmtlELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1887 AKKP---------KVQSTSDSIIQEYVDLRTRYSELTTLTSQYIKFI---TETLCRLNVEEKAAEKLKEEERRRLAEVEA 1954
Cdd:pfam05483 557 FIQKgdevkckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIenkNKNIEELHQENKALKKKGSAENKQLNAYEI 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1955 QLEK-QTQLAEAHAKAKAQAEKEAEELQ------RRMQEEVSKREVVAVDAEQQKQTIQQELQQlrqnsdmEIKSKAKKI 2027
Cdd:pfam05483 637 KVNKlELELASAKQKFEEIIDNYQKEIEdkkiseEKLLEEVEKAKAIADEAVKLQKEIDKRCQH-------KIAEMVALM 709
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2028 EEAEYNRRKIEEE----IHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDES 2094
Cdd:pfam05483 710 EKHKHQYDKIIEErdseLGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1987-2156 |
6.86e-08 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 59.39 E-value: 6.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1987 EVSKR-----EVVAvDAEQQKQTIQQELQQLrqnsdmeIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDE 2061
Cdd:COG1193 490 EIARRlglpeEIIE-RARELLGEESIDVEKL-------IEELERERRELEEEREEAERLREELEKLREELEEKLEELEEE 561
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2062 LQELRARA-EEAERQKKAAQEEAERLRRQVKDESQKKREAEEelkrkvqaekdaAREKqramedLQKFRSQAEEAERRMK 2140
Cdd:COG1193 562 KEEILEKArEEAEEILREARKEAEELIRELREAQAEEEELKE------------ARKK------LEELKQELEEKLEKPK 623
|
170
....*....|....*...
gi 1717010358 2141 QAE--VEKERQIKVAQEV 2156
Cdd:COG1193 624 KKAkpAKPPEELKVGDRV 641
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2920-3054 |
6.90e-08 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 59.26 E-value: 6.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2920 QKQKELAQEQA-RKFQEDKEQIEQQLAKEtegfQKSLEAERRQQLEitAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAE 2998
Cdd:PTZ00491 662 KSQEAAARHQAeLLEQEARGRLERQKMHD----KAKAEEQRTKLLE--LQAESAAVESSGQSRAEALAEAEARLIEAEAE 735
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2999 dfgnkLHQTELATKERMVVVQSlEIQRQQSGKEAE-ELRRAIAELEHEKEKLKQEAE 3054
Cdd:PTZ00491 736 -----VEQAELRAKALRIEAEA-ELEKLRKRQELElEYEQAQNELEIAKAKELADIE 786
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
754-849 |
7.65e-08 |
|
second 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 CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 54.23 E-value: 7.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 754 KLLL-WSQRMTESYqGLRCDNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNL------------------------- 807
Cdd:cd21224 3 SLLLkWCQAVCAHY-GVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 808 ----------ENLdQAFNVAERDLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 849
Cdd:cd21224 82 lssellanekRNF-KLVQQAVAELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2542-2743 |
7.93e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 7.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2542 AEETHRSKEKAEQEAEKQRQLALEEEQRrkeAEEKVRKILADEQEAARQRKAALEE-VERlkAKAEEAKRQKELAEKEAE 2620
Cdd:PRK05035 500 AAATQPIVIKAGARPDNSAVIAAREARK---AQARARQAEKQAAAAADPKKAAVAAaIAR--AKAKKAAQQAANAEAEEE 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2621 RQIQLAQEAAfkkieAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEE 2700
Cdd:PRK05035 575 VDPKKAAVAA-----AIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVA 649
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1717010358 2701 AERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAA-KRAHAEQAA 2743
Cdd:PRK05035 650 AAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAiARAKAKKAA 693
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1916-2127 |
8.43e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.35 E-value: 8.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1916 LTSQYIKFITETLCRLNVEEKAAEK---LKEEERRRLAEvEAQLEKQTQLAEAhAKAKAQAE---KEAEELQRRMQEEVS 1989
Cdd:COG2268 186 LDALGRRKIAEIIRDARIAEAEAEReteIAIAQANREAE-EAELEQEREIETA-RIAEAEAElakKKAEERREAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1990 KREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEeeihivrlqletmqkqKASAEDELQELRAra 2069
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRK----------------PAEAEKQAAEAEA-- 325
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2070 eEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQK 2127
Cdd:COG2268 326 -EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDK 382
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1990-2306 |
8.82e-08 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 57.99 E-value: 8.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1990 KREVVAVDAEQQKQTIQQELQQLRQnsdmEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARA 2069
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2070 EEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQ 2149
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2150 IKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEAL 2229
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2230 RLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLK 2306
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALA 333
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2980-3190 |
9.37e-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: 57.85 E-value: 9.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2980 SKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKN 3059
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3060 SQEmqvaQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEKAKLENLyedevrkaQKLKQEQEHQLKQLEEEKQQLKASM 3139
Cdd:COG4942 99 LEA----QKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYL--------KYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 3140 GEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRKLREKLEQLEE 3190
Cdd:COG4942 167 AELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAE 217
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2532-2685 |
1.10e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.96 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2532 ELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQ 2611
Cdd:COG2268 231 EREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADV 310
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2612 KELAEKEAERQIQLAqEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQ--EKSILDKLKEEAERAKRAAEDADYARM 2685
Cdd:COG2268 311 RKPAEAEKQAAEAEA-EAEAEAIRAKGLAEAEGKRALAEAWNKLGDAaiLLMLIEKLPEIAEAAAKPLEKIDKITI 385
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1949-2253 |
1.10e-07 |
|
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: 57.62 E-value: 1.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1949 LAEVEAQL-EKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKKI 2027
Cdd:pfam13868 21 NKERDAQIaEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2028 EEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQK--------KAAQEEAERLRRQVKDESQKKRE 2099
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEereederiLEYLKEKAEREEEREAEREEIEE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2100 AEEELKRKVQAEKDAAREKQRAMEDLqKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQL 2179
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDEL-RAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAERE 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2180 ElslkQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQK 2253
Cdd:pfam13868 260 E----EEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1892-2305 |
1.11e-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: 58.49 E-value: 1.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1892 VQSTSDSIIQE-YVDL-RTRYSELTTLTSQYIKFITETLCRLNV-EEKAAEKLKEEERRRLAEVEAQLEKQT-------- 1960
Cdd:NF033838 63 VESHLEKILSEiQKSLdKRKHTQNVALNKKLSDIKTEYLYELNVlKEKSEAELTSKTKKELDAAFEQFKKDTlepgkkva 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1961 ----QLAEAHAKAKAQAEKEaeelqRRMQEEVSKRevvavdaeqqkqTIQQELQQlrqnSDMEIKSKAKKIEEAEYNRRK 2036
Cdd:NF033838 143 eatkKVEEAEKKAKDQKEED-----RRNYPTNTYK------------TLELEIAE----SDVEVKKAELELVKEEAKEPR 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2037 IEEEIHIVRLQLETmQKQKASAEDELQELRARAEE-----AERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAE 2111
Cdd:NF033838 202 DEEKIKQAKAKVES-KKAEATRLEKIKTDREKAEEeakrrADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKKE 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2112 KDAAREKQRAMEDLQKFRSQAEEAerrmKQAEVEKerqiKVAQevAQQSAAAELNSKRMSFAEKTAQ-LELSLKQEHITV 2190
Cdd:NF033838 281 NDAKSSDSSVGEETLPSPSLKPEK----KVAEAEK----KVEE--AKKKAKDQKEEDRRNYPTNTYKtLELEIAESDVKV 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2191 thlqEEAE-RLKKQHEEAEKAREEAEKELEKWHQKANEALRL------RLQAEEVAHKKTlAQEEAEKQKEDAEREARKR 2263
Cdd:NF033838 351 ----KEAElELVKEEAKEPRNEEKIKQAKAKVESKKAEATRLekiktdRKKAEEEAKRKA-AEEDKVKEKPAEQPQPAPA 425
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1717010358 2264 AKAEESALRQKELAEDelEKQRKLADATAQQKFS--AEQELIRL 2305
Cdd:NF033838 426 PQPEKPAPKPEKPAEQ--PKAEKPADQQAEEDYArrSEEEYNRL 467
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2696-3193 |
1.42e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2696 QQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKE-AELEAAKRAHAEQAALKQKQLAdeemdkhkkfAEKTLRQKAQVEQE 2774
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEElEELEAELEELREELEKLEKLLQ----------LLPLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2775 LTKVKLQLEETDHQktllddesqrlKEEVTDAMRQKAQVEEELFKVKIQMEELIKlKLRIEEENKMLIMKDKdstqkfLA 2854
Cdd:COG4717 141 LAELPERLEELEER-----------LEELRELEEELEELEAELAELQEELEELLE-QLSLATEEELQDLAEE------LE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2855 EEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQrALAEKMLKEKMQAIQEATRLKAEAdmlqkqkelaqeQARKFQ 2934
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLG------------LGGSLL 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2935 EDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFkkqaeDFGNKLHQTELATKER 3014
Cdd:COG4717 270 SLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAAL-----GLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3015 MVVvqslEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQTtfLTEKHLLLEKEK 3094
Cdd:COG4717 345 RIE----ELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGEL 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3095 YIEKEKAKLENLyEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMgeamkKQKEAEESVRHKQDELHQLDKRRQEQEKLL 3174
Cdd:COG4717 419 EELLEALDEEEL-EEELEELEEELEELEEELEELREELAELEAEL-----EQLEEDGELAELLQELEELKAELRELAEEW 492
|
490
....*....|....*....
gi 1717010358 3175 AdENRKLREKLEQLEEEHR 3193
Cdd:COG4717 493 A-ALKLALELLEEAREEYR 510
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1891-2091 |
1.49e-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: 57.47 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1891 KVQSTSDSIIQEYVDLRTRYSELTTL---TSQYIKFITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHA 1967
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1968 KAKAQAEKEAEELQRRMQEEVSKREVvavDAEQQKQTiQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQ 2047
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARRE---QAEELRAD-LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL 200
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1717010358 2048 LETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVK 2091
Cdd:COG4942 201 LARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4733-4761 |
1.53e-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: 1.53e-07
10 20
....*....|....*....|....*....
gi 1717010358 4733 IVDPETGKEMSVYEAYRKGLIDQQTYTEL 4761
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2712-2963 |
1.57e-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: 57.08 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2712 AQAKAQAQDEAEKlrkeaELEAAKrahaeqaalKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTL 2791
Cdd:COG4942 15 AAAQADAAAEAEA-----ELEQLQ---------QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2792 LDDESQRLKEEVTDAMRQKAQVEEELFKVKI---QMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAA 2868
Cdd:COG4942 81 LEAELAELEKEIAELRAELEAQKEELAELLRalyRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2869 RLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKET 2948
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
250
....*....|....*
gi 1717010358 2949 EGFQKSLEAERRQQL 2963
Cdd:COG4942 241 ERTPAAGFAALKGKL 255
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2545-2767 |
1.63e-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: 57.65 E-value: 1.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2545 THRSKEKAEQE---AEKQRQLALEEEQRRKEAEEKvRKILADEQEAARQRKAALEEVERlkAKAEEAKRQKELAEKEAER 2621
Cdd:pfam15709 326 EKREQEKASRDrlrAERAEMRRLEVERKRREQEEQ-RRLQQEQLERAEKMREELELEQQ--RRFEEIRLRKQRLEEERQR 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2622 QiqlaqeaafkkieAEEKAHAAIVQQKEQEmlQTRKQEKSILDKLKEEaeRAKRAAEDADYARMRAEQEAALSRQQVEEA 2701
Cdd:pfam15709 403 Q-------------EEEERKQRLQLQAAQE--RARQQQEEFRRKLQEL--QRKKQQEEAERAEAEKQRQKELEMQLAEEQ 465
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2702 ERMKQRAEEEaqakaqaqdEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQ 2767
Cdd:pfam15709 466 KRLMEMAEEE---------RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2019-2164 |
1.66e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.58 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2019 EIKSKAKkIEEAEYNRrkiEEEIHIvRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDEsQKKR 2098
Cdd:COG2268 196 EIIRDAR-IAEAEAER---ETEIAI-AQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAE-AAYE 269
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2099 EAEEELKRKVQAEKDAA-REKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQ---EVAQQSAAAE 2164
Cdd:COG2268 270 IAEANAEREVQRQLEIAeREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEaeaEAIRAKGLAE 339
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2532-2693 |
1.73e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.12 E-value: 1.73e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2532 ELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEeakrq 2611
Cdd:PRK09510 110 RLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAK----- 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2612 kelAEKEAERQIQLAQEAAfKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKlKEEAERAkrAAEDADYARMRAEQEA 2691
Cdd:PRK09510 185 ---KKAEAEAAAKAAAEAK-KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEA-KAAAEKA--AAAKAAEKAAAAKAAA 257
|
..
gi 1717010358 2692 AL 2693
Cdd:PRK09510 258 EV 259
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2256-2465 |
2.27e-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: 56.70 E-value: 2.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2256 AEREARKRAKAEESALRQK-ELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAI 2334
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEiAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2335 QKRKKMEEELAKV---------RAEMEILLESKSRAEEESRSntEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQ 2405
Cdd:COG4942 97 AELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRL--QYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2406 -----IAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAEN--ERLRRLAEDEAYQRK 2465
Cdd:COG4942 175 elealLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEEleALIARLEAEAAAAAE 241
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1933-2145 |
2.49e-07 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 56.93 E-value: 2.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1933 VEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQl 2012
Cdd:pfam05262 178 SDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE- 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2013 RQNSDMEIKSKAKKIEEaeynrrKIEEEihivrlqletmqkQKASAEDELQELRARAEEAERQKKAAQEEAerlrrqvkd 2092
Cdd:pfam05262 257 AKNLPKPADTSSPKEDK------QVAEN-------------QKREIEKAQIEIKKNDEEALKAKDHKAFDL--------- 308
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2093 esqkKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVE 2145
Cdd:pfam05262 309 ----KQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDAID 357
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1943-2161 |
3.27e-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: 3.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1943 EEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKeaeelQRRMQEEVSKREvvavdAEQQKQTIQQELQQLRQnsdMEiks 2022
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRAERAE-----MRRLEVERKRRE-----QEEQRRLQQEQLERAEK---MR--- 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2023 kakkiEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDElqelRARAEEAERQKKAAQEEAER---LRRQVKDESQKKRE 2099
Cdd:pfam15709 376 -----EELELEQQRRFEEIRLRKQRLEEERQRQEEEERK----QRLQLQAAQERARQQQEEFRrklQELQRKKQQEEAER 446
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2100 AEEELKRKVQAEKDAAREKQRAM-----EDLQKFRSQAEEAERRMKQAE---VEKERQIKVAQEVAQQSA 2161
Cdd:pfam15709 447 AEAEKQRQKELEMQLAEEQKRLMemaeeERLEYQRQKQEAEEKARLEAEerrQKEEEAARLALEEAMKQA 516
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1950-2124 |
3.33e-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: 57.27 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1950 AEVEAQLEKQTQLAEAHAKAKAQAEKE---AEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQN-SDMEIKSKAK 2025
Cdd:COG3096 973 EDAVGLLGENSDLNEKLRARLEQAEEArreAREQLRQAQAQYSQYNQVLASLKSSRDAKQQTLQELEQElEELGVQADAE 1052
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2026 KIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAE-------RLRRQVKDESQKKR 2098
Cdd:COG3096 1053 AEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERR 1132
|
170 180
....*....|....*....|....*.
gi 1717010358 2099 eaeeeLKRKVQAEKDAarEKQRAMED 2124
Cdd:COG3096 1133 -----LHRRELAYLSA--DELRSMSD 1151
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2254-2617 |
3.55e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.41 E-value: 3.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2254 EDAEREARKRAKaeESALRQKELaEDELEKQRKLADATAQQKFSAEQELirlkaDTESGEQQRLLLEEELFRLKNEvnEA 2333
Cdd:pfam02029 5 EEAARERRRRAR--EERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSEL-----KPSGQGGLDEEEAFLDRTAKRE--ER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2334 IQKRKKMEEELAKvraemeillESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRqrqiaegeaAR 2413
Cdd:pfam02029 75 RQKRLQEALERQK---------EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETE---------IR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2414 QRAEAERILKEKLAAINEatrlkTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQatqhKQDIEEKIILLKKSSDNEL 2493
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEE-----EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEK----KVKYESKVFLDQKRGHPEV 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2494 ERQkNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELElnqlKNIAEETHRSKEKAEQEAEKQRQ------LALEEE 2567
Cdd:pfam02029 208 KSQ-NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAE----QKLEELRRRRQEKESEEFEKLRQkqqeaeLELEEL 282
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2568 QRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEK 2617
Cdd:pfam02029 283 KKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRRAEAAEK 332
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2550-2743 |
3.74e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.32 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2550 EKAEQEAEKQRQLALEEEQRrKEAEEKVRKILadeqeaarqrkAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEA 2629
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKK-EAEAIKKEALL-----------EAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2630 AFKKIEAEEKahaaivqqKEQEMLQTRK---QEKSILDKLKEEAERAKRAAEDadyarmRAEQEAALSRqqvEEA----- 2701
Cdd:PRK12704 98 LDRKLELLEK--------REEELEKKEKeleQKQQELEKKEEELEELIEEQLQ------ELERISGLTA---EEAkeill 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1717010358 2702 ERMKQRAEEEA-----QAKAQAQDEAEKLRKEAELEAAKRAHAEQAA 2743
Cdd:PRK12704 161 EKVEEEARHEAavlikEIEEEAKEEADKKAKEILAQAIQRCAADHVA 207
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1938-2420 |
4.00e-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: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1938 AEKLKEEERRRLAEVE--------AQLEKQTQLAEAhakAKAQAEKEAEELQRRMQE---EVSKREVVAVDAEQQKQTIQ 2006
Cdd:pfam05701 28 AHRIQTVERRKLVELElekvqeeiPEYKKQSEAAEA---AKAQVLEELESTKRLIEElklNLERAQTEEAQAKQDSELAK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2007 QELQQLRQNSDMEIKSKAKKIEEAEYNRR-KIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEA-----ERQKK--- 2077
Cdd:pfam05701 105 LRVEEMEQGIADEASVAAKAQLEVAKARHaAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAvsaskEIEKTvee 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2078 ----------------AAQEEAERLRRQV-----KDESQKKRE---AEEELKR---KVQAEKDAAREKQRAMEDLQKFRS 2130
Cdd:pfam05701 185 ltieliatkeslesahAAHLEAEEHRIGAalareQDKLNWEKElkqAEEELQRlnqQLLSAKDLKSKLETASALLLDLKA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2131 Q-AEEAERRMKQ--AEVEKERQIKVAQEVAQQSAAAEL------------NSKRMSFAEKTAQLEL--------SLKQEH 2187
Cdd:pfam05701 265 ElAAYMESKLKEeaDGEGNEKKTSTSIQAALASAKKELeevkaniekakdEVNCLRVAAASLRSELekekaelaSLRQRE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2188 ----ITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRlrlQAEEVAHKKTLAQEEAEKQKEDAErEARKR 2263
Cdd:pfam05701 345 gmasIAVSSLEAELNRTKSEIALVQAKEKEAREKMVELPKQLQQAAQ---EAEEAKSLAQAAREELRKAKEEAE-QAKAA 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2264 AKAEESALR--QKELAEDELEKQRKLADATAQQkfsaEQELIRLKADTESGEQQRLLLEeelfrlknEVNEAIQKRKKME 2341
Cdd:pfam05701 421 ASTVESRLEavLKEIEAAKASEKLALAAIKALQ----ESESSAESTNQEDSPRGVTLSL--------EEYYELSKRAHEA 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2342 EELAKVRAeMEILLESKSRAEEESRSntekskhmLEVEASKLRELAEEAARLRALSEEAKRQRQ---IAEGEAARQRAEA 2418
Cdd:pfam05701 489 EELANKRV-AEAVSQIEEAKESELRS--------LEKLEEVNREMEERKEALKIALEKAEKAKEgklAAEQELRKWRAEH 559
|
..
gi 1717010358 2419 ER 2420
Cdd:pfam05701 560 EQ 561
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2056-2298 |
4.49e-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: 4.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2056 ASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEA 2135
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2136 ERRMKQAevekERQIKVAQEVAQQSAAAELNSKRM---SFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKARE 2212
Cdd:COG3883 92 ARALYRS----GGSVSYLDVLLGSESFSDFLDRLSalsKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2213 EAEKELEKwHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATA 2292
Cdd:COG3883 168 AAKAELEA-QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASA 246
|
....*.
gi 1717010358 2293 QQKFSA 2298
Cdd:COG3883 247 AGAGAA 252
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2576-2947 |
5.37e-07 |
|
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: 55.31 E-value: 5.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2576 KVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKK-IEAEEKAHAAIVQQKEQEMLQ 2654
Cdd:pfam13868 19 KCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQeLEEQIEEREQKRQEEYEEKLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2655 TRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAA 2734
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2735 KRahaEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQEltkvklqleetdhqktlldDESQRLKEEvtDAMRQKAQVE 2814
Cdd:pfam13868 179 EE---EKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQ-------------------ERKERQKER--EEAEKKARQR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2815 EELFKVKIQMEELIKLKLRIEEENkmlimkdkdstqkflaEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDdlanQRAL 2894
Cdd:pfam13868 235 QELQQAREEQIELKERRLAEEAER----------------EEEEFERMLRKQAEDEEIEQEEAEKRRMKRLE----HRRE 294
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2895 AEKMLKEKmqaiqEATRLKAEADMLQKQKELAQEQARKfQEDKEQIEQQLAKE 2947
Cdd:pfam13868 295 LEKQIEER-----EEQRAAEREEELEEGERLREEEAER-RERIEEERQKKLKE 341
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2048-2294 |
5.60e-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: 56.11 E-value: 5.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2048 LETMQKQKASAEdelqelRARAEEAERQkkaaQEEAERLRRQvkdESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQK 2127
Cdd:pfam15709 325 LEKREQEKASRD------RLRAERAEMR----RLEVERKRRE---QEEQRRLQQEQLERAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2128 FRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSaaaelnskrmsfaektaQLELSLKQEHITVTHLQEEAERLKKQHEEA 2207
Cdd:pfam15709 392 RKQRLEEERQRQEEEERKQRLQLQAAQERARQQ-----------------QEEFRRKLQELQRKKQQEEAERAEAEKQRQ 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2208 EkareeaekelEKWHQKANEALRLRLQAEEvahkktlaqEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKL 2287
Cdd:pfam15709 455 K----------ELEMQLAEEQKRLMEMAEE---------ERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
....*..
gi 1717010358 2288 ADATAQQ 2294
Cdd:pfam15709 516 AQEQARQ 522
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2083-2294 |
6.60e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.65 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2083 AERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAE------EAERRMKQAEVEKERQIKVAQEV 2156
Cdd:COG2268 195 AEIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAElakkkaEERREAETARAEAEAAYEIAEAN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2157 AQQSAAAELNSkrmsfAEKTAQLELSlkqehitvthlQEEAERLKKQheeaekareeaekeLEKWHQKANEALRLRLQAE 2236
Cdd:COG2268 275 AEREVQRQLEI-----AEREREIELQ-----------EKEAEREEAE--------------LEADVRKPAEAEKQAAEAE 324
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2237 EVAhkktlaqeEAEKQKEDAEREA-RKRAKAE-ESALRQKELAEDELEKQRKLADATAQQ 2294
Cdd:COG2268 325 AEA--------EAEAIRAKGLAEAeGKRALAEaWNKLGDAAILLMLIEKLPEIAEAAAKP 376
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2048-2474 |
6.74e-07 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 55.68 E-value: 6.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2048 LETMQKQKASAEDELQELRARAEEAERQkkaaQEEAERLRRQVKdesQKKREAEEELKRKVQAEKDAAREKQRAMEDLQK 2127
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQ----QARLDELEALID---QWLAELEQVIALRRAGGLEAALALVRSGEGKAL 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2128 FRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEA 2207
Cdd:COG5278 151 MDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALA 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2208 EKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKL 2287
Cdd:COG5278 231 ALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAA 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2288 ADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRS 2367
Cdd:COG5278 311 AAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVEL 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2368 NTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKE 2447
Cdd:COG5278 391 EVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAA 470
|
410 420
....*....|....*....|....*..
gi 1717010358 2448 AENERLRRLAEDEAYQRKLLEEQATQH 2474
Cdd:COG5278 471 VAALAALAAAAAALAEAEAAAALAAAA 497
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2449-2774 |
7.28e-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: 55.79 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2449 ENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSD--NELERQKNIVEDTlRQRRIIEEEIRILKLNFEKASS 2526
Cdd:NF033838 54 ESQKEHAKEVESHLEKILSEIQKSLDKRKHTQNVALNKKLSDikTEYLYELNVLKEK-SEAELTSKTKKELDAAFEQFKK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2527 GKSDLELELNQLKNIAEEthrSKEKAEQEAEKQRQ---------LAL---EEEQRRKEAEEKVRKILADEQEAARQRKAA 2594
Cdd:NF033838 133 DTLEPGKKVAEATKKVEE---AEKKAKDQKEEDRRnyptntyktLELeiaESDVEVKKAELELVKEEAKEPRDEEKIKQA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2595 LEEVERLKAKA---EEAKRQKELAEKEAERqiqlaqeaafKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAE 2671
Cdd:NF033838 210 KAKVESKKAEAtrlEKIKTDREKAEEEAKR----------RADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2672 RAKRAAEDADYARMRAEQEAALSRQQVEEAERMKqraeEEAQAKAQAQDEAEKLR--------------------KEAEL 2731
Cdd:NF033838 280 ENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKV----EEAKKKAKDQKEEDRRNyptntyktleleiaesdvkvKEAEL 355
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1717010358 2732 EAAKRAHAEQAALKQKQLADEEMDKHKKFA---EKTLRQKAQVEQE 2774
Cdd:NF033838 356 ELVKEEAKEPRNEEKIKQAKAKVESKKAEAtrlEKIKTDRKKAEEE 401
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2862-3073 |
7.81e-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: 54.85 E-value: 7.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2862 QVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKmlkekmQAIQEATRLKAEADMLQKQKELAQ-EQARKFQEDKE-Q 2939
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK------QRAAEQARQKELEQRAAAEKAAKQaEQAAKQAEEKQkQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2940 IEQQLAKETEGFQKSLEAERRQQLEITA----EAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERm 3015
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEAEAERKAKEEAakqaEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE- 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 3016 vvvQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQ 3073
Cdd:TIGR02794 200 ---AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1932-2626 |
7.96e-07 |
|
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: 55.82 E-value: 7.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1932 NVEEKAAEKLKEEERRRLAEVEAQLekQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQeLQQ 2011
Cdd:TIGR00606 389 ERQIKNFHTLVIERQEDEAKTAAQL--CADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKE-LQQ 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2012 LRQNSDmEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAeDELQELRARAEEAER--QKKAAQEEAERLRRQ 2089
Cdd:TIGR00606 466 LEGSSD-RILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKA-DLDRKLRKLDQEMEQlnHHTTTRTQMEMLTKD 543
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2090 VKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMK--QAEVEKERQIKVAQEVAQQSAAAELns 2167
Cdd:TIGR00606 544 KMDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAklNKELASLEQNKNHINNELESKEEQL-- 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2168 krMSFAEKTAQLeLSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKA-------NEALRLRLQAEEVAH 2240
Cdd:TIGR00606 622 --SSYEDKLFDV-CGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENqsccpvcQRVFQTEAELQEFIS 698
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2241 KKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLE 2320
Cdd:TIGR00606 699 DLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIM 778
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2321 EELFRLKN-EVNEAIQKRKKMEEELAKVRAEMEIlleSKSRAEEESRSNTEKSKHMLEvEASKLRELAEEAARLRALSEE 2399
Cdd:TIGR00606 779 PEEESAKVcLTDVTIMERFQMELKDVERKIAQQA---AKLQGSDLDRTVQQVNQEKQE-KQHELDTVVSKIELNRKLIQD 854
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2400 AKRQRQ-------------IAEGEAARQRAEAERILKEKLAAINEATRLKTEA-------EIALKEKEAENERL------ 2453
Cdd:TIGR00606 855 QQEQIQhlksktnelksekLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAkeqdsplETFLEKDQQEKEELissket 934
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2454 -RRLAEDEAYQRKLLEEQATQHKQDIEEKII----LLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGK 2528
Cdd:TIGR00606 935 sNKKAQDKVNDIKEKVKNIHGYMKDIENKIQdgkdDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQE 1014
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2529 SDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEa 2608
Cdd:TIGR00606 1015 RWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELRE- 1093
|
730
....*....|....*...
gi 1717010358 2609 KRQKELAEKEAERQIQLA 2626
Cdd:TIGR00606 1094 PQFRDAEEKYREMMIVMR 1111
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2850-3151 |
9.29e-07 |
|
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: 9.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2850 QKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQ 2929
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2930 ARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMsKAQAKAEEDAKKFKKQAEdfgnklhqtel 3009
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKE-KAEREEEREAEREEIEEE----------- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3010 atKERMVVVQSLEIQRQQSGKEA-EELRRAIAELEHE---KEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQTTFLTE 3085
Cdd:pfam13868 182 --KEREIARLRAQQEKAQDEKAErDELRAKLYQEEQErkeRQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAERE 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 3086 KHLLLEKEKYIEKEKAKLENLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEE 3151
Cdd:pfam13868 260 EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEA 325
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2254-2612 |
9.85e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.26 E-value: 9.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2254 EDAEREAR-KRAKAEESALRQKELaEDELEKQRKLADATAQQKFSAEQELirlkaDTESGEQQRLLLEEELFRLKNEvnE 2332
Cdd:pfam02029 2 EDEEEAAReRRRRAREERRRQKEE-EEPSGQVTESVEPNEHNSYEEDSEL-----KPSGQGGLDEEEAFLDRTAKRE--E 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2333 AIQKRKKMEEELAKvraemeillESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRqrqiaegeaA 2412
Cdd:pfam02029 74 RRQKRLQEALERQK---------EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETE---------I 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2413 RQRAEAERILKEKLAAINEatrlkTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQatqhKQDIEEKIILLKKSSDNE 2492
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEE-----EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEK----KVKYESKVFLDQKRGHPE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2493 LERQkNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELE--LNQLKNIAEETHR--------SKEKAEQEAE----- 2557
Cdd:pfam02029 207 VKSQ-NGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEqkLEELRRRRQEKESeefeklrqKQQEAELELEelkkk 285
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2558 -KQRQLALEEEQRRKEAEEKVRKilADEQEAARQRKaalEEVERLKAKAEEaKRQK 2612
Cdd:pfam02029 286 rEERRKLLEEEEQRRKQEEAERK--LREEEEKRRMK---EEIERRRAEAAE-KRQK 335
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2793-2998 |
9.94e-07 |
|
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: 9.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2793 DDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLiMKDKDSTQKFLAEEAEKMRQVAEEAARLSI 2872
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2873 EAQEAARMRKLAE--------DDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQL 2944
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2945 AKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAE 2998
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
2059-2377 |
1.04e-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: 54.66 E-value: 1.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2059 EDELQELRARA----EEAERQKKAAQEEAERLRRQVKDESQKKREAE-EELKRKVQAEKDAARE--KQRAMEDLQKFRSQ 2131
Cdd:pfam15558 20 EQRMRELQQQAalawEELRRRDQKRQETLERERRLLLQQSQEQWQAEkEQRKARLGREERRRADrrEKQVIEKESRWREQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2132 AEEAE----RRMKQAEVE-------KERQIKVAQEVAQqsAAAELNS----KRMSFAEKTAQLELSLKQEHITVTHLQEE 2196
Cdd:pfam15558 100 AEDQEnqrqEKLERARQEaeqrkqcQEQRLKEKEEELQ--ALREQNSlqlqERLEEACHKRQLKEREEQKKVQENNLSEL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2197 AERLKKQHEEAekareeaekelekwHQKANEALRLRLQAEEvahKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKEL 2276
Cdd:pfam15558 178 LNHQARKVLVD--------------CQAKAEELLRRLSLEQ---SLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKW 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2277 AEDELEKQRK--------LADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEvNEAIQKRKKMEEELAKVR 2348
Cdd:pfam15558 241 RAEEKEEERQehkealaeLADRKIQQARQVAHKTVQDKAQRARELNLEREKNHHILKLKVE-KEEKCHREGIKEAIKKKE 319
|
330 340
....*....|....*....|....*....
gi 1717010358 2349 AEMEILLESKSRAEEESRSNTEKSKHMLE 2377
Cdd:pfam15558 320 QRSEQISREKEATLEEARKTARASFHMRE 348
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2049-2127 |
1.08e-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: 50.90 E-value: 1.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2049 ETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQK-----KREAEEELKR-KVQAEKDAAREKQRAM 2122
Cdd:cd06503 33 EKIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEIIEEARKEAEKikeeiLAEAKEEAERiLEQAKAEIEQEKEKAL 112
|
....*
gi 1717010358 2123 EDLQK 2127
Cdd:cd06503 113 AELRK 117
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2135-2295 |
1.10e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.88 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2135 AERRMKQAEVEKERQIKVAQ---EVAQQSAAAELNSKRMSFAEKTAqlELSLKQEHitvthLQEEAERLKkqheeaekar 2211
Cdd:COG2268 199 RDARIAEAEAERETEIAIAQanrEAEEAELEQEREIETARIAEAEA--ELAKKKAE-----ERREAETAR---------- 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2212 EEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADAT 2291
Cdd:COG2268 262 AEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAE 341
|
....
gi 1717010358 2292 AQQK 2295
Cdd:COG2268 342 GKRA 345
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1939-2155 |
1.19e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.95 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1939 EKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDM 2018
Cdd:PRK05035 465 EKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAAD 544
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2019 EIKS---------KAKKIEEAEYNRRKIEEEIH--------IVRLQLETMQKQKASAEDELQELRARAEEAerqKKAAQE 2081
Cdd:PRK05035 545 PKKAavaaaiaraKAKKAAQQAANAEAEEEVDPkkaavaaaIARAKAKKAAQQAASAEPEEQVAEVDPKKA---AVAAAI 621
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2082 EAERLRRQVKDESQKKREAEEELKRKVQAEkdAAREKQRAMEDLQKFRSQAEEAERRMKQ--AEVEKERQIKVAQE 2155
Cdd:PRK05035 622 ARAKAKKAEQQANAEPEEPVDPRKAAVAAA--IARAKARKAAQQQANAEPEEAEDPKKAAvaAAIARAKAKKAAQQ 695
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2574-2710 |
1.22e-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: 51.19 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2574 EEKVRKILADEQEAARQRKaALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEA--EEKAHAAIVQQKEQE 2651
Cdd:pfam05672 9 AEEAARILAEKRRQAREQR-EREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERrrEEEERQRKAEEEAEE 87
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2652 MLQTRKQEKSILDKLKEEAERakRAAEDAdyARMRAEQEaalSRQQVEEAERM--KQRAEE 2710
Cdd:pfam05672 88 REQREQEEQERLQKQKEEAEA--KAREEA--ERQRQERE---KIMQQEEQERLerKKRIEE 141
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4516-4553 |
1.26e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.86 E-value: 1.26e-06
10 20 30
....*....|....*....|....*....|....*...
gi 1717010358 4516 QKFLEGTSCIAGVYVEATKERFSVYQAMKKGFIRPGTA 4553
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2048-2298 |
1.41e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 54.60 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2048 LETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKD-----ESQKKREAEEELKRKVQAEKDAAREKQRAM 2122
Cdd:PRK07735 7 LEDLKKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNddmtiEEAKRRAAAAAKAKAAALAKQKREGTEEVT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2123 EDLQKFRSQAEEAERRMKQAEVEKERQiKVAQEVAQQSAAAelnSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKK 2202
Cdd:PRK07735 87 EEEKAKAKAKAAAAAKAKAAALAKQKR-EGTEEVTEEEKAA---AKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2203 QHEEAEKAREEAEKELEKWHQKANEAlrlRLQAEEVAHKktlaQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELE 2282
Cdd:PRK07735 163 EKAKAKAAAAAKAKAAALAKQKAAEA---GEGTEEVTEE----EKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDA 235
|
250
....*....|....*.
gi 1717010358 2283 KQRKLADATAQQKFSA 2298
Cdd:PRK07735 236 KAKAIAAAKAKAAAAA 251
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2585-2917 |
1.54e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 54.66 E-value: 1.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2585 QEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILD 2664
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2665 KLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAAL 2744
Cdd:COG3064 82 AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2745 KQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQM 2824
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2825 EELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQ 2904
Cdd:COG3064 242 EAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAA 321
|
330
....*....|...
gi 1717010358 2905 AIQEATRLKAEAD 2917
Cdd:COG3064 322 AAAGALVVRGGGA 334
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2455-2678 |
1.55e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.04 E-value: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2455 RLAEDEAYQRKLLEEQATQHKQDIEEkiilLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKsdlele 2534
Cdd:PRK09510 66 RQQQQQKSAKRAEEQRKKKEQQQAEE----LQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAE------ 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2535 lnqlKNIAEETHRSKEKAEQEAEkqrqlALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRqkel 2614
Cdd:PRK09510 136 ----EAAAKAAAAAKAKAEAEAK-----RAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKK---- 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2615 AEKEAERQiqlAQEAAFKKIEAEEKAHAAIVQQKEQEmlqtrKQEKSILDKLKEEAERAKRAAE 2678
Cdd:PRK09510 203 AEAEAKKK---AAAEAKKKAAAEAKAAAAKAAAEAKA-----AAEKAAAAKAAEKAAAAKAAAE 258
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
2550-2680 |
1.72e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 54.76 E-value: 1.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2550 EKAEQEAEKQRQLAleeEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKA-EEAKRQKELAEKEAERQIQLAQE 2628
Cdd:COG1193 517 EKLIEELERERREL---EEEREEAERLREELEKLREELEEKLEELEEEKEEILEKArEEAEEILREARKEAEELIRELRE 593
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2629 AafkkieaeekahaaivQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDA 2680
Cdd:COG1193 594 A----------------QAEEEELKEARKKLEELKQELEEKLEKPKKKAKPA 629
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2036-2180 |
1.96e-06 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 52.13 E-value: 1.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2036 KIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKRE--AEEELKRKVQAEKD 2113
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREdlAREALERKAELEAQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2114 AAREKQ---RAMEDLQKFRSQAEEAERRMKQAEVEKER---QIKVAQ---EVAQQSAAAELNSKRMSFA---EKTAQLE 2180
Cdd:COG1842 100 AEALEAqlaQLEEQVEKLKEALRQLESKLEELKAKKDTlkaRAKAAKaqeKVNEALSGIDSDDATSALErmeEKIEEME 178
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2621-2780 |
2.01e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 54.64 E-value: 2.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2621 RQIQLAQEAAFKKIEAEEKaHAAivQQKEQEMLQTRKQEKsILDKLKEEAER-------AKRAA-EDADYARMRAEQEAa 2692
Cdd:PTZ00491 651 KSVQLAIEITTKSQEAAAR-HQA--ELLEQEARGRLERQK-MHDKAKAEEQRtkllelqAESAAvESSGQSRAEALAEA- 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2693 lsrqqveEAERMKQRAE-EEAQAKAQAQD-----EAEKLRKEAELEAA-KRAHAEQAALKQKQLADEEMDKHKKFAE--- 2762
Cdd:PTZ00491 726 -------EARLIEAEAEvEQAELRAKALRieaeaELEKLRKRQELELEyEQAQNELEIAKAKELADIEATKFERIVEalg 798
|
170
....*....|....*....
gi 1717010358 2763 -KTLRQKAQVEQELtKVKL 2780
Cdd:PTZ00491 799 rETLIAIARAGPEL-QAKL 816
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1933-2148 |
2.04e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.10 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1933 VEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVavdaEQQKQTIQQELQQL 2012
Cdd:pfam02029 136 REKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVF----LDQKRGHPEVKSQN 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2013 RQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIvrlQLETMQKqkasaedeLQELRARAEEAERQkkaaqeEAERLRrqvkd 2092
Cdd:pfam02029 212 GEEEVTKLKVTTKRRQGGLSQSQEREEEAEV---FLEAEQK--------LEELRRRRQEKESE------EFEKLR----- 269
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2093 esQKKREAE---EELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKER 2148
Cdd:pfam02029 270 --QKQQEAElelEELKKKREERRKLLEEEEQRRKQEEAERKLREEEEKRRMKEEIERRR 326
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1943-2293 |
2.23e-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: 53.50 E-value: 2.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1943 EEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEA--EELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQ-NSDME 2019
Cdd:pfam15558 35 EELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQrkARLGREERRRADRREKQVIEKESRWREQAEDQENQRQeKLERA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2020 IKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKre 2099
Cdd:pfam15558 115 RQEAEQRKQCQEQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAK-- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2100 aEEELKRKVQAEkdaarekQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQL 2179
Cdd:pfam15558 193 -AEELLRRLSLE-------QSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERQEHKEALAELADRKI 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2180 ELSLKQEHITVthlQEEAERLKKQHeeaekareeaekeLEKwhQKANEALRLRLQAEEVAHKKTLaqeeaekqKEDAERE 2259
Cdd:pfam15558 265 QQARQVAHKTV---QDKAQRARELN-------------LER--EKNHHILKLKVEKEEKCHREGI--------KEAIKKK 318
|
330 340 350
....*....|....*....|....*....|....
gi 1717010358 2260 ARKRakaeESALRQKELAedeLEKQRKLADATAQ 2293
Cdd:pfam15558 319 EQRS----EQISREKEAT---LEEARKTARASFH 345
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4518-4556 |
2.27e-06 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 46.94 E-value: 2.27e-06
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 4518 FLEGTSCIAGVYVEATKERFSVYQAMKKGFIRPGTAFEL 4556
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2097-2481 |
2.33e-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: 54.25 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2097 KREAEEELKRKVQAEKDAAREKQRAmeDLQKFRSQAEEAERRM----KQAEVEKER-------------QIKVAQ-EVAQ 2158
Cdd:NF033838 108 KEKSEAELTSKTKKELDAAFEQFKK--DTLEPGKKVAEATKKVeeaeKKAKDQKEEdrrnyptntyktlELEIAEsDVEV 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2159 QSAAAELNSKRMsfaeKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREeaekelekwhqkanEALRLRLQAEEV 2238
Cdd:NF033838 186 KKAELELVKEEA----KEPRDEEKIKQAKAKVESKKAEATRLEKIKTDREKAEE--------------EAKRRADAKLKE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2239 AHKKTLAQEEAEKQKEDAEREA----------RKRAKAEESALRQKELAEDELEKQRKLADAtaqQKFSAEQElirLKAD 2308
Cdd:NF033838 248 AVEKNVATSEQDKPKRRAKRGVlgepatpdkkENDAKSSDSSVGEETLPSPSLKPEKKVAEA---EKKVEEAK---KKAK 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2309 TESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAemeillesksraeEESRsNTEKSKHMLEVEASKLrelaE 2388
Cdd:NF033838 322 DQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEA-------------KEPR-NEEKIKQAKAKVESKK----A 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2389 EAARLralsEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEA---YQRK 2465
Cdd:NF033838 384 EATRL----EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEKPADQQAeedYARR 459
|
410
....*....|....*...
gi 1717010358 2466 LLEE--QATQHKQDIEEK 2481
Cdd:NF033838 460 SEEEynRLTQQQPPKTEK 477
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
2664-2783 |
2.40e-06 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 53.72 E-value: 2.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2664 DKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEA-------------QAKAQAQDEAEKLRKEAE 2730
Cdd:PRK12472 193 ETLAREAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELkradkalaaaktdEAKARAEERQQKAAQQAA 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2731 LEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKtlrqKAQVEQELTKVKLQLE 2783
Cdd:PRK12472 273 EAATQLDTAKADAEAKRAAAAATKEAAKAAAAK----KAETAKAATDAKLALE 321
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2547-2744 |
2.46e-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: 53.85 E-value: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2547 RSKEKAEQEAEKQRQLAleeEQRRKEAEekvrkiladeqEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLA 2626
Cdd:pfam05262 185 ALREDNEKGVNFRRDMT---DLKERESQ-----------EDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2627 QEAAFKKIEAEEKAHAaivqqkeqemlQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALS-RQQVEEAERMK 2705
Cdd:pfam05262 251 RQKQQEAKNLPKPADT-----------SSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKAFDlKQESKASEKEA 319
|
170 180 190
....*....|....*....|....*....|....*....
gi 1717010358 2706 QRAEEEAQAKaqAQDEAEKLRKEAELEAAKRAHAEQAAL 2744
Cdd:pfam05262 320 EDKELEAQKK--REPVAEDLQKTKPQVEAQPTSLNEDAI 356
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1939-2159 |
2.49e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.25 E-value: 2.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1939 EKLKEEERRRLAEVEAQLEKQTQlaeahakakaQAEKEAEELQRRMQEEVSKREVVAVDAE-----QQKQTIQQELQQLR 2013
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLP----------ELRKELEEAEAALEEFRQKNGLVDLSEEaklllQQLSELESQLAEAR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2014 QNSdMEIKSKAKKIEEAEYNRRKIEEEIhIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDE 2093
Cdd:COG3206 233 AEL-AEAEARLAALRAQLGSGPDALPEL-LQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQE 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2094 SQKkreaeeeLKRKVQAEKDAAREKQRAMED-LQKFRSQAEEAERRMKQAEvEKERQIKVAQEVAQQ 2159
Cdd:COG3206 311 AQR-------ILASLEAELEALQAREASLQAqLAQLEARLAELPELEAELR-RLEREVEVARELYES 369
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2642-2979 |
2.79e-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: 53.00 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2642 AAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALS-RQQVEEAERMKQRAEEEAQAKAQAQD 2720
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQElEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2721 EAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKfaektLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLK 2800
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWK-----ELEKEEEREEDERILEYLKEKAEREEEREAEREEIE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2801 EEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLimkdkdstQKFLAEEAEKMRQvaEEAARLSIEAQEAARM 2880
Cdd:pfam13868 180 EEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKER--------QKEREEAEKKARQ--RQELQQAREEQIELKE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2881 RKLAEDdLANQRALAEKMLKEKMQAIQEATRLKaeadmlQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERR 2960
Cdd:pfam13868 250 RRLAEE-AEREEEEFERMLRKQAEDEEIEQEEA------EKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLRE 322
|
330
....*....|....*....
gi 1717010358 2961 QQLEITAEAERLKLQVLEM 2979
Cdd:pfam13868 323 EEAERRERIEEERQKKLKE 341
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2327-3013 |
2.81e-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: 53.87 E-value: 2.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2327 KNEVNEAIQKRKKMEEELAKVRAEME--------ILLESKSRAEEESRSNTE---------KSKHMLEVEASKLRELAEE 2389
Cdd:TIGR04523 25 KNIANKQDTEEKQLEKKLKTIKNELKnkekelknLDKNLNKDEEKINNSNNKikileqqikDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2390 AARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEaeiaLKEKEAENERLRRLAEDEAYQRKLLEE 2469
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2470 QatqhKQDIEEKIILLKKssdnelerQKNIVEDTLrqrriieeeirilkLNFEKASSGKSDLELELNQLKNIAEETHRSK 2549
Cdd:TIGR04523 181 E----KLNIQKNIDKIKN--------KLLKLELLL--------------SNLKKKIQKNKSLESQISELKKQNNQLKDNI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2550 EKAEQEAEKQrqlaleeEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEA 2629
Cdd:TIGR04523 235 EKKQQEINEK-------TTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2630 AFKKIEAEEKahaAIVQQKEQEMLQTRKQEKSIlDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAE 2709
Cdd:TIGR04523 308 WNKELKSELK---NQEKKLEEIQNQISQNNKII-SQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYK 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2710 EEAQA-KAQAQDEAEKLRKEAELEAAKRAHAEQAAlKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQ 2788
Cdd:TIGR04523 384 QEIKNlESQINDLESKIQNQEKLNQQKDEQIKKLQ-QEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2789 KTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRqvaeeaa 2868
Cdd:TIGR04523 463 RESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKE------- 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2869 rlsIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEatrLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKET 2948
Cdd:TIGR04523 536 ---KESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKE 609
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2949 egfqKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKE 3013
Cdd:TIGR04523 610 ----KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2359-3195 |
3.00e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.19 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2359 SRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEA---KRQRQI--AEGEAAR---QRAEAERILKEKL---- 2426
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELaelNEAESDleQDYQAASdhlNLVQTALRQQEKIeryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2427 AAINEATRLKTEAEIALK---EKEAENERLRRLAEDEA---------YQRKLLEEQ--ATQHKQDIE--EKIILLKKSSD 2490
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEeadEQQEENEARAEAAEEEVdelksqladYQQALDVQQtrAIQYQQAVQalERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2491 NELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEK-----AEQEAEKQRQLALE 2565
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWdvareLLRRLREQRHLAEQ 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2566 EEQRRKEaeekvrkiLAD-EQEAARQRKAaleevERLKAKAEEAKRQKELAEKEAER-QIQLAQEAAFKKIEAEEKAHAA 2643
Cdd:PRK04863 515 LQQLRMR--------LSElEQRLRQQQRA-----ERLLAEFCKRLGKNLDDEDELEQlQEELEARLESLSESVSEARERR 581
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2644 IVQQKEQEMLQTRKQEKSILdklkeeaERAKRAAEDAdYARMRAEQEAAL-SRQQVEEAerMKQRAEEEAQAKaQAQDEA 2722
Cdd:PRK04863 582 MALRQQLEQLQARIQRLAAR-------APAWLAAQDA-LARLREQSGEEFeDSQDVTEY--MQQLLERERELT-VERDEL 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2723 EKLRKEAELEAAKRAHAEQAALKQ-KQLA-------------DEEMDKHKKF--AEKTLRQkAQVEQELTKVKLQLEE-- 2784
Cdd:PRK04863 651 AARKQALDEEIERLSQPGGSEDPRlNALAerfggvllseiydDVSLEDAPYFsaLYGPARH-AIVVPDLSDAAEQLAGle 729
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2785 --------TDHQKTLLDD---ESQRLKEEVTD-----AMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDS 2848
Cdd:PRK04863 730 dcpedlylIEGDPDSFDDsvfSVEELEKAVVVkiadrQWRYSRFPEVPLFGRAAREKRIEQLRAEREELAERYATLSFDV 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2849 tQK----------FLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRA-----------------------LA 2895
Cdd:PRK04863 810 -QKlqrlhqafsrFIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQQQrsqleqakeglsalnrllprlnlLA 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2896 EKMLKEKMQAIQE--ATRLKAEADMLQKQKELAQ--EQARKFQEDKEQIEqQLAKETEGFQKSLEAERRQQLEITAEAER 2971
Cdd:PRK04863 889 DETLADRVEEIREqlDEAEEAKRFVQQHGNALAQlePIVSVLQSDPEQFE-QLKQDYQQAQQTQRDAKQQAFALTEVVQR 967
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2972 lklqvlemsKAQAKAEEDAKKFKKQAEdfgnklhqtelatkermvvvqsLEIQRQQSGKEAEELRRAIaeleheKEKLKQ 3051
Cdd:PRK04863 968 ---------RAHFSYEDAAEMLAKNSD----------------------LNEKLRQRLEQAEQERTRA------REQLRQ 1010
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3052 eaellqknsqemqvaQQEQLRQETQVLQttfltekhlllekekyiekekaklenlyedevrKAQKLKQEQEHQLKQLEEE 3131
Cdd:PRK04863 1011 ---------------AQAQLAQYNQVLA---------------------------------SLKSSYDAKRQMLQELKQE 1042
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 3132 KQQLKASMGEamkkqkEAEESVRHKQDELHQL----DKRRQEQEKLLADENRKLRE---KLEQLEEEHRIA 3195
Cdd:PRK04863 1043 LQDLGVPADS------GAEERARARRDELHARlsanRSRRNQLEKQLTFCEAEMDNltkKLRKLERDYHEM 1107
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1934-2274 |
3.16e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 53.33 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EEKAAEKLKE----EERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEE-------VSKREVVAVDAEQQK 2002
Cdd:pfam02029 3 DEEEAARERRrrarEERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafldrTAKREERRQKRLQEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2003 QTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQL---ETMQKQKASAEDELQELRARAEEAERQKKAA 2079
Cdd:pfam02029 83 LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYkeeETEIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2080 QEEAERLRRQV-KDESQKKREAEEELKRKVQAEKDAAREKQRamedlqkfrsqaeeAERRMKQAEVEkerqiKVAQEVAQ 2158
Cdd:pfam02029 163 SEEAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRGH--------------PEVKSQNGEEE-----VTKLKVTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2159 QSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEK--WHQKANEALRLRLQAE 2236
Cdd:pfam02029 224 KRRQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAELELEELKKKreERRKLLEEEEQRRKQE 303
|
330 340 350
....*....|....*....|....*....|....*...
gi 1717010358 2237 EvAHKKTLAQEEAEKQKEDAEreaRKRAKAEEsaLRQK 2274
Cdd:pfam02029 304 E-AERKLREEEEKRRMKEEIE---RRRAEAAE--KRQK 335
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2017-2159 |
3.26e-06 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 53.68 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2017 DMEIKSKAKKI--EEAEynrrKIEEEIhivrlqlETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQvkdES 2094
Cdd:PRK00409 500 PENIIEEAKKLigEDKE----KLNELI-------ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEE---ED 565
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2095 QKKREAEEELKRKVQAEKDAAREKQRAMEDLQKF------RSQAEEAERRMKQAEVEKERQIKVAQEVAQQ 2159
Cdd:PRK00409 566 KLLEEAEKEAQQAIKEAKKEADEIIKELRQLQKGgyasvkAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2538-2937 |
3.38e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 53.50 E-value: 3.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2538 LKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEK 2617
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2618 ---EAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKsilDKLKEEAERAKRAAEDADYARMRAEQEAALS 2694
Cdd:COG3064 85 aaaEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAE---EEAKRKAEEERKAAEAEAAAKAEAEAARAAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2695 RQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKtlRQKAQVEQE 2774
Cdd:COG3064 162 AAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR--EAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2775 LTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLA 2854
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2855 EEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQ 2934
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
...
gi 1717010358 2935 EDK 2937
Cdd:COG3064 400 LLG 402
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2704-2992 |
3.42e-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: 53.49 E-value: 3.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2704 MKQRAEEEAQAKAQAQDEAEKL-----RKEAELEAAKR---AHAEQAALKQKQLADEEMDKHKKFAEKTLRQkaQVEQEL 2775
Cdd:pfam05667 260 ALAGTEATSGASRSAQDLAELLssfsgSSTTDTGLTKGsrfTHTEKLQFTNEAPAATSSPPTKVETEEELQQ--QREEEL 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2776 TKVKLQLEETDHQKTLLDDESQRLK------EEVTDAMRQKAQVEEELFKVKIQMEELIKlklriEEENKMLIMkdkdst 2849
Cdd:pfam05667 338 EELQEQLEDLESSIQELEKEIKKLEssikqvEEELEELKEQNEELEKQYKVKKKTLDLLP-----DAEENIAKL------ 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2850 QKFLAEEAEKMRQVAE--EAARLSIEAQEAARMRKLAEDDLANQRALAE-KMLKEKMQAIQEATRLKAEA-DMLQKQKEL 2925
Cdd:pfam05667 407 QALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiKELREKIKEVAEEAKQKEELyKQLVAEYER 486
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2926 AQEQA------RKFQEDKEQIEQQlakeTEGFQKSLEAERRQQLEI---TAEAERLKLQVLEMSKAQAKAEEDAKK 2992
Cdd:pfam05667 487 LPKDVsrsaytRRILEIVKNIKKQ----KEEITKILSDTKSLQKEInslTGKLDRTFTVTDELVFKDAKKDESVRK 558
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2132-3049 |
3.58e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 53.81 E-value: 3.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2132 AEEAERRMKQA-EVEKERQIKVAQEVAQQSAAAELNSKrmsfAEKTAQLELSLKQEH-ITVTHLQ--EEAERLKKQheea 2207
Cdd:PRK04863 278 ANERRVHLEEAlELRRELYTSRRQLAAEQYRLVEMARE----LAELNEAESDLEQDYqAASDHLNlvQTALRQQEK---- 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2208 ekareeaekeLEKWHQKANEalrLRLQAEEVAHKKTLAQEEAEkqkedaEREARKRAkAEESALR-QKELAE-----DEL 2281
Cdd:PRK04863 350 ----------IERYQADLEE---LEERLEEQNEVVEEADEQQE------ENEARAEA-AEEEVDElKSQLADyqqalDVQ 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2282 EKqRKLADATAQQKFSAEQELIRLKADTESGEQQRLLL-EEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILlesKSR 2360
Cdd:PRK04863 410 QT-RAIQYQQAVQALERAKQLCGLPDLTADNAEDWLEEfQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLV---RKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2361 AEEESRSNTEKSKHMLEVEASKLRELAEEAARLRA-LSEEAKRQRQiaEGEAARQRAEAERILKEKLAAINEATRLKTEA 2439
Cdd:PRK04863 486 AGEVSRSEAWDVARELLRRLREQRHLAEQLQQLRMrLSELEQRLRQ--QQRAERLLAEFCKRLGKNLDDEDELEQLQEEL 563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2440 EIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIillkkSSDNELERQKNIVEDTLRQRRIIEEEIRILKL 2519
Cdd:PRK04863 564 EARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWL-----AAQDALARLREQSGEEFEDSQDVTEYMQQLLE 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2520 NFEKASSGKSDLELELNQLKniaEETHRSKEKAEQEAEKQRQLAleeeqrrkeaeEKVRKILADE-------QEAA---- 2588
Cdd:PRK04863 639 RERELTVERDELAARKQALD---EEIERLSQPGGSEDPRLNALA-----------ERFGGVLLSEiyddvslEDAPyfsa 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2589 ---RQRKAALeeVERLKAKAEEAKRQKELAEK--EAERQIQLAQEAAFkkiEAEEKAHAAIVQQKEQEM---------LQ 2654
Cdd:PRK04863 705 lygPARHAIV--VPDLSDAAEQLAGLEDCPEDlyLIEGDPDSFDDSVF---SVEELEKAVVVKIADRQWrysrfpevpLF 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2655 TRKQEKSILDKLKEEAER-----AKRAAEDADYARMRA------------------EQEAALSRQQVEEAERmkqraeEE 2711
Cdd:PRK04863 780 GRAAREKRIEQLRAEREElaeryATLSFDVQKLQRLHQafsrfigshlavafeadpEAELRQLNRRRVELER------AL 853
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2712 AQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALkqkqLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTL 2791
Cdd:PRK04863 854 ADHESQEQQQRSQLEQAKEGLSALNRLLPRLNL----LADETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSV 929
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2792 LD-DESQ--RLKEEVTDAMRQKAQVEEELFKVKiqmeELI--KLKLRIEEENKMLImKDKDSTQKFLA--EEAEKMRQVA 2864
Cdd:PRK04863 930 LQsDPEQfeQLKQDYQQAQQTQRDAKQQAFALT----EVVqrRAHFSYEDAAEMLA-KNSDLNEKLRQrlEQAEQERTRA 1004
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2865 EEAARlsiEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATrLKAEADMLQK---QKELAQEQARKFQEDKEQIE 2941
Cdd:PRK04863 1005 REQLR---QAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLG-VPADSGAEERaraRRDELHARLSANRSRRNQLE 1080
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2942 QQLAK---ETEGFQKSLEAERR---QQLEITAEAERLKLQVLEMSKAQakaeedakkfkkqaeDFGNKLHQTELATkerm 3015
Cdd:PRK04863 1081 KQLTFceaEMDNLTKKLRKLERdyhEMREQVVNAKAGWCAVLRLVKDN---------------GVERRLHRRELAY---- 1141
|
970 980 990
....*....|....*....|....*....|....
gi 1717010358 3016 vvvQSLEIQRQQSGKEAEELRRAIAELEHEKEKL 3049
Cdd:PRK04863 1142 ---LSADELRSMSDKALGALRLAVADNEHLRDVL 1172
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1944-2289 |
3.70e-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: 52.61 E-value: 3.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1944 EERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELqrrmqeevskREVVAVDAEQQKQTIQQELQQLRQNSDMEIKsk 2023
Cdd:pfam13868 12 NSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEM----------MEEERERALEEEEEKEEERKEERKRYRQELE-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2024 aKKIEEAEynRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAeRQKKAAQEEAERLRRQVKdESQKKREAEEE 2103
Cdd:pfam13868 80 -EQIEERE--QKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ-RQLREEIDEFNEEQAEWK-ELEKEEEREED 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2104 LKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAER---RMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLE 2180
Cdd:pfam13868 155 ERILEYLKEKAEREEEREAEREEIEEEKEREIARlraQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2181 LSLKQEHIT-VTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAERE 2259
Cdd:pfam13868 235 QELQQAREEqIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEEL 314
|
330 340 350
....*....|....*....|....*....|
gi 1717010358 2260 ARKRAKAEESALRQKELAEdelEKQRKLAD 2289
Cdd:pfam13868 315 EEGERLREEEAERRERIEE---ERQKKLKE 341
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2034-2127 |
3.75e-06 |
|
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: 49.79 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2034 RRKIEEEIHIVRLQLETMQKQKASAEDELQELRAraeEAERQKKAAQEEAERLRRQVKDesqkkrEAEEELKRKV-QAEK 2112
Cdd:COG0711 33 QEKIADGLAEAERAKEEAEAALAEYEEKLAEARA---EAAEIIAEARKEAEAIAEEAKA------EAEAEAERIIaQAEA 103
|
90
....*....|....*
gi 1717010358 2113 DAAREKQRAMEDLQK 2127
Cdd:COG0711 104 EIEQERAKALAELRA 118
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1940-2187 |
4.00e-06 |
|
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.
Pssm-ID: 432790 [Multi-domain] Cd Length: 238 Bit Score: 51.53 E-value: 4.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1940 KLKEEERRRLAEVEAQLEKQT-QLAEAHAKAKAQAEKEAEELQRRMQeevskrevvavDAEQQKQTIQQELQQLRQNSDM 2018
Cdd:pfam12795 1 KLDELEKAKLDEAAKKKLLQDlQQALSLLDKIDASKQRAAAYQKALD-----------DAPAELRELRQELAALQAKAEA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2019 EIKSKAKKIEEAEYNRRKIEEEIhivrlQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKR 2098
Cdd:pfam12795 70 APKEILASLSLEELEQRLLQTSA-----QLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQIRNRLNGPAPPGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2099 EAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERrmKQAEVEKERQikVAQEVAQQSAAAELNSKRMSFAEKTA- 2177
Cdd:pfam12795 145 PLSEAQRWALQAELAALKAQIDMLEQELLSNNNRQDLLK--ARRDLLTLRI--QRLEQQLQALQELLNEKRLQEAEQAVa 220
|
250
....*....|...
gi 1717010358 2178 ---QLELSLKQEH 2187
Cdd:pfam12795 221 qteQLAEEAAGDH 233
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2005-2364 |
4.11e-06 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 52.60 E-value: 4.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2005 IQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAE 2084
Cdd:COG4372 18 LRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2085 RLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQikvaqevAQQSAAAE 2164
Cdd:COG4372 98 QAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESL-------QEELAALE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2165 LNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTL 2244
Cdd:COG4372 171 QELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2245 AQEEAEKQkeDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELF 2324
Cdd:COG4372 251 LLEEVILK--EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1717010358 2325 RLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEE 2364
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2523-2673 |
4.39e-06 |
|
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: 51.24 E-value: 4.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2523 KASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQ-EAARQRKAALEEVERL 2601
Cdd:pfam13904 34 QSSSLTYARKLEGLKLERQPLEAYENWLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKyQEWLQRKARQQTKKRE 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2602 KAKAEEAKRQKELAEKEAERQIqlAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERA 2673
Cdd:pfam13904 114 ESHKQKAAESASKSLAKPERKV--SQEEAKEVLQEWERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4313-4346 |
4.41e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 4.41e-06
10 20 30
....*....|....*....|....*....|....
gi 1717010358 4313 LLDAQAATGFIIDPVKNEMLTVDEAVRKGVVGPE 4346
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
611-743 |
4.42e-06 |
|
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: 49.67 E-value: 4.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 611 ETVPAVGVSEMEDPTPAEDERDRVQKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR 681
Cdd:cd21325 1 EGICALGGTSELSSEGTQHSYSEEEKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 682 ----EKGRMRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 743
Cdd:cd21325 81 rainKKKLTPFIIQENLNLALNSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2809-2969 |
4.69e-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: 52.54 E-value: 4.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2809 QKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKM-----RQVAEEAARLSIEAQ---EAARM 2880
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKAKQAAEAKakaEAEAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2881 RKLAEDdlANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQArKFQEDKEQIEQQLAKETEGFQKSLEAERR 2960
Cdd:TIGR02794 142 RKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKA-KAEEAKAKAEAAKAKAAAEAAAKAEAEAA 218
|
....*....
gi 1717010358 2961 QQLEITAEA 2969
Cdd:TIGR02794 219 AAAAAEAER 227
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
635-742 |
4.80e-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: 49.66 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 635 QKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 701
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1717010358 702 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 742
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2442-2686 |
4.82e-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: 4.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2442 ALKEKEAENERLRRLAEDEAYQRKLLEEQATQHK------QDIEEKIILLKKSSdNELERQKNIVEDTLRQRRIIEeeir 2515
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKallkqlAALERRIAALARRI-RALEQELAALEAELAELEKEI---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2516 ilklnfekassgkSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAAL 2595
Cdd:COG4942 93 -------------AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2596 EEVERLKAKAEEAKRQKE--LAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERA 2673
Cdd:COG4942 160 AELAALRAELEAERAELEalLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
250
....*....|...
gi 1717010358 2674 KRAAEDADYARMR 2686
Cdd:COG4942 240 AERTPAAGFAALK 252
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1930-2114 |
4.88e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.86 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKakaqaeKEAEELQRRMQEEVSKREvvaVDAEQQKQTIQQEL 2009
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAK------EEIHKLRNEFEKELRERR---NELQKLEKRLLQKE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2010 QQLRqnsdmeikskaKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRaraEEAERQKKAAQEEA-ERLRR 2088
Cdd:PRK12704 96 ENLD-----------RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQL---QELERISGLTAEEAkEILLE 161
|
170 180 190
....*....|....*....|....*....|.
gi 1717010358 2089 QVKDESQKK-----REAEEELKRkvQAEKDA 2114
Cdd:PRK12704 162 KVEEEARHEaavliKEIEEEAKE--EADKKA 190
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2774-3191 |
4.96e-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: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2774 ELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQME-------ELIKLKLRIEEENKMLImKDK 2846
Cdd:TIGR04523 104 DLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEklnnkynDLKKQKEELENELNLLE-KEK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2847 DSTQKFLAEEAEKMRQVAEeaaRLSIEAQEAARMRKLAED--DLANQRALAEKMLKEKMQAIQEatrlkaeadmLQKQKE 2924
Cdd:TIGR04523 183 LNIQKNIDKIKNKLLKLEL---LLSNLKKKIQKNKSLESQisELKKQNNQLKDNIEKKQQEINE----------KTTEIS 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2925 LAQEQARKFQEDKEQIEQQLAKEtegfQKSLEAERRQQLEITAEAERLKLQVLEMSKAQA-----KAEEDAKKFKKQAED 2999
Cdd:TIGR04523 250 NTQTQLNQLKDEQNKIKKQLSEK----QKELEQNNKKIKELEKQLNQLKSEISDLNNQKEqdwnkELKSELKNQEKKLEE 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3000 FGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAE-------LEHEKEKLKQEAELL--QKNSQEMQVAQQEQ 3070
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEkqneiekLKKENQSYKQEIKNLesQINDLESKIQNQEK 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3071 LRQETQVLQTTFLTEKHLLLEKEKYIEKEKAK--------------LENLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLK 3136
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKnnseikdltnqdsvKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 3137 ASMGEAMKKQKEAEESVRHKQDelhqldkrRQEQEKLLADENRKLREKLEQLEEE 3191
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKE--------LEEKVKDLTKKISSLKEKIEKLESE 532
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2966-3180 |
5.26e-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: 5.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2966 TAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHE 3045
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3046 KEKLKQE-AELL---QKNSQE---MQVAQQEQLRQETQVLQ--TTFLTEKHLLLEKEKYIEKEKAKLENLYEDEVRKAQK 3116
Cdd:COG4942 99 LEAQKEElAELLralYRLGRQpplALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 3117 LKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRK 3180
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2550-2635 |
5.57e-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: 48.97 E-value: 5.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2550 EKAEQEAEKQRQlalEEEQRRKEAEEKVRKILAD-----EQEAARQRKAALEEVERLKAKA-EEAKRQKELAEKEAERQI 2623
Cdd:cd06503 43 EKAKEEAEELLA---EYEEKLAEARAEAQEIIEEarkeaEKIKEEILAEAKEEAERILEQAkAEIEQEKEKALAELRKEV 119
|
90
....*....|...
gi 1717010358 2624 -QLAQEAAFKKIE 2635
Cdd:cd06503 120 aDLAVEAAEKILG 132
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2616-2994 |
5.76e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.56 E-value: 5.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2616 EKEAERQIQLAQEAAFKKIEAEEKAhAAIVQQKEQEmlqtrkQEKSILDKLKEEAERAKRAAEdadyarmraEQEAALSR 2695
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEP-SGQVTESVEP------NEHNSYEEDSELKPSGQGGLD---------EEEAFLDR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2696 QQveEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQEL 2775
Cdd:pfam02029 68 TA--KREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKW 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2776 TKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEEN----KMLIMKDKDSTQK 2851
Cdd:pfam02029 146 STEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKsqngEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2852 FLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEddlaNQRALAEKMLKEKMQAIQEATRLKAEadMLQKQKELAQEQAR 2931
Cdd:pfam02029 226 RQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQE----KESEEFEKLRQKQQEAELELEELKKK--REERRKLLEEEEQR 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2932 KFQEDKeqiEQQLAKETEGFQKSLEAERRQqleitAEAERLKLQVLEMSKAqakaeEDAKKFK 2994
Cdd:pfam02029 300 RKQEEA---ERKLREEEEKRRMKEEIERRR-----AEAAEKRQKLPEDSSS-----EGKKPFK 349
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1946-2111 |
5.77e-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: 51.08 E-value: 5.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1946 RRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRrmqeEVSKREVVAVDAEQQKQTIQQELQQLRQNSdmEIKSKAK 2025
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVRNNK--EYEALQK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2026 KIEEAEYNRRKIEEEIhivrlqLETMqKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELK 2105
Cdd:COG1579 97 EIESLKRRISDLEDEI------LELM-ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
....*.
gi 1717010358 2106 RKVQAE 2111
Cdd:COG1579 170 AKIPPE 175
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2549-2999 |
6.16e-06 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 52.35 E-value: 6.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2549 KEKAEQEAEKQRQLALEEEQRRKEAEEKVR-KILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERqiqlaQ 2627
Cdd:COG3064 5 LEEKAAEAAAQERLEQAEAEKRAAAEAEQKaKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKK-----L 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2628 EAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDAdyARMRAEQEAALSRQQVEEAERMKQR 2707
Cdd:COG3064 80 AEAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEE--AKRKAEEERKAAEAEAAAKAEAEAA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2708 AEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDH 2787
Cdd:COG3064 158 RAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2788 QKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEelIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEA 2867
Cdd:COG3064 238 EATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALS--SGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEE 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2868 ARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKE 2947
Cdd:COG3064 316 AVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAA 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2948 TEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAED 2999
Cdd:COG3064 396 GGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGG 447
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4053-4089 |
6.40e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.94 E-value: 6.40e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1717010358 4053 IRILEAQIATGGIIDPVHSHRVPIDIAYKRGYFDEEM 4089
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1934-2137 |
6.41e-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: 52.65 E-value: 6.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHakakaQAEKEAEELQRRMQEEVSKRevvavdaeqqkqtiQQELQQLR 2013
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAE-----KMREELELEQQRRFEEIRLR--------------KQRLEEER 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2014 QNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEE---AERQKKAAQ-EEAERLRRQ 2089
Cdd:pfam15709 401 QRQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQEEAERAEAEKQRQKELEmqlAEEQKRLMEmAEEERLEYQ 480
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1717010358 2090 vkdesQKKREAEEelKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAER 2137
Cdd:pfam15709 481 -----RQKQEAEE--KARLEAEERRQKEEEAARLALEEAMKQAQEQAR 521
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4726-4758 |
7.06e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.55 E-value: 7.06e-06
10 20 30
....*....|....*....|....*....|...
gi 1717010358 4726 VRKRRVVIVDPETGKEMSVYEAYRKGLIDQQTY 4758
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1888-2262 |
7.33e-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: 52.72 E-value: 7.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1888 KKPKVQSTSDSIIQEYVDLRTRYSELTTLTSQYIKfitETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHA 1967
Cdd:TIGR04523 272 KQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQ---DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLK 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1968 KAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQ------ELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEI 2041
Cdd:TIGR04523 349 KELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNlesqinDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEI 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2042 HIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRA 2121
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2122 MEDLQKFRSQAEEAERRMKQAEVEKerqikvaqevaqqsaaAELNSKRMSFAEKTAQLELSLKQEHITvTHLQEEAERLK 2201
Cdd:TIGR04523 509 EEKVKDLTKKISSLKEKIEKLESEK----------------KEKESKISDLEDELNKDDFELKKENLE-KEIDEKNKEIE 571
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2202 KQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEvahkKTLAQEEAEKQKEDAEREARK 2262
Cdd:TIGR04523 572 ELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEE----KEKKISSLEKELEKAKKENEK 628
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2144-2451 |
7.55e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 52.64 E-value: 7.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2144 VEKERQIKVA-QEVAQQSAAAELNSKRmsFAEKTAQLElslkqehitvthlQEEAERLKKQHEEAEKAREEAEKELekwh 2222
Cdd:PRK05035 428 VQYYRQAKAEiRAIEQEKKKAEEAKAR--FEARQARLE-------------REKAAREARHKKAAEARAAKDKDAV---- 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2223 QKANEALRLRlQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESAlrQKELAEDELEKQRKLADATAqqkfsaeqel 2302
Cdd:PRK05035 489 AAALARVKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQARARQA--EKQAAAAADPKKAAVAAAIA---------- 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2303 iRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKkmeeelAKvRAEMEIllESKSRAEEESRSNTEKSKHMLEVEASK 2382
Cdd:PRK05035 556 -RAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAK------AK-KAAQQA--ASAEPEEQVAEVDPKKAAVAAAIARAK 625
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2383 LRELAEEAARLRALSEEAKRqrqiAEGEAARQRAEAERILKEKLAAINEAT----RLKTEAEIA-LKEKEAENE 2451
Cdd:PRK05035 626 AKKAEQQANAEPEEPVDPRK----AAVAAAIARAKARKAAQQQANAEPEEAedpkKAAVAAAIArAKAKKAAQQ 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2889-3151 |
7.78e-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: 51.69 E-value: 7.78e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2889 ANQRALAEKMLKEKMQAIQEATR----LKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLE 2964
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKelaaLKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2965 ITAEAERLKLQvleMSKAQAKAEEDAKKFKKQAEDFgnklhqteLATKERMVVVQSLEIQRQQsgkEAEELRRAIAELEH 3044
Cdd:COG4942 99 LEAQKEELAEL---LRALYRLGRQPPLALLLSPEDF--------LDAVRRLQYLKYLAPARRE---QAEELRADLAELAA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3045 EKEKLKQEAELLQKNSQEMQvAQQEQLRQETQVLQTTfltekhlllekekyiekekaklenlyedeVRKAQKLKQEQEHQ 3124
Cdd:COG4942 165 LRAELEAERAELEALLAELE-EERAALEALKAERQKL-----------------------------LARLEKELAELAAE 214
|
250 260
....*....|....*....|....*..
gi 1717010358 3125 LKQLEEEKQQLKASMGEAMKKQKEAEE 3151
Cdd:COG4942 215 LAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1950-2178 |
8.37e-06 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 52.61 E-value: 8.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1950 AEVEAQLE--KQTQLAEAHAKAKAQAEKEAEELqrrmqeeVSKREVVAVDAEQQKQTIQQELQQLRQNSDmEI---KSKA 2024
Cdd:PRK11281 39 ADVQAQLDalNKQKLLEAEDKLVQQDLEQTLAL-------LDKIDRQKEETEQLKQQLAQAPAKLRQAQA-ELealKDDN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2025 KKIEEAEYNR---RKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAE 2101
Cdd:PRK11281 111 DEETRETLSTlslRQLESRLAQTLDQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQQIRNLLKGGKVGGKALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2102 EELKRKVQAEK---DAAREKQR-------AMEDLQKfrSQAEEAERRMKQAevekERQIKVAQEVaqqsaaaeLNSKRMS 2171
Cdd:PRK11281 191 PSQRVLLQAEQallNAQNDLQRkslegntQLQDLLQ--KQRDYLTARIQRL----EHQLQLLQEA--------INSKRLT 256
|
....*..
gi 1717010358 2172 FAEKTAQ 2178
Cdd:PRK11281 257 LSEKTVQ 263
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2223-2483 |
8.38e-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: 51.77 E-value: 8.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2223 QKANEALRLRLQAEEVAHKKTLAQEEAEKQKEdaerEARKRAKAEESalRQKELAED-ELEKQRKLADATAQQKFSAEQE 2301
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQAE----EAEKQRAAEQA--RQKELEQRaAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2302 LIRLKADTESGEQQRLlleeelfrlknevnEAIQKRKKMEEelAKVRAEmeilLESKSRAEEESRSNTEKSKHMLEVEAs 2381
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKA--------------EAEAERKAKEE--AAKQAE----EEAKAKAAAEAKKKAEEAKKKAEAEA- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2382 KLRELAEEAARLRALSEEAKRQRQIAEGEAARqRAEAERILKEKLAAINEATRLKTEAEIAL-KEKEAENERLRRLAEDE 2460
Cdd:TIGR02794 180 KAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAA-KAEAEAAAAAAAEAERKADEAELGDIFGLaSGSNAEKQGGARGAAAG 258
|
250 260
....*....|....*....|...
gi 1717010358 2461 AYQRKLleeqATQHKQDIEEKII 2483
Cdd:TIGR02794 259 SEVDKY----AAIIQQAIQQNLY 277
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
2696-2799 |
8.49e-06 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 49.57 E-value: 8.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2696 QQVEEAE-RMKQRAEEEAQAK---AQAQDEAEKLRKEAE-------LEAAKRAHAEQAALKQKQLADEEMDKHKKFAEkt 2764
Cdd:PRK07352 57 QALKEAEeRLRQAAQALAEAQqklAQAQQEAERIRADAKaraeairAEIEKQAIEDMARLKQTAAADLSAEQERVIAQ-- 134
|
90 100 110
....*....|....*....|....*....|....*...
gi 1717010358 2765 LRQKAqVEQELTKVKLQLEET---DHQKTLLDDESQRL 2799
Cdd:PRK07352 135 LRREA-AELAIAKAESQLPGRldeDAQQRLIDRSIANL 171
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1701-2465 |
8.89e-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: 52.53 E-value: 8.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1701 EVHAVPSDSKELEATKAELKKLRSQVEGHQplfnTLEADLNKAKDVNEQMLRShsERDVDLDRYRERVQQLLERWQAILV 1780
Cdd:pfam12128 242 EFTKLQQEFNTLESAELRLSHLHFGYKSDE----TLIASRQEERQETSAELNQ--LLRTLDDQWKEKRDELNGELSAADA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1781 QIDLRQRELDQLGRQLRYYRETYdwlikwIKDAKQRQEQIQSVPiTDSKTMKEQLLQLKKLLEEIESN----RTKVDECQ 1856
Cdd:pfam12128 316 AVAKDRSELEALEDQHGAFLDAD------IETAAADQEQLPSWQ-SELENLEERLKALTGKHQDVTAKynrrRSKIKEQN 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1857 KYA----KQYIDAIKD-YELQLVTYKAQVEPVVSPAKKPKVQSTSDSIIQEYvDLRTRYSELTTLTSQYIkFITETLCRL 1931
Cdd:pfam12128 389 NRDiagiKDKLAKIREaRDRQLAVAEDDLQALESELREQLEAGKLEFNEEEY-RLKSRLGELKLRLNQAT-ATPELLLQL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1932 NVEEKAAEKLKEEERRRLAEVEAqlekqtqLAEAHAKAKAQAEKEAEELQrrmQEEVSKREVVAVDAEQQKQTIQQE--- 2008
Cdd:pfam12128 467 ENFDERIERAREEQEAANAEVER-------LQSELRQARKRRDQASEALR---QASRRLEERQSALDELELQLFPQAgtl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2009 LQQLRQNSDMEIKSKAKKIEEA---------EYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAA 2079
Cdd:pfam12128 537 LHFLRKEAPDWEQSIGKVISPEllhrtdldpEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSA 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2080 QEEAERLRRQVKdesqkkrEAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQaeeaerrMKQAEVEKERQIKVAQEVAQQ 2159
Cdd:pfam12128 617 REKQAAAEEQLV-------QANGELEKASREETFARTALKNARLDLRRLFDE-------KQSEKDKKNKALAERKDSANE 682
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2160 SaaaelnskrmsfaektaqlelslkqehitVTHLQEEAERLKKQHeeaekareeaEKELEKWHQKANEALRLRLQAEEVA 2239
Cdd:pfam12128 683 R-----------------------------LNSLEAQLKQLDKKH----------QAWLEEQKEQKREARTEKQAYWQVV 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2240 HKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLK--ADTESGEQQRL 2317
Cdd:pfam12128 724 EGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRrqEVLRYFDWYQE 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2318 LLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLesksRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLR--A 2395
Cdd:pfam12128 804 TWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRR----AKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKedA 879
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2396 LSEEAkrqrQIAEGEAARQRAEAERILK-EKLAAINEATRLKTeaEIALKEKEAENERLRRLAEDEAYQRK 2465
Cdd:pfam12128 880 NSEQA----QGSIGERLAQLEDLKLKRDyLSESVKKYVEHFKN--VIADHSGSGLAETWESLREEDHYQND 944
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2794-3009 |
8.96e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 8.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2794 DESQRLKEEVTDAMRQKAQVEeelFKVKIQMEELIKLKLRIEEENKmlimkdKDSTQKFLAEEAEKMrqvAEEAARLSIE 2873
Cdd:PRK09510 62 EQYNRQQQQQKSAKRAEEQRK---KKEQQQAEELQQKQAAEQERLK------QLEKERLAAQEQKKQ---AEEAAKQAAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2874 AQeaarmrKLAEDDLANQRALAEKMLKEKMQAIQEATRlKAEADmlQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQK 2953
Cdd:PRK09510 130 KQ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAE--AKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK 200
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2954 ---SLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTEL 3009
Cdd:PRK09510 201 kkaEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2904-3073 |
9.23e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.80 E-value: 9.23e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2904 QAIQEATRLKAEAdmlQKQKELAQEQARKFQEDKEqIEQQLAKETEGFQKSlEAE-RRQQLEITAEAERlklqvlemSKA 2982
Cdd:COG2268 196 EIIRDARIAEAEA---ERETEIAIAQANREAEEAE-LEQEREIETARIAEA-EAElAKKKAEERREAET--------ARA 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2983 QAKAEEDAKKFKKQAEdfgnKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAI-----------AELEHEKEKLKQ 3051
Cdd:COG2268 263 EAEAAYEIAEANAERE----VQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEaekqaaeaeaeAEAEAIRAKGLA 338
|
170 180
....*....|....*....|..
gi 1717010358 3052 EAELLQKNSQEMQVAQQEQLRQ 3073
Cdd:COG2268 339 EAEGKRALAEAWNKLGDAAILL 360
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2622-2749 |
9.80e-06 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 51.20 E-value: 9.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2622 QIQLAQ-EAAFKKIEAEEKAHAAIVQQKEQemlqtRKQEKSILDKLKEEAERAKRaaedaDYARMRA-EQEAALSRQQVE 2699
Cdd:COG1566 82 QAALAQaEAQLAAAEAQLARLEAELGAEAE-----IAAAEAQLAAAQAQLDLAQR-----ELERYQAlYKKGAVSQQELD 151
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2700 EAERMKQRAEEE-AQAKAQAQDEAEKLRKEAELEAAKRAHAE-QAALKQKQL 2749
Cdd:COG1566 152 EARAALDAAQAQlEAAQAQLAQAQAGLREEEELAAAQAQVAQaEAALAQAEL 203
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3722-3758 |
9.85e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.17 E-value: 9.85e-06
10 20 30
....*....|....*....|....*....|....*..
gi 1717010358 3722 IRLLDAQLATGGIIDPVNSHRVPLDVACKRGYLDEET 3758
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2650-2751 |
1.00e-05 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 48.62 E-value: 1.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2650 QEMLQTRKQeksildKLKEEAERAKRAAEDADYARMRAEQEAALSRQQ----VEEAErmKQRAEEEAQAKAQAQDEAEKL 2725
Cdd:PRK05759 30 MKALEERQK------KIADGLAAAERAKKELELAQAKYEAQLAEARAEaaeiIEQAK--KRAAQIIEEAKAEAEAEAARI 101
|
90 100
....*....|....*....|....*.
gi 1717010358 2726 RKEAELEAAKRAHAEQAALKqKQLAD 2751
Cdd:PRK05759 102 KAQAQAEIEQERKRAREELR-KQVAD 126
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
630-738 |
1.03e-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: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 630 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 700
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1717010358 701 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 738
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2625-2837 |
1.06e-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: 51.30 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2625 LAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKE-EAERAKRAAEDADYARMRAEQEAALSRQQVEEAER 2703
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAAlERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2704 MKQRAEEEAQ-----AKAQAQDEAEK----LRKEAELEAAKRAHAEQAALKQKQladEEMDKHKKFAEKTLRQKAQVEQE 2774
Cdd:COG4942 96 RAELEAQKEElaellRALYRLGRQPPlallLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAELEAE 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2775 LTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEE 2837
Cdd:COG4942 173 RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAE 235
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2651-3202 |
1.07e-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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2651 EMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAE-EEAQAKaqaQD-EAEKLR-K 2727
Cdd:pfam05701 32 QTVERRKLVELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQtEEAQAK---QDsELAKLRvE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2728 EAELEAAKRAHAeqAALKQKQLADEemdkhkkfaektlRQKAQVEqELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAM 2807
Cdd:pfam05701 109 EMEQGIADEASV--AAKAQLEVAKA-------------RHAAAVA-ELKSVKEELESLRKEYASLVSERDIAIKRAEEAV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2808 RQKAQVEEELFKVKIqmeELIKLKLRIE---------EENKMLIMKDKDstQKFLAEEAEkMRQVAEEAARLsieaqeaa 2878
Cdd:pfam05701 173 SASKEIEKTVEELTI---ELIATKESLEsahaahleaEEHRIGAALARE--QDKLNWEKE-LKQAEEELQRL-------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2879 rmrklaeddlaNQRALAEKMLKEKMQAIQEA-TRLKAE--ADMLQKQKELAQEQArKFQEDKEQIEQQLA---KETEGFQ 2952
Cdd:pfam05701 239 -----------NQQLLSAKDLKSKLETASALlLDLKAElaAYMESKLKEEADGEG-NEKKTSTSIQAALAsakKELEEVK 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2953 KSLE--AERRQQLEITAEAERLKL-----------QVLEM-SKAQAKAEEDAKKFKKQAEdfgnKLHQTELATKERMVvv 3018
Cdd:pfam05701 307 ANIEkaKDEVNCLRVAAASLRSELekekaelaslrQREGMaSIAVSSLEAELNRTKSEIA----LVQAKEKEAREKMV-- 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3019 qSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQetqvLQTTFLTEKhLLLEKEKYIEK 3098
Cdd:pfam05701 381 -ELPKQLQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKE----IEAAKASEK-LALAAIKALQE 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3099 EKAKLENLYEDEVRKAQKLKQEQEHQL-KQLEEEKQQLKASMGEAMKKQKEAEESvrhkqdELHQLDkRRQEQEKLLADE 3177
Cdd:pfam05701 455 SESSAESTNQEDSPRGVTLSLEEYYELsKRAHEAEELANKRVAEAVSQIEEAKES------ELRSLE-KLEEVNREMEER 527
|
570 580
....*....|....*....|....*
gi 1717010358 3178 NRKLREKLEQLEEEHRIALAQTREM 3202
Cdd:pfam05701 528 KEALKIALEKAEKAKEGKLAAEQEL 552
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2528-2756 |
1.14e-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: 52.14 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2528 KSDLELELNQL-----KNIAEETHRS-KEKAEQ-----EAEKQRQL-ALEEEQRRKEAEEKvrkiLADEQEAARQRKAAL 2595
Cdd:NF012221 1537 TSESSQQADAVskhakQDDAAQNALAdKERAEAdrqrlEQEKQQQLaAISGSQSQLESTDQ----NALETNGQAQRDAIL 1612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2596 EE-----------VERLKAKAEEAKRQKELAEKEAER---------QIQL--AQEAAFKKIEAEEKAHAA-------IVQ 2646
Cdd:NF012221 1613 EEsravtkelttlAQGLDALDSQATYAGESGDQWRNPfagglldrvQEQLddAKKISGKQLADAKQRHVDnqqkvkdAVA 1692
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2647 QKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKA-QAQDEAEKL 2725
Cdd:NF012221 1693 KSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKAnQAQADAKGA 1772
|
250 260 270
....*....|....*....|....*....|.
gi 1717010358 2726 rKEAELEAAKRAHAEQAALKQKQLADEEMDK 2756
Cdd:NF012221 1773 -KQDESDKPNRQGAAGSGLSGKAYSVEGVAE 1802
|
|
| SPFH_HflC |
cd03405 |
High frequency of lysogenization C (HflC) family; SPFH (stomatin, prohibitin, flotillin, and ... |
2657-2735 |
1.19e-05 |
|
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: 50.18 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2657 KQEKSILDKLKEEAE---------RAKR-----AAEDADYARMRAE--QEAALSRQQ-VEEAERMKQRAEEEAQA-KAQA 2718
Cdd:cd03405 120 ELMEEILEQANEEAKeygievvdvRIKRidlpeEVSESVYERMRAEreRIAAEYRAEgEEEAEKIRAEADRERTViLAEA 199
|
90
....*....|....*..
gi 1717010358 2719 QDEAEKLRKEAELEAAK 2735
Cdd:cd03405 200 YREAEEIRGEGDAEAAR 216
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2782-3217 |
1.20e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.83 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2782 LEETDHQKTLLDDESQRLKEEVTDAMRQKAQVE--EELFKVKIQ-MEELIKLKLRIEEENKMLIMKDKDStqKFLAEEAE 2858
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDelEALIDQWLAeLEQVIALRRAGGLEAALALVRSGEG--KALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2859 KMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKE 2938
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2939 QIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERMVVV 3018
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3019 QSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYIEK 3098
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3099 EKAKLENLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADEN 3178
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430
....*....|....*....|....*....|....*....
gi 1717010358 3179 RKLREKLEQLEEEHRIALAQTREMMIQTDDLAGSSQTKA 3217
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAE 514
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
611-742 |
1.20e-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: 48.47 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 611 ETVPAVGVSEMEDPTPAEDERDRVQKKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR 681
Cdd:cd21324 1 EGICAIGGTSEQSSAGTQHSYSEEEKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDE 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 682 ----EKGRMRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 742
Cdd:cd21324 81 rtinKKKLTPFTIQENLNLALNSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| RNase_Y_N |
pfam12072 |
RNase Y N-terminal region; |
2567-2725 |
1.22e-05 |
|
RNase Y N-terminal region;
Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 49.50 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2567 EQRRKEAEEKVRKILAD-EQEAARQRKAAL----EEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAH 2641
Cdd:pfam12072 26 EAKIGSAEELAKRIIEEaKKEAETKKKEALleakEEIHKLRAEAERELKERRNELQRQERRLLQKEETLDRKDESLEKKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2642 AAIvQQKEQEMLQTRKQeksiLDKLKEEAER--AKRAAEDADYARMRAEQEAALSRQQVEEA---ERMKQRAEEEAQAKA 2716
Cdd:pfam12072 106 ESL-EKKEKELEAQQQQ----LEEKEEELEEliEEQRQELERISGLTSEEAKEILLDEVEEElrhEAAVMIKEIEEEAKE 180
|
....*....
gi 1717010358 2717 QAQDEAEKL 2725
Cdd:pfam12072 181 EADKKAKEI 189
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2044-2156 |
1.29e-05 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 52.01 E-value: 1.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2044 VRLQLETMQKQKASAEDELQELRARAEEAER-QKKAAQEEAERLRrqvkDESQKKREAEEELKRKVQAEKDAAREKQRAM 2122
Cdd:COG0542 402 VRMEIDSKPEELDELERRLEQLEIEKEALKKeQDEASFERLAELR----DELAELEEELEALKARWEAEKELIEEIQELK 477
|
90 100 110
....*....|....*....|....*....|....
gi 1717010358 2123 EDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEV 2156
Cdd:COG0542 478 EELEQRYGKIPELEKELAELEEELAELAPLLREE 511
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1911-2158 |
1.33e-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: 52.14 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1911 SELTTLTSQYIKFITE---TLCRLNVEEKAaeklkEEERRRLAEveaqlEKQTQLAeahAKAKAQAEKEAEELQRRMQEE 1987
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERA-----EADRQRLEQ-----EKQQQLA---AISGSQSQLESTDQNALETNG 1604
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1988 VSKREvvAVDAEQQKQTiqQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIhivrlqLETMQKQ----KASAEDELQ 2063
Cdd:NF012221 1605 QAQRD--AILEESRAVT--KELTTLAQGLDALDSQATYAGESGDQWRNPFAGGL------LDRVQEQlddaKKISGKQLA 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2064 ELRARAE-------EAERQKKAAQEEAERLRRQVKDESQKKR-EAEeelKRKvqaeKDAAREKQRAMEDLQKFRSQAEEA 2135
Cdd:NF012221 1675 DAKQRHVdnqqkvkDAVAKSEAGVAQGEQNQANAEQDIDDAKaDAE---KRK----DDALAKQNEAQQAESDANAAANDA 1747
|
250 260
....*....|....*....|...
gi 1717010358 2136 ERRMKQAEVEKERQIKVAQEVAQ 2158
Cdd:NF012221 1748 QSRGEQDASAAENKANQAQADAK 1770
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2047-2448 |
1.33e-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: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2047 QLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKRE--AEEELKRKVQAEKDAAREKQRAMED 2124
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAelAAEAAKKLAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2125 LQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQH 2204
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2205 EEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQ 2284
Cdd:COG3064 177 GAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2285 RKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEE 2364
Cdd:COG3064 257 VGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAAS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2365 SRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALK 2444
Cdd:COG3064 337 LEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAAS 416
|
....
gi 1717010358 2445 EKEA 2448
Cdd:COG3064 417 AVEL 420
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2528-3058 |
1.39e-05 |
|
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: 51.56 E-value: 1.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2528 KSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLA------LEEEQRRKEAEEKVRKILADE--------QEAARQRKA 2593
Cdd:TIGR04523 119 KNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELeklnnkYNDLKKQKEELENELNLLEKEklniqkniDKIKNKLLK 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2594 ALEEVERLKAKAEEAKR-QKELAEKEaERQIQLAQEAAFKKIEAEEKAhaAIVQQKEQEMLQTRKQEKSILDKLKEEaer 2672
Cdd:TIGR04523 199 LELLLSNLKKKIQKNKSlESQISELK-KQNNQLKDNIEKKQQEINEKT--TEISNTQTQLNQLKDEQNKIKKQLSEK--- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2673 akraaedadyarmraeqeaalsRQQVEEAERMKQRAEEEAQakaQAQDEAEKLRKEAELEAAKRAHAE-QAALKQKQLAD 2751
Cdd:TIGR04523 273 ----------------------QKELEQNNKKIKELEKQLN---QLKSEISDLNNQKEQDWNKELKSElKNQEKKLEEIQ 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2752 EEMDKHKKFAEKTLRQKAQVEQELT-------KVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKiQM 2824
Cdd:TIGR04523 328 NQISQNNKIISQLNEQISQLKKELTnsesensEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQE-KL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2825 EELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDL---------------A 2889
Cdd:TIGR04523 407 NQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLkvlsrsinkikqnleQ 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2890 NQRALAEKMlKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAK-----ETEGFQKSLEAERRQQLE 2964
Cdd:TIGR04523 487 KQKELKSKE-KELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISDledelNKDDFELKKENLEKEIDE 565
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2965 ITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLhqtelatKERMVVVQSLEIQRQQSGKEAEELRRAIAELEH 3044
Cdd:TIGR04523 566 KNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKS 638
|
570
....*....|....
gi 1717010358 3045 EKEKLKQEAELLQK 3058
Cdd:TIGR04523 639 KKNKLKQEVKQIKE 652
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3321-3354 |
1.43e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.43e-05
10 20 30
....*....|....*....|....*....|....
gi 1717010358 3321 LLEAQAASGFIIDPVKNERLSVNEAVKENVIGPE 3354
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2712-2880 |
1.43e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 51.32 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2712 AQAKA-QAQDEAEKLRKEAELEAakrahaeQAALKQKQL-ADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEET-DHQ 2788
Cdd:PRK12704 29 AEAKIkEAEEEAKRILEEAKKEA-------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENlDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2789 KTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRI----EEENKMLIMkdkDSTQKFLAEEAEKMRQVA 2864
Cdd:PRK12704 102 LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERIsgltAEEAKEILL---EKVEEEARHEAAVLIKEI 178
|
170
....*....|....*.
gi 1717010358 2865 EEAARLsiEAQEAARM 2880
Cdd:PRK12704 179 EEEAKE--EADKKAKE 192
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1935-2185 |
1.49e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 51.49 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1935 EKAAEKLKEEERRRLAEVEAQLE-KQTQL----AEAHAKAKAQAEKEAEELQRRMQEEVSKrevVAVDAEQQKQTIQQEL 2009
Cdd:PRK05035 434 AKAEIRAIEQEKKKAEEAKARFEaRQARLerekAAREARHKKAAEARAAKDKDAVAAALAR---VKAKKAAATQPIVIKA 510
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2010 QQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEI-----HIVRLQLETMQKQKAsaedELQELRARAEEAERQKKAAQEEA- 2083
Cdd:PRK05035 511 GARPDNSAVIAAREARKAQARARQAEKQAAAAadpkkAAVAAAIARAKAKKA----AQQAANAEAEEEVDPKKAAVAAAi 586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2084 ----ERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMK-QAEVEKERQIKVAQEVAQ 2158
Cdd:PRK05035 587 arakAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAvAAAIARAKARKAAQQQAN 666
|
250 260
....*....|....*....|....*..
gi 1717010358 2159 QSAAAELNSKRMSFAEKTAQLELSLKQ 2185
Cdd:PRK05035 667 AEPEEAEDPKKAAVAAAIARAKAKKAA 693
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2046-2203 |
1.52e-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: 49.92 E-value: 1.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2046 LQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKrKVQAEKDAAREKQ---RAM 2122
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIE-EVEARIKKYEEQLgnvRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2123 EDLQKFRSQAEEAERRMKQAE---VEKERQIKVAQEvAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAER 2199
Cdd:COG1579 89 KEYEALQKEIESLKRRISDLEdeiLELMERIEELEE-ELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
....
gi 1717010358 2200 LKKQ 2203
Cdd:COG1579 168 LAAK 171
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2038-2270 |
1.53e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2038 EEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAARE 2117
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2118 KQRAMEDLQKFR-----SQAEEAERRMKQAEVEKERQIKVAQEvaQQSAAAELNSKRMSFAEKTAQLE---LSLKQEHIT 2189
Cdd:COG3883 95 LYRSGGSVSYLDvllgsESFSDFLDRLSALSKIADADADLLEE--LKADKAELEAKKAELEAKLAELEalkAELEAAKAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2190 VTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEES 2269
Cdd:COG3883 173 LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAA 252
|
.
gi 1717010358 2270 A 2270
Cdd:COG3883 253 G 253
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2616-3193 |
1.54e-05 |
|
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: 51.56 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2616 EKEAERQIQLAQ------EAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAaeDADYARMRAEQ 2689
Cdd:TIGR04523 35 EKQLEKKLKTIKnelknkEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKL--NSDLSKINSEI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2690 EAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAK------RAHAEQAALKQKQLADEEMDKHKKFAE- 2762
Cdd:TIGR04523 113 KNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNnkyndlKKQKEELENELNLLEKEKLNIQKNIDKi 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2763 --------------KTLRQK-AQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEEL 2827
Cdd:TIGR04523 193 knkllklelllsnlKKKIQKnKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEK 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2828 IKlklRIEEENKMLIMKDKDSTQkfLAEEAEKMRQVAEEAARLSIEAQEAARMRKLaeDDLANQRALAEKMLKEKMQAIQ 2907
Cdd:TIGR04523 273 QK---ELEQNNKKIKELEKQLNQ--LKSEISDLNNQKEQDWNKELKSELKNQEKKL--EEIQNQISQNNKIISQLNEQIS 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2908 --EATRLKAEADMLQKQKELAQ-----EQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMS 2980
Cdd:TIGR04523 346 qlKKELTNSESENSEKQRELEEkqneiEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2981 KAQAKAEEDAKKFKKQAEDFGNKLHQTELATKErmvvvqsLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEaeLLQKNS 3060
Cdd:TIGR04523 426 KEIERLKETIIKNNSEIKDLTNQDSVKELIIKN-------LDNTRESLETQLKVLSRSINKIKQNLEQKQKE--LKSKEK 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3061 Q-EMQVAQQEQLRQETQVL---QTTFLTEKHLLLEKEKYIEKEKAKLEN--LYEDEVRKAQKLKQEQEHQLKQLEEEKQQ 3134
Cdd:TIGR04523 497 ElKKLNEEKKELEEKVKDLtkkISSLKEKIEKLESEKKEKESKISDLEDelNKDDFELKKENLEKEIDEKNKEIEELKQT 576
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 3135 LKASMgeamKKQKEAEESVRHKQDELHQLDKRRQEQEKLLAdenrKLREKLEQLEEEHR 3193
Cdd:TIGR04523 577 QKSLK----KKQEEKQELIDQKEKEKKDLIKEIEEKEKKIS----SLEKELEKAKKENE 627
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
745-852 |
1.61e-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: 47.11 E-value: 1.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 745 QSEDMTAKEKLLLWSQRMTESyqgLRCDNFTTSWRDGRLFNAIIHRHKP-LLIDMNKVYRQTNLENLDQAFNVAERDLGV 823
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPgLCPDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 1717010358 824 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 852
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1953-2199 |
1.63e-05 |
|
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: 51.45 E-value: 1.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1953 EAQLEKQTQLAEAHaKAKAQAEKEAEELQRRMQEEVSKREvvavdaeQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEY 2032
Cdd:pfam15964 346 EANFEKTKALIQCE-QLKSELERQKERLEKELASQQEKRA-------QEKEALRKEMKKEREELGATMLALSQNVAQLEA 417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2033 NRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEK 2112
Cdd:pfam15964 418 QVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREYRTKTGRQLEIKDQEIEKLGLEL 497
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2113 DAAREKqraMEDLQKFRSQAEEAERRMKQAEVEKERQI---KVAQEVAQQSAAAElnSKRMSFAEKTAQLELSLKQEHIT 2189
Cdd:pfam15964 498 SESKQR---LEQAQQDAARAREECLKLTELLGESEHQLhltRLEKESIQQSFSNE--AKAQALQAQQREQELTQKMQQME 572
|
250
....*....|
gi 1717010358 2190 VTHLQEEAER 2199
Cdd:pfam15964 573 AQHDKTVNEQ 582
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2670-2769 |
1.65e-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: 47.86 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2670 AERAKRAAEDADYA-RMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKR-AHAEQAALKQK 2747
Cdd:COG0711 30 DERQEKIADGLAEAeRAKEEAEAALAEYEEKLAEARAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIiAQAEAEIEQER 109
|
90 100
....*....|....*....|....*..
gi 1717010358 2748 QLADEEMDKH-----KKFAEKTLRQKA 2769
Cdd:COG0711 110 AKALAELRAEvadlaVAIAEKILGKEL 136
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3395-3431 |
1.66e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.66e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1717010358 3395 IRLLEAQIATGGIIDPVDSHRVPLEVAYKRNYFDEEM 3431
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| 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 ... |
2574-2658 |
1.68e-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: 47.69 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2574 EEKVRKILADEQEAARQRKAALEEVERLKAKAE-EAKRQKELAEKEAERQIQLAQEAAFKKIEA-EEKAHAAIVQQKEQE 2651
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEAEQQLKEARaEAQEIIENAKKRAEKLKEEIVAAAEAEAERiIEQAAAEIEQEKDRA 111
|
....*..
gi 1717010358 2652 MLQTRKQ 2658
Cdd:pfam00430 112 LAELRQQ 118
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1993-2178 |
1.92e-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: 1.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1993 VVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEE- 2071
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2072 ------------------------------------AERQK------KAAQEEAERLRRQVKDESQKKREAEEELKRKVQ 2109
Cdd:COG3883 92 aralyrsggsvsyldvllgsesfsdfldrlsalskiADADAdlleelKADKAELEAKKAELEAKLAELEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2110 AEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQ 2178
Cdd:COG3883 172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
634-735 |
2.04e-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: 47.03 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 634 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLKHRQVKLV 709
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1717010358 710 NIRNDDIADGNPKLTLGLIWTIILHF 735
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2782-3057 |
2.13e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2782 LEETDhqktlLDDESQRLKEEVTDAMRQKAQVEEELFKVKI------QMEELIKLKLRIEEENKMLIMKDKDSTQKFLAE 2855
Cdd:COG4913 218 LEEPD-----TFEAADALVEHFDDLERAHEALEDAREQIELlepireLAERYAAARERLAELEYLRAALRLWFAQRRLEL 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2856 EAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLanqRALAEKMLKEKMQAIQeatRLKAEADMLQKQKELAQEQARKFQE 2935
Cdd:COG4913 293 LEAELEELRAELARLEAELERLEARLDALREEL---DELEAQIRGNGGDRLE---QLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2936 DKEQIEQQLAKETEGFQksleaerRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDfgnklHQTELAtkerm 3015
Cdd:COG4913 367 LLAALGLPLPASAEEFA-------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE-----LEAEIA----- 429
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1717010358 3016 vvvqSLEIQRQQSGKEAEELRRAIAE-LEHEKEKLKQEAELLQ 3057
Cdd:COG4913 430 ----SLERRKSNIPARLLALRDALAEaLGLDEAELPFVGELIE 468
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2550-2647 |
2.18e-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: 47.86 E-value: 2.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2550 EKAEQEAEKQRQlalEEEQRRKEAEEKVRKILAD-----EQEAARQRKAALEEVERLKAKAE-EAKRQKELAEKEAERQI 2623
Cdd:COG0711 44 ERAKEEAEAALA---EYEEKLAEARAEAAEIIAEarkeaEAIAEEAKAEAEAEAERIIAQAEaEIEQERAKALAELRAEV 120
|
90 100
....*....|....*....|....*..
gi 1717010358 2624 -QLAQEAAFKKI--EAEEKAHAAIVQQ 2647
Cdd:COG0711 121 aDLAVAIAEKILgkELDAAAQAALVDR 147
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2155-2442 |
2.30e-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: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2155 EVAQQSAAAELNSKRMSFAEK---TAQLELS---LKQEHITVTHLQEE-----AERLKKqheeaekareeaekeLEKWHQ 2223
Cdd:COG2268 135 AVAAQMTVEELNEDREKFAEKvqeVAGTDLAkngLELESVAITDLEDEnnyldALGRRK---------------IAEIIR 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2224 KANEALRLRLQAEEVAHKKtlAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFsaeqeli 2303
Cdd:COG2268 200 DARIAEAEAERETEIAIAQ--ANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAETARAEAEAAYEI------- 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2304 rlkadtesgeqqrllleeelfrlknevnEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKhmlEVEASKL 2383
Cdd:COG2268 271 ----------------------------AEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRK---PAEAEKQ 319
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2384 RELAEEAARLRALSEEAKrqrqiAEGEAARQRAEAERILKEklAAINEAtRLKTEAEIA 2442
Cdd:COG2268 320 AAEAEAEAEAEAIRAKGL-----AEAEGKRALAEAWNKLGD--AAILLM-LIEKLPEIA 370
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2853-3162 |
2.32e-05 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 51.14 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2853 LAEEAEKMRQVAE---EAArLSIE----AQEAARMRKlAEDDLAN--QRALAEKMLKEKMQAIQEATRlkaeaDMLQkqk 2923
Cdd:pfam13779 458 LARSDEALDEVADllwELA-LRIEdgdlSDAERRLRA-AQERLSEalERGASDEEIAKLMQELREALD-----DYMQ--- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2924 ELAQEQarkfqedkEQIEQQLAKETEGFQKSLeaeRRQQLEitaeaeRL--KLQVLEMSKAQAKAEEdakkfkkqaedfg 3001
Cdd:pfam13779 528 ALAEQA--------QQNPQDLQQPDDPNAQEM---TQQDLQ------RMldRIEELARSGRRAEAQQ------------- 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3002 nKLHQTELATkERMVVVQSLEIQRQQSGkEAEELRRAIAELEHEKEKLKQEAellQKNSQEMQVAQQEQLRQETQVLQTT 3081
Cdd:pfam13779 578 -MLSQLQQML-ENLQAGQPQQQQQQGQS-EMQQAMDELGDLLREQQQLLDET---FRQLQQQGGQQQGQPGQQGQQGQGQ 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3082 FLTEKhlllekekyieKEKAKLENLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQ-KEAEESVRHKQDEL 3160
Cdd:pfam13779 652 QPGQG-----------GQQPGAQMPPQGGAEALGDLAERQQALRRRLEELQDELKELGGKEPGQAlGDAGRAMRDAEEAL 720
|
..
gi 1717010358 3161 HQ 3162
Cdd:pfam13779 721 GQ 722
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1206-1298 |
2.34e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.17 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1206 HTFVSAATKELMWLNDKEEEEVNFDWSDRNTNMAAKKENYSGLMRELELKEKKIKEIQSSGDRLLREDHPGRQTVEAFQA 1285
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1717010358 1286 ALQTQWSWMLQLC 1298
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2658-2932 |
2.37e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 50.72 E-value: 2.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2658 QEKSildKLKEEAERAKRAAEdadyARMRAEQEAAlsRQQVEEAERmKQRAEEEAQAKAQAQDEAEKlrkeaelEAAKRA 2737
Cdd:PRK05035 433 QAKA---EIRAIEQEKKKAEE----AKARFEARQA--RLEREKAAR-EARHKKAAEARAAKDKDAVA-------AALARV 495
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2738 HAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEEL 2817
Cdd:PRK05035 496 KAKKAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2818 FKVKIQMEELI-KLKLRIEEENkmlimKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARM--RKLAEDDLANQRAL 2894
Cdd:PRK05035 576 DPKKAAVAAAIaRAKAKKAAQQ-----AASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANaePEEPVDPRKAAVAA 650
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1717010358 2895 AEKMLKEKMQAIQEATRLKAEADMLQKQK---ELAQEQARK 2932
Cdd:PRK05035 651 AIARAKARKAAQQQANAEPEEAEDPKKAAvaaAIARAKAKK 691
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2444-2739 |
2.43e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 50.36 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2444 KEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIE--EKIILLKKSSDNELERQKNIVEDTLRQrriieeeirilklnf 2521
Cdd:PRK07735 5 KDLEDLKKEAARRAKEEARKRLVAKHGAEISKLEEEnrEKEKALPKNDDMTIEEAKRRAAAAAKA--------------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2522 eKASsgksdlELELNQLKNIAEETHRSKEKAEQEA--EKQRQLALEEEQRRKEAEEkvrkiLADEQEAARQRKAALEEve 2599
Cdd:PRK07735 70 -KAA------ALAKQKREGTEEVTEEEKAKAKAKAaaAAKAKAAALAKQKREGTEE-----VTEEEKAAAKAKAAAAA-- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2600 rlKAKAEEAKRQKELAEKEAERQIQLAQEA-AFKKIEAEEKAHAAIVQQKEQemlqtrkQEKSILDKLKEEAERAKRAAE 2678
Cdd:PRK07735 136 --KAKAAALAKQKREGTEEVTEEEEETDKEkAKAKAAAAAKAKAAALAKQKA-------AEAGEGTEEVTEEEKAKAKAK 206
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2679 DADYARMRAeqeAALSRQQVEEA------ERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHA 2739
Cdd:PRK07735 207 AAAAAKAKA---AALAKQKASQGngdsgdEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQEE 270
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
772-849 |
2.51e-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: 2.51e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 772 DNFTTSWRDGRLFNAIIHRHKPLLIDMNKVYRQTNLENLDQAFNVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 849
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2427-2692 |
2.52e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 50.72 E-value: 2.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2427 AAINEATRLKTEAEIALKEKEAENERLRR-LAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNElERQKNIVEDTLR 2505
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEReKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAA-TQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2506 QRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKilADEQ 2585
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIAR--AKAK 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2586 EAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQiqlAQEAAFKKIEAEEKAHAAIvqQKEQEMLQTRKQEKSILDK 2665
Cdd:PRK05035 593 KAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKA---EQQANAEPEEPVDPRKAAV--AAAIARAKARKAAQQQANA 667
|
250 260
....*....|....*....|....*..
gi 1717010358 2666 LKEEAERAKRAAEDADYARMRAEQEAA 2692
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAIARAKAKKAAQ 694
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2327-2587 |
2.63e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.98 E-value: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2327 KNEVNEAIQK----RKKMEE---ELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAArlralsee 2399
Cdd:PRK00409 515 KEKLNELIASleelERELEQkaeEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEA-------- 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2400 AKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKteaEIALKEKEAENERLRrlAEDEAYQRKLleeqatqhkqdiE 2479
Cdd:PRK00409 587 DEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKK---EKKKKKQKEKQEELK--VGDEVKYLSL------------G 649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2480 EKIILLKKSSDNELERQKNIvedtlrqrriieeeiriLKLNfekassgksdleLELNQLKNIAEETHRSKEKAEQEAEKQ 2559
Cdd:PRK00409 650 QKGEVLSIPDDKEAIVQAGI-----------------MKMK------------VPLSDLEKIQKPKKKKKKKPKTVKPKP 700
|
250 260 270
....*....|....*....|....*....|.
gi 1717010358 2560 RQLALEEE---QRRKEAEEKVRKILADEQEA 2587
Cdd:PRK00409 701 RTVSLELDlrgMRYEEALERLDKYLDDALLA 731
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2111-2479 |
2.66e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 50.64 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2111 EKDAAREK-QRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAElnSKRMSFAEKTAQLELSLKQEhit 2189
Cdd:pfam02029 4 EEEAARERrRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGL--DEEEAFLDRTAKREERRQKR--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2190 vthLQEEAERLKKqheeaekareeaekeLEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDaerearkRAKAEES 2269
Cdd:pfam02029 79 ---LQEALERQKE---------------FDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLG-------RYKEEET 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2270 ALRQKElaedelEKQRKLADATAQqkfsAEQELIRLKADTEsgeqQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRA 2349
Cdd:pfam02029 134 EIREKE------YQENKWSTEVRQ----AEEEGEEEEDKSE----EAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2350 EMEILLESKSR-AEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALS--EEAKRQRQIAEGEaarqraEAERILKEKL 2426
Cdd:pfam02029 200 QKRGHPEVKSQnGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQklEELRRRRQEKESE------EFEKLRQKQQ 273
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2427 AAINEATRLKTEAEIALKEKEAEnERLRRLAEDEAYQRKllEEQATQHKQDIE 2479
Cdd:pfam02029 274 EAELELEELKKKREERRKLLEEE-EQRRKQEEAERKLRE--EEEKRRMKEEIE 323
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2331-2465 |
2.78e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2331 NEAIQKRKKM-EEELAKVRAEMEILLESKSRAEEEsrsnTEKSKHMLEVEASKLRELAEEAARLRA---------LSEEA 2400
Cdd:COG2268 211 ETEIAIAQANrEAEEAELEQEREIETARIAEAEAE----LAKKKAEERREAETARAEAEAAYEIAEanaerevqrQLEIA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2401 KRQRQI--AEGEAARQRAEAERILKEKLAAinEATRLKTEAeialkEKEAENERLRRLAEDEAYQRK 2465
Cdd:COG2268 287 EREREIelQEKEAEREEAELEADVRKPAEA--EKQAAEAEA-----EAEAEAIRAKGLAEAEGKRAL 346
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1854-2141 |
2.82e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.82 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1854 ECQKYAKQYIDAIKDYELQLVTYKAQVEPVVSPAKKPKVQSTSDSIIQEYVDLRTRYSELTTLTSQ---YIKFITETLCR 1930
Cdd:PRK10929 62 GSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQeqdRAREISDSLSQ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1931 LnveekaaEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAekeaeelqrrMQEEVSKREVVaVDaeqqkqtiQQELQ 2010
Cdd:PRK10929 142 L-------PQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA----------LQAESAALKAL-VD--------ELELA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2011 QLRQNsdmeikskakkieeaeyNRRKIeeeihiVRLQLETMQKQKASAEDELQELRARAeEAERQKKA--AQEEAERLRR 2088
Cdd:PRK10929 196 QLSAN-----------------NRQEL------ARLRSELAKKRSQQLDAYLQALRNQL-NSQRQREAerALESTELLAE 251
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2089 Q-------VKDESQKKREAEEELKRKVQaEKDAAREKQR-AMEDLQKFRsQAEEAERRMKQ 2141
Cdd:PRK10929 252 QsgdlpksIVAQFKINRELSQALNQQAQ-RMDLIASQQRqAASQTLQVR-QALNTLREQSQ 310
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2444-2643 |
2.91e-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: 49.84 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2444 KEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILlkkssdnELERQKNIVEDTLRQRRIIEEEIRIL-KLNFE 2522
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAA-------EQARQKELEQRAAAEKAAKQAEQAAKqAEEKQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2523 KASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEverLK 2602
Cdd:TIGR02794 119 KQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEE---AK 195
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1717010358 2603 AKAEEAkrqKELAEKEAERQIQLAQEAAfKKIEAEEKAHAA 2643
Cdd:TIGR02794 196 AKAEAA---KAKAAAEAAAKAEAEAAAA-AAAEAERKADEA 232
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2047-2453 |
3.01e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 50.29 E-value: 3.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2047 QLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQ 2126
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2127 KFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEE 2206
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2207 AEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRK 2286
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAAL 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2287 LADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESR 2366
Cdd:COG5278 351 LAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAE 430
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2367 SNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEK 2446
Cdd:COG5278 431 ALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLL 510
|
....*..
gi 1717010358 2447 EAENERL 2453
Cdd:COG5278 511 AAAEAAL 517
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1930-2132 |
3.06e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 50.60 E-value: 3.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKA--AEKLKEEERRRLAEVEAQLEKqtqLAEAHAKAKAQAEKEAEElqrrmqeevskrevvAVdaEQQKQTIQQ 2007
Cdd:PRK00409 529 ERELEQKAeeAEALLKEAEKLKEELEEKKEK---LQEEEDKLLEEAEKEAQQ---------------AI--KEAKKEADE 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2008 ELQQLRQNSDMEIKS-KAKKIEEAeynRRKIEEEIHIvrlqLETMQKQKASAEDELQE-----LRARAEEAE----RQKK 2077
Cdd:PRK00409 589 IIKELRQLQKGGYASvKAHELIEA---RKRLNKANEK----KEKKKKKQKEKQEELKVgdevkYLSLGQKGEvlsiPDDK 661
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2078 AAQEEAERLRRQVK-DESQKKREAEEELKRKVQAEKDAAREKQR-----------AMEDLQKFRSQA 2132
Cdd:PRK00409 662 EAIVQAGIMKMKVPlSDLEKIQKPKKKKKKKPKTVKPKPRTVSLeldlrgmryeeALERLDKYLDDA 728
|
|
| PRK11029 |
PRK11029 |
protease modulator HflC; |
2679-2735 |
3.17e-05 |
|
protease modulator HflC;
Pssm-ID: 182913 [Multi-domain] Cd Length: 334 Bit Score: 49.74 E-value: 3.17e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2679 DADYARMRAEQEAALSR---QQVEEAERMKQRAEEE-AQAKAQAQDEAEKLRKEAELEAAK 2735
Cdd:PRK11029 221 DAIYNRMRAEREAVARRhrsQGQEEAEKLRATADYEvTRTLAEAERQGRIMRGEGDAEAAK 281
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2609-2796 |
3.19e-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: 50.39 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2609 KRQKELAEKEAERQIQLAQEAA-FKKIEAEEKAHAAIVQQKEQEMLQTRkqeksiLDKLKEEAERAKRAAEDADYARMRA 2687
Cdd:pfam05262 180 KKVVEALREDNEKGVNFRRDMTdLKERESQEDAKRAQQLKEELDKKQID------ADKAQQKADFAQDNADKQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2688 EQEAALSRQ--QVEEAERMKQRAEEEAQAKAQAQDEAEKlrKEAELEAAKRAHAEQAALKQKQLADEEMDKhkkfAEKTL 2765
Cdd:pfam05262 254 QQEAKNLPKpaDTSSPKEDKQVAENQKREIEKAQIEIKK--NDEEALKAKDHKAFDLKQESKASEKEAEDK----ELEAQ 327
|
170 180 190
....*....|....*....|....*....|.
gi 1717010358 2766 RQKAQVEQELTKVKlqlEETDHQKTLLDDES 2796
Cdd:pfam05262 328 KKREPVAEDLQKTK---PQVEAQPTSLNEDA 355
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1901-2034 |
3.41e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 50.40 E-value: 3.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1901 QEYVDLRTRYS---------ELTT----LTSQYIKFITE-----TLCRLNVEEKAAEklkEEERRRLAEVEAQLEKQTQ- 1961
Cdd:PTZ00491 638 VEPVDERTRDSlqksvqlaiEITTksqeAAARHQAELLEqeargRLERQKMHDKAKA---EEQRTKLLELQAESAAVESs 714
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 1962 ---LAEAHAKAKA-QAEKEAEELQRRMQEEVSKREVVAvDAEQQKQTIQQELQQLRQNSDMEIKsKAKKIEEAEYNR 2034
Cdd:PTZ00491 715 gqsRAEALAEAEArLIEAEAEVEQAELRAKALRIEAEA-ELEKLRKRQELELEYEQAQNELEIA-KAKELADIEATK 789
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2531-2965 |
3.54e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.44 E-value: 3.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2531 LELELNQLKNiaeethrSKEKAEQEAEKQRQLALEEEQRRKEAEEKvrkiladeqeaARQRKAALEEVERLKAKAeeakR 2610
Cdd:PRK10929 28 ITQELEQAKA-------AKTPAQAEIVEALQSALNWLEERKGSLER-----------AKQYQQVIDNFPKLSAEL----R 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2611 QKELAEKEAERQIQLAQEAAfkkieaeekahaaivqQKEQEMLQTRKQeksILDKlkeeaerAKRAAEDADYARMRAEQE 2690
Cdd:PRK10929 86 QQLNNERDEPRSVPPNMSTD----------------ALEQEILQVSSQ---LLEK-------SRQAQQEQDRAREISDSL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2691 AALSRQQVEeaermKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKrahAEQAALKQKQladEEMDkhkkfaektLRQ-KA 2769
Cdd:PRK10929 140 SQLPQQQTE-----ARRQLNEIERRLQTLGTPNTPLAQAQLTALQ---AESAALKALV---DELE---------LAQlSA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2770 QVEQELTKVKLQLEETDHQKtlLDDESQRLKEEVTDAMRQKAqvEEELfkvkiqmeeliklklrieeENKMLIMKDKDST 2849
Cdd:PRK10929 200 NNRQELARLRSELAKKRSQQ--LDAYLQALRNQLNSQRQREA--ERAL-------------------ESTELLAEQSGDL 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2850 QKFLAEEAEKMRQVAEEaarLSIEAQE----AARMRKLAEDDLANQRALAekMLKEKMQ------AIQEATRLKAE--AD 2917
Cdd:PRK10929 257 PKSIVAQFKINRELSQA---LNQQAQRmdliASQQRQAASQTLQVRQALN--TLREQSQwlgvsnALGEALRAQVArlPE 331
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2918 MLQKQK---ELAQEQARKFQ-ED---KEQIEQQLAKE-----TEGFQKSLEAERRQQLEI 2965
Cdd:PRK10929 332 MPKPQQldtEMAQLRVQRLRyEDllnKQPQLRQIRQAdgqplTAEQNRILDAQLRTQREL 391
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2750-2986 |
3.87e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2750 ADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIK 2829
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2830 -LKLRIEEENKMLIMKDKDSTQKFLaEEAEKMRQVAEEAARLsIEAQEAARmrklaeDDLANQRALAEkmlkekmQAIQE 2908
Cdd:COG3883 94 aLYRSGGSVSYLDVLLGSESFSDFL-DRLSALSKIADADADL-LEELKADK------AELEAKKAELE-------AKLAE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2909 ATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKA 2986
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2670-2768 |
3.89e-05 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 47.08 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2670 AERAKRAAEDADYARmRAEQEAALSRQQVEEaermkqraeEEAQAKAQAQ---DEAEKlRKEAELEAAKrAHAEQAALKQ 2746
Cdd:PRK05759 34 EERQKKIADGLAAAE-RAKKELELAQAKYEA---------QLAEARAEAAeiiEQAKK-RAAQIIEEAK-AEAEAEAARI 101
|
90 100
....*....|....*....|..
gi 1717010358 2747 KQLADEEMDKHKKFAEKTLRQK 2768
Cdd:PRK05759 102 KAQAQAEIEQERKRAREELRKQ 123
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1930-2093 |
4.53e-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: 48.38 E-value: 4.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEevskrevvavDAEQQKQTI-QQE 2008
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK----------YEEQLGNVRnNKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2009 LQQLRQnsdmEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRR 2088
Cdd:COG1579 91 YEALQK----EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 1717010358 2089 QVKDE 2093
Cdd:COG1579 167 ELAAK 171
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2045-2728 |
4.60e-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: 49.82 E-value: 4.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2045 RLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKD------ESQKKREAEEELKRKVQAEKDaarek 2118
Cdd:pfam10174 52 AARISVLKEQYRVTQEENQHLQLTIQALQDELRAQRDLNQLLQQDFTTspvdgeDKFSTPELTEENFRRLQSEHE----- 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2119 qRAMEDLQKFRSQAEEAERRM---KQAEVEKERQIKVAQEVAQ-----QSAAAELNSKRMSFAEKTAQ---LELSLKQEH 2187
Cdd:pfam10174 127 -RQAKELFLLRKTLEEMELRIetqKQTLGARDESIKKLLEMLQskglpKKSGEEDWERTRRIAEAEMQlghLEVLLDQKE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2188 ITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDaerearkrakae 2267
Cdd:pfam10174 206 KENIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDEVQMLKTNGLLHTEDREEE------------ 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2268 esaLRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKV 2347
Cdd:pfam10174 274 ---IKQMEVYKSHSKFMKNKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDAL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2348 R---AEMEILLESKSR-----AEEESRSNTEKS--KHMLEVEASKLRELAEeaaRLRALSEEAK-RQRQIAEgeaarqra 2416
Cdd:pfam10174 351 RlrlEEKESFLNKKTKqlqdlTEEKSTLAGEIRdlKDMLDVKERKINVLQK---KIENLQEQLRdKDKQLAG-------- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2417 eaeriLKEKLAAI-----NEATRLKTEAEiALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILL------ 2485
Cdd:pfam10174 420 -----LKERVKSLqtdssNTDTALTTLEE-ALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALqpelte 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2486 KKSSDNEL-ERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDL----ELEL---------NQLKNIAEETHRSKEK 2551
Cdd:pfam10174 494 KESSLIDLkEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLkkahNAEEavrtnpeinDRIRLLEQEVARYKEE 573
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2552 AEQ-EAEKQRQL-ALEEEQRRKEAEEKvrKILADEQEAARQRKAALEEVERLKAKAEEAKRqkelaekeaeRQIQLAQEA 2629
Cdd:pfam10174 574 SGKaQAEVERLLgILREVENEKNDKDK--KIAELESLTLRQMKEQNKKVANIKHGQQEMKK----------KGAQLLEEA 641
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2630 AFKKIEAEEKAHaaivQQKEQEMLQTRKQEKSILD--KLKEEAERAKRAAEDADYARMRAEQeaalsRQQVEEAERMKQR 2707
Cdd:pfam10174 642 RRREDNLADNSQ----QLQLEELMGALEKTRQELDatKARLSSTQQSLAEKDGHLTNLRAER-----RKQLEEILEMKQE 712
|
730 740 750
....*....|....*....|....*....|....*.
gi 1717010358 2708 A---------------EEEAQAKAQAQDEAEKLRKE 2728
Cdd:pfam10174 713 AllaaisekdaniallELSSSKKKKTQEEVMALKRE 748
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2703-2873 |
4.76e-05 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 49.71 E-value: 4.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2703 RMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAAlkQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQL 2782
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQ--QRQEARREREELQREEERLVQKEEQLDARAEKLDNLE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2783 EETDHQKTLLDDESQRLKEEvtdamrqKAQVEEELFKVKIQMEELIK------LKLRIEEENKMLIMKDKDSTQkFLAEE 2856
Cdd:PRK12705 105 NQLEEREKALSARELELEEL-------EKQLDNELYRVAGLTPEQARklllklLDAELEEEKAQRVKKIEEEAD-LEAER 176
|
170 180
....*....|....*....|....
gi 1717010358 2857 ------AEKMRQVAEE-AARLSIE 2873
Cdd:PRK12705 177 kaqnilAQAMQRIASEtASDLSVS 200
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
632-731 |
4.81e-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: 4.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 632 DRVQKKTFTKWVNKHLIKA--QRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLKHRQVK 707
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1717010358 708 LVNIRNDDIADGNPKLTLGLIWTI 731
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2567-2727 |
5.29e-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: 5.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2567 EQRRKEAEEKVRKI---LADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEA-AFKKIEAEEKAHA 2642
Cdd:COG1579 23 EHRLKELPAELAELedeLAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkEYEALQKEIESLK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2643 AIVQQKEQEMLQTRKQEKSILDKLKEEaeRAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEA 2722
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAEL--EAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPPELLALY 180
|
....*
gi 1717010358 2723 EKLRK 2727
Cdd:COG1579 181 ERIRK 185
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2440-2860 |
5.33e-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: 49.57 E-value: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2440 EIALKEKEAENERLRRLAEDEAYQR--KLLEEQATQHKQDIEEKIILLK--KSSDNELERQKNIVEDTLRQRRIIEEEIR 2515
Cdd:COG5185 130 IVALKDELIKVEKLDEIADIEASYGevETGIIKDIFGKLTQELNQNLKKleIFGLTLGLLKGISELKKAEPSGTVNSIKE 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2516 ILKLNfekaSSGKSDLELELNQLKNIaEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAAR----QR 2591
Cdd:COG5185 210 SETGN----LGSESTLLEKAKEIINI-EEALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKrlneNA 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2592 KAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAE 2671
Cdd:COG5185 285 NNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIE 364
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2672 rakraaedadyaRMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAeLEAAKRAHAEQAALKQKQLAD 2751
Cdd:COG5185 365 ------------NIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILAT-LEDTLKAADRQIEELQRQIEQ 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2752 -----EEMDKHKKFAEKTLRQKAQVEQELTKVKLQlEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEE 2826
Cdd:COG5185 432 atssnEEVSKLLNELISELNKVMREADEESQSRLE-EAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
410 420 430
....*....|....*....|....*....|....
gi 1717010358 2827 LIKlKLRIEEENKMLIMKDKDSTQKFLAEEAEKM 2860
Cdd:COG5185 511 QLE-GVRSKLDQVAESLKDFMRARGYAHILALEN 543
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2326-2784 |
5.66e-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: 49.64 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2326 LKNEVNEAiqKRKKMEEELAKVRAEMEilLESKSRAEEESRSNTEKSKHMlEVEASKLRELA-------------EEAAR 2392
Cdd:pfam05701 47 VQEEIPEY--KKQSEAAEAAKAQVLEE--LESTKRLIEELKLNLERAQTE-EAQAKQDSELAklrveemeqgiadEASVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2393 LRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKE-KEAEnERLRRLAEDEAYQRKLLEEQA 2471
Cdd:pfam05701 122 AKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSAsKEIE-KTVEELTIELIATKESLESAH 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2472 TQHKQDIEEKI--ILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLK--NIAEETHR 2547
Cdd:pfam05701 201 AAHLEAEEHRIgaALAREQDKLNWEKELKQAEEELQRLNQQLLSAKDLKSKLETASALLLDLKAELAAYMesKLKEEADG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2548 SKEKAEQEAEKQRQLAleeeQRRKEAEEKVRKIladeqEAARqrkaalEEVERLKAKAE--EAKRQKELAEKEAERQIQL 2625
Cdd:pfam05701 281 EGNEKKTSTSIQAALA----SAKKELEEVKANI-----EKAK------DEVNCLRVAAAslRSELEKEKAELASLRQREG 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2626 AQEAAFKKIEAE---EKAHAAIVQQKEQE----------MLQTRKQE----KSI-------LDKLKEEAERAKRAAEDAD 2681
Cdd:pfam05701 346 MASIAVSSLEAElnrTKSEIALVQAKEKEarekmvelpkQLQQAAQEaeeaKSLaqaareeLRKAKEEAEQAKAAASTVE 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2682 yARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRK-----EAELEAAKRAH-AEQAALKQKQLADEEMD 2755
Cdd:pfam05701 426 -SRLEAVLKEIEAAKASEKLALAAIKALQESESSAESTNQEDSPRGvtlslEEYYELSKRAHeAEELANKRVAEAVSQIE 504
|
490 500
....*....|....*....|....*....
gi 1717010358 2756 KHKKFAEKTLRQKAQVEQELTKVKLQLEE 2784
Cdd:pfam05701 505 EAKESELRSLEKLEEVNREMEERKEALKI 533
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2075-2302 |
5.70e-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: 49.07 E-value: 5.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2075 QKKAAQEEAERLRRQVKDESQKKREAEEELKR-KVQAEKDAAREKQRAMEdlQKFRSQAEEAERRMKQAEVEKERQIKVA 2153
Cdd:TIGR02794 44 DPGAVAQQANRIQQQKKPAAKKEQERQKKLEQqAEEAEKQRAAEQARQKE--LEQRAAAEKAAKQAEQAAKQAEEKQKQA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2154 QEVAQQSAAaelnskrmsfaEKTAQlelslkqehitvthlqEEAERLKKQheeaekareeaekeLEKWHQKANEALRLRL 2233
Cdd:TIGR02794 122 EEAKAKQAA-----------EAKAK----------------AEAEAERKA--------------KEEAAKQAEEEAKAKA 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2234 QAEEVAHKKTLAQEEAEKQKEDAEREARKRA-----KAEESALRQKELAEDELEKQRKLADATAQQKFSAEQEL 2302
Cdd:TIGR02794 161 AAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAeeakaKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAEL 234
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1689-2160 |
5.71e-05 |
|
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: 50.05 E-value: 5.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1689 EEVVKTYEDQLKEVHAVPSDSKELEATKAELKKLRSQ---VEGHQPLFNTL---------------------EADLNKAK 1744
Cdd:TIGR00606 618 EEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQramLAGATAVYSQFitqltdenqsccpvcqrvfqtEAELQEFI 697
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1745 DVNEQMLRSHSERdvdLDRYRERVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYDWLIKWIKDAKQR-------- 1816
Cdd:TIGR00606 698 SDLQSKLRLAPDK---LKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDieeqetll 774
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1817 -----QEQIQSVPITDSKTMKEQLLQLKKLLEEIESNRTKVD------ECQKYAKQYIDaiKDYELQLVTYKAQVEPVVS 1885
Cdd:TIGR00606 775 gtimpEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAKLQgsdldrTVQQVNQEKQE--KQHELDTVVSKIELNRKLI 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1886 PAKKPKVQ---STSDSIIQEYVDLRTRYSELTTLTSQYIKFITEtLCRLNVEEKAAeklkeeeRRRLAEVEAQLEKQTQL 1962
Cdd:TIGR00606 853 QDQQEQIQhlkSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTE-VQSLIREIKDA-------KEQDSPLETFLEKDQQE 924
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1963 AEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQkqtIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIH 2042
Cdd:TIGR00606 925 KEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENK---IQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMR 1001
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2043 IVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELkRKVQAEKDAAREKQRAM 2122
Cdd:TIGR00606 1002 LMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENI-DLIKRNHVLALGRQKGY 1080
|
490 500 510
....*....|....*....|....*....|....*...
gi 1717010358 2123 EDlQKFRSQAEEAERRMKQAEvEKERQIKVAQEVAQQS 2160
Cdd:TIGR00606 1081 EK-EIKHFKKELREPQFRDAE-EKYREMMIVMRTTELV 1116
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2450-2686 |
5.84e-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: 5.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2450 NERLRRLAEDEAYQRKLLEEQATQHKQDIEEkiillkksSDNELE--RQKNIVEDTLRQRRIIEEEIRILKLNFEKASSG 2527
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEE--------AEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2528 KSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEkvRKILADEQEAARQRKAALEEVERLKAKAee 2607
Cdd:COG3206 235 LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAEL--SARYTPNHPDVIALRAQIAALRAQLQQE-- 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2608 akRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQ-TRKQE--KSILDKLKEEAERAkRAAEDADYAR 2684
Cdd:COG3206 311 --AQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRlEREVEvaRELYESLLQRLEEA-RLAEALTVGN 387
|
..
gi 1717010358 2685 MR 2686
Cdd:COG3206 388 VR 389
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2328-3056 |
6.46e-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: 49.57 E-value: 6.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2328 NEVNEAIQKRKKMEEELAKVRaemEILLESKSRAEEESRSNTEKS--KHMLEVE-------------ASKLRE------- 2385
Cdd:COG3096 278 NERRELSERALELRRELFGAR---RQLAEEQYRLVEMARELEELSarESDLEQDyqaasdhlnlvqtALRQQEkieryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2386 -LAEEAARLRALS---EEAKRQRQIAEGEAARQRAEAERiLKEKLA---------------------AINEATRLKTEAE 2440
Cdd:COG3096 355 dLEELTERLEEQEevvEEAAEQLAEAEARLEAAEEEVDS-LKSQLAdyqqaldvqqtraiqyqqavqALEKARALCGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2441 IALKEKEAENERLRRlAEDEAYQRKLLEEQ----ATQHKQDIEEKIILLKKSSDnELERQKniVEDTLRQRRIIEEEIRI 2516
Cdd:COG3096 434 LTPENAEDYLAAFRA-KEQQATEEVLELEQklsvADAARRQFEKAYELVCKIAG-EVERSQ--AWQTARELLRRYRSQQA 509
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2517 LKLNFEKASSGKSDLELELNQLKN---IAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKA 2593
Cdd:COG3096 510 LAQRLQQLRAQLAELEQRLRQQQNaerLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQ 589
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2594 ALEEVERLKAKAEEAKRQKELAEKEAErqiQLAQEAAFKkieAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERA 2673
Cdd:COG3096 590 LRARIKELAARAPAWLAAQDALERLRE---QSGEALADS---QEVTAAMQQLLEREREATVERDELAARKQALESQIERL 663
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2674 KRAAEDADyARMRAEQEA----------------------AL---SRQQ--VEEAERMKQRAEEEA---------QAKAQ 2717
Cdd:COG3096 664 SQPGGAED-PRLLALAERlggvllseiyddvtledapyfsALygpARHAivVPDLSAVKEQLAGLEdcpedlyliEGDPD 742
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2718 AQDEAekLRKEAELEAAKRAHAEQAALkqkqladeemdKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQ 2797
Cdd:COG3096 743 SFDDS--VFDAEELEDAVVVKLSDRQW-----------RYSRFPEVPLFGRAAREKRLEELRAERDELAEQYAKASFDVQ 809
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2798 RLK-----------------------EEVTDAMRQKAQVEEELFKVKIQM----EELIKLKLRIEEENKML----IMKDK 2846
Cdd:COG3096 810 KLQrlhqafsqfvgghlavafapdpeAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLADE 889
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2847 DSTQKFlaEEAEKMRQVAEEAAR-----------------------LSIEAQEAARMRKLAEDDLANQRALAekmLKEKM 2903
Cdd:COG3096 890 TLADRL--EELREELDAAQEAQAfiqqhgkalaqleplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFA---LSEVV 964
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2904 Q-----AIQEATRLKAEA----DMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQkSLEAERRQQLEITAEAERlKL 2974
Cdd:COG3096 965 QrrphfSYEDAVGLLGENsdlnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ-EL 1042
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2975 QVLEMsKAQAKAEEDAKKFKKQaedfgnkLHQTELATKERmvvVQSLEIQRQQSGKEAEELRRAIAELEhekEKLKQEAE 3054
Cdd:COG3096 1043 EELGV-QADAEAEERARIRRDE-------LHEELSQNRSR---RSQLEKQLTRCEAEMDSLQKRLRKAE---RDYKQERE 1108
|
..
gi 1717010358 3055 LL 3056
Cdd:COG3096 1109 QV 1110
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2530-2774 |
6.55e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 48.37 E-value: 6.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2530 DLELELNQLKNIAEETHRSKEKAEQEAEKQRQlaleeeqRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAK 2609
Cdd:COG1340 12 ELEEKIEELREEIEELKEKRDELNEELKELAE-------KRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2610 RQKELAEKEAERQIQLAQEAAFKKIEaEEKAHAAIvqQKEQEMLQTR----KQEKSILDK---LKEEAERAKRAAEDADY 2682
Cdd:COG1340 85 EKLNELREELDELRKELAELNKAGGS-IDKLRKEI--ERLEWRQQTEvlspEEEKELVEKikeLEKELEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2683 ARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQD---EAEKLRKEAEL---------EAAKRAHAEQAALKQK-QL 2749
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIElykEADELRKEADElhkeiveaqEKADELHEEIIELQKElRE 241
|
250 260
....*....|....*....|....*
gi 1717010358 2750 ADEEMDKHKKFAEKTLRQKAQVEQE 2774
Cdd:COG1340 242 LRKELKKLRKKQRALKREKEKEELE 266
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1924-2052 |
6.93e-05 |
|
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: 48.45 E-value: 6.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1924 ITETLcRLNVEEKAAEKLK---EEERRRLAEVEAQLEKQtqlaeahaKAKAQAEKEAEELQRRMQEEVSKREvvavdAEQ 2000
Cdd:cd03406 160 IPEAI-RRNYEAMEAEKTKlliAEQHQKVVEKEAETERK--------RAVIEAEKDAEVAKIQMQQKIMEKE-----AEK 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2001 QKQTIQQELQQLRQnsdmeiKSKA-----KKIEEAEYNRRKIEEEIhivrLQLETMQ 2052
Cdd:cd03406 226 KISEIEDEMHLARE------KARAdaeyyRALREAEANKLKLTPEY----LELKKYQ 272
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4862-4898 |
6.94e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.85 E-value: 6.94e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1717010358 4862 DPNEETGPIAGILDTDTLEKVSITEAMHRNLVDNITG 4898
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2522-2627 |
7.34e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 49.56 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2522 EKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQR-KAALEEVER 2600
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAaETSQERKQK 217
|
90 100
....*....|....*....|....*....
gi 1717010358 2601 LKAKAEEAKRQKELAEKEAERQI--QLAQ 2627
Cdd:PRK11448 218 RKEITDQAAKRLELSEEETRILIdqQLRK 246
|
|
| 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 ... |
2034-2127 |
7.45e-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: 45.77 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2034 RRKIEEEIHIVRLQLETMQKQKASAEDELQELRAraeEAERQKKAAQEEAERLRRQVKDESQKKREAEEElkrkvQAEKD 2113
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAALAEAEQQLKEARA---EAQEIIENAKKRAEKLKEEIVAAAEAEAERIIE-----QAAAE 103
|
90
....*....|....
gi 1717010358 2114 AAREKQRAMEDLQK 2127
Cdd:pfam00430 104 IEQEKDRALAELRQ 117
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2566-2788 |
7.57e-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: 7.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2566 EEQRRKEAEEKVRKILADEQEAARQRKAAleevERLKAKAEEAKRQKelaeKEAERQIQLAQEaafkKIEAEEKahaaiv 2645
Cdd:pfam15709 312 EEERSEEDPSKALLEKREQEKASRDRLRA----ERAEMRRLEVERKR----REQEEQRRLQQE----QLERAEK------ 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2646 QQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYAR-MRAEQEAAlsRQQVEEAERMKQRAEEEAQAKAQAQDEAEK 2724
Cdd:pfam15709 374 MREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLqLQAAQERA--RQQQEEFRRKLQELQRKKQQEEAERAEAEK 451
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2725 LRKEaELEaakrahaEQAALKQKQLADE------EMDKHKKFAEKTLRQKAQ--VEQELTKVKLQLEETDHQ 2788
Cdd:pfam15709 452 QRQK-ELE-------MQLAEEQKRLMEMaeeerlEYQRQKQEAEEKARLEAEerRQKEEEAARLALEEAMKQ 515
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2098-2418 |
7.70e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.18 E-value: 7.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2098 REAEEELKRKVQAEKDAAREKQRAmeDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQqsAAAELNSKRMSFAEKTA 2177
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARF--EARQARLEREKAAREARHKKAAEARAAKDKDAVAA--ALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2178 QLELSLKQEhiTVTHLQEEAERLKKQheeaekareeaekelekwhqkanealrlrlqaeevAHKKTLAQEEAEKQKEDAE 2257
Cdd:PRK05035 508 IKAGARPDN--SAVIAAREARKAQAR-----------------------------------ARQAEKQAAAAADPKKAAV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2258 REARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEqelirlKADTESGEQQRLLLEEELFRLKNEVNEAIQKR 2337
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAK------KAAQQAASAEPEEQVAEVDPKKAAVAAAIARA 624
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2338 KKMEEELAKVraemeillesksrAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAegeAARQRAE 2417
Cdd:PRK05035 625 KAKKAEQQAN-------------AEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVA---AAIARAK 688
|
.
gi 1717010358 2418 A 2418
Cdd:PRK05035 689 A 689
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2536-2836 |
7.99e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 49.52 E-value: 7.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2536 NQLKNIAE-ETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADeqeAARQRKAALEEVERLKAKAEEAKRQ--- 2611
Cdd:PRK11281 43 AQLDALNKqKLLEAEDKLVQQDLEQTLALLDKIDRQKEETEQLKQQLAQ---APAKLRQAQAELEALKDDNDEETREtls 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2612 ----KELAEKEAERQIQLAQ------EAAFKKIEAE---EKAHAAIVQQkeqemlQTRKQEksIldklkeeaeRAKRAAE 2678
Cdd:PRK11281 120 tlslRQLESRLAQTLDQLQNaqndlaEYNSQLVSLQtqpERAQAALYAN------SQRLQQ--I---------RNLLKGG 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2679 DADYARMRAEQEAALSRQQVEEAERMKQRaEEEAQAKAQAQDEAEKLRKEAELEAAKRAH---AEQAALKQKQLADeemd 2755
Cdd:PRK11281 183 KVGGKALRPSQRVLLQAEQALLNAQNDLQ-RKSLEGNTQLQDLLQKQRDYLTARIQRLEHqlqLLQEAINSKRLTL---- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2756 khkkfAEKTLRQkAQVEQELTKVK---LQLEETDHQKTLlddeSQRLKEEvTDAMRQKAQveEELfKVKIQMEELIKLKL 2832
Cdd:PRK11281 258 -----SEKTVQE-AQSQDEAARIQanpLVAQELEINLQL----SQRLLKA-TEKLNTLTQ--QNL-RVKNWLDRLTQSER 323
|
....
gi 1717010358 2833 RIEE 2836
Cdd:PRK11281 324 NIKE 327
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2640-2879 |
8.13e-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: 48.61 E-value: 8.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2640 AHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADyarmRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQ 2719
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----ALERRIAALARRIRALEQELAALEAELAELEKEI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2720 DEAEKLRKEAELEAAKRAhaeQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRL 2799
Cdd:COG4942 93 AELRAELEAQKEELAELL---RALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2800 KEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEeenkmlimKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAAR 2879
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLE--------KELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2234-2422 |
8.46e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 8.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2234 QAEEVAHKKtlaQEEAEKQKEDaereARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAeqeliRLKADTESGE 2313
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQL----EKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAA-----KAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2314 QQRLLLEEELFRLKNEVNEAIQKR----KKMEEELAKVRAEMeillESKSRAEEESRSNTEK-SKHMLEVEASKLRELAE 2388
Cdd:PRK09510 156 AAAAAKKAAAEAKKKAEAEAAKKAaaeaKKKAEAEAAAKAAA----EAKKKAEAEAKKKAAAeAKKKAAAEAKAAAAKAA 231
|
170 180 190
....*....|....*....|....*....|....
gi 1717010358 2389 EAArlRALSEEAKRQRQIAEGEAARQRAEAERIL 2422
Cdd:PRK09510 232 AEA--KAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2277-2473 |
8.60e-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: 8.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2277 AEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEM----- 2351
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2352 ------------EILLESKSRAEEESRSntekskHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAE 2419
Cdd:COG3883 94 alyrsggsvsylDVLLGSESFSDFLDRL------SALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2420 RILKEKLAAINEATRLKteAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQ 2473
Cdd:COG3883 168 AAKAELEAQQAEQEALL--AQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA 219
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1944-2098 |
8.90e-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: 45.80 E-value: 8.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1944 EERRRLAEVEAQLEKQTQLAEAHakakaQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQtiQQELQQLRqnsdmeiksk 2023
Cdd:pfam05672 17 AEKRRQAREQREREEQERLEKEE-----EERLRKEELRRRAEEERARREEEARRLEEERR--REEEERQR---------- 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2024 aKKIEEAEYNRRKIEEEihivrlqLETMQKQKASAEDELQElRARAEEAERQKKAAQEEAERLRRQVKDESQKKR 2098
Cdd:pfam05672 80 -KAEEEAEEREQREQEE-------QERLQKQKEEAEAKARE-EAERQRQEREKIMQQEEQERLERKKRIEEIMKR 145
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2651-2756 |
8.93e-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: 45.51 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2651 EMLQTRKQEksILDKLkEEAERAKRAAEdadyaRMRAEQEAALsrqqvEEAErmKQRAEEEAQAKAQAQDEAEKLRKEAE 2730
Cdd:cd06503 26 KALDEREEK--IAESL-EEAEKAKEEAE-----ELLAEYEEKL-----AEAR--AEAQEIIEEARKEAEKIKEEILAEAK 90
|
90 100
....*....|....*....|....*..
gi 1717010358 2731 LEAAK-RAHAEQAALKQKQLADEEMDK 2756
Cdd:cd06503 91 EEAERiLEQAKAEIEQEKEKALAELRK 117
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1932-2114 |
8.93e-05 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 49.25 E-value: 8.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1932 NVEEKAAEKLKEEERRRLAE-VEAQLEKQTQLAEAHAKAKAQA-EKEAE-ELQR-RMQEEVSkrevvavdAEQQKQTIqq 2007
Cdd:PTZ00491 632 NVDVQSVEPVDERTRDSLQKsVQLAIEITTKSQEAAARHQAELlEQEARgRLERqKMHDKAK--------AEEQRTKL-- 701
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2008 eLQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEihivrlqletmqkqkasAEDELQELRARAE------EAERQKKAAQE 2081
Cdd:PTZ00491 702 -LELQAESAAVESSGQSRAEALAEAEARLIEAE-----------------AEVEQAELRAKALrieaeaELEKLRKRQEL 763
|
170 180 190
....*....|....*....|....*....|...
gi 1717010358 2082 EAERLRRQVKDESQKKREAEEELKRKVQAEKDA 2114
Cdd:PTZ00491 764 ELEYEQAQNELEIAKAKELADIEATKFERIVEA 796
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2976-3200 |
9.30e-05 |
|
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: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2976 VLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAEL 3055
Cdd:COG3883 4 LALAAPTPAFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3056 LQKNSQEMQVAQQEQLRQETQVLQ-------TTFLTEKHLLlekekyiekekAKLENLYEDEVRKAQKLKQEQEHQLKQL 3128
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVllgsesfSDFLDRLSAL-----------SKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 3129 EEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRKLREKLEQLEEEHRIALAQTR 3200
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1930-2120 |
9.84e-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: 48.22 E-value: 9.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQEL 2009
Cdd:COG4942 31 QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2010 QQLRQNSDM---------------------------EIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDEL 2062
Cdd:COG4942 111 RALYRLGRQpplalllspedfldavrrlqylkylapARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAAL 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2063 QELRARAEEA----ERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQR 2120
Cdd:COG4942 191 EALKAERQKLlarlEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALK 252
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
2555-2675 |
9.97e-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: 48.06 E-value: 9.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2555 EAEKQRQLALEEEQRRKEAEEKVrKILADEQEAARQRKAaleevERLKAKaeeakRQKELAEKEAERQIQLAQEAAFKKI 2634
Cdd:pfam07767 206 EAEKKRLKEEEKLERVLEKIAES-AATAEAREEKRKTKA-----QRNKEK-----RRKEEEREAKEEKALKKKLAQLERL 274
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1717010358 2635 EAEEKAhaaiVQQKEQEMLQTRKQEKSILDKLKEEAERAKR 2675
Cdd:pfam07767 275 KEIAKE----IAEKEKEREEKAEARKREKRKKKKEEKKLRP 311
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2052-2149 |
1.07e-04 |
|
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: 45.80 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2052 QKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKfrsQ 2131
Cdd:pfam05672 26 QREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQK---Q 102
|
90
....*....|....*...
gi 1717010358 2132 AEEAERRMkQAEVEKERQ 2149
Cdd:pfam05672 103 KEEAEAKA-REEAERQRQ 119
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2603-2759 |
1.10e-04 |
|
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: 45.80 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2603 AKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSildklKEEAERAKRAAEDADY 2682
Cdd:pfam05672 13 ARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEEERR-----REEEERQRKAEEEAEE 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2683 ARMRAEQEAALSRQQVEEAErmkqraeeeaqakAQAQDEAEKLRKEAELEAAKrahAEQAALKQKQLADEEMDKHKK 2759
Cdd:pfam05672 88 REQREQEEQERLQKQKEEAE-------------AKAREEAERQRQEREKIMQQ---EEQERLERKKRIEEIMKRTRK 148
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2714-2950 |
1.13e-04 |
|
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: 49.06 E-value: 1.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2714 AKAQAQDEAEKLRKEAeleaaKRAHAEQAALKQKQLADEEMDKHKKfaektlrQKAQVEQELTKVKLQLEETDHQKTLLD 2793
Cdd:NF012221 1536 ATSESSQQADAVSKHA-----KQDDAAQNALADKERAEADRQRLEQ-------EKQQQLAAISGSQSQLESTDQNALETN 1603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2794 DESQR--LKEE---VTDAMRQKAQVEEELFKVKIQMEEL-IKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQ----- 2862
Cdd:NF012221 1604 GQAQRdaILEEsraVTKELTTLAQGLDALDSQATYAGESgDQWRNPFAGGLLDRVQEQLDDAKKISGKQLADAKQrhvdn 1683
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2863 ---VAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQ---ARKFQED 2936
Cdd:NF012221 1684 qqkVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQdasAAENKAN 1763
|
250
....*....|....
gi 1717010358 2937 KEQIEQQLAKETEG 2950
Cdd:NF012221 1764 QAQADAKGAKQDES 1777
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2680-3135 |
1.14e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2680 ADYarMRAEQEAALSRQQVEEAERMKQRAEEEaqaKAQAQDEAEKLRKEAELEAAKRAHAEQaalkQKQLADEemdkHKK 2759
Cdd:PRK04863 272 ADY--MRHANERRVHLEEALELRRELYTSRRQ---LAAEQYRLVEMARELAELNEAESDLEQ----DYQAASD----HLN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2760 FAEKTLRQKAQVEQ---ELTKVKLQLEEtdhQKTLlddeSQRLKEEVTDAMRQKAQVEEELFKVKIQmeeLIKLKLRIEE 2836
Cdd:PRK04863 339 LVQTALRQQEKIERyqaDLEELEERLEE---QNEV----VEEADEQQEENEARAEAAEEEVDELKSQ---LADYQQALDV 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2837 ENKMLIMKDKdstQKFLAEEAEKMRQVAEEAARLSIEAQEAARmrklAEDDLANQRALaekMLKEKMQAIQEATRLKAEA 2916
Cdd:PRK04863 409 QQTRAIQYQQ---AVQALERAKQLCGLPDLTADNAEDWLEEFQ----AKEQEATEELL---SLEQKLSVAQAAHSQFEQA 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2917 DMLQKQ--KELAQEQA-RKFQEDKEQIEQQLAketegfqkslEAERRQQLeitaeaeRLKLQVLEMSKAQAKAEEdakkf 2993
Cdd:PRK04863 479 YQLVRKiaGEVSRSEAwDVARELLRRLREQRH----------LAEQLQQL-------RMRLSELEQRLRQQQRAE----- 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2994 kKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQ--EQL 3071
Cdd:PRK04863 537 -RLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDalARL 615
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 3072 RQETQVlqtTFLTEKHLllekekyiekeKAKLENLYEDEvRKAQKLKQEQEHQLKQLEEEKQQL 3135
Cdd:PRK04863 616 REQSGE---EFEDSQDV-----------TEYMQQLLERE-RELTVERDELAARKQALDEEIERL 664
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2058-2440 |
1.17e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2058 AEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDaarEKQRAMEDLQKfrsQAEEAER 2137
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLD---EEEAFLDRTAK---REERRQK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2138 RMKQAEvekERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLElslkqehitvthlQEEAERLKKQHEEAEKAREEAEKE 2217
Cdd:pfam02029 78 RLQEAL---ERQKEFDPTIADEKESVAERKENNEEEENSSWEK-------------EEKRDSRLGRYKEEETEIREKEYQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2218 LEKWHQKANEAlrlrlqAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESaLRQKELAEDELEKQRKLADATAQQkfs 2297
Cdd:pfam02029 142 ENKWSTEVRQA------EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKE-KKVKYESKVFLDQKRGHPEVKSQN--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2298 AEQELIRLKADTESgeqqrllleeelfrlknevneaiqkRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLE 2377
Cdd:pfam02029 212 GEEEVTKLKVTTKR-------------------------RQGGLSQSQEREEEAEVFLEAEQKLEELRRRRQEKESEEFE 266
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2378 VEASKLRELAEEAARLRALSEEakRQRQIAEGEAARQRAEAERILKEKlaaiNEATRLKTEAE 2440
Cdd:pfam02029 267 KLRQKQQEAELELEELKKKREE--RRKLLEEEEQRRKQEEAERKLREE----EEKRRMKEEIE 323
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
1864-2196 |
1.21e-04 |
|
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: 48.53 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1864 DAIKDYELQLVTYKAQVEPVVSPAKKPKV-QSTSDSIIQEYVDLRTRYSELTTLTSQ---YIKFITETLCRLNVEEKAAE 1939
Cdd:pfam05622 128 DKVKKLEATVETYKKKLEDLGDLRRQVKLlEERNAEYMQRTLQLEEELKKANALRGQletYKRQVQELHGKLSEESKKAD 207
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1940 KLKEEERRRLAEVEA-QLEKQTQLAEAHAKAKAQAEKEAEELQRR-------------MQEEVSKREVVAVDAEQQKQTI 2005
Cdd:pfam05622 208 KLEFEYKKLEEKLEAlQKEKERLIIERDTLRETNEELRCAQLQQAelsqadallspssDPGDNLAAEIMPAEIREKLIRL 287
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2006 QQELQQLR----QNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQE 2081
Cdd:pfam05622 288 QHENKMLRlgqeGSYRERLTELQQLLEDANRRKNELETQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKLEE 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2082 EAERLrRQVKDESQKKREAEEELKRKVQAEKdaAREKQRAMEDLQKFRSQAEEAERRMKQAeVEKERQ-IKVAQEVAQQS 2160
Cdd:pfam05622 368 HLEKL-HEAQSELQKKKEQIEELEPKQDSNL--AQKIDELQEALRKKDEDMKAMEERYKKY-VEKAKSvIKTLDPKQNPA 443
|
330 340 350
....*....|....*....|....*....|....*..
gi 1717010358 2161 AAAELNSKRMSFAEKTAQLE-LSLKQEHITVTHLQEE 2196
Cdd:pfam05622 444 SPPEIQALKNQLLEKDKKIEhLERDFEKSKLQREQEE 480
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1934-2161 |
1.21e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.05 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EEKAAEKLKEEERRRLAEVEAqlEKQTQLA-EAHAKAKAQAEKEAEELqrrmqEEVSKREVVAVDAEQQKQTIQQELQQL 2012
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHG--AEISKLEeENREKEKALPKNDDMTI-----EEAKRRAAAAAKAKAAALAKQKREGTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2013 RQNSDMEIKSKAKKIEEAEYN----RRKIEEEIHIVRLQLETMQKQKASAedelqELRARAEEAERQKKAAQEEAERLRR 2088
Cdd:PRK07735 84 EVTEEEKAKAKAKAAAAAKAKaaalAKQKREGTEEVTEEEKAAAKAKAAA-----AAKAKAAALAKQKREGTEEVTEEEE 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2089 QVKDESQKKREAEeelKRKVQAEKDAAREKQRAMEDLQKfRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSA 2161
Cdd:PRK07735 159 ETDKEKAKAKAAA---AAKAKAAALAKQKAAEAGEGTEE-VTEEEKAKAKAKAAAAAKAKAAALAKQKASQGN 227
|
|
| Apolipoprotein |
pfam01442 |
Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a ... |
1948-2118 |
1.31e-04 |
|
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: 46.10 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1948 RLAEVEAQLEK-QTQLAEAHAKAKAQAEKEAEELQRRMQEEVSK-REVVAVDAEQQKQTIQQELQQLRQnsdmEIKSKAK 2025
Cdd:pfam01442 5 SLDELSTYAEElQEQLGPVAQELVDRLEKETEALRERLQKDLEEvRAKLEPYLEELQAKLGQNVEELRQ----RLEPYTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2026 KIEEAeyNRRKIEEEIHIVRLQLETMQKQKASAEDELQE-LRARAEEAERQ-KKAAQEEAERLRRQVKDESQKKREAEEE 2103
Cdd:pfam01442 81 ELRKR--LNADAEELQEKLAPYGEELRERLEQNVDALRArLAPYAEELRQKlAERLEELKESLAPYAEEVQAQLSQRLQE 158
|
170
....*....|....*
gi 1717010358 2104 LKRKVQAEKDAAREK 2118
Cdd:pfam01442 159 LREKLEPQAEDLREK 173
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2529-2719 |
1.33e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2529 SDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEA--------------------- 2587
Cdd:COG3883 40 DALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYRSggsvsyldvllgsesfsdfld 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2588 --------ARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAfKKIEAEEKAHAAIVQQKEQEmLQTRKQE 2659
Cdd:COG3883 120 rlsalskiADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAK-AELEAQQAEQEALLAQLSAE-EAAAEAQ 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2660 KSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQ 2719
Cdd:COG3883 198 LAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2333-2703 |
1.36e-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: 48.21 E-value: 1.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2333 AIQKRKKMEEELAKvraemeILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAA 2412
Cdd:pfam09731 122 SEQEKEKALEEVLK------EAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISREKATDSALQKAEALAEKL 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2413 RQRAE-AERILKEKLAAINEATRLKTEAEI-ALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIIllkkssd 2490
Cdd:pfam09731 196 KEVINlAKQSEEEAAPPLLDAAPETPPKLPeHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVSIFP------- 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2491 nelERQKNIVEDTlrqrriieeeirilKLNFEKASSGKSDLELELNQL-KNIAEEthrskeKAEQEAEKQRQLaleeeqr 2569
Cdd:pfam09731 269 ---DIIPVLKEDN--------------LLSNDDLNSLIAHAHREIDQLsKKLAEL------KKREEKHIERAL------- 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2570 rkeaeekvrkiladEQEAARQRKAALEEVERLKAKAEEAKRQKELaekEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKE 2649
Cdd:pfam09731 319 --------------EKQKEELDKLAEELSARLEEVRAADEAQLRL---EFEREREEIRESYEEKLRTELERQAEAHEEHL 381
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2650 QEMLQTRKQE--KSILDKLKE--EAERAKRAAE-DADYARMRAEQEAALSRQQVEEAER 2703
Cdd:pfam09731 382 KDVLVEQEIElqREFLQDIKEkvEEERAGRLLKlNELLANLKGLEKATSSHSEVEDENR 440
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2348-2984 |
1.49e-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: 48.28 E-value: 1.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2348 RAEMEILLESKSRAEEESRSNTEKskHMLEVEASKLRELAE----EAARLRALSEEAKRQRQIAEGEAARQraeaerilk 2423
Cdd:pfam10174 127 RQAKELFLLRKTLEEMELRIETQK--QTLGARDESIKKLLEmlqsKGLPKKSGEEDWERTRRIAEAEMQLG--------- 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2424 eklaaineatrlktEAEIALKEKEAENERLRrlaedEAYQRKLlEEQATQHKQDIEEKIILLKKSSDNELERQKNIVEDT 2503
Cdd:pfam10174 196 --------------HLEVLLDQKEKENIHLR-----EELHRRN-QLQPDPAKTKALQTVIEMKDTKISSLERNIRDLEDE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2504 LrqrriieeeiRILKLNfekASSGKSDLELELNQLKNIAEETHRSKEKAEQeaekqrqlaLEEEQRRKEAE--------- 2574
Cdd:pfam10174 256 V----------QMLKTN---GLLHTEDREEEIKQMEVYKSHSKFMKNKIDQ---------LKQELSKKESEllalqtkle 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2575 ---------EKVRKILADEQEAARQRKAALE-EVERLKAKAEE-----AKRQKELAEKEAERQIqLAQEAAFKKIEAEEK 2639
Cdd:pfam10174 314 tltnqnsdcKQHIEVLKESLTAKEQRAAILQtEVDALRLRLEEkesflNKKTKQLQDLTEEKST-LAGEIRDLKDMLDVK 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2640 AHAAIVQQKEQEMLQTRKQEKS-ILDKLKEEAERAKRAAEDADYA-----RMRAEQEAALSRQQVEEAERMKQRAEEEAQ 2713
Cdd:pfam10174 393 ERKINVLQKKIENLQEQLRDKDkQLAGLKERVKSLQTDSSNTDTAlttleEALSEKERIIERLKEQREREDRERLEELES 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2714 AKAQAQD--------EAEKLRKEAELEAAKRAHAEQA---ALKQKQLADEEMDKHKKFAE----KTLRQKAQVEQELTKV 2778
Cdd:pfam10174 473 LKKENKDlkekvsalQPELTEKESSLIDLKEHASSLAssgLKKDSKLKSLEIAVEQKKEEcsklENQLKKAHNAEEAVRT 552
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2779 KlqlEETDHQKTLLDDESQRLKEEvtdAMRQKAQVEEELFKVK-IQMEELIKLKlRIEEENKMLIMKDKDSTQKflaeeA 2857
Cdd:pfam10174 553 N---PEINDRIRLLEQEVARYKEE---SGKAQAEVERLLGILReVENEKNDKDK-KIAELESLTLRQMKEQNKK-----V 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2858 EKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLK-EKMQAIQEATRLKAEAdmlqkqkelaqeqarkfqed 2936
Cdd:pfam10174 621 ANIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGAlEKTRQELDATKARLSS-------------------- 680
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 1717010358 2937 keqiEQQLAKETEGFQKSLEAERRQQLEitaeaerlklQVLEMsKAQA 2984
Cdd:pfam10174 681 ----TQQSLAEKDGHLTNLRAERRKQLE----------EILEM-KQEA 713
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4016-4047 |
1.49e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.49e-04
10 20 30
....*....|....*....|....*....|..
gi 1717010358 4016 KLLSAEKAVTGYKDPYSGKTISVFEAMKKGLI 4047
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1935-2158 |
1.51e-04 |
|
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: 47.97 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1935 EKAAEKLKEE--ERRRL-AEVEAQLEKQTQLAEAHAKAK-AQAEKEAEELQrrMQEEVSKREVVAVDAEQQKQTIQQELQ 2010
Cdd:pfam07888 160 KKAGAQRKEEeaERKQLqAKLQQTEEELRSLSKEFQELRnSLAQRDTQVLQ--LQDTITTLTQKLTTAHRKEAENEALLE 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2011 QLRQNSDMEIKSKAK------KIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRAR-AEEAERQKKAAQEEA 2083
Cdd:pfam07888 238 ELRSLQERLNASERKveglgeELSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARwAQERETLQQSAEADK 317
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2084 ERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQ 2158
Cdd:pfam07888 318 DRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2701-2930 |
1.53e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2701 AERMKQRAEEEAQAKAQAQDEAEKLRKEAEleaakRAHAEQAALKQKQL---ADEEmdkhkkfAEKTLRQKAQVEQELTK 2777
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELE-----EAEAALEEFRQKNGlvdLSEE-------AKLLLQQLSELESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2778 VKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKA--QVEEELFKVKIQMEELiklKLRIEEENKMLimkdkdstQKFLAE 2855
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQLAELEAELAEL---SARYTPNHPDV--------IALRAQ 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2856 EAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEAD--------MLQKQKELAQ 2927
Cdd:COG3206 300 IAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEvarelyesLLQRLEEARL 379
|
...
gi 1717010358 2928 EQA 2930
Cdd:COG3206 380 AEA 382
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3283-3321 |
1.62e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 41.93 E-value: 1.62e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 3283 YLKGKSSIAGLLLKPSNEKMSIYEATKRKLLTPGTALIL 3321
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2070-2300 |
1.62e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.85 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2070 EEAERQKKAAQEEAERLRRQVKDESQkkreaEEELKRKVQAEKDAaREKQRAMEDLQKFRSQAEEAERRmKQAEVEKERQ 2149
Cdd:PRK12704 38 EEAKRILEEAKKEAEAIKKEALLEAK-----EEIHKLRNEFEKEL-RERRNELQKLEKRLLQKEENLDR-KLELLEKREE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2150 ikvaqevaqqsaaaELNSKRMSfaektaqlelslkqehitVTHLQEEAERLKKQheeaekareeaekeLEKWHQKANEAL 2229
Cdd:PRK12704 111 --------------ELEKKEKE------------------LEQKQQELEKKEEE--------------LEELIEEQLQEL 144
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2230 rlrlqaEEVAhkkTLAQEEA-----EKQKEDAEREARKRAKAEEsalrqkELAEDELEKQRKLADATAQQKFSAEQ 2300
Cdd:PRK12704 145 ------ERIS---GLTAEEAkeillEKVEEEARHEAAVLIKEIE------EEAKEEADKKAKEILAQAIQRCAADH 205
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2731-2990 |
1.74e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2731 LEAAKRAHAEQaalkQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVtdamrqk 2810
Cdd:COG3883 6 LAAPTPAFADP----QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEI------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2811 AQVEEELFKVKIQMEELIK-LKLRIEEENKMLIMKDKDSTQKFLaEEAEKMRQVAEEAARLsIEAQEAARmrklaeDDLA 2889
Cdd:COG3883 75 AEAEAEIEERREELGERARaLYRSGGSVSYLDVLLGSESFSDFL-DRLSALSKIADADADL-LEELKADK------AELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2890 NQRALAEKMLKEKMQAIQEATRLKAEadmLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEA 2969
Cdd:COG3883 147 AKKAELEAKLAELEALKAELEAAKAE---LEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250 260
....*....|....*....|.
gi 1717010358 2970 ERLKLQVLEMSKAQAKAEEDA 2990
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAAAA 244
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2573-2788 |
1.81e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2573 AEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKElaekEAERQIQLAQEAAfKKIEAE-EKAHAAIVQQKEQ- 2650
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYN----ELQAELEALQAEI-DKLQAEiAEAEAEIEERREEl 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2651 -EMLQTRKQEKSILDKLKE--EAERAKRAAEDADYARMRAEQEAALSRQQ---VEEAERMKQRAEEEAQAKAQAQDEAEK 2724
Cdd:COG3883 89 gERARALYRSGGSVSYLDVllGSESFSDFLDRLSALSKIADADADLLEELkadKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2725 LRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQ 2788
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2024-2197 |
1.84e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 47.69 E-value: 1.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2024 AKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEE- 2102
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKp 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2103 ----ELKRKVQAEKDAAREKQRAMEDLQKfrsQAEEAERRMKQAEVEKERQIKvAQEVAQQSAAAELNSKRMSFAEKTAQ 2178
Cdd:pfam05262 264 adtsSPKEDKQVAENQKREIEKAQIEIKK---NDEEALKAKDHKAFDLKQESK-ASEKEAEDKELEAQKKREPVAEDLQK 339
|
170
....*....|....*....
gi 1717010358 2179 LELSLKQEhitVTHLQEEA 2197
Cdd:pfam05262 340 TKPQVEAQ---PTSLNEDA 355
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2530-2748 |
1.85e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 1.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2530 DLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAeekvrkILADEQEAARqrkAALEEVERLKAKAEEAK 2609
Cdd:COG1842 34 DMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLA------LEKGREDLAR---EALERKAELEAQAEALE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2610 RQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEMlqtrkQEKSildklkeeaerakraaedadyarmrAEQ 2689
Cdd:COG1842 105 AQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKA-----QEKV-------------------------NEA 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2690 EAALSRQQVEEA-ERMKQRAEEEaQAKAQAQDE---AEKLRKE-AELEAAKRAHAEQAALKQKQ 2748
Cdd:COG1842 155 LSGIDSDDATSAlERMEEKIEEM-EARAEAAAElaaGDSLDDElAELEADSEVEDELAALKAKM 217
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1930-2109 |
1.90e-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: 47.64 E-value: 1.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEEERRRLAEVeaQLEKQTQLAEahakakaQAEKEAEELQRRMQEEVSKREvvavdAEQQKQTIQQEL 2009
Cdd:pfam15709 367 QLERAEKMREELELEQQRRFEEI--RLRKQRLEEE-------RQRQEEEERKQRLQLQAAQER-----ARQQQEEFRRKL 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2010 QQLRQNSDMEIKSKAkkieEAEYNRRKIEEEihivRLQLETMQKQKASAEDELQELRARAEEAERqkkaAQEEAERLRRQ 2089
Cdd:pfam15709 433 QELQRKKQQEEAERA----EAEKQRQKELEM----QLAEEQKRLMEMAEEERLEYQRQKQEAEEK----ARLEAEERRQK 500
|
170 180
....*....|....*....|
gi 1717010358 2090 vkdESQKKREAEEELKRKVQ 2109
Cdd:pfam15709 501 ---EEEAARLALEEAMKQAQ 517
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2695-2917 |
1.93e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2695 RQQVEEAErmKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQE 2774
Cdd:PRK09510 66 RQQQQQKS--AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2775 LTKVKLqleetdhqktllDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEEliklKLRIEEENKmlimkdkdstQKFLA 2854
Cdd:PRK09510 144 AAKAKA------------EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA----KKKAEAEAA----------AKAAA 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2855 EEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEAD 2917
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2873-3193 |
1.97e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 1.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2873 EAQEAAR-MRKLAEDDLANQRALAEKmlkekmqAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGF 2951
Cdd:pfam02029 3 DEEEAAReRRRRAREERRRQKEEEEP-------SGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2952 QKSLE--AERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSG 3029
Cdd:pfam02029 76 QKRLQeaLERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3030 KEAEELRRAIAElEHEKEKLKQEAELLQKNSQEMQVA-------QQEQLRQETQVLQTTFLTEKHLLLEKEKYIEKEKAK 3102
Cdd:pfam02029 156 GEEEEDKSEEAE-EVPTENFAKEEVKDEKIKKEKKVKyeskvflDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3103 LENLYEDEVRKAQKLKQEQEHQLKQLE-EEKQQLKasmgeamKKQKEAEEsvrhkqdELHQLDKRRQEQEKLLADENRKL 3181
Cdd:pfam02029 235 EREEEAEVFLEAEQKLEELRRRRQEKEsEEFEKLR-------QKQQEAEL-------ELEELKKKREERRKLLEEEEQRR 300
|
330
....*....|....*.
gi 1717010358 3182 R----EKLEQLEEEHR 3193
Cdd:pfam02029 301 KqeeaERKLREEEEKR 316
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
2036-2181 |
2.10e-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: 45.83 E-value: 2.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2036 KIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKRE--AEEELKRKVQAEKD 2113
Cdd:pfam04012 19 KAEDPEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAALTKGNEelAREALAEKKSLEKQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2114 AAREK-----QRAMEDlqKFRSQAEEAERRMKQAEVEK------ERQIKVAQEVAQQSAAAELNSKRMSFAE-KTAQLEL 2181
Cdd:pfam04012 99 AEALEtqlaqQRSAVE--QLRKQLAALETKIQQLKAKKnllkarLKAAKAQEAVQTSLGSLSTSSATDSFERiEEKIEER 176
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3685-3719 |
2.13e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.13e-04
10 20 30
....*....|....*....|....*....|....*
gi 1717010358 3685 KLLSAEKAVTGYKDPYTGNTISLFQALKRGLIPNE 3719
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1933-2086 |
2.20e-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: 47.15 E-value: 2.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1933 VEEKAAEKLKEEERRRLAEVEAQLE--KQTQLAEAHAKAKAQAE-KEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQEl 2009
Cdd:TIGR02794 98 AAAEKAAKQAEQAAKQAEEKQKQAEeaKAKQAAEAKAKAEAEAErKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAE- 176
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2010 qqlrqnsdmeikSKAKKIEEAEynrRKIEEEiHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERL 2086
Cdd:TIGR02794 177 ------------AEAKAKAEAE---AKAKAE-EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDI 237
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1978-2143 |
2.31e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 47.55 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1978 EELQRRMQEEVSKREVVAVDAEQQKQTIQQElqqlrqnsdmEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMqkqkas 2057
Cdd:COG2433 383 EELIEKELPEEEPEAEREKEHEERELTEEEE----------EIRRLEEQVERLEAEVEELEAELEEKDERIERL------ 446
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2058 aEDELQELRARAEE---AERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQA-E 2133
Cdd:COG2433 447 -ERELSEARSEERReirKDREISRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEAiR 525
|
170
....*....|
gi 1717010358 2134 EAERRMKQAE 2143
Cdd:COG2433 526 RLEEEYGLKE 535
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
2383-2744 |
2.34e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.93 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2383 LRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAI---NEATRLKTEAEIALKEKEAENERLRRLAED 2459
Cdd:COG3899 747 LLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARayaNLGLLLLGDYEEAYEFGELALALAERLGDR 826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2460 EAYQRKLLEEQATQH-KQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILklnfekassgksDLELELNQL 2538
Cdd:COG3899 827 RLEARALFNLGFILHwLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAA------------LAAAAAAAA 894
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2539 KNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKE 2618
Cdd:COG3899 895 RLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAA 974
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2619 AERQIQLAQEAAfkKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQV 2698
Cdd:COG3899 975 AAAAAAAAAAAA--AAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAA 1052
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1717010358 2699 EEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAAL 2744
Cdd:COG3899 1053 AAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALA 1098
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2057-2127 |
2.49e-04 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 44.77 E-value: 2.49e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2057 SAEDELQELRARAEEAERQKK--AAQ--EEAERLRRQVKDEsqKKREAEEELKR-KVQAEKDAAREKQRAMEDLQK 2127
Cdd:PRK05759 49 RAKKELELAQAKYEAQLAEARaeAAEiiEQAKKRAAQIIEE--AKAEAEAEAARiKAQAQAEIEQERKRAREELRK 122
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1689-2131 |
2.57e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.75 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1689 EEVVKTYEDQLKEVHAVPSDSKELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKDVNEQMlRSHSERDVDLDryRERV 1768
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL-ERLKKRLTGLT--PEKL 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1769 QQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYDWLIKWIKDAKqRQEQIQSVPITDSKTmKEQLLQLKKLLEEIESN 1848
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAK-GKCPVCGRELTEEHR-KELLEEYTAELKRIEKE 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1849 RTKVDECQKYAKQY---IDAIKDYELQLVTYKAQVEPVVSPAKKPKVQSTSdsiiqeyvDLRTRYSELTTLTSQYIKFIT 1925
Cdd:PRK03918 468 LKEIEEKERKLRKElreLEKVLKKESELIKLKELAEQLKELEEKLKKYNLE--------ELEKKAEEYEKLKEKLIKLKG 539
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1926 EtlcrLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQ--EEVSKREVVAVDAEQQKQ 2003
Cdd:PRK03918 540 E----IKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKelEPFYNEYLELKDAEKELE 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2004 TIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEE-EIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEE 2082
Cdd:PRK03918 616 REEKELKKLEEELDKAFEELAETEKRLEELRKELEElEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2083 AERLRRQVKDESQKKREAE---------EELKRKVQAEKdaAREKQRAMEDLQKFRSQ 2131
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEklekalervEELREKVKKYK--ALLKERALSKVGEIASE 751
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1936-2152 |
2.67e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.51 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1936 KAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEvskrevvavdAEQQKQTIQQELQQLRQn 2015
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEK----------KEKLQEEEDKLLEEAEK- 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2016 sdmEIKskaKKIEEAeynrrkiEEEIHIVRLQLETMQKQKASA------EDELQELRARAEEAERQKKAAQEEAERLrrQ 2089
Cdd:PRK00409 574 ---EAQ---QAIKEA-------KKEADEIIKELRQLQKGGYASvkahelIEARKRLNKANEKKEKKKKKQKEKQEEL--K 638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2090 VKDE------SQK--------KREAEEE---LKRKVQaekdaarekqraMEDLQKFRSQAEEaERRMKQAEVEKERQIKV 2152
Cdd:PRK00409 639 VGDEvkylslGQKgevlsipdDKEAIVQagiMKMKVP------------LSDLEKIQKPKKK-KKKKPKTVKPKPRTVSL 705
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2857-3277 |
2.81e-04 |
|
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: 47.64 E-value: 2.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2857 AEKMRQvAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKE--KMQAIQEA--TRLKAEADMLQK-QKEL-AQEQA 2930
Cdd:COG3096 271 ADYMRH-ANERRELSERALELRRELFGARRQLAEEQYRLVEMAREleELSARESDleQDYQAASDHLNLvQTALrQQEKI 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2931 RKFQEDKEQIEQQLAketegfqksleaerrQQLEITAEAErlklQVLEMSKAQAK-AEEDAKKFKKQAEDFGNKLHqtel 3009
Cdd:COG3096 350 ERYQEDLEELTERLE---------------EQEEVVEEAA----EQLAEAEARLEaAEEEVDSLKSQLADYQQALD---- 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3010 atkermvVVQSLEIQRQQsgkeaeelrrAIAELEhEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLqttfLTEKHLL 3089
Cdd:COG3096 407 -------VQQTRAIQYQQ----------AVQALE-KARALCGLPDLTPENAEDYLAAFRAKEQQATEEV----LELEQKL 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3090 LEKEKYIEKEKAKLENLYE--DEVRKAQKLKQ---------EQEHQLKQLEEEKQQLkASMGEAMKKQKEAEE-----SV 3153
Cdd:COG3096 465 SVADAARRQFEKAYELVCKiaGEVERSQAWQTarellrryrSQQALAQRLQQLRAQL-AELEQRLRQQQNAERlleefCQ 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3154 RHKQ--DELHQLDKRRQEQEklladenrklrEKLEQLEEEHRIALAQTREMMIQTDDLAGSSQ--TKAMPNGRDAVDGLA 3229
Cdd:COG3096 544 RIGQqlDAAEELEELLAELE-----------AQLEELEEQAAEAVEQRSELRQQLEQLRARIKelAARAPAWLAAQDALE 612
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3230 QngmtelgfdgLRQKVTAEKLSNAGILN--KDTLEKLKRGQVTVEEISQR 3277
Cdd:COG3096 613 R----------LREQSGEALADSQEVTAamQQLLEREREATVERDELAAR 652
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2416-2643 |
2.82e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2416 AEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKiillkkssDNELER 2495
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA--------EAEIEE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2496 QKNIVEDTLRQRRIIEEEIRILKL---------------NFEKASSGKSDLELELNQLKNIAEEThrsKEKAEQEAEKQR 2560
Cdd:COG3883 84 RREELGERARALYRSGGSVSYLDVllgsesfsdfldrlsALSKIADADADLLEELKADKAELEAK---KAELEAKLAELE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2561 QLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKA 2640
Cdd:COG3883 161 ALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
...
gi 1717010358 2641 HAA 2643
Cdd:COG3883 241 AAA 243
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2589-2742 |
2.82e-04 |
|
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: 45.85 E-value: 2.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2589 RQRKAALEEVERLKAKAEEAKRQKELAEKEAERQiqlaqEAAFKKIEAEEKaHAAIVQQKEQEMLQTRKQEKSILDKLKE 2668
Cdd:pfam13904 51 RQPLEAYENWLAAKQRQRQKELQAQKEEREKEEQ-----EAELRKRLAKEK-YQEWLQRKARQQTKKREESHKQKAAESA 124
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2669 EAERAKRaaedadyARMRAEQEAalsRQQVEEAERMKQRaeeeaQAKAQAQDEAEKLRKEAELEAAKRAHAEQA 2742
Cdd:pfam13904 125 SKSLAKP-------ERKVSQEEA---KEVLQEWERKKLE-----QQQRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2554-3054 |
2.87e-04 |
|
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: 46.99 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2554 QEAEKQRQLALEEeqrrkeaeekvRKILADEQEAARQRKAALEEVERLKAKAeeAKRQKELaekeaERQIQLAQEAAFK- 2632
Cdd:pfam05622 17 HELDQQVSLLQEE-----------KNSLQQENKKLQERLDQLESGDDSGTPG--GKKYLLL-----QKQLEQLQEENFRl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2633 -------KIEAEEKAHAAIVQQKEQEMLQTRKQE----KSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQqveea 2701
Cdd:pfam05622 79 etarddyRIKCEELEKEVLELQHRNEELTSLAEEaqalKDEMDILRESSDKVKKLEATVETYKKKLEDLGDLRRQ----- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2702 erMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLaDEEMDKHKK--FAEKTLRQKAQVeqeLTKVK 2779
Cdd:pfam05622 154 --VKLLEERNAEYMQRTLQLEEELKKANALRGQLETYKRQVQELHGKL-SEESKKADKleFEYKKLEEKLEA---LQKEK 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2780 LQL-EETDHQKTLLDD----ESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKFLA 2854
Cdd:pfam05622 228 ERLiIERDTLRETNEElrcaQLQQAELSQADALLSPSSDPGDNLAAEIMPAEIREKLIRLQHENKMLRLGQEGSYRERLT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2855 EeaekMRQVAEEAARlsieaqeaaRMRKL-AEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQK-ELAQEQARK 2932
Cdd:pfam05622 308 E----LQQLLEDANR---------RKNELeTQNRLANQRILELQQQVEELQKALQEQGSKAEDSSLLKQKlEEHLEKLHE 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2933 FQEDKEQIEQQLAkETEGFQKSLEAERRQQLEitaeaERLKLQVLEMskaqAKAEEDAKKFKKQAEDFGNKL--HQTELA 3010
Cdd:pfam05622 375 AQSELQKKKEQIE-ELEPKQDSNLAQKIDELQ-----EALRKKDEDM----KAMEERYKKYVEKAKSVIKTLdpKQNPAS 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1717010358 3011 TKErmvvVQSLEIQRQQSGKEAEELrraiaELEHEKEKLKQEAE 3054
Cdd:pfam05622 445 PPE----IQALKNQLLEKDKKIEHL-----ERDFEKSKLQREQE 479
|
|
| CCDC47 |
pfam07946 |
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ... |
2567-2622 |
2.91e-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: 46.41 E-value: 2.91e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2567 EQRRKEAEEKVRKILADE-QEAARQRKAALEEVERLKAKAEE-AKRQKELAEKEAERQ 2622
Cdd:pfam07946 263 KKTREEEIEKIKKAAEEErAEEAQEKKEEAKKKEREEKLAKLsPEEQRKYEEKERKKE 320
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2065-2302 |
3.02e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 47.32 E-value: 3.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2065 LRARAEEAERQKKAAQEEAERLRRQVkdesqkkREAEEELKR--------KVQAEKDAAREKQRAMED-LQKFRSQAEEA 2135
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKEL-------EEAEAALEEfrqknglvDLSEEAKLLLQQLSELESqLAEARAELAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2136 ERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKqheeaekareeae 2215
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRA------------- 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2216 kelekwhQKANEALRLRLQAEevahkktlAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQK 2295
Cdd:COG3206 306 -------QLQQEAQRILASLE--------AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESL 370
|
....*..
gi 1717010358 2296 FSAEQEL 2302
Cdd:COG3206 371 LQRLEEA 377
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
1109-1203 |
3.06e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 43.09 E-value: 3.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1109 LRYLQELLSWVEENQRRINSAEWGVDLPSVESHLGSHRGLHQSIDEFRAKIERARADEAQI---SPGSRSSYRDYLGKLD 1185
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1717010358 1186 LQYAKLLNSSKSRLRHLE 1203
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2888-3192 |
3.07e-04 |
|
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: 46.73 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2888 LANQRALAEKMLKEKMQAiqeatrlkaEADMLQKQKELAQEQARKFQEDKEQIE--QQLAKETEGFQKSLEAERRQQLEI 2965
Cdd:pfam15905 50 PATARKVKSLELKKKSQK---------NLKESKDQKELEKEIRALVQERGEQDKrlQALEEELEKVEAKLNAAVREKTSL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2966 TAEAERLKLQVLEMSKA----QAKAEEDA--KKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAI 3039
Cdd:pfam15905 121 SASVASLEKQLLELTRVnellKAKFSEDGtqKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKV 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3040 AELEH---EKEKLKQEaellQKNSQEMQVAQQEQLRQETQVLQTtfltekhlllekekyiekekaklenlYEDEVRKAQK 3116
Cdd:pfam15905 201 AQLEEklvSTEKEKIE----EKSETEKLLEYITELSCVSEQVEK--------------------------YKLDIAQLEE 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 3117 LKQEQEHQLKQLeeeKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRKLREKLEQLEEEH 3192
Cdd:pfam15905 251 LLKEKNDEIESL---KQSLEEKEQELSKQIKDLNEKCKLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEH 323
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
628-732 |
3.19e-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: 43.59 E-value: 3.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 628 EDERdrvqkKTFTKWVNK---------HLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRM--RFH 689
Cdd:cd21294 5 EDER-----REFTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLINDSVPDTIdervlnkPPRKNKPlnNFQ 79
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1717010358 690 KLQNVQIALDYLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 732
Cdd:cd21294 80 MIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
2462-2785 |
3.32e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 47.24 E-value: 3.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2462 YQRKLLEEQATQHKQDIEEKIILlkKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSD------LELEL 2535
Cdd:PLN03188 947 HEHKLLKEKYENHPEVLRTKIEL--KRVQDELEHYRNFYDMGEREVLLEEIQDLRSQLQYYIDSSLPSArkrnslLKLTY 1024
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2536 NQLKNIAEETHRSKEKAEQEAEKQrqlaLEEEQRR-KEAEEK---VRKILADEQEAARqrkaALeeVERLKAKAEEAKRQ 2611
Cdd:PLN03188 1025 SCEPSQAPPLNTIPESTDESPEKK----LEQERLRwTEAESKwisLAEELRTELDASR----AL--AEKQKHELDTEKRC 1094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2612 KElaekEAERQIQLAQEAAFKKIEaeekaHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEA 2691
Cdd:PLN03188 1095 AE----ELKEAMQMAMEGHARMLE-----QYADLEEKHIQLLARHRRIQEGIDDVKKAAARAGVRGAESKFINALAAEIS 1165
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2692 ALSRQQveEAERMKQRAEEEAqAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFaEKTLRQKAQV 2771
Cdd:PLN03188 1166 ALKVER--EKERRYLRDENKS-LQAQLRDTAEAVQAAGELLVRLKEAEEALTVAQKRAMDAEQEAAEAY-KQIDKLKRKH 1241
|
330
....*....|....
gi 1717010358 2772 EQELTKVKLQLEET 2785
Cdd:PLN03188 1242 ENEISTLNQLVAES 1255
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1918-2506 |
3.36e-04 |
|
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: 47.35 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1918 SQYIKFITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQaEKEAEELQRRMQEEVSKREVVAVD 1997
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDE-ESDLERLKEEIEKSSKQRAMLAGA 661
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1998 AEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRrKIEEEIHIVRLQLETMQKQKASAEDELQEL----RARAEEAE 2073
Cdd:TIGR00606 662 TAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFIS-DLQSKLRLAPDKLKSTESELKKKEKRRDEMlglaPGRQSIID 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2074 RQKKAAQEEAERLRRQVKDESQKKR--EAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAevekerqik 2151
Cdd:TIGR00606 741 LKEKEIPELRNKLQKVNRDIQRLKNdiEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQ--------- 811
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2152 vaqevaqqsaAAELNSkrmsfaektAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRL 2231
Cdd:TIGR00606 812 ----------AAKLQG---------SDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSE 872
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2232 RLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTES 2311
Cdd:TIGR00606 873 KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKN 952
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2312 geqqrllLEEELFRLKNEVNEAIQKRKKMEE-ELAKVRAEMEILLESKSRAEEESRSNTEkskhmlEVEASKLRE--LAE 2388
Cdd:TIGR00606 953 -------IHGYMKDIENKIQDGKDDYLKQKEtELNTVNAQLEECEKHQEKINEDMRLMRQ------DIDTQKIQErwLQD 1019
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2389 EAARLRALSE--EAKRQRQIAEGEAARQRAEAERILKEKLAaiNEATRLKTEAEIAL-KEKEAENERLRrlaedeaYQRK 2465
Cdd:TIGR00606 1020 NLTLRKRENElkEVEEELKQHLKEMGQMQVLQMKQEHQKLE--ENIDLIKRNHVLALgRQKGYEKEIKH-------FKKE 1090
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1717010358 2466 LLEEQATQHKQDIEEKIILLK--KSSDNELERQKNIVEDTLRQ 2506
Cdd:TIGR00606 1091 LREPQFRDAEEKYREMMIVMRttELVNKDLDIYYKTLDQAIMK 1133
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1928-2303 |
3.39e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 47.02 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1928 LCRLNVEEKAAEKLKEEE--RRRLAEVEAQLEKQTQLAEAHAKAKAqAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTI 2005
Cdd:pfam03528 13 LEKENAEFYRLKQQLEAEfnQKRAKFKELYLAKEEDLKRQNAVLQE-AQVELDALQNQLALARAEMENIKAVATVSENTK 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2006 QQELQQLRQNSDMEIKSKAKKIEEAEynrRKIEEEIHIvRLQLETMQ--KQKASAEDELQELRARAEEAERQK------K 2077
Cdd:pfam03528 92 QEAIDEVKSQWQEEVASLQAIMKETV---REYEVQFHR-RLEQERAQwnQYRESAEREIADLRRRLSEGQEEEnledemK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2078 AAQEEAERLRRQVkdesqkkreaeeelkrkVQAEKDAAREKQRAMedlqkfrsqaeEAERRMKQAEVEKERQIKVAQEva 2157
Cdd:pfam03528 168 KAQEDAEKLRSVV-----------------MPMEKEIAALKAKLT-----------EAEDKIKELEASKMKELNHYLE-- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2158 qqsaaaelnskrmsfAEKTAQ--LELSLKQEHITVTHLQEEAERLKKQHEE---AEKAREEAEKELEKWHQKAN----EA 2228
Cdd:pfam03528 218 ---------------AEKSCRtdLEMYVAVLNTQKSVLQEDAEKLRKELHEvchLLEQERQQHNQLKHTWQKANdqflES 282
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2229 LRLRLQ----AEEVAHKKTLAQEEaEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELI 2303
Cdd:pfam03528 283 QRLLMRdmqrMESVLTSEQLRQVE-EIKKKDQEEHKRARTHKEKETLKSDREHTVSIHAVFSPAGVETSAPLSNVEEQI 360
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4387-4424 |
3.41e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.41e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1717010358 4387 LKLLDAQLATGGIIDPRFGFHLSLEISYQRGYLNRETY 4424
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1930-2170 |
3.50e-04 |
|
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: 46.45 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEEERRRlaevEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQEL 2009
Cdd:pfam13868 100 REQMDEIVERIQEEDQAEA----EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAER 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2010 QQLRQNSDMEIKSKAKKIEEAEYNRRKIEEeihiVRLQLETMQKQKASAEDELQELRARAEEAERQKKaAQEEAERLRRQ 2089
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQDEKAERDE----LRAKLYQEEQERKERQKEREEAEKKARQRQELQQ-AREEQIELKER 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2090 VKDESQKKREAEEELKRKVQAEKDaAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKR 2169
Cdd:pfam13868 251 RLAEEAEREEEEFERMLRKQAEDE-EIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRE 329
|
.
gi 1717010358 2170 M 2170
Cdd:pfam13868 330 R 330
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1950-2307 |
3.52e-04 |
|
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: 46.81 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1950 AEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQR-RMQEEVSKREVvavdaEQQKQTIQQELQQLRQnsdmEIKSKAKKIE 2028
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRdREQWERQRREL-----ESRVAELKEELRQSRE----KHEELEEKYK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2029 EAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAErqkkaaqEEAERLRRQVKDESQKKREAEEElKRKV 2108
Cdd:pfam07888 105 ELSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERE-------TELERMKERAKKAGAQRKEEEAE-RKQL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2109 QAEKDAAREKQRAM-EDLQKFRSQAEEaerrmkqaevekerqiKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEH 2187
Cdd:pfam07888 177 QAKLQQTEEELRSLsKEFQELRNSLAQ----------------RDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2188 ITVTHL---QEEAERLKKQHEEAEKAREEAEKELekwHQKANEALRLRLQAEEV-----------AHKKTLAQEEAEKQK 2253
Cdd:pfam07888 241 SLQERLnasERKVEGLGEELSSMAAQRDRTQAEL---HQARLQAAQLTLQLADAslalregrarwAQERETLQQSAEADK 317
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2254 EDAEREARKRAKAEES---ALRQKELAEDELEKQRklaDATAQQKFSAEQELIRLKA 2307
Cdd:pfam07888 318 DRIEKLSAELQRLEERlqeERMEREKLEVELGREK---DCNRVQLSESRRELQELKA 371
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
635-732 |
3.67e-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: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 635 QKKTFTKWVN---------KHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 701
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1717010358 702 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 732
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2300-2742 |
3.76e-04 |
|
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: 46.60 E-value: 3.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2300 QELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEM---EILLESKSRAEEESRSN-TEKSKHM 2375
Cdd:pfam19220 41 RELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLaklEAALREAEAAKEELRIElRDKTAQA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2376 ------LEVEASKLRELAEEaarLRALSEEAKrqrqiaEGEAARQRAEAERI-LKEKLAAIneatrlkteaeialkekEA 2448
Cdd:pfam19220 121 ealerqLAAETEQNRALEEE---NKALREEAQ------AAEKALQRAEGELAtARERLALL-----------------EQ 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2449 ENERLRRLAEDEAYQRKLLEeqatqhkqdieekiillKKSSDNELERqkniveDTLRQRRiieeeirilklnfekassgk 2528
Cdd:pfam19220 175 ENRRLQALSEEQAAELAELT-----------------RRLAELETQL------DATRARL-------------------- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2529 SDLELELnqlkniaeethrskekAEQEAEKQRQLALEEEQRrkEAEEKVRKILADEQEAARQRKAALeevERLKAKAEEA 2608
Cdd:pfam19220 212 RALEGQL----------------AAEQAERERAEAQLEEAV--EAHRAERASLRMKLEALTARAAAT---EQLLAEARNQ 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2609 KRQKELAEKEAER---QIQLAQEAAFKKIEAEEKAHAAIVQQKeQEMLQTRkqeksilDKLKEEAERAKRAAEDADYARM 2685
Cdd:pfam19220 271 LRDRDEAIRAAERrlkEASIERDTLERRLAGLEADLERRTQQF-QEMQRAR-------AELEERAEMLTKALAAKDAALE 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2686 RAEQEAALSRQQVEEAErmkQRAEEEAQAKAQAqdeAEKLRKEAELEAAKRAHAEQA 2742
Cdd:pfam19220 343 RAEERIASLSDRIAELT---KRFEVERAALEQA---NRRLKEELQRERAERALAQGA 393
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2823-3135 |
3.78e-04 |
|
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: 46.45 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2823 QMEELIKLKLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEK 2902
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2903 MQAIQEATRLKAEADmLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAER---RQQLEITAEAERLKLQVLEM 2979
Cdd:pfam13868 107 VERIQEEDQAEAEEK-LEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKekaEREEEREAEREEIEEEKERE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2980 SKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAE----- 3054
Cdd:pfam13868 186 IARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEeefer 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3055 LLQKNSQEMQVAQQEQLRQETQVLQTTFLTEKHLLLEKEKYiekekaklENLYEDEVRKAQKLKQEQEHQLKQLEEEKQQ 3134
Cdd:pfam13868 266 MLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQR--------AAEREEELEEGERLREEEAERRERIEEERQK 337
|
.
gi 1717010358 3135 L 3135
Cdd:pfam13868 338 K 338
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3610-3648 |
3.80e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.77 E-value: 3.80e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 3610 YLKGTTAIAGVLVEPTGEKLSFYDALKKNLLKPEVAYNL 3648
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2059-2396 |
3.90e-04 |
|
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: 47.25 E-value: 3.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2059 EDELQELRARAEEAERQKKAAQEEAERLRRQVkdesQKKREAEEELKRKV-QAEKDAAREKQRAMEDLQKFRSQAEEAER 2137
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQL----DQLKEQLQLLNKLLpQANLLADETLADRLEELREELDAAQEAQA 910
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2138 RMKQ---AEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLEL-SLKQEHITVTHL--QEEAERLKKQheeaekar 2211
Cdd:COG3096 911 FIQQhgkALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIfALSEVVQRRPHFsyEDAVGLLGEN-------- 982
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2212 eeaekelekwhQKANEALRLRL-QAEEVAHKKTLAQEEAEKQKEDAERE-----ARKRAKAEESALRQKELAEDELEkqr 2285
Cdd:COG3096 983 -----------SDLNEKLRARLeQAEEARREAREQLRQAQAQYSQYNQVlaslkSSRDAKQQTLQELEQELEELGVQ--- 1048
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2286 klADATAQQKfsAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEES 2365
Cdd:COG3096 1049 --ADAEAEER--ARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVQAKAGWCAVLRLA 1124
|
330 340 350
....*....|....*....|....*....|....*
gi 1717010358 2366 R-SNTEKSKH---MLEVEASKLRELAEEAarLRAL 2396
Cdd:COG3096 1125 RdNDVERRLHrreLAYLSADELRSMSDKA--LGAL 1157
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2357-2622 |
3.95e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2357 SKSRAEEESRSNTEKSKhmLEVEASKLRELAEEAARLrALSEEAKRQRQiAEGEAARQRAEAEriLKEKLAAINEATRLK 2436
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAK--ARFEARQARLEREKAARE-ARHKKAAEARA-AKDKDAVAAALAR--VKAKKAAATQPIVIK 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2437 TEAEIALKEKEAEnERLRRLAEDEAYQRKLLEEQATQHKQDIEEKI--ILLKKSSDNELERQKNIVEDTLRQRRIIEEEI 2514
Cdd:PRK05035 510 AGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDPKKAAVAAAIAR 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2515 RILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAeekvrkiLADEQEAARQRKAA 2594
Cdd:PRK05035 589 AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-------VAAAIARAKARKAA 661
|
250 260 270
....*....|....*....|....*....|....
gi 1717010358 2595 LEEVERLKAKAEEAKRQK------ELAEKEAERQ 2622
Cdd:PRK05035 662 QQQANAEPEEAEDPKKAAvaaaiaRAKAKKAAQQ 695
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2920-3054 |
4.12e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.34 E-value: 4.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2920 QKQKELAQEQArKFQEDKEQIEQQLAKETEGfQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEED-AKKFKKQAE 2998
Cdd:PRK09510 87 QQAEELQQKQA-AEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKrAAAAAKKAA 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2999 DFGNKLHQTELATKermvvvqsleiQRQQSGKEAEELRRAIAELEhEKEKLKQEAE 3054
Cdd:PRK09510 165 AEAKKKAEAEAAKK-----------AAAEAKKKAEAEAAAKAAAE-AKKKAEAEAK 208
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2770-3084 |
4.13e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.93 E-value: 4.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2770 QVEQELTKVKLQ-LEETDHQKTLLDDESQRLK-----EEVTDAMRQKAQVEEELFKVKIQMEELIKlKLRIEEENKMLIM 2843
Cdd:COG3206 60 LVEPQSSDVLLSgLSSLSASDSPLETQIEILKsrpvlERVVDKLNLDEDPLGEEASREAAIERLRK-NLTVEPVKGSNVI 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2844 kdkdsTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKL--AEDDLANQRALAEKMLKEKMQAIQEaTRLKAEADMLQK 2921
Cdd:COG3206 139 -----EISYTSPDPELAAAVANALAEAYLEQNLELRREEArkALEFLEEQLPELRKELEEAEAALEE-FRQKNGLVDLSE 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2922 QKELAQEQARKFQEDKEQIEQQLAkETEGFQKSLEAERRQQLEITAEAERLK-LQVLEMSKAQAKAEEDakkfkKQAEDF 3000
Cdd:COG3206 213 EAKLLLQQLSELESQLAEARAELA-EAEARLAALRAQLGSGPDALPELLQSPvIQQLRAQLAELEAELA-----ELSARY 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3001 GNKlHQTELATKERMvvvQSLEIQ-RQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLR--QETQV 3077
Cdd:COG3206 287 TPN-HPDVIALRAQI---AALRAQlQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRleREVEV 362
|
....*..
gi 1717010358 3078 LQTTFLT 3084
Cdd:COG3206 363 ARELYES 369
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1757-2280 |
4.18e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 4.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1757 RDVDLDRYRERVQQLLERWQAILVQIDLRQRELDQLGRQLRYYRETYDWLIKWIKDAKQRQEQIQSvpitdsktmkeqll 1836
Cdd:COG4717 44 RAMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEA-------------- 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1837 qlkklleeiesnrtKVDECQKYAKQYIDAIKDYELqlvtykaqvepvvspakkpkvqstsdsiIQEYVDLRTRYSELTTl 1916
Cdd:COG4717 110 --------------ELEELREELEKLEKLLQLLPL----------------------------YQELEALEAELAELPE- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1917 tsqyikfitetlcRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvav 1996
Cdd:COG4717 147 -------------RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA---- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1997 DAEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRA--------R 2068
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFlvlgllalL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2069 AEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKR---KVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVE 2145
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPALEELEEEELEELLAAlglPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELE 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2146 KERQIKVAQ----EVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQE--EAERLKKQHEEAEKAREEAEKELE 2219
Cdd:COG4717 370 QEIAALLAEagveDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEalDEEELEEELEELEEELEELEEELE 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2220 KWHQK--ANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDE 2280
Cdd:COG4717 450 ELREElaELEAELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4275-4313 |
4.37e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.77 E-value: 4.37e-04
10 20 30
....*....|....*....|....*....|....*....
gi 1717010358 4275 YLYGTGCVAGIQIPTTKEIISFYQALKRGLISPEVAHAL 4313
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2536-2755 |
4.42e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.55 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2536 NQLKNIAEETHRSKEKAEQEAEKQRQlALEEeqrrkeAEEKVRKILADEQ--EAARQRKAALEEVERLKAKAEEAKRQke 2613
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRK-ELEE------AEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAE-- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2614 LAEKEAERQiQLAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEE-----AERAKRAAEDADYA----R 2684
Cdd:COG3206 235 LAEAEARLA-ALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNhpdviALRAQIAALRAQLQqeaqR 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2685 MRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHaeQAALKQKQLADEEMD 2755
Cdd:COG3206 314 ILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVARELY--ESLLQRLEEARLAEA 382
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1710-2134 |
4.43e-04 |
|
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: 46.87 E-value: 4.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1710 KELEATKAELKKLRSQVEGHQPLFNTLEADLNKAKD----VNEQMlrSHSERdvdLDRYRERVQQLLERWQAILVQIDLR 1785
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhlnlVQTAL--RQQEK---IERYQEDLEELTERLEEQEEVVEEA 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1786 QRELDQLGRQLRYYRETYDWLIKWIKDAKQrqeqiqsvpitdsktmkeqllqlkklleeiesnrtKVDECQKYAKQYIDA 1865
Cdd:COG3096 374 AEQLAEAEARLEAAEEEVDSLKSQLADYQQ-----------------------------------ALDVQQTRAIQYQQA 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1866 IKDYElqlvtyKAQV---EPVVSPAKKPKVQSTS----DSIIQEYVDLRTRYSELTTLTSQYIKFItETLCRLN--VEEK 1936
Cdd:COG3096 419 VQALE------KARAlcgLPDLTPENAEDYLAAFrakeQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAgeVERS 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1937 AAEKLKEEERRRLAEVEAQLEKQTQLAEAHakakAQAEKEAEELQ--RRMQEEVSKREVVAVDAEQQKQTIQQELQQLRq 2014
Cdd:COG3096 492 QAWQTARELLRRYRSQQALAQRLQQLRAQL----AELEQRLRQQQnaERLLEEFCQRIGQQLDAAEELEELLAELEAQL- 566
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2015 nsdmeikskakkiEEAEynrrkieeeihivrLQLETMQKQKASAEDELQELRARAEEAERQKKA---AQEEAERLRRQVK 2091
Cdd:COG3096 567 -------------EELE--------------EQAAEAVEQRSELRQQLEQLRARIKELAARAPAwlaAQDALERLREQSG 619
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1717010358 2092 DESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEE 2134
Cdd:COG3096 620 EALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIER 662
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1937-2290 |
4.49e-04 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 46.89 E-value: 4.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1937 AAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNS 2016
Cdd:COG4995 103 LAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAALALLAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2017 DMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQK 2096
Cdd:COG4995 183 LLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAA 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2097 KREAEEELKRkvQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKT 2176
Cdd:COG4995 263 ALLLLAALAA--LAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLA 340
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2177 AQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDA 2256
Cdd:COG4995 341 AAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAALALLL 420
|
330 340 350
....*....|....*....|....*....|....
gi 1717010358 2257 EREARKRAKAEESALRQKELAEDELEKQRKLADA 2290
Cdd:COG4995 421 ALAAYAAARLALLALIEYIILPDRLYAFVQLYQL 454
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2278-2659 |
4.51e-04 |
|
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: 46.43 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2278 EDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLES 2357
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2358 KSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRqrqiaegeAARQRAEAErilkeklaaineatrlkT 2437
Cdd:pfam07888 117 KDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKK--------AGAQRKEEE-----------------A 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2438 EAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSsdNELERQKNIVEDTLRQrriIEEEIRIL 2517
Cdd:pfam07888 172 ERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL--TTAHRKEAENEALLEE---LRSLQERL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2518 KLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEK--QRQLALEEEQRRKEAEekvRKILADEQEAARQRKAAL 2595
Cdd:pfam07888 247 NASERKVEGLGEELSSMAAQRDRTQAELHQARLQAAQLTLQlaDASLALREGRARWAQE---RETLQQSAEADKDRIEKL 323
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2596 -EEVERLKAKAEEAKRQKELAEKE--AERQIQLAQEAAFKKIEAEEKAhAAIVQQKEQEMLQTRKQE 2659
Cdd:pfam07888 324 sAELQRLEERLQEERMEREKLEVElgREKDCNRVQLSESRRELQELKA-SLRVAQKEKEQLQAEKQE 389
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2410-2788 |
4.54e-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: 46.82 E-value: 4.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2410 EAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDE--------AYQRKLLEEQATQHKQDIEEK 2481
Cdd:pfam15964 325 EAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKElasqqekrAQEKEALRKEMKKEREELGAT 404
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2482 IILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHrsKEKAEQEAEKQRQ 2561
Cdd:pfam15964 405 MLALSQNVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCGEMRYQLNQTKMKKDEAE--KEHREYRTKTGRQ 482
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2562 LALEEEQRRK---EAEEKVRKILADEQEAARQRKAALEEVERLKakaeEAKRQKELAEKEaerqiqlaQEAAFKKIEAEE 2638
Cdd:pfam15964 483 LEIKDQEIEKlglELSESKQRLEQAQQDAARAREECLKLTELLG----ESEHQLHLTRLE--------KESIQQSFSNEA 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2639 KAHAAIVQQKEQEMLQTRKQEKSILDklKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQA 2718
Cdd:pfam15964 551 KAQALQAQQREQELTQKMQQMEAQHD--KTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEITQKSRSEVEQLSQEKEYL 628
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2719 QDEAEKLRKE-AELEAAKRAHAEQAALKQKQLadEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQ 2788
Cdd:pfam15964 629 QDRLEKLQKRnEELEEQCVQHGRMHERMKQRL--RQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQS 697
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1938-2097 |
4.56e-04 |
|
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: 46.67 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1938 AEKLKEEERRRLAEVEAQLEKQTQLA-EAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNS 2016
Cdd:pfam07111 511 AREQGEAERQQLSEVAQQLEQELQRAqESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQEKVAEVETRL 590
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2017 DMEIKSKAKKIEEAeynRRKIEEEIhivrLQLETMQKQKASAEDELQELRARAEEAERqkkaaqEEAERLRRQVKDESQK 2096
Cdd:pfam07111 591 REQLSDTKRRLNEA---RREQAKAV----VSLRQIQHRATQEKERNQELRRLQDEARK------EEGQRLARRVQELERD 657
|
.
gi 1717010358 2097 K 2097
Cdd:pfam07111 658 K 658
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2048-2163 |
4.67e-04 |
|
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: 43.20 E-value: 4.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2048 LETMQKQKASAEDELQELRARAEEAERqkkaAQEEAERLRRQVKDESQKKREaeeelkrkvQAEKDAAREKQRAMEDLQk 2127
Cdd:cd06503 25 LKALDEREEKIAESLEEAEKAKEEAEE----LLAEYEEKLAEARAEAQEIIE---------EARKEAEKIKEEILAEAK- 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1717010358 2128 frsqaEEAERRMKQAEVEKERQIKVA-----QEVAQQSAAA 2163
Cdd:cd06503 91 -----EEAERILEQAKAEIEQEKEKAlaelrKEVADLAVEA 126
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2250-2448 |
4.72e-04 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 46.13 E-value: 4.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2250 EKQKEDAEREARKRAKAEE----SALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFR 2325
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEArkrlVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2326 LKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTE-KSKHMLEVEASKLRELAEEAARLRALSEEAKRQR 2404
Cdd:PRK07735 84 EVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKaKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKE 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1717010358 2405 QIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEA 2448
Cdd:PRK07735 164 KAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKA 207
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2520-2838 |
4.76e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2520 NFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVE 2599
Cdd:COG4372 32 QLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2600 RLKAKAEEAKRQKELAEKEAerqiqlaqeaafKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAED 2679
Cdd:COG4372 112 ELQEELEELQKERQDLEQQR------------KQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2680 ADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKK 2759
Cdd:COG4372 180 EAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKE 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2760 FAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEEN 2838
Cdd:COG4372 260 IEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAE 338
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
2547-2723 |
5.07e-04 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 46.57 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2547 RSKEKAEQEAEKQRQLalEEEQRRKEAEekvrkilADEQEAARQRKAALEEVErlKAKAEEAKRQKELAEKEAERQ---I 2623
Cdd:PRK10811 620 RRDTRDNRTRREGREN--REENRRNRRQ-------AQQQTAETRESQQAEVTE--KARTQDEQQQAPRRERQRRRNdekR 688
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2624 QLAQEAafKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAer 2703
Cdd:PRK10811 689 QAQQEA--KALNVEEQSVQETEQEERVQQVQPRRKQRQLNQKVRIEQSVAEEAVAPVVEETVAAEPVVQEVPAPRTEL-- 764
|
170 180
....*....|....*....|
gi 1717010358 2704 mkqrAEEEAQAKAQAQDEAE 2723
Cdd:PRK10811 765 ----VKVPLPVVAQTAPEQD 780
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1940-2149 |
5.39e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 45.67 E-value: 5.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1940 KLKEEERRRLAEVEAQLEKQTQLAEAHAKaKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQelqqlrqnsdme 2019
Cdd:COG1340 75 ELKEERDELNEKLNELREELDELRKELAE-LNKAGGSIDKLRKEIERLEWRQQTEVLSPEEEKELVEK------------ 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2020 IKSKAKKIEEAEyNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKRE 2099
Cdd:COG1340 142 IKELEKELEKAK-KALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE 220
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2100 AEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQ 2149
Cdd:COG1340 221 AQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
1999-2186 |
5.48e-04 |
|
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: 46.38 E-value: 5.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1999 EQQKQTIQQELQQLRQNsDMEIKSKAKKIEEAEYNRRKieeeihivrlqlETMQKQKasaedELQELRARAEEAERQKKA 2078
Cdd:pfam09726 401 EQDIKKLKAELQASRQT-EQELRSQISSLTSLERSLKS------------ELGQLRQ-----ENDLLQTKLHNAVSAKQK 462
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2079 AQEEAERLRRQVKDESQKKREAE----EELKRKVQAEKDAAREKQRAM----EDLQKFRSQAEEAERRMKQAEVE---KE 2147
Cdd:pfam09726 463 DKQTVQQLEKRLKAEQEARASAEkqlaEEKKRKKEEEATAARAVALAAasrgECTESLKQRKRELESEIKKLTHDiklKE 542
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1717010358 2148 RQIKVAQEVAQQSAAAELNSKR----MS----FAEKTAQLELSLKQE 2186
Cdd:pfam09726 543 EQIRELEIKVQELRKYKESEKDtevlMSalsaMQDKNQHLENSLSAE 589
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2683-3141 |
5.52e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2683 ARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEK---LRKEAELEAAKRAHAEQAAlkqKQLADEemdkhkk 2759
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQviaLRRAGGLEAALALVRSGEG---KALMDE------- 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2760 faektLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENK 2839
Cdd:COG5278 154 -----IRARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2840 MLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADML 2919
Cdd:COG5278 229 LAALELLAALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLL 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2920 QKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAED 2999
Cdd:COG5278 309 AAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAV 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3000 FGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQ 3079
Cdd:COG5278 389 ELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEEL 468
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 3080 TTFLTEKHLLLEKEKYIEKEKAKLENLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGE 3141
Cdd:COG5278 469 AAVAALAALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2327-2635 |
6.07e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 6.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2327 KNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEEsrsnTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQI 2406
Cdd:COG4372 30 SEQLRKALFELDKLQEELEQLREELEQAREELEQLEEE----LEQARSELEQLEEELEELNEQLQAAQAELAQAQEELES 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2407 AEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLK 2486
Cdd:COG4372 106 LQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQAL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2487 KSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEE 2566
Cdd:COG4372 186 DELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELEL 265
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2567 EQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIE 2635
Cdd:COG4372 266 AILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAI 334
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2532-2706 |
6.12e-04 |
|
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: 46.17 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2532 ELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRR-KEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKR 2610
Cdd:pfam05667 305 KLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQlEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEK 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2611 QKELAEK------EAERQIQ----LAQEAAFKKIEAE---EKAHAAIVQQKEQEMLQTRKQE---KSILDKLKEEAERAK 2674
Cdd:pfam05667 385 QYKVKKKtldllpDAEENIAklqaLVDASAQRLVELAgqwEKHRVPLIEEYRALKEAKSNKEdesQRKLEEIKELREKIK 464
|
170 180 190
....*....|....*....|....*....|..
gi 1717010358 2675 RAAEDadyARMRAEqeaaLSRQQVEEAERMKQ 2706
Cdd:pfam05667 465 EVAEE---AKQKEE----LYKQLVAEYERLPK 489
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
2077-2678 |
6.25e-04 |
|
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: 46.17 E-value: 6.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2077 KAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAareKQRAMEDLQKFRSQAEEAERRMKQAEVEkERQIKvaqev 2156
Cdd:pfam05701 27 KAHRIQTVERRKLVELELEKVQEEIPEYKKQSEAAEAA---KAQVLEELESTKRLIEELKLNLERAQTE-EAQAK----- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2157 aQQSAAAELNSKRMsfaEKTAQLELSlkqehitvTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAE 2236
Cdd:pfam05701 98 -QDSELAKLRVEEM---EQGIADEAS--------VAAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2237 EVAHKKTLAQEEAEKQKEDAEREARKRAKAEESAlrqkELAEDELEKQRKLADATAQQKFS--------AEQELIRLKAD 2308
Cdd:pfam05701 166 KRAEEAVSASKEIEKTVEELTIELIATKESLESA----HAAHLEAEEHRIGAALAREQDKLnwekelkqAEEELQRLNQQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2309 TESgeqqrllleeeLFRLKNEVNEAiqkrkkmEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHML-EVEASKLRELA 2387
Cdd:pfam05701 242 LLS-----------AKDLKSKLETA-------SALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIqAALASAKKELE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2388 EEAARLRALSEEAKRQRQIaegeAARQRAEAERiLKEKLAAINeatRLKTEAEIALKEKEAENERLRrlAEDEAYQRKll 2467
Cdd:pfam05701 304 EVKANIEKAKDEVNCLRVA----AASLRSELEK-EKAELASLR---QREGMASIAVSSLEAELNRTK--SEIALVQAK-- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2468 eeqatqHKQDIEEKIILLKKssdneLERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHR 2547
Cdd:pfam05701 372 ------EKEAREKMVELPKQ-----LQQAAQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKA 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2548 SKEKAEQEAEkqrqlALEEEQRRKEAEEKVrkiladeqEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQ 2627
Cdd:pfam05701 441 SEKLALAAIK-----ALQESESSAESTNQE--------DSPRGVTLSLEEYYELSKRAHEAEELANKRVAEAVSQIEEAK 507
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2628 EAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAE 2678
Cdd:pfam05701 508 ESELRSLEKLEEVNREMEERKEALKIALEKAEKAKEGKLAAEQELRKWRAE 558
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1946-2124 |
6.26e-04 |
|
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: 45.49 E-value: 6.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1946 RRRLAEVEAQLEK-QTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAeqQKQTIQQELQQLRQNsdmeikska 2024
Cdd:pfam00529 57 QAALDSAEAQLAKaQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQA--AVKAAQAQLAQAQID--------- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2025 kkieeaeYNRRKIEEEI-HIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKR-EAEE 2102
Cdd:pfam00529 126 -------LARRRVLAPIgGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIaEAEA 198
|
170 180
....*....|....*....|..
gi 1717010358 2103 ELKrkvQAEKDAAREKQRAMED 2124
Cdd:pfam00529 199 ELK---LAKLDLERTEIRAPVD 217
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4274-4310 |
6.33e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 6.33e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1717010358 4274 KYLYGTGCVAGIQIPTTKEIISFYQALKRGLISPEVA 4310
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2530-2802 |
6.55e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.87 E-value: 6.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2530 DLELELNQLKNIAEETHRSKEKAEQEAEKQRQ------LALEEEQRRKEAeekVRKILADEQEAAR-QRKAALEEVERLK 2602
Cdd:pfam03528 5 DLQQRVAELEKENAEFYRLKQQLEAEFNQKRAkfkelyLAKEEDLKRQNA---VLQEAQVELDALQnQLALARAEMENIK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2603 AKAEEAKRQKELAEKEAERQIQ---LAQEAAFKKI--EAEEKAHAAIVQQKEQEMLQTRKQEKSILD---KLKEEAERA- 2673
Cdd:pfam03528 82 AVATVSENTKQEAIDEVKSQWQeevASLQAIMKETvrEYEVQFHRRLEQERAQWNQYRESAEREIADlrrRLSEGQEEEn 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2674 -----KRAAEDADYAR---MRAEQEAALSRQQVEEAE---------RMKQ-----RAEEEAQA------------KAQAQ 2719
Cdd:pfam03528 162 ledemKKAQEDAEKLRsvvMPMEKEIAALKAKLTEAEdkikeleasKMKElnhylEAEKSCRTdlemyvavlntqKSVLQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2720 DEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRL 2799
Cdd:pfam03528 242 EDAEKLRKELHEVCHLLEQERQQHNQLKHTWQKANDQFLESQRLLMRDMQRMESVLTSEQLRQVEEIKKKDQEEHKRART 321
|
...
gi 1717010358 2800 KEE 2802
Cdd:pfam03528 322 HKE 324
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2048-2163 |
6.80e-04 |
|
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: 43.24 E-value: 6.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2048 LETMQKQKASAEDELqelraraEEAERQKKAAQEEAERLRRQVkdesqkkREAEEELKRKV-QAEKDAAREKQRAMEDLQ 2126
Cdd:COG0711 26 LKALDERQEKIADGL-------AEAERAKEEAEAALAEYEEKL-------AEARAEAAEIIaEARKEAEAIAEEAKAEAE 91
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 2127 kfrsqaEEAERRMKQAEVEKERQIKVAQEVAQQSAAA 2163
Cdd:COG0711 92 ------AEAERIIAQAEAEIEQERAKALAELRAEVAD 122
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1930-2104 |
6.84e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEeerrRLAEVEAQLEKQTQLAEahakakaQAEKEAEELQRRMQEEVSKREVvavdAEQQKQTIQQEL 2009
Cdd:PRK04863 979 MLAKNSDLNEKLRQ----RLEQAEQERTRAREQLR-------QAQAQLAQYNQVLASLKSSYDA----KRQMLQELKQEL 1043
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2010 QQL--RQNSDMEIKSKAKkieeaeynRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAE--- 2084
Cdd:PRK04863 1044 QDLgvPADSGAEERARAR--------RDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVnak 1115
|
170 180
....*....|....*....|....
gi 1717010358 2085 ----RLRRQVKDESQKKREAEEEL 2104
Cdd:PRK04863 1116 agwcAVLRLVKDNGVERRLHRREL 1139
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2034-2158 |
6.97e-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: 6.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2034 RRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLrrqvkdeSQKKREAEEELKRKVQAEKD 2113
Cdd:pfam20492 1 REEAEREKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEM 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1717010358 2114 AAREKQRAMEDLQKFRSQAE--EAERRMKQAEVEKERQIKVAQEVAQ 2158
Cdd:pfam20492 74 EAEEKEQLEAELAEAQEEIArlEEEVERKEEEARRLQEELEEAREEE 120
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1856-2199 |
7.12e-04 |
|
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: 46.10 E-value: 7.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1856 QKYAKQYIDAIKDYELQLVTYKAQVEPVVSpAKKPKVQSTSDSIIQEYvDLRTRYSELTTLTSQYIKFITETLCRLNVEE 1935
Cdd:COG5185 165 FGKLTQELNQNLKKLEIFGLTLGLLKGISE-LKKAEPSGTVNSIKESE-TGNLGSESTLLEKAKEIINIEEALKGFQDPE 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1936 KAAEKLKEEERR-----------RLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQ-----------EEVSKREV 1993
Cdd:COG5185 243 SELEDLAQTSDKleklveqntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKsidikkateslEEQLAAAE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1994 VAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRL--QLETMQKQKASAEDELQELRARAEE 2071
Cdd:COG5185 323 AEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSseELDSFKDTIESTKESLDEIPQNQRG 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2072 A--------ERQKKAAQEEAERLRRQVKdesQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQA-EEAERRMKQA 2142
Cdd:COG5185 403 YaqeilatlEDTLKAADRQIEELQRQIE---QATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAyDEINRSVRSK 479
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2143 EVEKERQI-KVAQEVAQQSAAAELNSKRMS-----FAEKTAQLELSLKQEHITVTHLQEEAER 2199
Cdd:COG5185 480 KEDLNEELtQIESRVSTLKATLEKLRAKLErqlegVRSKLDQVAESLKDFMRARGYAHILALE 542
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
3041-3197 |
7.29e-04 |
|
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: 45.39 E-value: 7.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3041 ELEHEKEKLKQEAELLQKNSQEMQVAQQeQLRQETQVLQTTFLTEKHLllekekyiekeKAKLENLYEDEVRKAQ-KLKQ 3119
Cdd:smart00787 148 GLDENLEGLKEDYKLLMKELELLNSIKP-KLRDRKDALEEELRQLKQL-----------EDELEDCDPTELDRAKeKLKK 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3120 EQEH------QLKQLEEEKQQLKASMGEAMKKQKEAEesvrhkqDELHQLDKRRQEQEKLLADENRKLREKLEQLEEEHR 3193
Cdd:smart00787 216 LLQEimikvkKLEELEEELQELESKIEDLTNKKSELN-------TEIAEAEKKLEQCRGFTFKEIEKLKEQLKLLQSLTG 288
|
....
gi 1717010358 3194 IALA 3197
Cdd:smart00787 289 WKIT 292
|
|
| ZUO1 |
COG5269 |
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / ... |
2565-2682 |
7.80e-04 |
|
Ribosome-associated chaperone zuotin [Translation, ribosomal structure and biogenesis / Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 227594 [Multi-domain] Cd Length: 379 Bit Score: 45.41 E-value: 7.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2565 EEEQRRKEAEEKVRKILADE--QEAARQRK---AALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKiEAEEK 2639
Cdd:COG5269 191 EERDRKRYSEAKNREKRAKLknQDNARLKRlvqIAKKRDPRIKSFKEQEKEMKKIRKWEREAGARLKALAALKG-KAEAK 269
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1717010358 2640 AHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERA-KRAAEDADY 2682
Cdd:COG5269 270 NKAEIEAEALASATAVKKKAKEVMKKALKMEKKAiKNAAKDADY 313
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2539-2678 |
7.88e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 7.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2539 KNIAEEthrsKEKAEQEAEKQRQLALEEEQRRKEAEEKvrkiladEQEAARQRKAALEEVERLKAKAEEAKRQkelAEKE 2618
Cdd:PRK00409 509 KLIGED----KEKLNELIASLEELERELEQKAEEAEAL-------LKEAEKLKEELEEKKEKLQEEEDKLLEE---AEKE 574
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2619 AERQIQLAQEAAFKKI-EAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAE 2678
Cdd:PRK00409 575 AQQAIKEAKKEADEIIkELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQE 635
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
2856-2989 |
8.01e-04 |
|
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: 44.97 E-value: 8.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2856 EAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRalaekmlkekMQAIQEATRlKAEADMLQKQKELA--QEQARKF 2933
Cdd:pfam12037 77 KIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKR----------YQDQLEAQR-RRNEELLRKQEESVakQEAMRIQ 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2934 QEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKlqvLEMSKAQAKAEED 2989
Cdd:pfam12037 146 AQRRQTEEHEAELRRETERAKAEAEAEARAKEERENEDLN---LEQLREKANEERE 198
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2859-3029 |
8.25e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 45.47 E-value: 8.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2859 KMRQVAEEAARLSIEAQEAARmRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKE 2938
Cdd:PRK12705 27 KRQRLAKEAERILQEAQKEAE-EKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2939 QIEQQLAK--ETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKF-KKQAEDFgnKLHQTELATKerm 3015
Cdd:PRK12705 106 QLEEREKAlsARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRvKKIEEEA--DLEAERKAQN--- 180
|
170
....*....|....
gi 1717010358 3016 VVVQSleIQRQQSG 3029
Cdd:PRK12705 181 ILAQA--MQRIASE 192
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
3031-3191 |
8.43e-04 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 45.84 E-value: 8.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3031 EAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQTTFLTEKhlllekekyiekekaklenlyeDE 3110
Cdd:COG0542 412 ELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEK----------------------EL 469
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3111 VRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRhkqdelhqldkrrqEQE--------------KLLAD 3176
Cdd:COG0542 470 IEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT--------------EEDiaevvsrwtgipvgKLLEG 535
|
170
....*....|....*
gi 1717010358 3177 EnrklREKLEQLEEE 3191
Cdd:COG0542 536 E----REKLLNLEEE 546
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2641-3085 |
8.51e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.06 E-value: 8.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2641 HAAIVQQKEQEMLQTRKQEKSILDKLKeeaeraKRAAEDADYARMRAEQEAALS-----RQQVEEAERMKQRAEEEAQAK 2715
Cdd:PRK11281 23 SSAFARAASNGDLPTEADVQAQLDALN------KQKLLEAEDKLVQQDLEQTLAlldkiDRQKEETEQLKQQLAQAPAKL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2716 AQAQDEAEKLRKEAELEAAKRAhaeqAALKQKQLadeemdkhkkfaEKTLrqkAQVEQELTKVKLQLEETDHQKTLLDDE 2795
Cdd:PRK11281 97 RQAQAELEALKDDNDEETRETL----STLSLRQL------------ESRL---AQTLDQLQNAQNDLAEYNSQLVSLQTQ 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2796 SQRLKEEVTDAMRQKAQVEEELFKVKIQmeeliKLKLRIEEENKMLImkdkdsTQKFLAEEAEKMRQVAEEAARLSIEAQ 2875
Cdd:PRK11281 158 PERAQAALYANSQRLQQIRNLLKGGKVG-----GKALRPSQRVLLQA------EQALLNAQNDLQRKSLEGNTQLQDLLQ 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2876 E-----AARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADmLQKQKELAQEQARkfqedKEQIEQQLAKETEG 2950
Cdd:PRK11281 227 KqrdylTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAAR-IQANPLVAQELEI-----NLQLSQRLLKATEK 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2951 ----FQKSLEAerRQQLEITAEAER-LKLQV------LEMSK---AQAKAEEDAKKFKKQAEDFGN-KLHQTELaTKERM 3015
Cdd:PRK11281 301 lntlTQQNLRV--KNWLDRLTQSERnIKEQIsvlkgsLLLSRilyQQQQALPSADLIEGLADRIADlRLEQFEI-NQQRD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3016 VVVQSLE----IQRQQSGKEAEELRRAIAELehekekLKQEAELL-----QKNSQ-----EMQVAQQeQLRQETQVLQTT 3081
Cdd:PRK11281 378 ALFQPDAyidkLEAGHKSEVTDEVRDALLQL------LDERRELLdqlnkQLNNQlnlaiNLQLNQQ-QLLSVSDSLQST 450
|
....
gi 1717010358 3082 fLTE 3085
Cdd:PRK11281 451 -LTQ 453
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2375-2671 |
8.68e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 8.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2375 MLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAarqraeaeRILKEKLAAINEATR-LKTEAEIALKEKEAENERL 2453
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEEL--------KELAEKRDELNAQVKeLREEAQELREKRDELNEKV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2454 RRLAE--DEAYQR-KLLEEQATQHKQDIEEkiILLKKSSDNELERQKNIVEDTLrqrriieeEIRILKLNFEKassgksD 2530
Cdd:COG1340 74 KELKEerDELNEKlNELREELDELRKELAE--LNKAGGSIDKLRKEIERLEWRQ--------QTEVLSPEEEK------E 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2531 LELELNQLKNIAEEthrsKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKI--LADE-QEAARQRKAALEEVERLKAKAEE 2607
Cdd:COG1340 138 LVEKIKELEKELEK----AKKALEKNEKLKELRAELKELRKEAEEIHKKIkeLAEEaQELHEEMIELYKEADELRKEADE 213
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2608 AKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQEmlqtRKQEKSILDKLKEEAE 2671
Cdd:COG1340 214 LHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALK----REKEKEELEEKAEEIF 273
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1998-2161 |
8.69e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.54 E-value: 8.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1998 AEQQKQTIQQELQQLRQNSDMEIKSKAKKIEeaeynrRKIEEEIHIVRLQLEtmqKQKASAEDELQELRARAEEAERQKK 2077
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKKEAEAIKKEAL------LEAKEEIHKLRNEFE---KELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2078 AAQEEAERLRRQVKDESQKKREAEEELKRKvQAEKDAAREKQRA-MEDLQKFrsQAEEAERRM-----KQAEVEKERQIK 2151
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKK-EEELEELIEEQLQeLERISGL--TAEEAKEILlekveEEARHEAAVLIK 176
|
170
....*....|
gi 1717010358 2152 VAQEVAQQSA 2161
Cdd:PRK12704 177 EIEEEAKEEA 186
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1977-2680 |
8.86e-04 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 45.84 E-value: 8.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1977 AEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSK-AKKIEEA-------EYNRRKIEEeihIVRLQL 2048
Cdd:COG5022 748 ATRIQRAIRGRYLRRRYLQALKRIKKIQVIQHGFRLRRLVDYELKWRlFIKLQPLlsllgsrKEYRSYLAC---IIKLQK 824
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2049 ETMQKQKASAEDElQELRARAEE--------AERQKKAAQEEAERLRRQVKDESQKKReaeeelkRKVQAEKDAARE--- 2117
Cdd:COG5022 825 TIKREKKLRETEE-VEFSLKAEVliqkfgrsLKAKKRFSLLKKETIYLQSAQRVELAE-------RQLQELKIDVKSiss 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2118 -KQRAMEDLQK---FRSQAEEAERRMKQ------AEVEK---ERQIKVAQ--EVAQQSAAAELNSKRMSFAEKTAQLELS 2182
Cdd:COG5022 897 lKLVNLELESEiieLKKSLSSDLIENLEfkteliARLKKllnNIDLEEGPsiEYVKLPELNKLHEVESKLKETSEEYEDL 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2183 LKQEHITVthlqeeaERLKKQheeaekareeaEKELEKWHQKANEAL--RLRLQAEEVAHKktlaqeeaEKQKEDAEREA 2260
Cdd:COG5022 977 LKKSTILV-------REGNKA-----------NSELKNFKKELAELSkqYGALQESTKQLK--------ELPVEVAELQS 1030
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2261 RKRAKAEESALRQKELAEDELEKQRKLadatAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKm 2340
Cdd:COG5022 1031 ASKIISSESTELSILKPLQKLKGLLLL----ENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEVTN- 1105
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2341 eEELAKVRAEMEILL--ESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEA 2418
Cdd:COG5022 1106 -RNLVKPANVLQFIVaqMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPPPFAALSEKRLYQ 1184
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2419 ERILKEKLAA------------INEATRLKTEAEIALKEKEAENERLRRLAEDEAYQ--RKLLEEQATQHKQDIeEKIIL 2484
Cdd:COG5022 1185 SALYDEKSKLsssevndlknelIALFSKIFSGWPRGDKLKKLISEGWVPTEYSTSLKgfNNLNKKFDTPASMSN-EKLLS 1263
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2485 LKKSSDNELE---RQKNIVEDTLRQRRIIEEEIRilklnFEKASSGKSDLELElnQLKNIAEETHRSKEKAEQEAEKQRQ 2561
Cdd:COG5022 1264 LLNSIDNLLSsykLEEEVLPATINSLLQYINVGL-----FNALRTKASSLRWK--SATEVNYNSEELDDWCREFEISDVD 1336
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2562 LALEEEQRRKEAEEKVRKILADEQEAARQRKAALE-EVERLKAKAE----EAKRQKELAEK-EAERQIQLAQEAAFKKIE 2635
Cdd:COG5022 1337 EELEELIQAVKVLQLLKDDLNKLDELLDACYSLNPaEIQNLKSRYDpadkENNLPKEILKKiEALLIKQELQLSLEGKDE 1416
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 1717010358 2636 AEEKAHAAIVQQKEQEMLQTR-KQEKSILDKLKEEAERAKRAAEDA 2680
Cdd:COG5022 1417 TEVHLSEIFSEEKSLISLDRNsIYKEEVLSSLSALLTKEKIALLDR 1462
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2766-3074 |
8.97e-04 |
|
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: 45.29 E-value: 8.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2766 RQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKD 2845
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2846 KDSTQKFLAEEAEKMRQVAEEAARL------SIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKAEADML 2919
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLreeideFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2920 QKQKELAQEQARKfQEDKEQIEQQLAKETEGfqkslEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEd 2999
Cdd:pfam13868 184 REIARLRAQQEKA-QDEKAERDELRAKLYQE-----EQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEA- 256
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 3000 fgnklhQTELATKERMVVVQSLEIQRQQsgKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQE 3074
Cdd:pfam13868 257 ------EREEEEFERMLRKQAEDEEIEQ--EEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREE 323
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2911-3074 |
9.14e-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: 45.71 E-value: 9.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2911 RLKAEAdmlQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQleitAEAERLKLQVLEMSKAQAKAEEDA 2990
Cdd:pfam15709 337 RLRAER---AEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRR----FEEIRLRKQRLEEERQRQEEEERK 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2991 KKFKKQAEDFGNKLHQTELATKermvvVQSLEIQRQQsgkeaEELRRAIAELEHEKE---KLKQEAELLQKNSQEMQVAQ 3067
Cdd:pfam15709 410 QRLQLQAAQERARQQQEEFRRK-----LQELQRKKQQ-----EEAERAEAEKQRQKElemQLAEEQKRLMEMAEEERLEY 479
|
....*..
gi 1717010358 3068 QEQLRQE 3074
Cdd:pfam15709 480 QRQKQEA 486
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4350-4386 |
9.76e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 9.76e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1717010358 4350 RLLSAERAVTGYRDPYSEQMISLFQAMKKDLIPSEQA 4386
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| HflC |
COG0330 |
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational ... |
2041-2161 |
9.94e-04 |
|
Regulator of protease activity HflC, stomatin/prohibitin superfamily [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440099 [Multi-domain] Cd Length: 279 Bit Score: 44.45 E-value: 9.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2041 IHIVRLQLetmqkQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEElkrkvQAEKDAAREKQR 2120
Cdd:COG0330 153 IEVVDVEI-----KDIDPPEEVQDAMEDRMKAEREREAAILEAEGYREAAIIRAEGEAQRAII-----EAEAYREAQILR 222
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1717010358 2121 AMEDLQKFRSQAEEAErrmKQAEVEKERQIKVAQEVAQQSA 2161
Cdd:COG0330 223 AEGEAEAFRIVAEAYS---AAPFVLFYRSLEALEEVLSPNS 260
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2247-2607 |
1.08e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2247 EEAEKQKEDAEREARKRAKAEESALRQKELAEDELEKQRKLADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRL 2326
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2327 KNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEE-AKRQRQ 2405
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2406 IAEGEAARQR---AEAERILKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKI 2482
Cdd:COG4372 166 LAALEQELQAlseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2483 ILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQL 2562
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 1717010358 2563 ALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEE 2607
Cdd:COG4372 326 KKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2738-2901 |
1.11e-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: 44.15 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2738 HAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEEL 2817
Cdd:COG1579 3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2818 FKVKIQME------ELIKLKLRIEE-ENKML-IMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLA 2889
Cdd:COG1579 83 GNVRNNKEyealqkEIESLKRRISDlEDEILeLMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|..
gi 1717010358 2890 NQRALAEKMLKE 2901
Cdd:COG1579 163 AEREELAAKIPP 174
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2897-3193 |
1.14e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 45.44 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2897 KMLKEKMQAIQEAtrLKAEADMLQKQKELAQEQARKFQEDKE--QIEQQLAKETEGfqksLEAERRQQLEITAEAERLKL 2974
Cdd:PRK03918 172 KEIKRRIERLEKF--IKRTENIEELIKEKEKELEEVLREINEisSELPELREELEK----LEKEVKELEELKEEIEELEK 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2975 QVLEMSKAQAKAEEDAKKFKKQAEdfGNKLHQTELATKERMVV-VQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEA 3053
Cdd:PRK03918 246 ELESLEGSKRKLEEKIRELEERIE--ELKKEIEELEEKVKELKeLKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3054 ELLQKNSQEMQ--VAQQEQLRQETQVLQttfltekhlllekekyieKEKAKLENLYEDEVRKAQKLKQEQEHQLKQLEEE 3131
Cdd:PRK03918 324 NGIEERIKELEekEERLEELKKKLKELE------------------KRLEELEERHELYEEAKAKKEELERLKKRLTGLT 385
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 3132 KQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLaDENRKLREKL----EQLEEEHR 3193
Cdd:PRK03918 386 PEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAI-EELKKAKGKCpvcgRELTEEHR 450
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
641-731 |
1.17e-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: 41.90 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 641 KWVNKHLIKAQR---HVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLkhRQVKLVN-IRN 713
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1717010358 714 DDIADGNPKLTLGLIWTI 731
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2687-2882 |
1.17e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 45.07 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2687 AEQEAALSRQQVEEAERMKQ-RAEEEAQAKA-----QAQDEAEKLRKE--------AELEAAKRAH----AEQ--AALKQ 2746
Cdd:PRK11637 57 AAKEKSVRQQQQQRASLLAQlKKQEEAISQAsrklrETQNTLNQLNKQidelnasiAKLEQQQAAQerllAAQldAAFRQ 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2747 KQ-------LADEEMDKHKKFA----------EKTLRQKAQVEQELTKVKLQLEET-DHQKTLLDDE-SQRLKEEVTDAM 2807
Cdd:PRK11637 137 GEhtglqliLSGEESQRGERILayfgylnqarQETIAELKQTREELAAQKAELEEKqSQQKTLLYEQqAQQQKLEQARNE 216
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2808 RQK--AQVEEELFKVKIQMEELIKLKLRIeeenkmlimkdKDSTQKflAEEAEKMRqvaeeAARlsiEAQEAARMRK 2882
Cdd:PRK11637 217 RKKtlTGLESSLQKDQQQLSELRANESRL-----------RDSIAR--AEREAKAR-----AER---EAREAARVRD 272
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1942-2270 |
1.20e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.03 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1942 KEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREvvavdAEQQKQTIQQELQQLRQNSDMEik 2021
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQ-----AEEEAREAKAEAEQRAAELAAE-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2022 sKAKKIEEAEYNRRKIEEEIHivrlqlETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAE 2101
Cdd:COG3064 75 -AAKKLAEAEKAAAEAEKKAA------AEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2102 EELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLEL 2181
Cdd:COG3064 148 AAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2182 SLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREAR 2261
Cdd:COG3064 228 ASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAEL 307
|
....*....
gi 1717010358 2262 KRAKAEESA 2270
Cdd:COG3064 308 LGAVAAEEA 316
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2768-2952 |
1.22e-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: 44.49 E-value: 1.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2768 KAQVEQELTKVKLQLEETDHQK--TLLDDESQRLKEEVTDA-----------MRQKAQVEEELFKVK---IQMEELIK-- 2829
Cdd:cd16269 96 MEQLEEKKEEFCKQNEEASSKRcqALLQELSAPLEEKISQGsysvpggyqlyLEDREKLVEKYRQVPrkgVKAEEVLQef 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2830 LKLRIEEENKMLIMkDKDSTQKFLAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEddlaNQRALAE--KMLKEKMQaiQ 2907
Cdd:cd16269 176 LQSKEAEAEAILQA-DQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLED----QERSYEEhlRQLKEKME--E 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1717010358 2908 EATRLKAEADMLQKQKElaQEQARKFQEDKEQIEQQLAKETEGFQ 2952
Cdd:cd16269 249 ERENLLKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2523-2663 |
1.25e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 45.15 E-value: 1.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2523 KASSGKSDLELELNqlkniaEETHRSKEKAEQE--------AEKQRQLALEEEQ--RRKEAEEKVRKILADEQEAARQRK 2592
Cdd:PRK12704 50 EAEAIKKEALLEAK------EEIHKLRNEFEKElrerrnelQKLEKRLLQKEENldRKLELLEKREEELEKKEKELEQKQ 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2593 aalEEVERLKAKAEEAKRQkelAEKEAERQIQLAQEAA----FKKIEAEEKAHAA-IVQQKEQEMLQTRKQE-KSIL 2663
Cdd:PRK12704 124 ---QELEKKEEELEELIEE---QLQELERISGLTAEEAkeilLEKVEEEARHEAAvLIKEIEEEAKEEADKKaKEIL 194
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
2952-3073 |
1.27e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 43.66 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2952 QKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTELATKERMVvvQSLEIQRQQSGKE 3031
Cdd:COG1842 36 EEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQA--EALEAQLAQLEEQ 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1717010358 3032 AEELRRAIAELEHEKEKLKQEAELL--QKNSQEMQVAQQEQLRQ 3073
Cdd:COG1842 114 VEKLKEALRQLESKLEELKAKKDTLkaRAKAAKAQEKVNEALSG 157
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1934-2123 |
1.32e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.32 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVV--AVDAEQQKQTIQQELQQ 2011
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVaaAIARAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2012 LRQNSDMEIKSKAKKIEEAeynrrkieeeihIVRLQLETMQKQKASAEDELQELRARAEEAE----RQKKAAQEEAErlr 2087
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAA------------IARAKAKKAEQQANAEPEEPVDPRKAAVAAAiaraKARKAAQQQAN--- 666
|
170 180 190
....*....|....*....|....*....|....*.
gi 1717010358 2088 rqvkdesQKKREAEEELKRKVQAEKDAAREKQRAME 2123
Cdd:PRK05035 667 -------AEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2651-3046 |
1.33e-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: 44.67 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2651 EMLQTRKQEKSILDKLkeeaeRAKRAAEDADYARMRAEQEAALSRQQVEEAE--RMKQRAEEEAQAKAQAQDEAEKLRKE 2728
Cdd:pfam19220 38 AILRELPQAKSRLLEL-----EALLAQERAAYGKLRRELAGLTRRLSAAEGEleELVARLAKLEAALREAEAAKEELRIE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2729 aelEAAKRAHAEQAalkQKQLADEEmdkhkkfaektlRQKAQVEQELTKVKLQLEETDHQKtllddesQRLKEEVTDAMR 2808
Cdd:pfam19220 113 ---LRDKTAQAEAL---ERQLAAET------------EQNRALEEENKALREEAQAAEKAL-------QRAEGELATARE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2809 QKAQVEEELFKVKIQMEE----LIKLKLRIEEENKMLimkdkdstqkflaeEAEKMRQVAEEAarlSIEAQEAARMRKLA 2884
Cdd:pfam19220 168 RLALLEQENRRLQALSEEqaaeLAELTRRLAELETQL--------------DATRARLRALEG---QLAAEQAERERAEA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2885 EDDLANQRALAEKM-LKEKMQAIQeaTRLKAEADMLQKQKELAQEQARKFQE-DKEQIEQQLAKET-EGFQKSLEAERRQ 2961
Cdd:pfam19220 231 QLEEAVEAHRAERAsLRMKLEALT--ARAAATEQLLAEARNQLRDRDEAIRAaERRLKEASIERDTlERRLAGLEADLER 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2962 QLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLH-QTELATKERMVVVQSLEIQRqqsgkeaeelRRAIA 3040
Cdd:pfam19220 309 RTQQFQEMQRARAELEERAEMLTKALAAKDAALERAEERIASLSdRIAELTKRFEVERAALEQAN----------RRLKE 378
|
....*.
gi 1717010358 3041 ELEHEK 3046
Cdd:pfam19220 379 ELQRER 384
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2541-2911 |
1.37e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2541 IAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAE 2620
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2621 RQIQLAQEAAFKKIEAEEKAHAAIVQQKE-QEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARmRAEQEAALSRQQVE 2699
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEElQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-EEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2700 EAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVK 2779
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2780 LQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEenkmLIMKDKDSTQKFLAEEAEK 2859
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLA----LLLNLAALSLIGALEDALL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2860 MRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATR 2911
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2293-2829 |
1.40e-03 |
|
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: 45.01 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2293 QQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEESrSNTEKS 2372
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNI-DKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2373 KHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAER---ILKEKLAAINEATRLKTEAEIALKEKEAE 2449
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEkttEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2450 NERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIIllkKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKS 2529
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQDWN---KELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELT 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2530 DLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAA-------LEEVERLK 2602
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLqqekellEKEIERLK 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2603 AKAEEAKRQ-KELAEKEAERQIQL--------AQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERA 2673
Cdd:TIGR04523 433 ETIIKNNSEiKDLTNQDSVKELIIknldntreSLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2674 KRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAK------RAHAEQAALKQK 2747
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEELKqtqkslKKKQEEKQELID 592
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2748 QLADEEMDKHKKFAEKTlRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTdamrqkaQVEEELFKVKIQMEEL 2827
Cdd:TIGR04523 593 QKEKEKKDLIKEIEEKE-KKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVK-------QIKETIKEIRNKWPEI 664
|
..
gi 1717010358 2828 IK 2829
Cdd:TIGR04523 665 IK 666
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2683-2857 |
1.43e-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: 44.99 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2683 ARMRAEQEAALSRQQveEAERMKQRAEEEAQAKAQ-AQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFA 2761
Cdd:pfam05262 184 EALREDNEKGVNFRR--DMTDLKERESQEDAKRAQqLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLP 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2762 EKTLRQKAQVEQELTKVKLQLEETDHQKT-LLDDESQRLKEEVTDAMRQKAQVEEelfKVKIQMEELIKLKLRIEEENKM 2840
Cdd:pfam05262 262 KPADTSSPKEDKQVAENQKREIEKAQIEIkKNDEEALKAKDHKAFDLKQESKASE---KEAEDKELEAQKKREPVAEDLQ 338
|
170
....*....|....*..
gi 1717010358 2841 LIMKDKDSTQKFLAEEA 2857
Cdd:pfam05262 339 KTKPQVEAQPTSLNEDA 355
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1933-2594 |
1.44e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1933 VEEKAAEKLKEEERRRLAEVEaQLEKQTQLA-------EAHAKAKA-----QAEKEAEELQRRMQEEVSKREVVAVDAEQ 2000
Cdd:PRK04863 371 VEEADEQQEENEARAEAAEEE-VDELKSQLAdyqqaldVQQTRAIQyqqavQALERAKQLCGLPDLTADNAEDWLEEFQA 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2001 QKQTIQQELQQLRQNsdMEIKSKAKKIEEAEYNR-RKIEEEI------HIVRLQLETMQKQKASAEdELQELRARAEEAE 2073
Cdd:PRK04863 450 KEQEATEELLSLEQK--LSVAQAAHSQFEQAYQLvRKIAGEVsrseawDVARELLRRLREQRHLAE-QLQQLRMRLSELE 526
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2074 rQKKAAQEEAERLRRQVKDESQKKREAEEELKRkVQAEKDAAREkqrameDLQKfrSQAEEAERRMKQAEVEKERQIKVA 2153
Cdd:PRK04863 527 -QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQ-LQEELEARLE------SLSE--SVSEARERRMALRQQLEQLQARIQ 596
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2154 QEVAQ----------------QSAAAELNSKR-MSFAEKTAQLELSLKQEHItvtHLQEEAERLKKQheeaekareeaek 2216
Cdd:PRK04863 597 RLAARapawlaaqdalarlreQSGEEFEDSQDvTEYMQQLLERERELTVERD---ELAARKQALDEE------------- 660
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2217 eLEKWHQK-ANEALRLRLQAEEV---------------------------AH----------KKTLAQEE---------- 2248
Cdd:PRK04863 661 -IERLSQPgGSEDPRLNALAERFggvllseiyddvsledapyfsalygpaRHaivvpdlsdaAEQLAGLEdcpedlylie 739
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2249 ------------AEKQKED-----------------------AEREARK---RAKAEESALRQKELAEDELEKQRKLADA 2290
Cdd:PRK04863 740 gdpdsfddsvfsVEELEKAvvvkiadrqwrysrfpevplfgrAAREKRIeqlRAEREELAERYATLSFDVQKLQRLHQAF 819
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2291 TAqqkFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAIQ----KRKKMEEELAKVRA---------------EM 2351
Cdd:PRK04863 820 SR---FIGSHLAVAFEADPEAELRQLNRRRVELERALADHESQEQqqrsQLEQAKEGLSALNRllprlnlladetladRV 896
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2352 EILLESKSRAEEESRSNTEKSKHM--LEVEASKLRELAEEAARLRALSEEAKRQRQiaegeAARQRAEAeriLKEklaAI 2429
Cdd:PRK04863 897 EEIREQLDEAEEAKRFVQQHGNALaqLEPIVSVLQSDPEQFEQLKQDYQQAQQTQR-----DAKQQAFA---LTE---VV 965
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2430 NEATRLKTEAEIALKEKEAE-NERLR-RLAEDEAyQRKLLEEQATQHKQDIEEKIILLK--KSS-----DNELERQKNIV 2500
Cdd:PRK04863 966 QRRAHFSYEDAAEMLAKNSDlNEKLRqRLEQAEQ-ERTRAREQLRQAQAQLAQYNQVLAslKSSydakrQMLQELKQELQ 1044
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2501 EDTLRQRRIIEeeirilklnfEKASSGKSDLELELnqlkniaeetHRSKEKAEQeAEKQRQLaleEEQRRKEAEEKVRKI 2580
Cdd:PRK04863 1045 DLGVPADSGAE----------ERARARRDELHARL----------SANRSRRNQ-LEKQLTF---CEAEMDNLTKKLRKL 1100
|
810
....*....|....
gi 1717010358 2581 LADEQEAARQRKAA 2594
Cdd:PRK04863 1101 ERDYHEMREQVVNA 1114
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2614-2730 |
1.48e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.77 E-value: 1.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2614 LAEKEAERQIQLAQEAAFK-----KIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAaedadyarmrAE 2688
Cdd:PRK12704 24 VRKKIAEAKIKEAEEEAKRileeaKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRL----------LQ 93
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1717010358 2689 QEAALSRQQvEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAE 2730
Cdd:PRK12704 94 KEENLDRKL-ELLEKREEELEKKEKELEQKQQELEKKEEELE 134
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1919-2112 |
1.53e-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: 44.52 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1919 QYIKFITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKRevvavda 1998
Cdd:pfam13868 159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKA------- 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1999 eQQKQTIQQELQQLRQnsdmeikskAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKA 2078
Cdd:pfam13868 232 -RQRQELQQAREEQIE---------LKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....
gi 1717010358 2079 AQEEAERLRRQVKDESQKKREAEEELKRKVQAEK 2112
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEER 335
|
|
| ftsN |
TIGR02223 |
cell division protein FtsN; FtsN is a poorly conserved protein active in cell division in a ... |
2548-2750 |
1.54e-03 |
|
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: 44.30 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2548 SKEKAEQEAEKQRQLALEEEQRRK---EAEEKVRKILADEQeaarqRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQ 2624
Cdd:TIGR02223 51 SKQANEPETLQPKNQTENGETAADlppKPEERWSYIEELEA-----REVLINDPEEPSNGGGVEESAQLTAEQRQLLEQM 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2625 LAQEAAFKKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARmrAEQEAALSRQQVEEAERM 2704
Cdd:TIGR02223 126 QADMRAAEKVLATAPSEQTVAVEARKQTAEKKPQKARTAEAQKTPVETEKIASKVKEAKQ--KQKALPKQTAETQSNSKP 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1717010358 2705 KQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLA 2750
Cdd:TIGR02223 204 IETAPKADKADKTKPKPKEKAERAAALQCGAYANKEQAESVRAKLA 249
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2071-2161 |
1.62e-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: 42.34 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2071 EAERQKKAAQEEAERLRRqvkdESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQI 2150
Cdd:pfam05672 28 EREEQERLEKEEEERLRK----EELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAEEREQREQEEQERLQKQK 103
|
90
....*....|.
gi 1717010358 2151 KVAQEVAQQSA 2161
Cdd:pfam05672 104 EEAEAKAREEA 114
|
|
| PRK14475 |
PRK14475 |
F0F1 ATP synthase subunit B; Provisional |
2044-2161 |
1.67e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184697 [Multi-domain] Cd Length: 167 Bit Score: 42.62 E-value: 1.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2044 VRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKreAEEELKRKvqaekdaarekqrame 2123
Cdd:PRK14475 46 IQAELDEAQRLREEAQALLADVKAEREEAERQAAAMLAAAKADARRMEAEAKEK--LEEQIKRR---------------- 107
|
90 100 110
....*....|....*....|....*....|....*....
gi 1717010358 2124 dlqkfrsqAEEAERRMKQAEVEKERQIKVAQ-EVAQQSA 2161
Cdd:PRK14475 108 --------AEMAERKIAQAEAQAAADVKAAAvDLAAQAA 138
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2536-2747 |
1.77e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2536 NQLK----NIAEethrsKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILADEQEAARQRKAALEEVERLKAKAE--EAK 2609
Cdd:PRK11637 47 DQLKsiqqDIAA-----KEKSVRQQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAKLEqqQAA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2610 RQKELAEK--EAERQ-----IQLA-------------------QEAAFKKIEAEEKAHAAIVQQKeQEMLQTRKQEKSIL 2663
Cdd:PRK11637 122 QERLLAAQldAAFRQgehtgLQLIlsgeesqrgerilayfgylNQARQETIAELKQTREELAAQK-AELEEKQSQQKTLL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2664 DKLKEEaeraKRAAEDADYARMR--AEQEAALSRQQVEEAErMKQRAEEEAQAKAQAQDEAeKLRKEAELEAAKRAHAEQ 2741
Cdd:PRK11637 201 YEQQAQ----QQKLEQARNERKKtlTGLESSLQKDQQQLSE-LRANESRLRDSIARAEREA-KARAEREAREAARVRDKQ 274
|
....*.
gi 1717010358 2742 AALKQK 2747
Cdd:PRK11637 275 KQAKRK 280
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
630-738 |
1.78e-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: 41.51 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 630 ERDRVQKKTFTKWVNKhlIKAQRHVTDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 700
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1717010358 701 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 738
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
2603-2785 |
1.79e-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: 43.95 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2603 AKAEEAKRQKELAekeaerQIQLAQEAAFKKIEAEEKAHAAIvQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADY 2682
Cdd:pfam00529 56 YQAALDSAEAQLA------KAQAQVARLQAELDRLQALESEL-AISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2683 ARMRAEQeAALSRQQVEEAER--MKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEmdKHKKF 2760
Cdd:pfam00529 129 RRVLAPI-GGISRESLVTAGAlvAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAEL--KLAKL 205
|
170 180
....*....|....*....|....*
gi 1717010358 2761 AEKTLRQKAQVEQELTKVKLQLEET 2785
Cdd:pfam00529 206 DLERTEIRAPVDGTVAFLSVTVDGG 230
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2327-2479 |
1.81e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2327 KNEVNEAIQKRKKMEEElAKVRAEMEILLEsksRAEEEsrsntEKSKHMLEVEASKLRELAEEAARLRALSE-EAKRQRQ 2405
Cdd:PTZ00491 662 KSQEAAARHQAELLEQE-ARGRLERQKMHD---KAKAE-----EQRTKLLELQAESAAVESSGQSRAEALAEaEARLIEA 732
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2406 IAEGEAARQRAEAERILkeklaaineatrlkTEAEIAL--KEKEAENERLRRLAEDE-AYQRKLLEEQATQHKQDIE 2479
Cdd:PTZ00491 733 EAEVEQAELRAKALRIE--------------AEAELEKlrKRQELELEYEQAQNELEiAKAKELADIEATKFERIVE 795
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
3025-3191 |
1.83e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3025 RQQSGKEAEELRRAIAELEHEKEKLKQEAELLqknsqemqvaqqEQLRQETqvlqttfltekhlllekekyiekekaklE 3104
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEA------------EALLKEA----------------------------E 547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3105 NLYEDEVRKAQKLKQEQEHQLKQLEEEKQQ-LKASMGEAMKKQKEaeesVRHKQDELHQLDKRRQEQEKLladenRKLRE 3183
Cdd:PRK00409 548 KLKEELEEKKEKLQEEEDKLLEEAEKEAQQaIKEAKKEADEIIKE----LRQLQKGGYASVKAHELIEAR-----KRLNK 618
|
....*...
gi 1717010358 3184 KLEQLEEE 3191
Cdd:PRK00409 619 ANEKKEKK 626
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2659-3061 |
1.88e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.20 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2659 EKSILDKLKEEAERAKRAAEDADYARMRAEQ----------EAALSRQQVEEAERMKQRAEEEAQAKAQA----QDEAEK 2724
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEEARKRLVAKHGAEIskleeenrekEKALPKNDDMTIEEAKRRAAAAAKAKAAAlakqKREGTE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2725 LRKEAELEAAKRAHAEQAALKQKQLAdeemdkhkkfaektlRQKAQVEQELTkvklqleetdhqktllddesqrlkeevt 2804
Cdd:PRK07735 84 EVTEEEKAKAKAKAAAAAKAKAAALA---------------KQKREGTEEVT---------------------------- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2805 damrqkaqvEEELFKVKIQMEELIKLKLrieeenkmlimkdkdstqkflAEEAEKMRQVAEEAARLSIEAQEAARMRKLA 2884
Cdd:PRK07735 121 ---------EEEKAAAKAKAAAAAKAKA---------------------AALAKQKREGTEEVTEEEEETDKEKAKAKAA 170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2885 EDDLANQRALAEKMLKEKMQAIQEATRlkaEADMLQKQKELAQEQARKFQEDKEQieqqlAKETEGfqksleaerrqqle 2964
Cdd:PRK07735 171 AAAKAKAAALAKQKAAEAGEGTEEVTE---EEKAKAKAKAAAAAKAKAAALAKQK-----ASQGNG-------------- 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2965 iTAEAERLKLQVLEMSKAQAKAEEDAKkfKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEA------EELRRA 3038
Cdd:PRK07735 229 -DSGDEDAKAKAIAAAKAKAAAAARAK--TKGAEGKKEEEPKQEEPSVNQPYLNKYVEVIKEKLGEDVledsyiNKLSKD 305
|
410 420
....*....|....*....|...
gi 1717010358 3039 IAELEHEKEKLKQEAELLQKNSQ 3061
Cdd:PRK07735 306 VPTLVVEPEKYYEVAELLRFHEQ 328
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2496-2715 |
1.88e-03 |
|
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: 44.37 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2496 QKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQL-KNIAEETHRSKEKAEQEAEKQRQLA-LEEEQRRKEA 2573
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALeRRIAALARRIRALEQELAALEAELAeLEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2574 EEKVRKILADEQEAARQR-------------KAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKA 2640
Cdd:COG4942 98 ELEAQKEELAELLRALYRlgrqpplalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELE 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2641 HAAIVQQKEQEMLQTRKQEK-SILDKL-KEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAK 2715
Cdd:COG4942 178 ALLAELEEERAALEALKAERqKLLARLeKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1963-2161 |
1.98e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 44.65 E-value: 1.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1963 AEAHAKAKAQAEKEAEELQRRMQEEVSKRevvavdaeQQKQTIQQELQQLRQNSDMEIKSKAKkiEEAEYNRRKieeeih 2042
Cdd:PRK10811 582 GGEETKPQEQPAPKAEAKPERQQDRRKPR--------QNNRRDRNERRDTRDNRTRREGRENR--EENRRNRRQ------ 645
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2043 ivrlqletMQKQKASAEDELQELRARAEEAERQKKaAQEEAERLRRQvkdeSQKKREAEEELKRKVQAEKDAA------- 2115
Cdd:PRK10811 646 --------AQQQTAETRESQQAEVTEKARTQDEQQ-QAPRRERQRRR----NDEKRQAQQEAKALNVEEQSVQeteqeer 712
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2116 ------REKQRAMEdlQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSA 2161
Cdd:PRK10811 713 vqqvqpRRKQRQLN--QKVRIEQSVAEEAVAPVVEETVAAEPVVQEVPAPRT 762
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2877-3184 |
1.99e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 44.62 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2877 AARMRKLAEDdLANQRALAE--KMLKEKmqaIQEATRlkaEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKS 2954
Cdd:PHA02562 149 APARRKLVED-LLDISVLSEmdKLNKDK---IRELNQ---QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNK 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2955 LEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTelatkermvvvqSLEIQRQQSGKEAEE 3034
Cdd:PHA02562 222 YDELVEEAKTIKAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQF------------QKVIKMYEKGGVCPT 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3035 LRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEqlrqetqvlqttfltekhlllekekyiekekaklENLYEDEVRKA 3114
Cdd:PHA02562 290 CTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDE----------------------------------LEEIMDEFNEQ 335
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 3115 QKLKQEqehqLK-QLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEKLLADENRKLREK 3184
Cdd:PHA02562 336 SKKLLE----LKnKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSELVKEK 402
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1936-2011 |
2.11e-03 |
|
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: 42.08 E-value: 2.11e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 1936 KAAEKLKEEERRRLAEVEAQLEK-QTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVA-VDAEQQKQTIQQELQQ 2011
Cdd:COG0711 41 AEAERAKEEAEAALAEYEEKLAEaRAEAAEIIAEARKEAEAIAEEAKAEAEAEAERIIAQAeAEIEQERAKALAELRA 118
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
2620-2776 |
2.11e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 44.07 E-value: 2.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2620 ERQIQLAQEaaFKKIEAEEKAHAAIVQQKEQEMLQTRKQEK--SILdklkeeaeRAKRAAEdadyarMRAeQEAALSRQQ 2697
Cdd:PRK00247 274 ERKYPLTDE--FKEHHAEQRAQYREKQKEKKAFLWTLRRNRlrMII--------TPWRAPE------LHA-ENAEIKKTR 336
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1717010358 2698 VEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELT 2776
Cdd:PRK00247 337 TAEKNEAKARKKEIAQKRRAAEREINREARQERAAAMARARARRAAVKAKKKGLIDASPNEDTPSENEESKGSPPQVEA 415
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1934-2180 |
2.15e-03 |
|
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: 44.25 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQeevsKREVVAVDAEQQKQTIQQELQQLR 2013
Cdd:pfam05667 210 ERNAAELAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAAL----AGTEATSGASRSAQDLAELLSSFS 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2014 ------------------------QNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARA 2069
Cdd:pfam05667 286 gssttdtgltkgsrfthteklqftNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSI 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2070 EEAERQKKAAQEEAERLRRQVKdesQKKR------EAEE---ELKRKVQAEkdAAR--------EKQRAmEDLQKFRSQA 2132
Cdd:pfam05667 366 KQVEEELEELKEQNEELEKQYK---VKKKtldllpDAEEniaKLQALVDAS--AQRlvelagqwEKHRV-PLIEEYRALK 439
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1717010358 2133 EEAERRMKQAEVEKErQIKVAQEVAQQsAAAELNSKRMSFAEKTAQLE 2180
Cdd:pfam05667 440 EAKSNKEDESQRKLE-EIKELREKIKE-VAEEAKQKEELYKQLVAEYE 485
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1898-2466 |
2.36e-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: 44.56 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1898 SIIQEYVDLRTRYS---ELTTLTSQYIKfitetlcRLNVEEKAAEKLKEEerrrLAEVEAQLEKQTQLAEAHAKAKAQAE 1974
Cdd:COG3096 516 QLRAQLAELEQRLRqqqNAERLLEEFCQ-------RIGQQLDAAEELEEL----LAELEAQLEELEEQAAEAVEQRSELR 584
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1975 KEAEELQRRMQEeVSKREVVAVDAEQQKQTIQ----------QELQQLRQNsdMEIKSKAKKIEEAEYNRRKIEEEIHIV 2044
Cdd:COG3096 585 QQLEQLRARIKE-LAARAPAWLAAQDALERLReqsgealadsQEVTAAMQQ--LLEREREATVERDELAARKQALESQIE 661
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2045 RLQletmqkQKASAEDelQELRARAEE------AERQKKAAQEEA-------------------ERLRRQVK-------- 2091
Cdd:COG3096 662 RLS------QPGGAED--PRLLALAERlggvllSEIYDDVTLEDApyfsalygparhaivvpdlSAVKEQLAgledcped 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2092 -----------DESQkkREAEEELKRKVQAEKD----------------AAREKQramedLQKFRSQAEEAERRMKQAEV 2144
Cdd:COG3096 734 lyliegdpdsfDDSV--FDAEELEDAVVVKLSDrqwrysrfpevplfgrAAREKR-----LEELRAERDELAEQYAKASF 806
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2145 EKERQIKVAQE----VAQQSA-------AAELNSKRmsfaEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREE 2213
Cdd:COG3096 807 DVQKLQRLHQAfsqfVGGHLAvafapdpEAELAALR----QRRSELERELAQHRAQEQQLRQQLDQLKEQLQLLNKLLPQ 882
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2214 AEKELEKWHQKANEALRLRLQAEEVA------HKKTLAQEE-------AEKQKEDAEREARKRAKAEESALRQKELAEDE 2280
Cdd:COG3096 883 ANLLADETLADRLEELREELDAAQEAqafiqqHGKALAQLEplvavlqSDPEQFEQLQADYLQAKEQQRRLKQQIFALSE 962
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2281 LEKQRK-LADATAQQKFSAEQELI-RLKADTESGEQQRLLLEEELFRLKNEVNEAIQ-------KRKKMEEELAKVRAEM 2351
Cdd:COG3096 963 VVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSQYNQvlaslksSRDAKQQTLQELEQEL 1042
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2352 EIL-LESKSRAEEESRSntekskhmleveasKLRELAEEAARLRALSEEAKRQRQIAEGE---AARQRAEAERilkekla 2427
Cdd:COG3096 1043 EELgVQADAEAEERARI--------------RRDELHEELSQNRSRRSQLEKQLTRCEAEmdsLQKRLRKAER------- 1101
|
650 660 670
....*....|....*....|....*....|....*....
gi 1717010358 2428 ainEATRLKTEAEIALkekeAENERLRRLAEDEAYQRKL 2466
Cdd:COG3096 1102 ---DYKQEREQVVQAK----AGWCAVLRLARDNDVERRL 1133
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2684-2849 |
2.36e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2684 RMRAEQEAALSRQQVEEAERMKQR--------AEEEAQAKAQAQDEAEKLRKEAELEAAK--RAHAEQAALKQKQLADEE 2753
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEEleekkeklQEEEDKLLEEAEKEAQQAIKEAKKEADEiiKELRQLQKGGYASVKAHE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2754 M-DKHKKFAEKTLRQKAQVEQELTKVKlQLEETDHQKTLlddeSQRLKEEVTDAMRQK-AQVEEELFKVKIQMEELIKLK 2831
Cdd:PRK00409 609 LiEARKRLNKANEKKEKKKKKQKEKQE-ELKVGDEVKYL----SLGQKGEVLSIPDDKeAIVQAGIMKMKVPLSDLEKIQ 683
|
170
....*....|....*....
gi 1717010358 2832 LRIEEENKMLI-MKDKDST 2849
Cdd:PRK00409 684 KPKKKKKKKPKtVKPKPRT 702
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
3019-3193 |
2.40e-03 |
|
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: 43.87 E-value: 2.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3019 QSLEIQRQQSGKEAEELRRAiaeLEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQE-TQVLQTTFLTEKHLLLEKEKYIE 3097
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRR---DQKRQETLERERRLLLQQSQEQWQAEKEQRKARlGREERRRADRREKQVIEKESRWR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3098 KEKAKLENLYEDEVRKAQK----LKQEQEHQLKQLEEEKQQLKASMGEAMkkQKEAEESVRHKQDELHQLDKRRQE---Q 3170
Cdd:pfam15558 98 EQAEDQENQRQEKLERARQeaeqRKQCQEQRLKEKEEELQALREQNSLQL--QERLEEACHKRQLKEREEQKKVQEnnlS 175
|
170 180
....*....|....*....|...
gi 1717010358 3171 EKLLADENRKLREKLEQLEEEHR 3193
Cdd:pfam15558 176 ELLNHQARKVLVDCQAKAEELLR 198
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2949-3199 |
2.41e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2949 EGFQKSLEAERRQQLEITAEAerLKLQVLEMSKAQAKAEEDAKKFKKQaedfgNKLHQTELATKERMVVVQSLEIQRQQS 3028
Cdd:COG3206 159 EAYLEQNLELRREEARKALEF--LEEQLPELRKELEEAEAALEEFRQK-----NGLVDLSEEAKLLLQQLSELESQLAEA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3029 GKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQE-QLRQETQVLQTTFlTEKHlllekekyiekekaklenly 3107
Cdd:COG3206 232 RAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLaELEAELAELSARY-TPNH-------------------- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3108 edevRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDELHQ----LDKRRQEQEKLL--ADENRKL 3181
Cdd:COG3206 291 ----PDVIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEArlaeLPELEAELRRLEreVEVAREL 366
|
250
....*....|....*...
gi 1717010358 3182 REKLEQLEEEHRIALAQT 3199
Cdd:COG3206 367 YESLLQRLEEARLAEALT 384
|
|
| rpsP |
PRK14521 |
30S ribosomal protein S16; Provisional |
2643-2743 |
2.41e-03 |
|
30S ribosomal protein S16; Provisional
Pssm-ID: 237744 [Multi-domain] Cd Length: 186 Bit Score: 42.46 E-value: 2.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2643 AIVQQKEQEMLQTRKQEKSilDKLKEEAERAKRAAEDADYARMRAEQEAALSRqqvEEAERMKQRAEEEAQAKAQAQDEA 2722
Cdd:PRK14521 93 AFTEAQAEAKFEAWKEEKE--GKVNAKKDKLSKAKKAAKKAALEAEKKVNEAR---AEAVAEKKAAEAAAVAAEEAAAAE 167
|
90 100
....*....|....*....|.
gi 1717010358 2723 EklrKEAELEAAKRAHAEQAA 2743
Cdd:PRK14521 168 E---EEAEEAPAEEAPAEESA 185
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4870-4901 |
2.44e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.44e-03
10 20 30
....*....|....*....|....*....|..
gi 1717010358 4870 IAGILDTDTLEKVSITEAMHRNLVDNITGQRL 4901
Cdd:pfam00681 8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2194-2420 |
2.46e-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: 43.68 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2194 QEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKKTLAQEEAEKQKEDAEREARKRAKAEESALRQ 2273
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2274 KELAEDELEKQRKLADATAQQKFSAEQELIRLKAdtesgeqqrllleeelfrlKNEVNEAIQKRKKMEEELAKVRAEmei 2353
Cdd:TIGR02794 142 RKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKA-------------------EAEAKAKAEAEAKAKAEEAKAKAE--- 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2354 llESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQiaeGEAARQRAEAER 2420
Cdd:TIGR02794 200 --AAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ---GGARGAAAGSEV 261
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
2003-2109 |
2.53e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.28 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2003 QTIQQELQQL---RQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQ-------ELRARAEEA 2072
Cdd:pfam05911 684 KRLKEEFEQLkseKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQLKcmaesyeDLETRLTEL 763
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1717010358 2073 ERQKKAAQEEAERLRRQVKDESQKKREAE---EELKRKVQ 2109
Cdd:pfam05911 764 EAELNELRQKFEALEVELEEEKNCHEELEakcLELQEQLE 803
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2831-2999 |
2.54e-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: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2831 KLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVA-EEAARLSIEAQEAARMRKLAEDDLANQRalaekmlKEKMQAIQEA 2909
Cdd:pfam05262 185 ALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLkEELDKKQIDADKAQQKADFAQDNADKQR-------DEVRQKQQEA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2910 TRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQlaKETEGFQKSLEaerrqqleitAEAERLKLQVLEMSK-AQAKAEE 2988
Cdd:pfam05262 258 KNLPKPADTSSPKEDKQVAENQKREIEKAQIEIK--KNDEEALKAKD----------HKAFDLKQESKASEKeAEDKELE 325
|
170
....*....|.
gi 1717010358 2989 DAKKFKKQAED 2999
Cdd:pfam05262 326 AQKKREPVAED 336
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
2061-2181 |
2.61e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 44.09 E-value: 2.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2061 ELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKR--KVQAEKDAAREKQRAMEDLQKFRSQAEEAERR 2138
Cdd:PRK12472 198 EAEDAARAADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRadKALAAAKTDEAKARAEERQQKAAQQAAEAATQ 277
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1717010358 2139 MKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLEL 2181
Cdd:PRK12472 278 LDTAKADAEAKRAAAAATKEAAKAAAAKKAETAKAATDAKLAL 320
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2783-2988 |
2.64e-03 |
|
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: 42.73 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2783 EETDHQKTLLDDESQRLKEEVTDAMRQ-KAQVEEEL-FKVKIQ-MEELIKLKLRIEEENKMLIMKDKDSTqkflaeEAEK 2859
Cdd:pfam15665 14 AEIQALKEAHEEEIQQILAETREKILQyKSKIGEELdLKRRIQtLEESLEQHERMKRQALTEFEQYKRRV------EERE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2860 MRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEATRLKA-EADMLQKQKelaQEQARKFQEDKE 2938
Cdd:pfam15665 88 LKAEAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAKHRqEIQELLTTQ---RAQSASSLAEQE 164
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2939 QIEQQLAKETEGFQKSLEAERRQQLEITAEAERlklqvlEMSKAQAKAEE 2988
Cdd:pfam15665 165 KLEELHKAELESLRKEVEDLRKEKKKLAEEYEQ------KLSKAQAFYER 208
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
610-766 |
2.65e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.16 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 610 METVPAVGVSEMEDPTpAEDERdrvQKKTFTKWVNKHLIKAQrhVTDLYEDLRDGHNLISLLEVLSGD---SLPREKGR- 685
Cdd:COG5069 359 QEPLEEEEKPEIEEFD-AEGEF---EARVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQp 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 686 ------MRFHKLQNVQIALDYLKHRQVKLVNIRNDDIADGNpKLTLGLIWTIILHFQISDIQVSGQSEDMTAKEKLLLWS 759
Cdd:COG5069 433 asgieeNRFKAFENENYAVDLGITEGFSLVGIKGLEILDGI-RLKLTLVWQVLRSNTALFNHVLKKDGCGLSDSDLCAWL 511
|
....*..
gi 1717010358 760 QRMTESY 766
Cdd:COG5069 512 GSLGLKG 518
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3608-3645 |
2.82e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.82e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1717010358 3608 KKYLKGTTAIAGVLVEPTGEKLSFYDALKKNLLKPEVA 3645
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2872-3214 |
2.94e-03 |
|
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: 44.27 E-value: 2.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2872 IEAQEAARMRKLAEDDLANQRALAEKMLKekmQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQlaketegf 2951
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLK---QYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNR-------- 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2952 QKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKL---HQTELATKERMVVVQSLEIQRQQs 3028
Cdd:TIGR00606 254 LKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLyhnHQRTVREKERELVDCQRELEKLN- 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3029 gKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQE-QLRQETQVLQTTFLTEKH------LLLEKEKYIEKEKA 3101
Cdd:TIGR00606 333 -KERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSlATRLELDGFERGPFSERQiknfhtLVIERQEDEAKTAA 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3102 KLENLYEDEVRKAQ----------------------KLKQEQEhQLKQLEEEKQQLKASMGEAMKKQKEAEESVRH---- 3155
Cdd:TIGR00606 412 QLCADLQSKERLKQeqadeirdekkglgrtielkkeILEKKQE-ELKFVIKELQQLEGSSDRILELDQELRKAERElska 490
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3156 -KQDELHQLDKRRQEQEKLLADENRKLREKLEQLEEEHRIALAQTREMMIQTDDLAGSSQ 3214
Cdd:TIGR00606 491 eKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQ 550
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2332-2497 |
2.97e-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: 2.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2332 EAIQKRKKMEEELAKVRAEMEILLESKsRAEEESRSNTEKSKHMLEVEASKLRE--LAEEAARLRALSEEAKRQRQI--- 2406
Cdd:TIGR02794 79 EAEKQRAAEQARQKELEQRAAAEKAAK-QAEQAAKQAEEKQKQAEEAKAKQAAEakAKAEAEAERKAKEEAAKQAEEeak 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2407 --AEGEAARQRAEAERILKEKLAAINEATRlKTEAEIALKEKEAENERLRRLAEDEAYQ-RKLLEEQATQHKQDIEEKII 2483
Cdd:TIGR02794 158 akAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAAKAKAAAEAAAKAEAeAAAAAAAEAERKADEAELGD 236
|
170
....*....|....
gi 1717010358 2484 LLKKSSDNELERQK 2497
Cdd:TIGR02794 237 IFGLASGSNAEKQG 250
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1934-2590 |
2.99e-03 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 44.02 E-value: 2.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EEKAAEKLKEEErrrLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLR 2013
Cdd:PRK10246 273 EEKAQPQLAALS---LAQPARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLN 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2014 QnsdmeikskakkiEEAEYNR-RKIEEEIHIVRLQLetmqKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKD 2092
Cdd:PRK10246 350 T-------------WLAEHDRfRQWNNELAGWRAQF----SQQTSDREQLRQWQQQLTHAEQKLNALPAITLTLTADEVA 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2093 ESQKKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEeaerrmkqaevekerqikvaQEVAQQSAAaeLNSKRMSF 2172
Cdd:PRK10246 413 AALAQHAEQRPLRQRLVALHGQIVPQQKRLAQLQVAIQNVT--------------------QEQTQRNAA--LNEMRQRY 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2173 AEKTaqlelslkQEHITVTHLQEEAERLKKQheeaekareeaekelekwhqkanEALRLRLQA----------EEVAHKK 2242
Cdd:PRK10246 471 KEKT--------QQLADVKTICEQEARIKDL-----------------------EAQRAQLQAgqpcplcgstSHPAVEA 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2243 TLAQEEAEKQKEDAEREARKRAKAEESALRQKELaeDELEKQRKLADATAQQKFSAEQELIrlkadteSGEQQRLLLEEE 2322
Cdd:PRK10246 520 YQALEPGVNQSRLDALEKEVKKLGEEGAALRGQL--DALTKQLQRDESEAQSLRQEEQALT-------QQWQAVCASLNI 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2323 LFRLKNEVNEAIQKRKKMEEELAKV--RAEMEILLESKSRAEEESRSNTEKSKHMLEVE----ASKLRELAEEAARLRAL 2396
Cdd:PRK10246 591 TLQPQDDIQPWLDAQEEHERQLRLLsqRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTAlagyALTLPQEDEEASWLATR 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2397 SEEAKR-QRQIAEGEAARQRAEAERILKEKLAAINEATrlkTEAEIALKE--KEAENERLRRLAEDEAYQRKLLEEQA-- 2471
Cdd:PRK10246 671 QQEAQSwQQRQNELTALQNRIQQLTPLLETLPQSDDLP---HSEETVALDnwRQVHEQCLSLHSQLQTLQQQDVLEAQrl 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2472 TQHKQDIEEKI-------------ILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQL 2538
Cdd:PRK10246 748 QKAQAQFDTALqasvfddqqaflaALLDEETLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQI 827
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2539 KN-IAEETHRSKEKAEQEAEKQRQLALEEEQRRKEaeekvRKILADEQEAARQ 2590
Cdd:PRK10246 828 QQeLAQLAQQLRENTTRQGEIRQQLKQDADNRQQQ-----QALMQQIAQATQQ 875
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3648-3682 |
3.02e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 3.02e-03
10 20 30
....*....|....*....|....*....|....*
gi 1717010358 3648 LLEAQAGTGYIIDPVKNEKFPVEEAVKASVVGPEF 3682
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2671-3003 |
3.04e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 3.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2671 ERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLA 2750
Cdd:COG4372 6 EKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2751 DEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTDAMRQKAQVEEELFKVKIQMEELIKL 2830
Cdd:COG4372 86 NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2831 KLRIEEENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAA-----RLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQA 2905
Cdd:COG4372 166 LAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAeaeklIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2906 IQEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAK 2985
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....*...
gi 1717010358 2986 AEEDAKKFKKQAEDFGNK 3003
Cdd:COG4372 326 KKLELALAILLAELADLL 343
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2589-2710 |
3.11e-03 |
|
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: 41.09 E-value: 3.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2589 RQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEAAfKKIEAEEKAHAAIVQQKeQEMLQTRKQEKSILDKLKE 2668
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQ-QNYERELVLHAEDIKAL-QALREELNELKAEIAELKA 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1717010358 2669 EAERAKRAAEdadyarmraEQEAALSRQQV---EEAERMKQRAEE 2710
Cdd:pfam07926 79 EAESAKAELE---------ESEESWEEQKKeleKELSELEKRIED 114
|
|
| Laminin_I |
pfam06008 |
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ... |
1941-2143 |
3.15e-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: 42.78 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1941 LKEEERRRLAEV-EAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDME 2019
Cdd:pfam06008 33 SPENAHKIQIEIlEKELSSLAQETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLIDNIKEINEKVATLGEND 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2020 IKSKAKKIEEAEYNRRKIEEEIHIVRLQletmqKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDE----SQ 2095
Cdd:pfam06008 113 FALPSSDLSRMLAEAQRMLGEIRSRDFG-----TQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANALRDSlaeyEA 187
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1717010358 2096 KKREAEEELKRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRMKQAE 2143
Cdd:pfam06008 188 KLSDLRELLREAAAKTRDANRLNLANQANLREFQRKKEEVSEQKNQLE 235
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2688-2801 |
3.30e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.17 E-value: 3.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2688 EQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKE--------AELEAAKRA-HAEQAALKQKQLADEemdkhk 2758
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQElvaleglaAELEEKQQElEAQLEQLQEKAAETS------ 211
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1717010358 2759 kfAEKTLRQKAQVEQELTKVKLQLEETdhqKTLLDdesQRLKE 2801
Cdd:PRK11448 212 --QERKQKRKEITDQAAKRLELSEEET---RILID---QQLRK 246
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
2547-2647 |
3.31e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 41.30 E-value: 3.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2547 RSKEKAEQeAEKQRQLALEE-----EQRRKEAEEKVRKILAD-----EQEAARQRKAALEEVERLKAKAEEAKRQK---- 2612
Cdd:PRK05759 49 RAKKELEL-AQAKYEAQLAEaraeaAEIIEQAKKRAAQIIEEakaeaEAEAARIKAQAQAEIEQERKRAREELRKQvadl 127
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 2613 --ELAEKEAERQIQlaqeaafkkieaeEKAHAAIVQQ 2647
Cdd:PRK05759 128 avAGAEKILGRELD-------------AAAQSDLIDK 151
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2836-3010 |
3.38e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2836 EENKMLIMKDKDSTQKFLAEEAEKMRQVAEEAAR-----------LSIEAQEAARMRKLAE------------DDLANQR 2892
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAaleefrqknglVDLSEEAKLLLQQLSElesqlaearaelAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2893 ALAEKMLKEKMQAIQEATRLKAEADMLQKQKELAQEQAR---KFQED--------------KEQIEQQLAKETEGFQKSL 2955
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAElsaRYTPNhpdvialraqiaalRAQLQQEAQRILASLEAEL 322
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2956 EAERRQQLEITAEAERLKLQVLEMSKAQAKAEE---DAKKFKKQAEDFGNKLHQTELA 3010
Cdd:COG3206 323 EALQAREASLQAQLAQLEARLAELPELEAELRRlerEVEVARELYESLLQRLEEARLA 380
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
2538-2641 |
3.39e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 41.86 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2538 LKNIAEETHRSKEKAEQEAE---KQRQLALEEEQRR-KEAEEKVRKILADEQ---EAARQR--KAALEEVERLKAKAEea 2608
Cdd:PRK07352 44 LGKILEERREAILQALKEAEerlRQAAQALAEAQQKlAQAQQEAERIRADAKaraEAIRAEieKQAIEDMARLKQTAA-- 121
|
90 100 110
....*....|....*....|....*....|....*..
gi 1717010358 2609 krqKELaEKEAERQI-QLAQEA---AFKKIEAEEKAH 2641
Cdd:PRK07352 122 ---ADL-SAEQERVIaQLRREAaelAIAKAESQLPGR 154
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
2685-2960 |
3.47e-03 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 43.57 E-value: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2685 MRAEQEAAlsRQQVEE----AERMKQRAEEEAQAKAQAQDEAEKLRKEAeleaakRAHAEQAALKQKQLADEEMDkhkkf 2760
Cdd:PRK13428 30 MAARQDTV--RQQLAEsataADRLAEADQAHTKAVEDAKAEAARVVEEA------REDAERIAEQLRAQADAEAE----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2761 aektlRQKAQVEQELTKVKLQLeeTDHQKTLLDDESQRLKEE-----VTDAMRQKAQVEEELfkvkiqmEELIKLKLRIE 2835
Cdd:PRK13428 97 -----RIKVQGARQVQLLRAQL--TRQLRLELGHESVRQAGElvrnhVADPAQQSATVDRFL-------DELDAMAPSTA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2836 EENKMLIMKDKDSTQKFLAEEAEKMRQVAEEA-----ARLSIEAQEAARM--------RKLAE--DDLANQRALAEKMLK 2900
Cdd:PRK13428 163 DVDYPLLAKMRSASRRALASLVDRFDSVAADLdnqalTTLADELVSVAKLldrepvltKHLTEpaEDAAPKIRLVERLFS 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2901 EK-----MQAIQEAT--RLKAEADM---LQKQKELAQEQARKFQEDKEQIEQQLAKetegFQKSLEAERR 2960
Cdd:PRK13428 243 GKvgaptLEVLRTAVsqRWSANSDLidaLEHVARLALLERAERAGQVDEVEDQLFR----FSRILDAQPR 308
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1935-2147 |
3.48e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 42.50 E-value: 3.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1935 EKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSK-REVVAVDAEQQKQTIQQELQQLr 2013
Cdd:COG1842 25 EKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKgREDLAREALERKAELEAQAEAL- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2014 qnsdmeikskakkieeaeynrrkiEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEaERLRRQVKDE 2093
Cdd:COG1842 104 ------------------------EAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQ-EKVNEALSGI 158
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2094 SQKK-REAEEELKRKVQAEKDAArekqRAMEDLQKFRSQAEEAERRMKQAEVEKE 2147
Cdd:COG1842 159 DSDDaTSALERMEEKIEEMEARA----EAAAELAAGDSLDDELAELEADSEVEDE 209
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1619-2158 |
3.53e-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: 44.27 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1619 ELEGIKKNLDKVSEKTQKVLAQKEQSTSTPLLRTEHEITLQKMDQVYSLSTiylEKLKTINLVIRSTHGAEEVVKTY--E 1696
Cdd:TIGR01612 1023 EKEKATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDEIEKEIGKNIELLNK---EILEEAEINITNFNEIKEKLKHYnfD 1099
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1697 DQLKEVHAVPSDskELEATKAELKKLRSQVEGHqplFNTLEADLNKAKD-VNEQMLRSHSERDV-DLDRYRERVQQLLER 1774
Cdd:TIGR01612 1100 DFGKEENIKYAD--EINKIKDDIKNLDQKIDHH---IKALEEIKKKSENyIDEIKAQINDLEDVaDKAISNDDPEEIEKK 1174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1775 WQAILVQIDLRQRELDQLGRQLRYYREtydwlikwIKDAKQRQEQIQSVPITDSKTMKEQLLQLkklleeIESNRTKVDE 1854
Cdd:TIGR01612 1175 IENIVTKIDKKKNIYDEIKKLLNEIAE--------IEKDKTSLEEVKGINLSYGKNLGKLFLEK------IDEEKKKSEH 1240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1855 CQKYAKQYIDAIKDYELQLVTYKAQVEPVVSPAKKPKVQSTSDSIIQEYVDLRTRYSE-LTTLTSQYIKFITETLCRLNV 1933
Cdd:TIGR01612 1241 MIKAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFNISHDDDKDHHIISKKHDEnISDIREKSLKIIEDFSEESDI 1320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1934 EE--KAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAK--------AQAEKEAEELQRRMQEEVSKREVVA------VD 1997
Cdd:TIGR01612 1321 NDikKELQKNLLDAQKHNSDINLYLNEIANIYNILKLNKikkiidevKEYTKEIEENNKNIKDELDKSEKLIkkikddIN 1400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1998 AEQQKQTIQ------------QELQQLRQ-------NSDMEIKSKAKKIEEAEYNRRKIE----EEIHIVRLQLETMQKQ 2054
Cdd:TIGR01612 1401 LEECKSKIEstlddkdideciKKIKELKNhilseesNIDTYFKNADENNENVLLLFKNIEmadnKSQHILKIKKDNATND 1480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2055 KASAEDELQELRARA----EEAERQKKAAQEEAERLRRQVKDESQK-KREAEEELKRKVQAEKDAAREKQRAMEDLQ-KF 2128
Cdd:TIGR01612 1481 HDFNINELKEHIDKSkgckDEADKNAKAIEKNKELFEQYKKDVTELlNKYSALAIKNKFAKTKKDSEIIIKEIKDAHkKF 1560
|
570 580 590
....*....|....*....|....*....|
gi 1717010358 2129 RSQAEEAERRMKqaEVEKErQIKVAQEVAQ 2158
Cdd:TIGR01612 1561 ILEAEKSEQKIK--EIKKE-KFRIEDDAAK 1587
|
|
| 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 ... |
2672-2783 |
3.55e-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: 40.76 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2672 RAKRAAEDADYARMRAEQEAALsrqqvEEAERMKQRAEEEAQA-KAQAQDEAEKLRKEAEleaakrAHAEQAALKQKQLA 2750
Cdd:pfam00430 32 RELIADEIAEAEERRKDAAAAL-----AEAEQQLKEARAEAQEiIENAKKRAEKLKEEIV------AAAEAEAERIIEQA 100
|
90 100 110
....*....|....*....|....*....|...
gi 1717010358 2751 DEEMDKHKKFAEKTLRQKAqVEQELTKVKLQLE 2783
Cdd:pfam00430 101 AAEIEQEKDRALAELRQQV-VALAVQIAEKLLE 132
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2091-2298 |
3.55e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.43 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2091 KDESQKKREAEE---ELKRKVQAEKDAAREKQRAMEDLQKFRSQAeeaerrmKQAEVEKERQIKVAQEVAQQSAAAELNS 2167
Cdd:PRK07735 5 KDLEDLKKEAARrakEEARKRLVAKHGAEISKLEEENREKEKALP-------KNDDMTIEEAKRRAAAAAKAKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2168 KRMSFAEKTAQLELSLKQEhiTVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKAN---EALRLRLQAEEVAHKKTl 2244
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAK--AAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAakaKAAALAKQKREGTEEVT- 154
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2245 aQEEAEKQKEDAEREARKRAKAEESALRQKELAE--DELEKQRKLADATAQQKFSA 2298
Cdd:PRK07735 155 -EEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEagEGTEEVTEEEKAKAKAKAAA 209
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
636-694 |
3.65e-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: 39.95 E-value: 3.65e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 636 KKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREK----GRMRFHKLQNV 694
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVV 65
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
635-732 |
3.69e-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: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 635 QKKTFTKWVNKHL---------IKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDY 700
Cdd:cd21293 2 EKGSYVDHINRYLgddpflkqfLPIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1717010358 701 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 732
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
1969-2160 |
3.80e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 43.70 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1969 AKAQAEKEAEELQ--RRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNSDMEIKSKAKKIeeaeynRRKIEEEIHIVRL 2046
Cdd:PRK00106 24 IKMKSAKEAAELTllNAEQEAVNLRGKAERDAEHIKKTAKRESKALKKELLLEAKEEARKY------REEIEQEFKSERQ 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2047 ---QLETMQKQKASAEDELQE-LRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRAm 2122
Cdd:PRK00106 98 elkQIESRLTERATSLDRKDEnLSSKEKTLESKEQSLTDKSKHIDEREEQVEKLEEQKKAELERVAALSQAEAREIILA- 176
|
170 180 190
....*....|....*....|....*....|....*....
gi 1717010358 2123 edlQKFRSQAEEAERRMKQAEVE-KERQIKVAQEVAQQS 2160
Cdd:PRK00106 177 ---ETENKLTHEIATRIREAEREvKDRSDKMAKDLLAQA 212
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2856-3053 |
3.89e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.78 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2856 EAEKMRQVAEEAARLSiEAQEAARMRKlAEDDLANQRALAEkmLKEKMQAIQEATRLKAEADMLQKQkELAQEQARKFQE 2935
Cdd:PRK05035 456 EARQARLEREKAAREA-RHKKAAEARA-AKDKDAVAAALAR--VKAKKAAATQPIVIKAGARPDNSA-VIAAREARKAQA 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2936 DKEQIEQQLAKETEGFQKSLEA------ERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEDFGNKLHQTEL 3009
Cdd:PRK05035 531 RARQAEKQAAAAADPKKAAVAAaiarakAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEV 610
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 3010 ATKERMVV-------VQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEA 3053
Cdd:PRK05035 611 DPKKAAVAaaiarakAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAA 661
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2550-2744 |
3.93e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 43.85 E-value: 3.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2550 EKAEQEAEKQRQLALE------EEQRRKEAEEKvrkiladEQEAarqrKAALEEvERL--KAKAEEAKRqkELAEKEAER 2621
Cdd:PTZ00491 643 ERTRDSLQKSVQLAIEittksqEAAARHQAELL-------EQEA----RGRLER-QKMhdKAKAEEQRT--KLLELQAES 708
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2622 Q-IQLAQEAafkKIEAEEKAHAAIVQQkEQEMLQTRkqeksildkLKEEAERAKRAAEdadYARMRAEQEAALS-RQQVE 2699
Cdd:PTZ00491 709 AaVESSGQS---RAEALAEAEARLIEA-EAEVEQAE---------LRAKALRIEAEAE---LEKLRKRQELELEyEQAQN 772
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2700 EAERMKqraeeeaqAKAQAQDEAEKLRKEAE------LEAAKRAHAE-QAAL 2744
Cdd:PTZ00491 773 ELEIAK--------AKELADIEATKFERIVEalgretLIAIARAGPElQAKL 816
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
2058-2159 |
4.12e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 41.48 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2058 AEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEElkrkvQAEKDAAREKQRAMEDLQKFRSQAEEAER 2137
Cdd:PRK07352 62 AEERLRQAAQALAEAQQKLAQAQQEAERIRADAKARAEAIRAEIEK-----QAIEDMARLKQTAAADLSAEQERVIAQLR 136
|
90 100
....*....|....*....|....*.
gi 1717010358 2138 R----MKQAEVEKERQIKVAQEVAQQ 2159
Cdd:PRK07352 137 ReaaeLAIAKAESQLPGRLDEDAQQR 162
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
2574-2658 |
4.17e-03 |
|
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: 40.93 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2574 EEKVRKILADEQEAARQRK---AALEEVERLKAKAE-EAKRQKELAEKEAERQIQLAQEAAFKKIEAE-EKAHAAIVQQK 2648
Cdd:COG0711 30 DERQEKIADGLAEAERAKEeaeAALAEYEEKLAEARaEAAEIIAEARKEAEAIAEEAKAEAEAEAERIiAQAEAEIEQER 109
|
90
....*....|
gi 1717010358 2649 EQEMLQTRKQ 2658
Cdd:COG0711 110 AKALAELRAE 119
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
634-736 |
4.26e-03 |
|
second calponin homology (CH) domain found in alpha-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. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin 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: 409186 Cd Length: 129 Bit Score: 40.75 E-value: 4.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 634 VQKKTFTKWVNKHLIKAQRHVTDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLKHRQVKLV 709
Cdd:cd21337 20 VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQDGGLEKP 99
|
90 100
....*....|....*....|....*..
gi 1717010358 710 NIRNDDIADGNPKLTLGLIWTIILHFQ 736
Cdd:cd21337 100 KPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3281-3318 |
4.27e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.85 E-value: 4.27e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1717010358 3281 KKYLKGKSSIAGLLLKPSNEKMSIYEATKRKLLTPGTA 3318
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1943-2040 |
4.36e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 43.79 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1943 EEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEelqrRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNS---DME 2019
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAE----AQQQELVALEGLAAELEEKQQELEAQLEQLQEKAaetSQE 213
|
90 100
....*....|....*....|.
gi 1717010358 2020 IKSKAKKIEEAEYNRRKIEEE 2040
Cdd:PRK11448 214 RKQKRKEITDQAAKRLELSEE 234
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
2548-2636 |
4.36e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 40.76 E-value: 4.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2548 SKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKILAD-EQEAARQRKAALEEVERlkakaeEAKRQKELAEKEAERQIQLA 2626
Cdd:PRK07353 44 NRAEAKERLAEAEKLEAQYEQQLASARKQAQAVIAEaEAEADKLAAEALAEAQA------EAQASKEKARREIEQQKQAA 117
|
90
....*....|
gi 1717010358 2627 QEAAFKKIEA 2636
Cdd:PRK07353 118 LAQLEQQVDA 127
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2875-3172 |
4.58e-03 |
|
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: 43.67 E-value: 4.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2875 QEAARMRKLAEDDLANQRALAEKMlkekmqaiqeatrlKAEADmlqKQKeLAQEQArkfqedkeqieQQLAkETEGFQKS 2954
Cdd:NF012221 1542 QQADAVSKHAKQDDAAQNALADKE--------------RAEAD---RQR-LEQEKQ-----------QQLA-AISGSQSQ 1591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2955 LEAERRQQLEITAEAERlklqvlemskaqakaeeDAkkFKKQAEDFgnklhqtelaTKERMVVVQSLEI---QRQQSGKE 3031
Cdd:NF012221 1592 LESTDQNALETNGQAQR-----------------DA--ILEESRAV----------TKELTTLAQGLDAldsQATYAGES 1642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3032 AEELRRAIAE--LEHEKEKL--------KQEAELLQKNSQEMQVAQQEQLRQETQVLQttflTEKHLLlekekyiekeka 3101
Cdd:NF012221 1643 GDQWRNPFAGglLDRVQEQLddakkisgKQLADAKQRHVDNQQKVKDAVAKSEAGVAQ----GEQNQA------------ 1706
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 3102 KLENLYEDevRKAQKLKQEQEHQLKQLEEEKQQLKAS-MGEAMKKQKEAEESVRHKQDELHQLDKRRQEQEK 3172
Cdd:NF012221 1707 NAEQDIDD--AKADAEKRKDDALAKQNEAQQAESDANaAANDAQSRGEQDASAAENKANQAQADAKGAKQDE 1776
|
|
| V-ATPase_G_2 |
pfam16999 |
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ... |
2553-2634 |
4.59e-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: 39.73 E-value: 4.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2553 EQEAEKQRQLALEEEQRRKEAEEKVRkilADEQEAARQRKAALEEVERLKAK-----AEEAKRQKELAEKEAERQIQLAQ 2627
Cdd:pfam16999 8 SELAEREAALDQQIEAARKEAEREVE---AAEAEAARILREAEAKAKALQAEyrqelAAETARIREEARARAEAEAQAVR 84
|
....*..
gi 1717010358 2628 EAAFKKI 2634
Cdd:pfam16999 85 TRAEGRL 91
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1930-2170 |
4.60e-03 |
|
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: 43.10 E-value: 4.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1930 RLNVEEKAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEaeELQRRMQEEVSKREvvavdAEQQKQTIQQEL 2009
Cdd:pfam15558 57 QQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQ--ENQRQEKLERARQE-----AEQRKQCQEQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2010 QQ----LRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQK---KAAQEE 2082
Cdd:pfam15558 130 KEkeeeLQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELLRRLsleQSLQRS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2083 AERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQRamEDLQKFRSQAEEAERRMKQAEVEKERQIK-VAQEVAQQSA 2161
Cdd:pfam15558 210 QENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE--ERQEHKEALAELADRKIQQARQVAHKTVQdKAQRARELNL 287
|
....*....
gi 1717010358 2162 AAELNSKRM 2170
Cdd:pfam15558 288 EREKNHHIL 296
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1939-2149 |
4.74e-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: 43.13 E-value: 4.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1939 EKLKEEERRRLAEVEAQLEKQTqlaEAHAKAKAQAEKEAEELQRRMQEEVSKREVVAVDAEQQKQTIQQELQQLRQNsDM 2018
Cdd:pfam19220 201 ETQLDATRARLRALEGQLAAEQ---AERERAEAQLEEAVEAHRAERASLRMKLEALTARAAATEQLLAEARNQLRDR-DE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2019 EIKSKAKKIEEAEYNRRKIEEEihivrlqLETMQKQKASAEDELQEL-RARAEEAER----QKKAAQEEAERLRRQVKDE 2093
Cdd:pfam19220 277 AIRAAERRLKEASIERDTLERR-------LAGLEADLERRTQQFQEMqRARAELEERaemlTKALAAKDAALERAEERIA 349
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2094 SQKKREaeEELKRKVQAEKDAAREKQRAM-EDLQkfrsqAEEAERRMKQAEVEKERQ 2149
Cdd:pfam19220 350 SLSDRI--AELTKRFEVERAALEQANRRLkEELQ-----RERAERALAQGALEIARE 399
|
|
| PRK09098 |
PRK09098 |
HrpE/YscL family type III secretion apparatus protein; |
2625-2743 |
4.95e-03 |
|
HrpE/YscL family type III secretion apparatus protein;
Pssm-ID: 181646 [Multi-domain] Cd Length: 233 Bit Score: 42.10 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2625 LAQEAAFKKIEAE-EKAHAAIVQQKEQEMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSR---QQVEE 2700
Cdd:PRK09098 28 LALDAALAAVHAErDAVLAAARARAERIVAEARAQAEAILEAARREADRSARRGYAAGLRQALAEWHARGADhafAERRA 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 2701 AERMKQRAEE---------------------EAQAKAQAQDEAEKLR---KEAELEAAKRAHAEQAA 2743
Cdd:PRK09098 108 ARRMRERLAEivaaaveqivlgedraalfarAAQTLERVVDGASYLTvrvHPADLDAARAAFGAAAA 174
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2663-2792 |
4.98e-03 |
|
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: 40.31 E-value: 4.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2663 LDKLKEEAERAKRAAEDADYARMRAEQEaalSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEA-ELEAAKRAHAEQ 2741
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQED---LEKQAEIAREAQQNYERELVLHAEDIKALQALREELnELKAEIAELKAE 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 2742 AALKQKQLADEEmdkhkkfaEKTLRQKAQVEQELTKVKLQLEETDHQKTLL 2792
Cdd:pfam07926 80 AESAKAELEESE--------ESWEEQKKELEKELSELEKRIEDLNEQNKLL 122
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2137-2458 |
5.02e-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: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2137 RRMKQAEVEKERQIKVAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEK 2216
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2217 ELEKWHQKANEALRLRLQAE-EVAHKKTLAQEEAEKQKEDAEREARK---RAKAEESALRQKELAEDELEKQRKLADATA 2292
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEiDEFNEEQAEWKELEKEEEREEDERILeylKEKAEREEEREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2293 QQkfsaeQELIRLKADTESGEQQRLLLEEELFRLKNEVnEAIQKRKKMEEELAKVRAEmEILLESKSRAEEesrsnteks 2372
Cdd:pfam13868 192 QQ-----EKAQDEKAERDELRAKLYQEEQERKERQKER-EEAEKKARQRQELQQAREE-QIELKERRLAEE--------- 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2373 KHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAENER 2452
Cdd:pfam13868 256 AEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEER 335
|
....*.
gi 1717010358 2453 LRRLAE 2458
Cdd:pfam13868 336 QKKLKE 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2880-3054 |
5.08e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 5.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2880 MRKLAEDDLANQRALAEKMLKE---KMQAIQEATRLKAEADMLQKQKELAQEQARKFQEDKEQiEQQLAKETEGFQKSLE 2956
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEakkEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKL-EKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2957 AERRQQLEITAEAERLKLQVLEMSKAQAKAEEDAKKFKKQAEdfgnklhqtELA--TKE--RMVVVQSLEiqrqqsgkea 3032
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELE---------RISglTAEeaKEILLEKVE---------- 164
|
170 180
....*....|....*....|...
gi 1717010358 3033 EELRRAIAELEHEKEKL-KQEAE 3054
Cdd:PRK12704 165 EEARHEAAVLIKEIEEEaKEEAD 187
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2809-2988 |
5.24e-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: 43.02 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2809 QKAQVEEELFKVKIQMEELIKLKLRIEEENKMLIMKDKDSTQKflAEEAEKMRQVAEEAARLSIEAQEAARMRKLAEDDL 2888
Cdd:pfam15709 360 QRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR--QEEEERKQRLQLQAAQERARQQQEEFRRKLQELQR 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2889 ANQRALAEKMLKEKMQAIQEATRLKAEADMLQkqkELAQEQARKFQEDKEQIEQQLAKETEgfqksleaERRQQLEitaE 2968
Cdd:pfam15709 438 KKQQEEAERAEAEKQRQKELEMQLAEEQKRLM---EMAEEERLEYQRQKQEAEEKARLEAE--------ERRQKEE---E 503
|
170 180
....*....|....*....|
gi 1717010358 2969 AERLKLQVLeMSKAQAKAEE 2988
Cdd:pfam15709 504 AARLALEEA-MKQAQEQARQ 522
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
3013-3185 |
5.28e-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: 41.83 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3013 ERMVVVQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELL---------QKNSQEMQVAQQEQLRQETQVLQTTFL 3083
Cdd:COG1579 7 RALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAkteledlekEIKRLELEIEEVEARIKKYEEQLGNVR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3084 TEKHLllekekyiekekakleNLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKASMGEAMKKQKEAEESVRHKQDEL--- 3160
Cdd:COG1579 87 NNKEY----------------EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELdee 150
|
170 180 190
....*....|....*....|....*....|...
gi 1717010358 3161 --------HQLDKRRQEQEKLLADENRKLREKL 3185
Cdd:COG1579 151 laeleaelEELEAEREELAAKIPPELLALYERI 183
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
2063-2168 |
5.30e-03 |
|
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: 42.67 E-value: 5.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2063 QELRARAEEAERQKKAAQEEAERLRRqvKDESQKKREAEEELKRKVQAEKdaAREKQRAMEDlqkfRSQAEEAERRMKQA 2142
Cdd:pfam07767 198 QELLQKAVEAEKKRLKEEEKLERVLE--KIAESAATAEAREEKRKTKAQR--NKEKRRKEEE----REAKEEKALKKKLA 269
|
90 100
....*....|....*....|....*...
gi 1717010358 2143 EVEKERQIK--VAQEVAQQSAAAELNSK 2168
Cdd:pfam07767 270 QLERLKEIAkeIAEKEKEREEKAEARKR 297
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1705-1879 |
5.45e-03 |
|
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: 41.66 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1705 VPSDSKELEATKAELKKLRSQVEGHQPLFNTLEAdlnkakdVNEQMLRSHSERDVDLdryRERVQQLLERWQAILVQIDL 1784
Cdd:cd00176 28 YGDDLESVEALLKKHEALEAELAAHEERVEALNE-------LGEQLIEEGHPDAEEI---QERLEELNQRWEELRELAEE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1785 RQRELDQLGRQLRYYRETYDwLIKWIKDAKQRQEQIQsvPITDSKTMKEQLLQLKKLLEEIESNRTKVDECQKYAKQYID 1864
Cdd:cd00176 98 RRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEELLE 174
|
170
....*....|....*
gi 1717010358 1865 AIKDYELQLVTYKAQ 1879
Cdd:cd00176 175 EGHPDADEEIEEKLE 189
|
|
| PRK00247 |
PRK00247 |
putative inner membrane protein translocase component YidC; Validated |
2034-2155 |
5.47e-03 |
|
putative inner membrane protein translocase component YidC; Validated
Pssm-ID: 178945 [Multi-domain] Cd Length: 429 Bit Score: 42.92 E-value: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2034 RRKIEEEIHIVRLQLETMQKQKASA---EDELQELRARAEEAERQKKAAQEEaERLRRqvKDESQKKREAEEELKRKVQA 2110
Cdd:PRK00247 291 RAQYREKQKEKKAFLWTLRRNRLRMiitPWRAPELHAENAEIKKTRTAEKNE-AKARK--KEIAQKRRAAEREINREARQ 367
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1717010358 2111 EKDAAREKQRAmedlqkfRSQAEEAERRMKQAEVEKERQIKVAQE 2155
Cdd:PRK00247 368 ERAAAMARARA-------RRAAVKAKKKGLIDASPNEDTPSENEE 405
|
|
| PRK13428 |
PRK13428 |
F0F1 ATP synthase subunit delta; Provisional |
1922-2069 |
5.52e-03 |
|
F0F1 ATP synthase subunit delta; Provisional
Pssm-ID: 184048 [Multi-domain] Cd Length: 445 Bit Score: 42.80 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1922 KFITETLCRLnveekaAEKLKEEERRRLAEVEAQLEKQTQLAEAHAKAKAQAEKEAEELQRRMQEEVSK-----REVVAV 1996
Cdd:PRK13428 20 RFVVPPVRRL------MAARQDTVRQQLAESATAADRLAEADQAHTKAVEDAKAEAARVVEEAREDAERiaeqlRAQADA 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 1997 DAEQQKQTIQQELQQLRQNSDMEIKSK--AKKIEEAEynrrkieeeiHIVRLQLETMQKQKASAEDELQELRARA 2069
Cdd:PRK13428 94 EAERIKVQGARQVQLLRAQLTRQLRLElgHESVRQAG----------ELVRNHVADPAQQSATVDRFLDELDAMA 158
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2246-2465 |
5.54e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 5.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2246 QEEAEKQKEDAEREARKRAKAEESALRQKELAEDE----LEKQRKLADAtaQQKFSAEQElirlkadtesgeqqrlllee 2321
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQErlkqLEKERLAAQE--QKKQAEEAA-------------------- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2322 elfrlknevNEAIQKRKKMEEELAKVRAEmeilleSKSRAEEESRSNTEKSKHMlEVEASKLrelAEEAARLRAlSEEAK 2401
Cdd:PRK09510 125 ---------KQAALKQKQAEEAAAKAAAA------AKAKAEAEAKRAAAAAKKA-AAEAKKK---AEAEAAKKA-AAEAK 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2402 RQrqiAEGEAA-------RQRAEAERILKEKLAAINEATRL-KTEAEIALKEKEAENERLRRLAEDEAYQRK 2465
Cdd:PRK09510 185 KK---AEAEAAakaaaeaKKKAEAEAKKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2530-2669 |
5.57e-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: 41.83 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2530 DLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRRKEAEEKVRKI--------LADEQEAARQRKAALEEVERl 2601
Cdd:COG1579 35 ELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyeaLQKEIESLKRRISDLEDEIL- 113
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2602 kaKAEEAKRQKELAEKEAERQIQLAQEaafkKIEAEEKAHAAIVQQKEQEMLQTRKQEKSILDKLKEE 2669
Cdd:COG1579 114 --ELMERIEELEEELAELEAELAELEA----ELEEKKAELDEELAELEAELEELEAEREELAAKIPPE 175
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2025-2139 |
5.61e-03 |
|
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: 39.90 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2025 KKIEEAEYNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEEL 2104
Cdd:pfam20492 6 REKQELEERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAEL 85
|
90 100 110
....*....|....*....|....*....|....*
gi 1717010358 2105 KRKVQAEKDAAREKQRAMEDLQKFRSQAEEAERRM 2139
Cdd:pfam20492 86 AEAQEEIARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
3018-3230 |
5.65e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.89 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3018 VQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQ---VAQQEQLRQETQVLQTTfltekhlllekek 3094
Cdd:COG3883 32 LEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEaeiEERREELGERARALYRS------------- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3095 yiEKEKAKLENL-----YEDEVRKAQKLKQEQEHQ------LKQLEEEKQQLKAsmgEAMKKQKEAEESVRHKQDELHQL 3163
Cdd:COG3883 99 --GGSVSYLDVLlgsesFSDFLDRLSALSKIADADadlleeLKADKAELEAKKA---ELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1717010358 3164 DKRRQEQEKLLADENRKLREKLEQLEEEHRIALAQTREMMIQTDDLAGSSQTKAMPNGRDAVDGLAQ 3230
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
2541-2614 |
5.67e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 43.32 E-value: 5.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2541 IAEETHRSKEK-AEQEAEKQRQlalEEEQRRKEAEekvrkiladeqeaarqrKAAlEEVERLKAKAEEAKRQKEL 2614
Cdd:PLN02316 250 LLEEKRRELEKlAKEEAERERQ---AEEQRRREEE-----------------KAA-MEADRAQAKAEVEKRREKL 303
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2045-2159 |
5.73e-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: 41.61 E-value: 5.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2045 RLQLETMQKQKASAEDELQELRAR-AEEAER---QKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAAREKQR 2120
Cdd:pfam13904 68 RQKELQAQKEEREKEEQEAELRKRlAKEKYQewlQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVLQEW 147
|
90 100 110
....*....|....*....|....*....|....*....
gi 1717010358 2121 AMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQ 2159
Cdd:pfam13904 148 ERKKLEQQQRKREEEQREQLKKEEEEQERKQLAEKAWQK 186
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2053-2147 |
5.78e-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: 42.18 E-value: 5.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2053 KQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAE-KDAAREKQRAMEDLQKFRSQ 2131
Cdd:cd16269 191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEErENLLKEQERALESKLKEQEA 270
|
90
....*....|....*.
gi 1717010358 2132 AEEAERRMKQAEVEKE 2147
Cdd:cd16269 271 LLEEGFKEQAELLQEE 286
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2395-2622 |
5.83e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 5.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2395 ALSEEAKRQRQiaeGEAARQRAEAERILKEKlaaineatrlkTEAEIALKEKEAENERLRRLAedeayQRKLLEEQatQH 2474
Cdd:PRK09510 59 AVVEQYNRQQQ---QQKSAKRAEEQRKKKEQ-----------QQAEELQQKQAAEQERLKQLE-----KERLAAQE--QK 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2475 KQDIEEKIILLKKSSDNELERQKNIVEDTLRQRRIIEEEIRILKlnfeKASSGKSDLELELNQLKNIAEethrSKEKAEQ 2554
Cdd:PRK09510 118 KQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAK----KAAAEAKKKAEAEAAKKAAAE----AKKKAEA 189
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2555 EAeKQRQLALEEEQRRKEAEEKVrKILADEQEAARQRKAALEEVERLKAKAEEAKRQKELAEKEAERQ 2622
Cdd:PRK09510 190 EA-AAKAAAEAKKKAEAEAKKKA-AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1957-2115 |
5.96e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 40.53 E-value: 5.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1957 EKQTQLAEAHAKAKaQAEKEAEELQRRMQEEVSKrevvavdAEQQKQTIqqelqqlrqnsdmeikskakkIEEAEYNRRK 2036
Cdd:PRK05759 35 ERQKKIADGLAAAE-RAKKELELAQAKYEAQLAE-------ARAEAAEI---------------------IEQAKKRAAQ 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2037 IEEEIhivrlqletmqkqKASAEDELQELRARA-EEAERQKKAAQEEaerLRRQVKDESQKKreAEEELKRKVQAEKDAA 2115
Cdd:PRK05759 86 IIEEA-------------KAEAEAEAARIKAQAqAEIEQERKRAREE---LRKQVADLAVAG--AEKILGRELDAAAQSD 147
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2537-2640 |
6.20e-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: 42.18 E-value: 6.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2537 QLKNIAEETHRSKEKAEQEAEKQrqlaLEEEQRRKEAEEKVRKILADEQEAARQRKAA-----LEEVERLKAKAEEaKRQ 2611
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKE----IEAERAKAEAAEQERKLLEEQQRELEQKLEDqersyEEHLRQLKEKMEE-ERE 251
|
90 100
....*....|....*....|....*....
gi 1717010358 2612 KELAEKEAERQIQLAQEAAFKKIEAEEKA 2640
Cdd:cd16269 252 NLLKEQERALESKLKEQEALLEEGFKEQA 280
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2856-2990 |
6.27e-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: 6.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2856 EAEKMRQVAEEAARLSIEAQEAARMRKLAEDDLANQRALAEKMLKEKMQAIQEAtrlKAEADMLQKQKELAQEQARKFQE 2935
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1717010358 2936 DKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERLKLQVLEMSKAQAKAEEDA 2990
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA 327
|
|
| PRK10476 |
PRK10476 |
multidrug transporter subunit MdtN; |
2638-2754 |
6.29e-03 |
|
multidrug transporter subunit MdtN;
Pssm-ID: 182488 [Multi-domain] Cd Length: 346 Bit Score: 42.32 E-value: 6.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2638 EKAHAAIVQQKEQEMLQTR--KQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAA---LSRQQVEEAERMKQRAEEE- 2711
Cdd:PRK10476 89 AQAQADLALADAQIMTTQRsvDAERSNAASANEQVERARANAKLATRTLERLEPLLAkgyVSAQQVDQARTAQRDAEVSl 168
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1717010358 2712 AQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADEEM 2754
Cdd:PRK10476 169 NQALLQAQAAAAAVGGVDALVAQRAAREAALAIAELHLEDTTV 211
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2337-2784 |
6.38e-03 |
|
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: 42.82 E-value: 6.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2337 RKKMEEELAKVRAEMEILLEsksraEEESRSNTEKSKHMLEVEASklrelaEEAARLRALSEEAKRQRQIAEGEAARQRA 2416
Cdd:pfam09731 33 RDFFEEYIPYGEEVVLYALG-----EDPPLAPKPKTFRPLQPSVV------SAVTGESKEPKEEKKQVKIPRQSGVSSEV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2417 EaerilKEKLAAINEATRLKTEAEIALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSDNELERQ 2496
Cdd:pfam09731 102 A-----EEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEIS 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2497 KNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEkAEQEAEKQRQLALEEEQRRKEAEEk 2576
Cdd:pfam09731 177 REKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDN-VEEKVEKAQSLAKLVDQYKELVAS- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2577 vrkilaDEQEAARQRKAALEEV-----ERLKAKAEEAKRqkeLAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQE 2651
Cdd:pfam09731 255 ------ERIVFQQELVSIFPDIipvlkEDNLLSNDDLNS---LIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEEL 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2652 mlqtRKQEKSILDKLKEEAErakraaedADYARMRAEQEAALSRQQveeaERMKqraeeeaqakaqaqdeaEKLRKE-AE 2730
Cdd:pfam09731 326 ----DKLAEELSARLEEVRA--------ADEAQLRLEFEREREEIR----ESYE-----------------EKLRTElER 372
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2731 LEAAKRAHAEQAALKQKQLADEEMDKHKKfaEKTLRQKAQVEQELTKVKLQLEE 2784
Cdd:pfam09731 373 QAEAHEEHLKDVLVEQEIELQREFLQDIK--EKVEEERAGRLLKLNELLANLKG 424
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2683-2837 |
6.40e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.15 E-value: 6.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2683 ARMRAEQEAALsrQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAELEAAKRAHAEQAALKQKQLADeemdkhKKFAE 2762
Cdd:COG0542 400 ARVRMEIDSKP--EELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAE------KELIE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2763 KTLRQKAQVEQELTKVKLQLEETDHQKTLLDDESQRLKEEVTdamrqkaqvEEELFKV----------KIQMEELIKLkL 2832
Cdd:COG0542 472 EIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVT---------EEDIAEVvsrwtgipvgKLLEGEREKL-L 541
|
....*
gi 1717010358 2833 RIEEE 2837
Cdd:COG0542 542 NLEEE 546
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
2032-2127 |
6.48e-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: 39.84 E-value: 6.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2032 YNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAERQKKA-------AQEEAERLRRQVKDESQK-KREAEEE 2103
Cdd:COG3599 20 YDEDEVDEFLDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETlqktlvvAQETAEEVKENAEKEAELiIKEAELE 99
|
90 100
....*....|....*....|....
gi 1717010358 2104 LKRKVQAEKDAAREKQRAMEDLQK 2127
Cdd:COG3599 100 AEKIIEEAQEKARKIVREIEELKR 123
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
2024-2108 |
6.67e-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: 40.11 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2024 AKKIEEAEYNRRKIEEeihivrlQLETMQKQKASAEDELQELRARA-----EEAERQKKAAQEEAERLRRQVKDE-SQKK 2097
Cdd:cd06503 36 AESLEEAEKAKEEAEE-------LLAEYEEKLAEARAEAQEIIEEArkeaeKIKEEILAEAKEEAERILEQAKAEiEQEK 108
|
90
....*....|.
gi 1717010358 2098 REAEEELKRKV 2108
Cdd:cd06503 109 EKALAELRKEV 119
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
2332-2786 |
6.90e-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: 6.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2332 EAIQKRKKMEEELAKvRAEMEILLESKSRAEEESRSNTEKSKHMLEVEASKLRELAEEAARLRALSEEAKRQRQIAEGEA 2411
Cdd:COG3064 19 EQAEAEKRAAAEAEQ-KAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKAAAEAEKKAAAEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2412 ARQRAEAERILKEKLAAINEATRLKTEAEI-ALKEKEAENERLRRLAEDEAYQRKLLEEQATQHKQDIEEKIILLKKSSD 2490
Cdd:COG3064 98 AKAAKEAEAAAAAEKAAAAAEKEKAEEAKRkAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2491 NELERQKNIVEDTLRQRRIIEEEIRILKLNFEKASSGKSDLELELNQLKNIAEETHRSKEKAEQEAEKQRQLALEEEQRR 2570
Cdd:COG3064 178 AAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2571 KEAEEKVRKILADEQEAARQRKAALEEVERLKAKAEEAKRQKElAEKEAERQIQLAQEAAFKKIEAEEKAHAAIVQQKEQ 2650
Cdd:COG3064 258 GVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDS-AALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAAS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2651 EMLQTRKQEKSILDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEAQAKAQAQDEAEKLRKEAE 2730
Cdd:COG3064 337 LEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAAS 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2731 LEAAKRAHAEQAALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQLEETD 2786
Cdd:COG3064 417 AVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALD 472
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2919-3054 |
6.93e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 6.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2919 LQKQKELAQ--EQARKFQEDK--EQIEQQLAKETEGfQKSLEAERRQQLEITAEAERLKLQVLEMSK----AQAKAEEDA 2990
Cdd:PRK09510 67 QQQQQKSAKraEEQRKKKEQQqaEELQQKQAAEQER-LKQLEKERLAAQEQKKQAEEAAKQAALKQKqaeeAAAKAAAAA 145
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1717010358 2991 KKfKKQAEDfgnklHQTELATKERMVVVQSLEIQRQQSGKEAEELRRAIAElehEKEKLKQEAE 3054
Cdd:PRK09510 146 KA-KAEAEA-----KRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAE---AAAKAAAEAK 200
|
|
| DivIVA |
COG3599 |
Cell division septum initiation protein DivIVA, interacts with FtsZ and MinD [Cell cycle ... |
2663-2752 |
7.00e-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: 39.84 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2663 LDKLKEEAERAKRAAEDADYARMRAEQEAALSRQQVEEAERMKQRAEEEA-QAKAQAQDEAEKLRKEAELEAAKraHAEQ 2741
Cdd:COG3599 29 LDEVAEDYERLIRENKELKEKLEELEEELEEYRELEETLQKTLVVAQETAeEVKENAEKEAELIIKEAELEAEK--IIEE 106
|
90
....*....|.
gi 1717010358 2742 AALKQKQLADE 2752
Cdd:COG3599 107 AQEKARKIVRE 117
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2936-3209 |
7.00e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 43.12 E-value: 7.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2936 DKEQIEQQLaKETEGFQKSLEAErrqqleiTAEAERLKLQVLEMSKAqakAEEDAKKFKKQAEDFgNKLHQtELatkerm 3015
Cdd:PRK10929 24 DEKQITQEL-EQAKAAKTPAQAE-------IVEALQSALNWLEERKG---SLERAKQYQQVIDNF-PKLSA-EL------ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3016 vvvqsleiqRQQSGKEAEELRR-----AIAELEHEkeklkqeaeLLQKNSQEMQVAQQEQlrQEtqvlqttfltekhlll 3090
Cdd:PRK10929 85 ---------RQQLNNERDEPRSvppnmSTDALEQE---------ILQVSSQLLEKSRQAQ--QE---------------- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3091 ekekyiekekaklenlyEDEVRKA----QKLKQEQEHQLKQLEEEKQQLKA------SMGEAMKKQKEAeESVRHK---- 3156
Cdd:PRK10929 129 -----------------QDRAREIsdslSQLPQQQTEARRQLNEIERRLQTlgtpntPLAQAQLTALQA-ESAALKalvd 190
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 3157 QDELHQLD-KRRQEQEKLLADENRKLREKLE------------QLEEEHRIALAQTREMMIQTDDL 3209
Cdd:PRK10929 191 ELELAQLSaNNRQELARLRSELAKKRSQQLDaylqalrnqlnsQRQREAERALESTELLAEQSGDL 256
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1926-2069 |
7.02e-03 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 42.34 E-value: 7.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1926 ETLCRLNVEE-----KAAEKLKEEERRRLAEVEAQLEKQTQLAEAHAK-AKAQAE-KEAEELQRRMQeEVSKREVVavdA 1998
Cdd:COG1566 71 QVLARLDPTDlqaalAQAEAQLAAAEAQLARLEAELGAEAEIAAAEAQlAAAQAQlDLAQRELERYQ-ALYKKGAV---S 146
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1717010358 1999 EQQKQTIQQELQQLRQNsdmeIKSKAKKIEEAEyNRRKIEEEIHIVRLQLETMQKQKASAEDELQELRARA 2069
Cdd:COG1566 147 QQELDEARAALDAAQAQ----LEAAQAQLAQAQ-AGLREEEELAAAQAQVAQAEAALAQAELNLARTTIRA 212
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2917-3137 |
7.10e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 7.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2917 DMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKSLEAERRQQLEITAEAERL--KLQVLEMSKAQAKAEEDAKKFK 2994
Cdd:COG4717 45 AMLLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELeeELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2995 KQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSgkeaEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQE 3074
Cdd:COG4717 125 LQLLPLYQELEALEAELAELPERLEELEERLEEL----RELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 3075 TQVLQTTfltekhlllekekyiekekaklENLYEDEVRKAQKLKQEQEHQLKQLEEEKQQLKA 3137
Cdd:COG4717 201 LEELQQR----------------------LAELEEELEEAQEELEELEEELEQLENELEAAAL 241
|
|
| DUF6481 |
pfam20089 |
Family of unknown function (DUF6481); This family of proteins is functionally uncharacterized. ... |
2581-2692 |
7.37e-03 |
|
Family of unknown function (DUF6481); This family of proteins is functionally uncharacterized. This family of proteins is found in bacteria. Proteins in this family are approximately 120 amino acids in length.
Pssm-ID: 437921 [Multi-domain] Cd Length: 119 Bit Score: 39.70 E-value: 7.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2581 LADEQEAARQRKAALeeVERLKAKAeeAKRQKELAEKEAERQIQLAQEAAFKKIEAEEKAHAAivQQKEQEMLQTRKQEK 2660
Cdd:pfam20089 9 FADRLKAAAEAKKAL--LAKFKPKP--AVTDPEFEERAAERAAELAAVRAAREAERAAARRAA--AEAEEAAREAAAAAA 82
|
90 100 110
....*....|....*....|....*....|..
gi 1717010358 2661 sildklkEEAERAKRAAEDADYARMRAEQEAA 2692
Cdd:pfam20089 83 -------AEALDAKRAERKERKAALKAEQKAA 107
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
1397-1440 |
7.46e-03 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 37.64 E-value: 7.46e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1717010358 1397 QAVCDYKQME---ITVHKGDECVLLNNSQPYKWKVLNASGSESVVPS 1440
Cdd:cd11768 3 VALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPS 49
|
|
| PRK13455 |
PRK13455 |
F0F1 ATP synthase subunit B; Provisional |
2051-2185 |
7.53e-03 |
|
F0F1 ATP synthase subunit B; Provisional
Pssm-ID: 184062 [Multi-domain] Cd Length: 184 Bit Score: 40.94 E-value: 7.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2051 MQKQKASAEDELQELRARAEEA-------ERQKKAAQEEAERLRRQVKDESQkkREAEeelkrkvQAEKDAAREKQRAME 2123
Cdd:PRK13455 56 LDKRAEGIRSELEEARALREEAqtllasyERKQREVQEQADRIVAAAKDEAQ--AAAE-------QAKADLEASIARRLA 126
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1717010358 2124 DLQKFRSQAEEAERRmkqaEVeKERQIKVAqeVAqqsAAAELNSKRMSFAEKTAQLELSLKQ 2185
Cdd:PRK13455 127 AAEDQIASAEAAAVK----AV-RDRAVSVA--VA---AAADVIAKQMTAADANALIDEAIKE 178
|
|
| Tropomyosin |
pfam00261 |
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ... |
1939-2148 |
7.65e-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: 41.55 E-value: 7.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1939 EKLKEEERRRLAEVEAQLEKQTQLAEAHAKAkAQAEKEAEELQRRMQ--EEVSKRevvavdAEQQKQTIQQELQQLRQNS 2016
Cdd:pfam00261 1 KKMQQIKEELDEAEERLKEAMKKLEEAEKRA-EKAEAEVAALNRRIQllEEELER------TEERLAEALEKLEEAEKAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2017 DMEIKSKaKKIEEAEynrRKIEEEIHIVRLQLETMQKQKASAEDELqelraraEEAERQKKAAQEEAERLRRQVKDESQK 2096
Cdd:pfam00261 74 DESERGR-KVLENRA---LKDEEKMEILEAQLKEAKEIAEEADRKY-------EEVARKLVVVEGDLERAEERAELAESK 142
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2097 KREAEEELK------RKVQAEKDAAREKQRAMED--------LQKFRSQAEEAERRMKQAEVEKER 2148
Cdd:pfam00261 143 IVELEEELKvvgnnlKSLEASEEKASEREDKYEEqirfltekLKEAETRAEFAERSVQKLEKEVDR 208
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2328-2483 |
7.91e-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: 41.45 E-value: 7.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2328 NEVNEAIQKRKKMEEELAKVRAEMEILLESKSRAEEEsRSNTEKSKHMLEveaSKLRELAEEAARLRALSEEAKRQRQIA 2407
Cdd:COG1579 17 SELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLE---LEIEEVEARIKKYEEQLGNVRNNKEYE 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2408 -----EGEAARQRAEAERILKEKLAAINEATRLKTEAEIALKEKEAE-----NERLRRLAEDEAyQRKLLEEQATQHKQD 2477
Cdd:COG1579 93 alqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAEleekkAELDEELAELEA-ELEELEAEREELAAK 171
|
....*.
gi 1717010358 2478 IEEKII 2483
Cdd:COG1579 172 IPPELL 177
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1995-2127 |
8.11e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.98 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1995 AVDAEQQKQTIQQELQQLRQnsdmEIKSKAKKIEEAEYNRRKIEEEIhivrlqletmQKQKASAEDELQeLRARAEEAER 2074
Cdd:pfam12718 16 AEELEEKVKELEQENLEKEQ----EIKSLTHKNQQLEEEVEKLEEQL----------KEAKEKAEESEK-LKTNNENLTR 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1717010358 2075 QKKAAQEEAERLRRQVKDESQKKREAE---EELKRKVQAEKDAAREKQRAMEDLQK 2127
Cdd:pfam12718 81 KIQLLEEELEESDKRLKETTEKLRETDvkaEHLERKVQALEQERDEWEKKYEELEE 136
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
2728-3052 |
8.41e-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: 41.86 E-value: 8.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2728 EAELEAAKRAHAEqaALKQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKVKLQ---LEE-----TDHQKTLLDDESQRL 2799
Cdd:pfam09728 17 EEKLAALCKKYAE--LLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAkskLEKlcrelQKQNKKLKEESKKLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2800 KEEVTDAMRQKAQVEEELFKVKIQMEELIKLKLRIEEENKMliMKDKdstQKFLAEEAEKMRQVAEEAARlSIEAQEAAR 2879
Cdd:pfam09728 95 KEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEE--LREK---LKSLIEQYELRELHFEKLLK-TKELEVQLA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2880 MRKLAEDDLANQRALAEKMLKekmqaiqEATRLKAEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEGFQKsleaer 2959
Cdd:pfam09728 169 EAKLQQATEEEEKKAQEKEVA-------KARELKAQVQTLSETEKELREQLNLYVEKFEEFQDTLNKSNEVFTT------ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2960 rqqleitaeaerLKLQVLEMSKAQAKAEEDAKKFKKQAEdfgnKLHQTELATKErmvvvqsleiQRQQSGKEAEELRRAI 3039
Cdd:pfam09728 236 ------------FKKEMEKMSKKIKKLEKENLTWKRKWE----KSNKALLEMAE----------ERQKLKEELEKLQKKL 289
|
330
....*....|...
gi 1717010358 3040 AELEHEKEKLKQE 3052
Cdd:pfam09728 290 EKLENLCRALQAE 302
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
1890-2280 |
8.62e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 42.73 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1890 PKVQSTSDSIIQEYVDLRTRYSelttlTSQYIKFITETlcRLNVEEKAAEKLKEEERRRLAEVE-------AQLEKQTQL 1962
Cdd:PTZ00108 938 GVLEQWEEEGIEKVFKLKSTIS-----TTNMVLFDENG--KIKKYSDALDILKEFYLVRLDLYKkrkeyllGKLERELAR 1010
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1963 AEAHAK-AKAQAEKEAEELQRRMQ---EEVSKREVVAVDAEQQKQ----TIQQELQQLRQNSDMEIKSKAKKIEEAEYNR 2034
Cdd:PTZ00108 1011 LSNKVRfIKHVINGELVITNAKKKdlvKELKKLGYVRFKDIIKKKsekiTAEEEEGAEEDDEADDEDDEEELGAAVSYDY 1090
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2035 --------------RKIEEEIHIVRLQLETMQKQKASA--EDELQELRARAEEAERQKKAAQEEAERL---RRQVKDESQ 2095
Cdd:PTZ00108 1091 llsmpiwsltkekvEKLNAELEKKEKELEKLKNTTPKDmwLEDLDKFEEALEEQEEVEEKEIAKEQRLkskTKGKASKLR 1170
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2096 KKREAEEELKRKVQAEKDAAR----------EKQRAMEDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQSAAAEL 2165
Cdd:PTZ00108 1171 KPKLKKKEKKKKKSSADKSKKasvvgnskrvDSDEKRKLDDKPDNKKSNSSGSDQEDDEEQKTKPKKSSVKRLKSKKNNS 1250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2166 NSKRM---SFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKAREEAEKELEKWHQKANEALRLRLQAEEVAHKK 2242
Cdd:PTZ00108 1251 SKSSEdndEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRPDGESNGGSKPSSPTKKKVKKRLEGSLAALKKKKKSEKK 1330
|
410 420 430
....*....|....*....|....*....|....*...
gi 1717010358 2243 TLAQEEAEKQKEDAEREARKRAKAEESALRQKELAEDE 2280
Cdd:PTZ00108 1331 TARKKKSKTRVKQASASQSSRLLRRPRKKKSDSSSEDD 1368
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
2544-3058 |
8.63e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2544 ETHRSKEKAEQEAEKQRQLaLEEEQRRKEAEEKVRKILADEQEAARQRKA-ALEEVER------LKAKAEEA----KRQK 2612
Cdd:COG5022 784 RRLVDYELKWRLFIKLQPL-LSLLGSRKEYRSYLACIIKLQKTIKREKKLrETEEVEFslkaevLIQKFGRSlkakKRFS 862
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2613 ELAEKEAERQIQLAQEAAFK-----KIEAEEKAHAAIVQ-QKEQEMLQTRKQEKSILDK----LKEEAERAKRAAEDADY 2682
Cdd:COG5022 863 LLKKETIYLQSAQRVELAERqlqelKIDVKSISSLKLVNlELESEIIELKKSLSSDLIEnlefKTELIARLKKLLNNIDL 942
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2683 ----ARMRAEQEAALSRQQVEeaERMKQRAEE-EAQAKAQAQDEAEKLRKEAELEAAKR-------------AHAEQAAL 2744
Cdd:COG5022 943 eegpSIEYVKLPELNKLHEVE--SKLKETSEEyEDLLKKSTILVREGNKANSELKNFKKelaelskqygalqESTKQLKE 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2745 KQKQLADEEMDKHKKFAEKTLRQKAQVEQELTKvKLQLEETDHQKTLLD-----------------DESQRLKE---EVT 2804
Cdd:COG5022 1021 LPVEVAELQSASKIISSESTELSILKPLQKLKG-LLLLENNQLQARYKAlklrrensllddkqlyqLESTENLLktiNVK 1099
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2805 DAMRQKAQVEEELFKVKIQMEELIKLKLRIEEEN----KMLIMKDKDSTQKFLAEEAEKMRQVAEEAARLSIEaqeaarm 2880
Cdd:COG5022 1100 DLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKflsqLVNTLEPVFQKLSVLQLELDGLFWEANLEALPSPP------- 1172
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2881 rklAEDDLANQRALAEKMLKEKMQAIQEATRLKaEADMLQKQKELAQEQARKFQEDKEQIEQQLAKETEgfqKSLEAERR 2960
Cdd:COG5022 1173 ---PFAALSEKRLYQSALYDEKSKLSSSEVNDL-KNELIALFSKIFSGWPRGDKLKKLISEGWVPTEYS---TSLKGFNN 1245
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2961 QQLEITAEAERLKLQVLEMSKaqaKAEEDAKKFKKQAEDFGNKLHQT----------ELATKER-MVVVQSLEIQRQQSG 3029
Cdd:COG5022 1246 LNKKFDTPASMSNEKLLSLLN---SIDNLLSSYKLEEEVLPATINSLlqyinvglfnALRTKASsLRWKSATEVNYNSEE 1322
|
570 580
....*....|....*....|....*....
gi 1717010358 3030 KEAEELRRAIAELEHEKEKLKQEAELLQK 3058
Cdd:COG5022 1323 LDDWCREFEISDVDEELEELIQAVKVLQL 1351
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2258-2629 |
8.64e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 42.58 E-value: 8.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2258 REARKRAKAEESALRQKELAEDELEKQRKL---ADATAQQKFSAEQELIRLKADTESGEQQRLLLEEELFRLKNEVNEAI 2334
Cdd:PLN02939 36 RARRRGFSSQQKKKRGKNIAPKQRSSNSKLqsnTDENGQLENTSLRTVMELPQKSTSSDDDHNRASMQRDEAIAAIDNEQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2335 QKRKKMEEELAKVRAE--MEILlesksraeeesrSNTEKSKHMLEveasklrelaeeAARLRALSEeakRQRQIAEGEAA 2412
Cdd:PLN02939 116 QTNSKDGEQLSDFQLEdlVGMI------------QNAEKNILLLN------------QARLQALED---LEKILTEKEAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2413 RQRAEaerILKEKLAAINEATRLKTEAEIALKEKEAENERLR-----RLAEDEAYQRKL------LEEQATQHKQDIE-- 2479
Cdd:PLN02939 169 QGKIN---ILEMRLSETDARIKLAAQEKIHVEILEEQLEKLRnelliRGATEGLCVHSLskeldvLKEENMLLKDDIQfl 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2480 -EKIILLKKSSDN--ELERQKNIVEDTLRQRRIIEEEIRIlklNFEKASSGKSDLELElnQLKNIAEETHRSKEKAEQEA 2556
Cdd:PLN02939 246 kAELIEVAETEERvfKLEKERSLLDASLRELESKFIVAQE---DVSKLSPLQYDCWWE--KVENLQDLLDRATNQVEKAA 320
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2557 ekqrqLALEEEQrrkEAEEKVRKILADEQEAaRQRKAALEEVERLKAKAEEAKRQKELAEKEAERQIQLAQEA 2629
Cdd:PLN02939 321 -----LVLDQNQ---DLRDKVDKLEASLKEA-NVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQES 384
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2979-3210 |
8.97e-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: 42.25 E-value: 8.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2979 MSKAQAKAEEDAKK---FKKQAEDFGNKLHQTELATKERMVVVQSLEIQRQQSGKEAEELRRA---IAELEHEKEKLKQE 3052
Cdd:pfam15709 309 MESEEERSEEDPSKallEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAekmREELELEQQRRFEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3053 AELLQKNSQEMQVAQQEQLRQETQVLQTtfltekhlllekekyiekekaklenlyedEVRKAQKLKQEQEHQLKQLEEEK 3132
Cdd:pfam15709 389 IRLRKQRLEEERQRQEEEERKQRLQLQA-----------------------------AQERARQQQEEFRRKLQELQRKK 439
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3133 QQLKASMGEAMK-KQKEAEESVRHKQDEL------HQLDKRRQEQEkllADENRKLREKLEQLEEEHRIALAQtREMMIQ 3205
Cdd:pfam15709 440 QQEEAERAEAEKqRQKELEMQLAEEQKRLmemaeeERLEYQRQKQE---AEEKARLEAEERRQKEEEAARLAL-EEAMKQ 515
|
....*
gi 1717010358 3206 TDDLA 3210
Cdd:pfam15709 516 AQEQA 520
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1999-2112 |
9.10e-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: 41.23 E-value: 9.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1999 EQQKQTIQQELQQLRQNSDMEIKSKAKKIEEA--EYNRRKiEEEIHIVRLQLETMQKQKASAEDELQELRARAEEAER-- 2074
Cdd:pfam13904 65 QRQRQKELQAQKEEREKEEQEAELRKRLAKEKyqEWLQRK-ARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKev 143
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1717010358 2075 -----QKKAAQEEAERLRRQvkdeSQKKREAEEELKRKVQAEK 2112
Cdd:pfam13904 144 lqeweRKKLEQQQRKREEEQ----REQLKKEEEEQERKQLAEK 182
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2596-2702 |
9.21e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 9.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2596 EEVERLKAKAEEAKRQKELAEKEAERQiqlaqeaafkkiEAEEKAHAAIVQQKEQEMLQTRKQeksiLDKLKEEAERAkr 2675
Cdd:PRK11448 149 QEVLTLKQQLELQAREKAQSQALAEAQ------------QQELVALEGLAAELEEKQQELEAQ----LEQLQEKAAET-- 210
|
90 100
....*....|....*....|....*..
gi 1717010358 2676 AAEDADYARMRAEQeaALSRQQVEEAE 2702
Cdd:PRK11448 211 SQERKQKRKEITDQ--AAKRLELSEEE 235
|
|
| Macoilin |
pfam09726 |
Macoilin family; The Macoilin proteins has an N-terminal portion that is composed of 5 ... |
3018-3190 |
9.46e-03 |
|
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: 42.53 E-value: 9.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3018 VQSLEIQRQQSGKEAEELRRAIAELEHEKEKLKQEAELLQKNSQEMQVAQQEQLRQETQVLQTTFLTEKhlllekekyie 3097
Cdd:pfam09726 404 IKKLKAELQASRQTEQELRSQISSLTSLERSLKSELGQLRQENDLLQTKLHNAVSAKQKDKQTVQQLEK----------- 472
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 3098 kekaklenlyedevrkaqKLKQEQEHQL---KQLEEEKQQLKA-------SMGEAMKKQKEAEESVRHKQDELHQLDKRR 3167
Cdd:pfam09726 473 ------------------RLKAEQEARAsaeKQLAEEKKRKKEeeataarAVALAAASRGECTESLKQRKRELESEIKKL 534
|
170 180
....*....|....*....|...
gi 1717010358 3168 QEQEKLLADENRKLREKLEQLEE 3190
Cdd:pfam09726 535 THDIKLKEEQIRELEIKVQELRK 557
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4593-4624 |
9.48e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 9.48e-03
10 20 30
....*....|....*....|....*....|..
gi 1717010358 4593 KLLSAERAVIGYKDPYSGKLISLFQAMKKGLI 4624
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1969-2160 |
9.51e-03 |
|
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: 40.80 E-value: 9.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1969 AKAQAEKEA--EELQRRMQEEVSKREVVAVDAEQQKQtIQQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIE------EE 2040
Cdd:pfam15665 14 AEIQALKEAheEEIQQILAETREKILQYKSKIGEELD-LKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEerelkaEA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2041 IHIVRL-----QLETMQKQkasAEDELQELRARAEEAERQKKAAQEEaerLRRQVKDESQKKREAEEELKRKVQAEKDAA 2115
Cdd:pfam15665 93 EHRQRVvelsrEVEEAKRA---FEEKLESFEQLQAQFEQEKRKALEE---LRAKHRQEIQELLTTQRAQSASSLAEQEKL 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1717010358 2116 REKQRAmeDLQKFRSQAEEAERRMKQAEVEKERQIKVAQEVAQQS 2160
Cdd:pfam15665 167 EELHKA--ELESLRKEVEDLRKEKKKLAEEYEQKLSKAQAFYERE 209
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1924-2115 |
9.65e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.12 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1924 ITETLCRLNVEEKAAEKLKEEERRRLAEVEAQLEK-QTQLAEAHAKAkAQAEKEAEELQRRMQEE--------------- 1987
Cdd:COG3883 35 AQAELDALQAELEELNEEYNELQAELEALQAEIDKlQAEIAEAEAEI-EERREELGERARALYRSggsvsyldvllgses 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 1988 ----VSKREVVAVDAEQQKQTI------QQELQQLRQNSDMEIKSKAKKIEEAEYNRRKIEEEIHIVRLQLETMQKQKAS 2057
Cdd:COG3883 114 fsdfLDRLSALSKIADADADLLeelkadKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1717010358 2058 AEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKRKVQAEKDAA 2115
Cdd:COG3883 194 AEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGA 251
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
2133-2251 |
9.67e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 9.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2133 EEAERRMKQAEVEKERQIKvAQEVAQQSAAAELNSKRMSFAEKTAQLELSLKQEHITVTHLQEEAERLKKQHEEAEKARE 2212
Cdd:COG0542 414 DELERRLEQLEIEKEALKK-EQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEK 492
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 1717010358 2213 EAEKELEKWHQKaNEALRLRLQAEEVAH---KKT------LAQEEAEK 2251
Cdd:COG0542 493 ELAELEEELAEL-APLLREEVTEEDIAEvvsRWTgipvgkLLEGEREK 539
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
2047-2176 |
9.69e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 9.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1717010358 2047 QLETMQKQKASAEDELQELRARAEEAERQKKAAQEEAERLRRQVKDESQKKREAEEELKR-KVQAEKDAArekqramEDL 2125
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQlQEKAAETSQ-------ERK 215
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1717010358 2126 QKFRSQAEEAERRMKQAEVEKERQIKvaqevaQQSAAA--ELNSKRMSFAEKT 2176
Cdd:PRK11448 216 QKRKEITDQAAKRLELSEEETRILID------QQLRKAgwEADSKTLRFSKGA 262
|
|
| |
