|
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 ... |
22-126 |
9.87e-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: 244.23 E-value: 9.87e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 22 DRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNI 101
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1389908286 102 RNDDIADGNPKLTLGLIWTIILHFQ 126
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
19-137 |
4.10e-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: 240.31 E-value: 4.10e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 19 DERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 98
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908286 99 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 137
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
11-135 |
5.87e-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: 234.49 E-value: 5.87e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 11 ETLIQRGQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDF 90
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDY 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1389908286 91 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 135
Cdd:cd21236 84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
139-244 |
4.18e-67 |
|
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: 222.59 E-value: 4.18e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 139 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 218
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1389908286 219 PEDVDVPHPDEKSIITYVSSLYDVMP 244
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
140-244 |
5.78e-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: 216.49 E-value: 5.78e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 219
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1389908286 220 EDVDVPHPDEKSIITYVSSLYDVMP 244
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
19-136 |
1.74e-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: 206.81 E-value: 1.74e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 19 DERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 98
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1389908286 99 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 136
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
140-244 |
1.67e-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: 1.67e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAEReLGVTKLLDP 219
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1389908286 220 EDVDVPHPDEKSIITYVSSLYDVMP 244
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
138-244 |
5.85e-51 |
|
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: 176.39 E-value: 5.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 138 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAEReLGVTKLL 217
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1389908286 218 DPEDVDVPHPDEKSIITYVSSLYDVMP 244
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
24-127 |
1.53e-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: 1.53e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 24 VQKKTFTKWVNKHLVKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 102
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1389908286 103 NDDIADGNPKLTLGLIWTIILHFQI 127
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
9-123 |
2.26e-49 |
|
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: 172.17 E-value: 2.26e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 9 FMETLIQRGQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIA 87
Cdd:cd21246 1 FERSRIKALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1389908286 88 LDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 123
Cdd:cd21246 81 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
140-240 |
3.51e-46 |
|
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: 162.58 E-value: 3.51e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 219
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1389908286 220 EDVDVPHPDEKSIITYVSSLY 240
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
9-123 |
5.03e-46 |
|
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: 162.47 E-value: 5.03e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 9 FMETLIQRGQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIA 87
Cdd:cd21193 1 FEKGRIRALQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 1389908286 88 LDFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 123
Cdd:cd21193 81 LAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
140-240 |
1.56e-44 |
|
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: 157.94 E-value: 1.56e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 219
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1389908286 220 EDVDVPHPDEKSIITYVSSLY 240
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
20-127 |
1.74e-44 |
|
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: 158.31 E-value: 1.74e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 20 ERDRVQKKTFTKWVNKHLVKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 95
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1389908286 96 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 127
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
7-123 |
7.84e-43 |
|
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: 154.06 E-value: 7.84e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 7 RDFMETLIQRGQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQ 85
Cdd:cd21317 14 RLFERSRIKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVD 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1389908286 86 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 123
Cdd:cd21317 94 KALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
23-240 |
1.34e-42 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 168.20 E-value: 1.34e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 23 RVQKKTFTKWVNKHLVKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLV 99
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 100 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSWRDGKLFSAII 178
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 179 HKHRPALIDMNQVYRQSNQE--NLEQAFSVAERELGVTKLLDPEDV-DVPHPDEKSIITYVSSLY 240
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
19-123 |
5.91e-42 |
|
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: 152.10 E-value: 5.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 19 DERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVK 97
Cdd:cd21318 33 DEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQRVH 112
|
90 100
....*....|....*....|....*.
gi 1389908286 98 LVNIRNDDIADGNPKLTLGLIWTIIL 123
Cdd:cd21318 113 LENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
20-127 |
3.33e-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: 148.87 E-value: 3.33e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 20 ERDRVQKKTFTKWVNKHLVKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 95
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQpiVINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1389908286 96 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 127
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
887-963 |
1.18e-39 |
|
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: 142.74 E-value: 1.18e-39
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 887 SWQYLMRDIHIIKTWNISMFKTLRVEEYRLALRNLEQHYQDFLRDSQDSQMFGAEDRMQVESNYNKANQHYNTMVTS 963
Cdd:pfam18373 2 SWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
127-240 |
1.33e-39 |
|
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: 144.43 E-value: 1.33e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 127 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 206
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908286 207 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 240
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
139-244 |
3.53e-39 |
|
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: 142.84 E-value: 3.53e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 139 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 218
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1389908286 219 PEDVDVPHPDEKSIITYVSSLYDVMP 244
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
140-240 |
6.18e-39 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 142.45 E-value: 6.18e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 219
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1389908286 220 EDVDVPHPDEKSIITYVSSLY 240
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
24-125 |
2.38e-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: 2.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 24 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 101
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1389908286 102 RNDDIADGNPKLTLGLIWTIILHF 125
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
20-127 |
3.25e-38 |
|
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: 139.97 E-value: 3.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 20 ERDRVQKKTFTKWVNKHLVKAQ--RHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 97
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1389908286 98 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 127
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
22-123 |
7.42e-38 |
|
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: 138.68 E-value: 7.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 22 DRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVKLVN 100
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1389908286 101 IRNDDIADGNPKLTLGLIWTIIL 123
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
136-240 |
1.16e-37 |
|
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: 139.04 E-value: 1.16e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 136 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTK 215
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1389908286 216 LLDPEDVDVPHPDEKSIITYVSSLY 240
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
139-240 |
2.41e-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: 137.69 E-value: 2.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 139 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 218
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1389908286 219 PEDVDVPHPDEKSIITYVSSLY 240
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
143-244 |
1.09e-36 |
|
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: 135.63 E-value: 1.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 143 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 221
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1389908286 222 VDVPHPDEKSIITYVSSLYDVMP 244
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1316-2129 |
6.12e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 152.22 E-value: 6.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1316 VNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKE-EERRKMAEIQAELDKQKQMAEAHAKSVAKAEqealelkm 1394
Cdd:PTZ00121 1060 AEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKaEEAKKTETGKAEEARKAEEAKKKAEDARKAE-------- 1131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1395 kmkeEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAEL 1474
Cdd:PTZ00121 1132 ----EARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1475 QELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQA 1554
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAE 1287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1555 EEEKIRQIRVVEEVAQksaATQLQTKAmsfsEQTTKLEESLKKEQgnvlKLQEEADKLKKQQKEANTAREEAEQELEiwr 1634
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKK---ADEAKKKA----EEAKKADEAKKKAE----EAKKKADAAKKKAEEAKKAAEAAKAEAE--- 1353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1635 QKANEALRLRLQAEEEAQKKSHAQEEAEkqklEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEC 1714
Cdd:PTZ00121 1354 AAADEAEAAEEKAEAAEKKKEEAKKKAD----AAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEE 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1715 IRlKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLE-----DELNKVRSEMDSLLQMKINAEKASmvntEKSKQLLE 1789
Cdd:PTZ00121 1430 KK-KADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEeakkaDEAKKKAEEAKKADEAKKKAEEAK----KKADEAKK 1504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1790 SEALKMKqlADEAARmrsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLA-AINEATRLKT-----EAEMALKAKEAENE 1863
Cdd:PTZ00121 1505 AAEAKKK--ADEAKK----AEEAKKADEAKKAEEAKKADEAKKAEEKKKAdELKKAEELKKaeekkKAEEAKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1864 RLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDS-----ELGRQKNIVEETLKQKKVVEEEIHiiKINFHKASK 1938
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAkikaeELKKAEEEKKKVEQLKKKEAEEKK--KAEELKKAE 1656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1939 EKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEE----VERLK 2014
Cdd:PTZ00121 1657 EENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAK 1736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2015 KKAEDANKQKEKAEKEAEKqvvlaKEAAQKCTAAEQKAQDVLSKNKEDVLAQE--------------KLRDEFENAKKL- 2079
Cdd:PTZ00121 1737 KEAEEDKKKAEEAKKDEEE-----KKKIAHLKKEEEKKAEEIRKEKEAVIEEEldeedekrrmevdkKIKDIFDNFANIi 1811
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 2080 -------------AQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQR 2129
Cdd:PTZ00121 1812 eggkegnlvindsKEMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEK 1874
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
19-127 |
1.79e-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: 1.79e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 19 DERDRVQKKTFTKWVNKHLVKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 97
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1389908286 98 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 127
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
124-240 |
2.71e-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: 132.49 E-value: 2.71e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 124 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQA 203
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1389908286 204 FSVAERELGVTKLLDPEDVDVPHPDEKSIITYVSSLY 240
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1483-2399 |
5.62e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 148.75 E-value: 5.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1483 EAEKLRKAAQDEAERLRKQVAEETQRKKNAEDElkrksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEekirqI 1562
Cdd:PTZ00121 1059 KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADE------ATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAED-----A 1127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1563 RVVEEVAQksaatqlqtkamsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQ--KEANTAR--EEAEQELEIwrQKAN 1638
Cdd:PTZ00121 1128 RKAEEARK--------------AEDARKAEEARKAEDAKRVEIARKAEDARKAEeaRKAEDAKkaEAARKAEEV--RKAE 1191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1639 EalrlrLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEaaLKQKENAEKELDKQRKfaeqiAQQKLSAEQECIRLK 1718
Cdd:PTZ00121 1192 E-----LRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEA--VKKAEEAKKDAEEAKK-----AEEERNNEEIRKFEE 1259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1719 ADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQleDELNKVRsEMDSLLQMKINAEKASMVNTEKSKqlleseALKMKQL 1798
Cdd:PTZ00121 1260 ARMAHFARRQAAIKAEEARKADELKKAEEKKKA--DEAKKAE-EKKKADEAKKKAEEAKKADEAKKK------AEEAKKK 1330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1799 ADEAARMrsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEN--ERLKRQAEEEAYQR 1876
Cdd:PTZ00121 1331 ADAAKKK---AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKkaDEAKKKAEEDKKKA 1407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1877 KLLEDQAAQHKQDIEEKITQLQTSSDSELgrqkniveetlkqKKVVEEeihiikinfhkasKEKADlesELKKLKGIADE 1956
Cdd:PTZ00121 1408 DELKKAAAAKKKADEAKKKAEEKKKADEA-------------KKKAEE-------------AKKAD---EAKKKAEEAKK 1458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1957 TQKSKLKAEE--EAEKLKKlaaeeerrrkeaeekvkritaaEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQ 2034
Cdd:PTZ00121 1459 AEEAKKKAEEakKADEAKK----------------------KAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAK 1516
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2035 VVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENE 2114
Cdd:PTZ00121 1517 KAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEE 1596
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2115 AAKQAkaqnDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQkvl 2194
Cdd:PTZ00121 1597 VMKLY----EEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKK--- 1669
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2195 lDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLaeEAEKMKSLAEEAGRLS 2274
Cdd:PTZ00121 1670 -AEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKI--KAEEAKKEAEEDKKKA 1746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2275 VEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKlkaeaEKLQKQKDQAQETAKRLQEDKQQIQqrldketegf 2354
Cdd:PTZ00121 1747 EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELD-----EEDEKRRMEVDKKIKDIFDNFANII---------- 1811
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 1389908286 2355 qkslEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ 2399
Cdd:PTZ00121 1812 ----EGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADAFEKH 1852
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1530-2514 |
1.52e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 147.59 E-value: 1.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1530 KQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTkamsFSEQTTKLEESLKKEQGNVlklqEEA 1609
Cdd:PTZ00121 1043 KEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEA----TEEAFGKAEEAKKTETGKA----EEA 1114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1610 DKLKKQQKEANTAR--EEAEQELEIwrQKANEALRlrlqaEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKE 1687
Cdd:PTZ00121 1115 RKAEEAKKKAEDARkaEEARKAEDA--RKAEEARK-----AEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1688 NAEKELDKqrkfAEQIAQQKLSAEQECIRLKADFEHAEQQRGLldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL 1767
Cdd:PTZ00121 1188 RKAEELRK----AEDARKAEAARKAEEERKAEEARKAEDAKKA---EAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEA 1260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1768 QMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSV--AEEAKKQrqiAEEeaARQRSEAEKILKEklaAINEAT 1845
Cdd:PTZ00121 1261 RMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKkkADEAKKK---AEE--AKKADEAKKKAEE---AKKKAD 1332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1846 RLKTEAEMALKAKEAenerlkRQAEEEAYQRKLledQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEE 1925
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEA------AKAEAEAAADEA---EAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1926 ihiikinfhkasKEKADlesELKKLKGIADETQKSKLKAEE--EAEKLKKlaaeeerrrkeaeekvkritAAEEeaarqc 2003
Cdd:PTZ00121 1404 ------------KKKAD---ELKKAAAAKKKADEAKKKAEEkkKADEAKK--------------------KAEE------ 1442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2004 kaaQEEVERLKKKAEDANKqkekaekeaekqvvlAKEAAQKctAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEa 2083
Cdd:PTZ00121 1443 ---AKKADEAKKKAEEAKK---------------AEEAKKK--AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADE- 1501
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2084 ekakekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKE 2163
Cdd:PTZ00121 1502 -------------AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEE 1568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2164 AEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRR 2243
Cdd:PTZ00121 1569 AKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKK 1648
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2244 LMQKDKDSTQKLLAEEAEKMKslAEEAGRLSVE---AEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAE 2320
Cdd:PTZ00121 1649 AEELKKAEEENKIKAAEEAKK--AEEDKKKAEEakkAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEE 1726
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2321 KlqkQKDQAQETAKRLQEDKQQIQQRldKETEGFQKSLEAERKRQLEASAEAEKLKLRV--KELSLAQTKAEDEAKKFKK 2398
Cdd:PTZ00121 1727 E---NKIKAEEAKKEAEEDKKKAEEA--KKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVieEELDEEDEKRRMEVDKKIK 1801
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2399 QADEVKAQLQRTEKHTTEIVVQKLETQrLQSTREADDLKSAIADleeerkklkkeaeelQRKSKEMANAQQEQIEQQKAE 2478
Cdd:PTZ00121 1802 DIFDNFANIIEGGKEGNLVINDSKEME-DSAIKEVADSKNMQLE---------------EADAFEKHKFNKNNENGEDGN 1865
|
970 980 990
....*....|....*....|....*....|....*.
gi 1389908286 2479 LQQSFLTEKGLLLKREKEVEgEKKRFEKQLEDEMKK 2514
Cdd:PTZ00121 1866 KEADFNKEKDLKEDDEEEIE-EADEIEKIDKDDIER 1900
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
140-240 |
1.91e-34 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 129.45 E-value: 1.91e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 219
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1389908286 220 EDVDVPHPDEKSIITYVSSLY 240
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1739-2603 |
2.55e-34 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 146.82 E-value: 2.55e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1739 KNEVNSTEKQR---KQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQllESEALKMKQLADEAARMRSV------- 1808
Cdd:PTZ00121 1063 KAHVGQDEGLKpsyKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE--ARKAEEAKKKAEDARKAEEArkaedar 1140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1809 -AEEAKKQRQIAEEEAARQRSEAEKI---LKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAA 1884
Cdd:PTZ00121 1141 kAEEARKAEDAKRVEIARKAEDARKAeeaRKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKA 1220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1885 QHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKlkgiADETQKS-KLK 1963
Cdd:PTZ00121 1221 EDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKK----AEEKKKAdEAK 1296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1964 AEEEAEKLKKLAAEEERRRKEAEEKVKritaaEEEAARQCKAAQEEVERLKKKAEdANKQKEKAEKEAEKQVVLAKEAAQ 2043
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADEAKKK-----AEEAKKKADAAKKKAEEAKKAAE-AAKAEAEAAADEAEAAEEKAEAAE 1370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2044 KCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAAlLRQKAEE---AEKQKKAAEnEAAKQAK 2120
Cdd:PTZ00121 1371 KKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADE-AKKKAEEkkkADEAKKKAE-EAKKADE 1448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2121 AQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKEltvvklqldetdkqkvlldQELQ 2200
Cdd:PTZ00121 1449 AKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA-------------------AEAK 1509
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2201 RVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKmkslAEEAGRLSVEAEET 2280
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKK----AEEDKNMALRKAEE 1585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2281 ARQRQiaesnlaeqralaEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgfqkslea 2360
Cdd:PTZ00121 1586 AKKAE-------------EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAE-------- 1644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2361 ERKRQLEASAEAEKLKLRVKELSlaqTKAEDEakkfKKQADEVKAQlQRTEKHTTEIVVQKLETQrlqstREADDLKSAI 2440
Cdd:PTZ00121 1645 EKKKAEELKKAEEENKIKAAEEA---KKAEED----KKKAEEAKKA-EEDEKKAAEALKKEAEEA-----KKAEELKKKE 1711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2441 ADleeerkklkkeaeeLQRKSKEMANAqqEQIEQQKAElqqsfltekglLLKREKEVEGEKKRFEKQLEDEMKKAKALKD 2520
Cdd:PTZ00121 1712 AE--------------EKKKAEELKKA--EEENKIKAE-----------EAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2521 EQErqrKLMEEERKKLQAIMDEAVrKQKEAEEEMKNKQREMDVLDKKRLEQEKQlAEENKKLREQLQTFEISSKTVSQTK 2600
Cdd:PTZ00121 1765 EEE---KKAEEIRKEKEAVIEEEL-DEEDEKRRMEVDKKIKDIFDNFANIIEGG-KEGNLVINDSKEMEDSAIKEVADSK 1839
|
...
gi 1389908286 2601 ESQ 2603
Cdd:PTZ00121 1840 NMQ 1842
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
7-123 |
4.74e-34 |
|
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: 129.78 E-value: 4.74e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 7 RDFMETLIQRGQDERDRVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQ 85
Cdd:cd21316 36 RLFERSRIKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVD 115
|
90 100 110
....*....|....*....|....*....|....*...
gi 1389908286 86 IALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 123
Cdd:cd21316 116 KALQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
139-237 |
1.13e-33 |
|
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: 127.15 E-value: 1.13e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 139 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 218
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1389908286 219 PEDVDVPHPDEKSIITYVS 237
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1739-2638 |
3.78e-33 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 142.97 E-value: 3.78e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1739 KNEVNSTEKQRKQL--EDELNKVRSEMDSLLQMKINAEKASmvnTEKSKQLLESEALKMKQLADEAARMRSV---AEEAK 1813
Cdd:PTZ00121 1052 IDGNHEGKAEAKAHvgQDEGLKPSYKDFDFDAKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDAR 1128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1814 KQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEeayQRKLLEDQAAQHKQDIE-- 1891
Cdd:PTZ00121 1129 KAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEaa 1205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1892 ---EKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEihiikinfHKASKEKADLESELKKLKGIADETQKSKLKAEEEA 1968
Cdd:PTZ00121 1206 rkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEA--------KKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEA 1277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1969 EKLKKLAAeeerrrkeaeekvkritAAEEEAARQCKAAQE--EVERLKKKAEDANKQKEKAEKeaekqvvlAKEAAQKCT 2046
Cdd:PTZ00121 1278 RKADELKK-----------------AEEKKKADEAKKAEEkkKADEAKKKAEEAKKADEAKKK--------AEEAKKKAD 1332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2047 AAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEE---AEKQKKAAENEAAKQAKAQN 2123
Cdd:PTZ00121 1333 AAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkADEAKKKAEEDKKKADELKK 1412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2124 DTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKeltvvklqldetdkqkvlldQELQRVK 2203
Cdd:PTZ00121 1413 AAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKK--------------------AEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2204 GEVNDAFKQKSQVEvelarvriqmeelvKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKmkslAEEAgRLSVEAEETARQ 2283
Cdd:PTZ00121 1473 DEAKKKAEEAKKAD--------------EAKKKAEEAKKKADEAKKAAEAKKKADEAKK----AEEA-KKADEAKKAEEA 1533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2284 RQIAESNLAEQRALAEKILKekmqaiQEATKlKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERK 2363
Cdd:PTZ00121 1534 KKADEAKKAEEKKKADELKK------AEELK-KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2364 RQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEV-KAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIAD 2442
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2443 LEEERKklkkeaeelQRKSKEMANAQQEQIEQQKAELQQsflteKGLLLKREKEVEGEK-KRFEKQLEDEMKKAKALKDE 2521
Cdd:PTZ00121 1687 EKKAAE---------ALKKEAEEAKKAEELKKKEAEEKK-----KAEELKKAEEENKIKaEEAKKEAEEDKKKAEEAKKD 1752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2522 QERQRKLmeEERKKLQAIMDEAVRKQKEAEEEmknkqREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKE 2601
Cdd:PTZ00121 1753 EEEKKKI--AHLKKEEEKKAEEIRKEKEAVIE-----EELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK 1825
|
890 900 910
....*....|....*....|....*....|....*..
gi 1389908286 2602 SQTVSVEKLVAVttvgTSKGVLNGSTEVDGVKKEGDS 2638
Cdd:PTZ00121 1826 EMEDSAIKEVAD----SKNMQLEEADAFEKHKFNKNN 1858
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
139-237 |
8.33e-33 |
|
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: 124.56 E-value: 8.33e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 139 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD 218
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1389908286 219 PEDVDVPHPDEKSIITYVS 237
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
127-240 |
1.36e-32 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 124.18 E-value: 1.36e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 127 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 206
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908286 207 AERELGVTKLLDPEDV-DVPHPDEKSIITYVSSLY 240
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
23-128 |
2.28e-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: 124.10 E-value: 2.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 23 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQ-VKLV 99
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1389908286 100 NIRNDDIADGNPKLTLGLIWTIILHFQIS 128
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
145-240 |
8.75e-32 |
|
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: 121.69 E-value: 8.75e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 145 LLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED-VD 223
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1389908286 224 VPHPDEKSIITYVSSLY 240
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1338-2590 |
1.21e-31 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 137.26 E-value: 1.21e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1338 DAQRRLEDDEKASEKLKEEERRKMAEIQAELdkqkqmaeaHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNI 1417
Cdd:NF041483 91 DAERELRDARAQTQRILQEHAEHQARLQAEL---------HTEAVQRRQQLDQELAERRQTVESHVNENVAWAEQLRART 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1418 QQELQHLKSLSDQEIksknqqlEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAaEAEKLRKAAQDEAer 1497
Cdd:NF041483 162 ESQARRLLDESRAEA-------EQALAAARAEAERLAEEARQRLGSEAESARAEAEAILRRARK-DAERLLNAASTQA-- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1498 lrkqvaeetQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKirqirVVEEvAQKSAATQL 1577
Cdd:NF041483 232 ---------QEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALREARAEAEK-----VVAE-AKEAAAKQL 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1578 QTkAMSFSEQTTKleesLKKEQgnVLKLQEEAdklkkqQKEANTAREEAEQ-------ELEIWRQKANEALRlRLQAEEE 1650
Cdd:NF041483 297 AS-AESANEQRTR----TAKEE--IARLVGEA------TKEAEALKAEAEQaladaraEAEKLVAEAAEKAR-TVAAEDT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1651 AQKKSHAQEEAEKQKLEAERDAKK--RGKAEEAALKQKEnAEKELDKQRKFAEQIAQQKLSA---------------EQE 1713
Cdd:NF041483 363 AAQLAKAARTAEEVLTKASEDAKAttRAAAEEAERIRRE-AEAEADRLRGEAADQAEQLKGAakddtkeyraktvelQEE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1714 CIRLKADfehAEQQRGLLDNELQRLKNE-----VNSTEKQRKQLEDELNKVRSEMDSLLQ-MKINAEKASMVNTEKSKQL 1787
Cdd:NF041483 442 ARRLRGE---AEQLRAEAVAEGERIRGEarreaVQQIEEAARTAEELLTKAKADADELRStATAESERVRTEAIERATTL 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1788 LESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKILKEKLA-AINEATRLKTEAEMALKAKE------ 1859
Cdd:NF041483 519 RRQAEETLERTRAEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEERLTAAEealada 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1860 -AENERLKRQAEEEAYQrklLEDQAAqhkqdieEKITQLQTSSDSElgrqknivEETLKQKKVVEeeihiikinfhkASK 1938
Cdd:NF041483 599 rAEAERIRREAAEETER---LRTEAA-------ERIRTLQAQAEQE--------AERLRTEAAAD------------ASA 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1939 EKADLESELKKLKG-IADETQKSKLKAEEEAEKLKklAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQE--------- 2008
Cdd:NF041483 649 ARAEGENVAVRLRSeAAAEAERLKSEAQESADRVR--AEAAAAAERVGTEAAEALAAAQEEAARRRREAEEtlgsaraea 726
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2009 --EVERLKKKAEDANKQKEKAEKEAEKQVV-LAKEAAQKCT----AAEQKAQDVlsknkedvlaqeklRDEFENAKKLAQ 2081
Cdd:NF041483 727 dqERERAREQSEELLASARKRVEEAQAEAQrLVEEADRRATelvsAAEQTAQQV--------------RDSVAGLQEQAE 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2082 EAEKAkekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRkeaeeeaarrAAAEAAALKQKQQADAemskhk 2161
Cdd:NF041483 793 EEIAG----------LRSAAEHAAERTRTEAQEEADRVRSDAYAERER----------ASEDANRLRREAQEET------ 846
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2162 kEAEQALQQKSqvekeltvVKLQLDETDKQKVLLDQELQRVKGEVNDAFkqkSQVEVELARVRIQM-EELVKLKLKIEEE 2240
Cdd:NF041483 847 -EAAKALAERT--------VSEAIAEAERLRSDASEYAQRVRTEASDTL---ASAEQDAARTRADArEDANRIRSDAAAQ 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2241 NRRLMQKDKDSTQKLLAE---EAEKMKSLA-EEAGRLSVEAEETARQRQIAESNLAEQ-RALAEKILKekmQAIQEATKL 2315
Cdd:NF041483 915 ADRLIGEATSEAERLTAEaraEAERLRDEArAEAERVRADAAAQAEQLIAEATGEAERlRAEAAETVG---SAQQHAERI 991
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2316 KAEAEKLqkqKDQAQETAKRLQEDKQQIQQRLDKETEgfqkslEAERKRQLEASAEAEKLKLRV-----KELSLAQTKAE 2390
Cdd:NF041483 992 RTEAERV---KAEAAAEAERLRTEAREEADRTLDEAR------KDANKRRSEAAEQADTLITEAaaeadQLTAKAQEEAL 1062
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2391 DEAKKFKKQADE-VKAQLQRTEKHTTEIVVQKlETQRLQSTREADDL-------KSAIADLEEERKKLKKEA-----EEL 2457
Cdd:NF041483 1063 RTTTEAEAQADTmVGAARKEAERIVAEATVEG-NSLVEKARTDADELlvgarrdATAIRERAEELRDRITGEieelhERA 1141
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2458 QRKSKEMANAQQEQIEQ--QKAELQQSFLTEKGLLLKREKEVEGEKKRFekqleDEMKKAKALKDEQERQRKLMEEERKK 2535
Cdd:NF041483 1142 RRESAEQMKSAGERCDAlvKAAEEQLAEAEAKAKELVSDANSEASKVRI-----AAVKKAEGLLKEAEQKKAELVREAEK 1216
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 2536 LQAimdEAVRkqkEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLrEQLQTFE 2590
Cdd:NF041483 1217 IKA---EAEA---EAKRTVEEGKRELDVLVRRREDINAEISRVQDVL-EALESFE 1264
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
24-127 |
1.48e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 120.86 E-value: 1.48e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 24 VQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 101
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1389908286 102 RNDDIADGNPKLTLGLIWTIILHFQI 127
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
143-245 |
2.01e-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: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 143 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ-ENLEQAFSVAERELGVTKLLDPE 220
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSAtERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1389908286 221 DVDVPHPDEKSIITYVSSLYDVMPR 245
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
24-127 |
2.52e-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: 120.50 E-value: 2.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 24 VQKKTFTKWVNKHLVKAQR-HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 102
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1389908286 103 NDDIADGNPKLTLGLIWTIILHFQI 127
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
20-129 |
9.73e-31 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 118.84 E-value: 9.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 20 ERDRVQKKTFTKWVNKHLVKAQR--HVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQ 95
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1389908286 96 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 129
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
143-244 |
1.50e-30 |
|
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: 118.14 E-value: 1.50e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 143 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 221
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1389908286 222 VDVPHPDEKSIITYVSSLYDVMP 244
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1342-1973 |
3.78e-30 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 131.98 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1342 RLED--DEKAS--EKLKEEER--RKMAEIQAELDKQKQMAEAHAKSVAKAEQEALElkmkmkEEASKRQDVAADAEKQKQ 1415
Cdd:COG1196 190 RLEDilGELERqlEPLERQAEkaERYRELKEELKELEAELLLLKLRELEAELEELE------AELEELEAELEELEAELA 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1416 NIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIeeeihiiriqlekttahkaksEAELQELRDRAAEAEKLRKAAQDEA 1495
Cdd:COG1196 264 ELEAELEELR----LELEELELELEEAQAEEYEL---------------------LAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1496 ERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQkykmQAEEAERRMKQAEEEKIRQIRvveevAQKSAAT 1575
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA----EAEEALLEAEAELAEAEEELE-----ELAEELL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1576 QLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIwRQKANEALRLRLQAEEEAQKKS 1655
Cdd:COG1196 390 EALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-AAEEEAELEEEEEALLELLAEL 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1656 HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNEL 1735
Cdd:COG1196 469 LEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAAL 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1736 QRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASmvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQ 1815
Cdd:COG1196 549 QNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAA----ALARGAIGAAVDLVASDLREADARYYVLGDTLLG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1816 RQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKIT 1895
Cdd:COG1196 625 RTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEE 704
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1896 QLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfhkASKEKADLESELKKLKGIADETQksklkAEEEAEKLKK 1973
Cdd:COG1196 705 EERELAEAEEERLEEELEEEALEEQLEAEREELLEEL---LEEEELLEEEALEELPEPPDLEE-----LERELERLER 774
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
23-125 |
1.08e-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: 115.66 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 23 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 99
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1389908286 100 NIRNDDIADGNPKLTLGLIWTIILHF 125
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1313-1892 |
1.69e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 130.06 E-value: 1.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1313 QEYVNLRTRYSEL-MTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALE 1391
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1392 LKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSE 1471
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAEL-EEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1472 AELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRM 1551
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1552 KQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQgNVLKLQEEADKLKKQQKEANTAREEAEQELE 1631
Cdd:COG1196 452 AELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA-EADYEGFLEGVKAALLLAGLRGLAGAVAVLI 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1632 IWRQKANEALRLRLQAEEEAQkksHAQEEAEKQKLEAERDAKKRGKAEEAALkqkeNAEKELDKQRKFAEQIAQQKLSAE 1711
Cdd:COG1196 531 GVEAAYEAALEAALAAALQNI---VVEDDEVAAAAIEYLKAAKAGRATFLPL----DKIRARAALAAALARGAIGAAVDL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1712 QECIRLKADFEHAEQQRGLLDNELQRLKNEvnSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKAsmvnTEKSKQLLESE 1791
Cdd:COG1196 604 VASDLREADARYYVLGDTLLGRTLVAARLE--AALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----RRELLAALLEA 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1792 ALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEE 1871
Cdd:COG1196 678 EAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELP 757
|
570 580
....*....|....*....|.
gi 1389908286 1872 EAYQRKLLEDQAAQHKQDIEE 1892
Cdd:COG1196 758 EPPDLEELERELERLEREIEA 778
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
143-242 |
3.44e-29 |
|
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: 113.92 E-value: 3.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 143 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED- 221
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1389908286 222 VDVPHPDEKSIITYVSSLYDV 242
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
8-127 |
9.77e-28 |
|
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: 110.62 E-value: 9.77e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 8 DFMETLIQRGQDERDRVQKKTFTKWVNKHLVKAQRHV--TDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNV 84
Cdd:cd21247 4 EYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKNGAKIeiTDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENN 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1389908286 85 QIALDFLKHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 127
Cdd:cd21247 84 SKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1100-1966 |
1.07e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 124.87 E-value: 1.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1100 AEETLKNYEARLRDVSKVPSEQKEVEKHRSQMKSMRSE-----AEADQVMFDRLQDDLRKAttvhDKMTRIHSERDADLE 1174
Cdd:PTZ00121 1100 AEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEdarkaEEARKAEDAKRVEIARKA----EDARKAEEARKAEDA 1175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1175 HYRQLVNGLLERWQAvfaqielRLRELDLLGRHMNSYRDSYEwlIRWLTEARQRQEKIQAVPISDSRALREQLTDEKKll 1254
Cdd:PTZ00121 1176 KKAEAARKAEEVRKA-------EELRKAEDARKAEAARKAEE--ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKK-- 1244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1255 GEIEKNKDKIDDCHKNAKAYidsvkdYEFQILTYKALQDPIASPLKKPKMECASDDIiqeyvnlrtRYSELMTLTNQYIK 1334
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAH------FARRQAAIKAEEARKADELKKAEEKKKADEA---------KKAEEKKKADEAKK 1309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1335 FIIDAQRRLEDDEKASE-KLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRqdvaADAEKQ 1413
Cdd:PTZ00121 1310 KAEEAKKADEAKKKAEEaKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKK----ADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1414 KQNIQQELQHLKSLSdQEIKSKNQQLEDALVSRRKIEEEIHIIRiqlEKTTAHKAKSEAElqelrdRAAEAEKLRKAAQD 1493
Cdd:PTZ00121 1386 KAEEKKKADEAKKKA-EEDKKKADELKKAAAAKKKADEAKKKAE---EKKKADEAKKKAE------EAKKADEAKKKAEE 1455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1494 --EAERLRKQvAEETQR----KKNAEDelKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEE 1567
Cdd:PTZ00121 1456 akKAEEAKKK-AEEAKKadeaKKKAEE--AKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEE 1532
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1568 VAQKSAATQlqtkamsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLrlqA 1647
Cdd:PTZ00121 1533 AKKADEAKK--------AEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKL---Y 1601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1648 EEEAQKKSHAQEEAEKQKLEAERDAK-KRGKAEEAALKQKENAEKELDKQRKFAEQiaQQKLSAEQECIRLKADFEHAEQ 1726
Cdd:PTZ00121 1602 EEEKKMKAEEAKKAEEAKIKAEELKKaEEEKKKVEQLKKKEAEEKKKAEELKKAEE--ENKIKAAEEAKKAEEDKKKAEE 1679
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1727 QRGllDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMR 1806
Cdd:PTZ00121 1680 AKK--AEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1807 SVAEEAKKQRQIAEEeaarQRSEAEKILKEKLAAINEATRLKTE---------AEMALKAKEAENERLKRQAEEEAYQRK 1877
Cdd:PTZ00121 1758 KIAHLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDkkikdifdnFANIIEGGKEGNLVINDSKEMEDSAIK 1833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1878 LLEDQAAQHKQDIEEkITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESEL--KKLKGIAD 1955
Cdd:PTZ00121 1834 EVADSKNMQLEEADA-FEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREIpnNNMAGKNN 1912
|
890
....*....|.
gi 1389908286 1956 ETQKSKLKAEE 1966
Cdd:PTZ00121 1913 DIIDDKLDKDE 1923
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1500-2406 |
2.98e-27 |
|
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: 122.86 E-value: 2.98e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1500 KQVAEETQRK-KNAEDELKRKSDAEKEAAKQkqralddLQKYKMQAEEAERRMKQAEEEKIRQIRV----VEEVAQKSAA 1574
Cdd:TIGR02168 171 KERRKETERKlERTRENLDRLEDILNELERQ-------LKSLERQAEKAERYKELKAELRELELALlvlrLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1575 TQLQTKAM-----SFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEE 1649
Cdd:TIGR02168 244 LQEELKEAeeeleELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1650 EaqkkshaQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRG 1729
Cdd:TIGR02168 324 Q-------LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1730 LLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSL----LQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARM 1805
Cdd:TIGR02168 397 SLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAelkeLQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1806 RSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENerlKRQAEEEAYQRKLLEDQAAQ 1885
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDE---GYEAAIEAALGGRLQAVVVE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1886 HKQDIEEKITQLqtsSDSELGRQKNIVEETLKQKKVVEEEIHIIKiNFHKASKEKADLESELKKLKG----------IAD 1955
Cdd:TIGR02168 554 NLNAAKKAIAFL---KQNELGRVTFLPLDSIKGTEIQGNDREILK-NIEGFLGVAKDLVKFDPKLRKalsyllggvlVVD 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1956 ETQksklkaeeEAEKLKKLAAEEERRRKEAEEKVKR---ITAAEEEAARQCKAAQEEVERLKKKAEdankqkekaekeae 2032
Cdd:TIGR02168 630 DLD--------NALELAKKLRPGYRIVTLDGDLVRPggvITGGSAKTNSSILERRREIEELEEKIE-------------- 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2033 kqvvlakEAAQKCTAAEQKAQDVLSKnkedvlaQEKLRDEFENAKKLAQEaekakekaekeaalLRQKAEEAEKQKKAAE 2112
Cdd:TIGR02168 688 -------ELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEE--------------LSRQISALRKDLARLE 739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2113 NEAAKQAKAQNDTEKQRKEAEeeaarraaaeaaalKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQK 2192
Cdd:TIGR02168 740 AEVEQLEERIAQLSKELTELE--------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREAL 805
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2193 VLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEEnrrlmqkdkdstqklLAEEAEKMKSLAEEAGR 2272
Cdd:TIGR02168 806 DELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED---------------IESLAAEIEELEELIEE 870
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2273 LSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQEtakRLQEDKQQIQQRLDKETE 2352
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLEL---RLEGLEVRIDNLQERLSE 947
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 2353 GFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTK-------AEDEAKKFKKQADEVKAQ 2406
Cdd:TIGR02168 948 EYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKElgpvnlaAIEEYEELKERYDFLTAQ 1008
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1100-1897 |
4.48e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 122.94 E-value: 4.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1100 AEETLKNYEARLRDVSKVPSEQKEVEKHRSQMKSMRSEaEADQVMFDRLQDDLRKATTVH--DKMTRIHSERDADLEHYR 1177
Cdd:PTZ00121 1136 AEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAE-DAKKAEAARKAEEVRKAEELRkaEDARKAEAARKAEEERKA 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1178 QLVNGLLERWQAVFAQIELRLRELDLLGRHMNSYRDSYEwlIRWLTEAR-----QRQEKIQAVPISDSRALRE------- 1245
Cdd:PTZ00121 1215 EEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE--IRKFEEARmahfaRRQAAIKAEEARKADELKKaeekkka 1292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1246 ---QLTDEKKLLGEIEKN----------KDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIASPLKKPKMECASDDII 1312
Cdd:PTZ00121 1293 deaKKAEEKKKADEAKKKaeeakkadeaKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKK 1372
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1313 QEYVNlrtRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLK--EEERRKMAEIQAELDKQKQMAEAHAKsvAKAEQEAL 1390
Cdd:PTZ00121 1373 KEEAK---KKADAAKKKAEEKKKADEAKKKAEEDKKKADELKkaAAAKKKADEAKKKAEEKKKADEAKKK--AEEAKKAD 1447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1391 ELKmKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKS 1470
Cdd:PTZ00121 1448 EAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE 1526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1471 EAELQELR--DRAAEAEKLRKAAQ-DEAERLRK--QVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAE 1545
Cdd:PTZ00121 1527 AKKAEEAKkaDEAKKAEEKKKADElKKAEELKKaeEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKK 1606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1546 EAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAmsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE 1625
Cdd:PTZ00121 1607 MKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKE---AEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA 1683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1626 AEQEleiwrQKANEALRlrlQAEEEAQKKshaqEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQ 1705
Cdd:PTZ00121 1684 EEDE-----KKAAEALK---KEAEEAKKA----EELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKK 1751
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1706 QklsaEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKsk 1785
Cdd:PTZ00121 1752 D----EEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFANIIEGGKEGNLVINDSK-- 1825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1786 qllESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQ-----RSEAEKILKEKLAAINEATRLKTEAEMALKAKEA 1860
Cdd:PTZ00121 1826 ---EMEDSAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDgnkeaDFNKEKDLKEDDEEEIEEADEIEKIDKDDIEREI 1902
|
810 820 830
....*....|....*....|....*....|....*..
gi 1389908286 1861 ENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQL 1897
Cdd:PTZ00121 1903 PNNNMAGKNNDIIDDKLDKDEYIKRDAEETREEIIKI 1939
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
23-125 |
4.50e-27 |
|
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: 108.34 E-value: 4.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 23 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 99
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1389908286 100 NIRNDDIADGNPKLTLGLIWTIILHF 125
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1539-2207 |
9.35e-27 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 120.81 E-value: 9.35e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 KYKMQAEEAERRMKQAEE--EKIRQIRvvEEVAQksaatQLqtkamsfseqttkleESLKKEQGNVLK---LQEEADKLK 1613
Cdd:COG1196 169 KYKERKEEAERKLEATEEnlERLEDIL--GELER-----QL---------------EPLERQAEKAERyreLKEELKELE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1614 KQQKEAntAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKEL 1693
Cdd:COG1196 227 AELLLL--KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDI 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1694 DKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINA 1773
Cdd:COG1196 305 ARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEE-ELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1774 EKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAtrlkTEAEM 1853
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL----EEEEE 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1854 ALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIhiikinf 1933
Cdd:COG1196 460 ALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV------- 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1934 hKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKlaaeeerrrkeaeekvKRITAAEEEAARQCKAAQEEVERL 2013
Cdd:COG1196 533 -EAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKA----------------GRATFLPLDKIRARAALAAALARG 595
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2014 KKKAEDANKQKEKAEKEAEKQVVLAKEAaqkctAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKE 2093
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDTLL-----GRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRREL 670
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2094 AALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQ 2173
Cdd:COG1196 671 LAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEE 750
|
650 660 670
....*....|....*....|....*....|....
gi 1389908286 2174 VEKELTVVKLQLDETDKQKVLLDQELQRvKGEVN 2207
Cdd:COG1196 751 EALEELPEPPDLEELERELERLEREIEA-LGPVN 783
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
23-128 |
1.99e-26 |
|
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: 107.04 E-value: 1.99e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 23 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKHRQVKLV 99
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1389908286 100 NIRNDDIADGNPKLTLGLIWTIILHFQIS 128
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1539-2402 |
3.49e-26 |
|
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: 119.39 E-value: 3.49e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 KYKMQAEEAERRMKQAEEEKIRQIRVVEEvaqksaatqlqtkamsfseqttkLEESLKKeqgnvLKLQ-EEADKLKKQQK 1617
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNE-----------------------LERQLKS-----LERQaEKAERYKELKA 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1618 EantaREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEeaALKQKENAEKELdkqr 1697
Cdd:TIGR02168 221 E----LRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE--LEEEIEELQKEL---- 290
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1698 kfaeqiaqQKLSAEQEciRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmkinaekas 1777
Cdd:TIGR02168 291 --------YALANEIS--RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKE--------- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1778 mvntekskqllesealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMAlka 1857
Cdd:TIGR02168 352 ----------------ELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERL--- 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1858 kEAENERLKRQAEEEayQRKLLEDQAAQHKQDIEEKITQLqtssdselgrqknivEETLKQKKVVEEEIHIIKINFHKAS 1937
Cdd:TIGR02168 413 -EDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEEL---------------EELQEELERLEEALEELREELEEAE 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1938 KEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEE-------------------- 1997
Cdd:TIGR02168 475 QALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGyeaaieaalggrlqavvven 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1998 -EAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENA 2076
Cdd:TIGR02168 555 lNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNA 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2077 KKLAQEAEKAKEKAEKEAALL--------------------RQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEA 2136
Cdd:TIGR02168 635 LELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELEKALAELRKELEELEEEL 714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2137 ARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNdafKQKSQV 2216
Cdd:TIGR02168 715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE---ELEAQI 791
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2217 EVELARVRIQMEELVKLKLKIEEENRRLMQK--DKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQ 2294
Cdd:TIGR02168 792 EQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL 871
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2295 RALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKsLEAERKRQLEASAEAEK 2374
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYS 950
|
890 900 910
....*....|....*....|....*....|...
gi 1389908286 2375 LKL-----RVKELSLAQTKAEDEAKKFKKQADE 2402
Cdd:TIGR02168 951 LTLeeaeaLENKIEDDEEEARRRLKRLENKIKE 983
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1483-2582 |
4.27e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.16 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1483 EAEKLRKAAQDEAERLRkqvaeetqrkKNAEDELkrksdaeKEAAKQKQRALDDL--QKYKMQAE---EAERRMKQAEEE 1557
Cdd:NF041483 73 QAEQLLRNAQIQADQLR----------ADAEREL-------RDARAQTQRILQEHaeHQARLQAElhtEAVQRRQQLDQE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1558 KIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQ-----QKEANTAREEAEQeleI 1632
Cdd:NF041483 136 LAERRQTVESHVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAERLAEEarqrlGSEAESARAEAEA---I 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1633 WRQKANEALRLRLQAEEEAQK-KSHAQ----------EEAEKQKLEAERDAKKRGKAEEAALKQkenAEKELDKQRKFAE 1701
Cdd:NF041483 213 LRRARKDAERLLNAASTQAQEaTDHAEqlrsstaaesDQARRQAAELSRAAEQRMQEAEEALRE---ARAEAEKVVAEAK 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1702 QIAQQKLSAEQECirlkadfehAEQQRGLLDNELQRLKNE-VNSTEKQRKQLEDELNKVRSEMDSLLQMKinAEKASMVN 1780
Cdd:NF041483 290 EAAAKQLASAESA---------NEQRTRTAKEEIARLVGEaTKEAEALKAEAEQALADARAEAEKLVAEA--AEKARTVA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1781 TEKS-----KQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKE-KLAAIN------------ 1842
Cdd:NF041483 359 AEDTaaqlaKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDdtkeyraktvel 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1843 --EATRLKTEAEMALKAKEAENERLKRQAEEEAYQR-----KLLEDQAAQHKQDIEEkiTQLQTSSDSELGRQKNI---- 1911
Cdd:NF041483 439 qeEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADE--LRSTATAESERVRTEAIerat 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1912 -----VEETLKQKKvVEEEIHIIKINfHKASKEKADLESELKKLKgiADETQKSKLKAEEEAEKLKKLAAEEErrrkeae 1986
Cdd:NF041483 517 tlrrqAEETLERTR-AEAERLRAEAE-EQAEEVRAAAERAARELR--EETERAIAARQAEAAEELTRLHTEAE------- 585
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1987 ekvKRITAAEE-------EAARQCKAAQEEVERLkkKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKN 2059
Cdd:NF041483 586 ---ERLTAAEEaladaraEAERIRREAAEETERL--RTEAAERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAVRL 660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2060 KEDVLAQ-EKLRDEfenAKKLAQeaekakekaekeaallRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKeaeeeaar 2138
Cdd:NF041483 661 RSEAAAEaERLKSE---AQESAD----------------RVRAEAAAAAERVGTEAAEALAAAQEEAARRRR-------- 713
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2139 raaaeaaalkqkqQADAEMSKHKKEAEQALQQ-KSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQ-V 2216
Cdd:NF041483 714 -------------EAEETLGSARAEADQERERaREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQqV 780
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2217 EVELARVRIQM-EELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEA-EETARQRQIAESNLAEQ 2294
Cdd:NF041483 781 RDSVAGLQEQAeEEIAGLRSAAEHAAERTRTEAQEEADRVRSDAYAERERASEDANRLRREAqEETEAAKALAERTVSEA 860
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2295 RALAEKILKEK---------------MQAIQEATKLKAEA-EKLQKQKDQAQETAKRL------QEDKQQIQQRLDKETE 2352
Cdd:NF041483 861 IAEAERLRSDAseyaqrvrteasdtlASAEQDAARTRADArEDANRIRSDAAAQADRLigeatsEAERLTAEARAEAERL 940
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2353 GFQKSLEAERKR----------QLEASAEAEKLKLRVKE-LSLAQTKAE---DEAKKFKKQADEVKAQLQRTEKHTTEIV 2418
Cdd:NF041483 941 RDEARAEAERVRadaaaqaeqlIAEATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEAERLRTEAREEADRT 1020
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2419 VQklETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIE------QQKAELQQSFLTEKGLLLk 2492
Cdd:NF041483 1021 LD--EARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTTTEAEAQADtmvgaaRKEAERIVAEATVEGNSL- 1097
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2493 rekeVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAimdeavRKQKEAEEEMKNKQREMDVLDKKRLEQE 2572
Cdd:NF041483 1098 ----VEKARTDADELLVGARRDATAIRERAEELRDRITGEIEELHE------RARRESAEQMKSAGERCDALVKAAEEQL 1167
|
1210
....*....|
gi 1389908286 2573 KQLAEENKKL 2582
Cdd:NF041483 1168 AEAEAKAKEL 1177
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1995-2647 |
4.82e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.48 E-value: 4.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1995 AEEEAARQCKAAQEE--VERLKKKAEDANKQKEKAEKEAEKQVVLAKEA-----------------AQKCTAAEQKAQDV 2055
Cdd:PTZ00121 1100 AEEAKKTETGKAEEArkAEEAKKKAEDARKAEEARKAEDARKAEEARKAedakrveiarkaedarkAEEARKAEDAKKAE 1179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2056 LSKNKEDVLAQEKLR--------------DEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQ--- 2118
Cdd:PTZ00121 1180 AARKAEEVRKAEELRkaedarkaeaarkaEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfee 1259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2119 --------AKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHK----KEAEQALQQKSQVEKELTVVKLQLD 2186
Cdd:PTZ00121 1260 armahfarRQAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKaeeaKKADEAKKKAEEAKKKADAAKKKAE 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2187 ETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVK----------LKLKIEEENRRLMQKDKDSTQKLL 2256
Cdd:PTZ00121 1340 EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKkaeekkkadeAKKKAEEDKKKADELKKAAAAKKK 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2257 AEEAEKMKSLAEEAGRLSVEAEETARQRQIAESnlAEQRALAEKILK--EKMQAIQEATKLKAEAEKLQKQKDQAQETAK 2334
Cdd:PTZ00121 1420 ADEAKKKAEEKKKADEAKKKAEEAKKADEAKKK--AEEAKKAEEAKKkaEEAKKADEAKKKAEEAKKADEAKKKAEEAKK 1497
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2335 RLQEDKQQIQQRldKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHT 2414
Cdd:PTZ00121 1498 KADEAKKAAEAK--KKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEED 1575
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2415 TEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKRE 2494
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2495 KEVEGEKKRFE-KQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQ-REMDVLDKKRLEQE 2572
Cdd:PTZ00121 1656 EEENKIKAAEEaKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEElKKAEEENKIKAEEA 1735
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2573 KQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL----VAVTTVGTSKGVLNGSTEVDgvKKEGDSPLSFEGIRE 2647
Cdd:PTZ00121 1736 KKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIrkekEAVIEEELDEEDEKRRMEVD--KKIKDIFDNFANIIE 1812
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
125-240 |
5.09e-26 |
|
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: 105.94 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 125 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAF 204
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1389908286 205 SVAERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 240
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
145-240 |
1.38e-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: 103.77 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 145 LLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED-VD 223
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1389908286 224 VPHPDEKSIITYVSSLY 240
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
127-240 |
1.98e-25 |
|
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: 104.01 E-value: 1.98e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 127 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 206
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908286 207 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 240
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1341-2103 |
2.79e-25 |
|
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: 116.31 E-value: 2.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1341 RRLEDDEKASEKL-----KEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEeaskrqdvaadAEKQKQ 1415
Cdd:TIGR02168 216 KELKAELRELELAllvlrLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1416 NIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEA 1495
Cdd:TIGR02168 285 ELQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1496 ERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRAlddlqkyKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT 1575
Cdd:TIGR02168 361 EELEAELEELESRLEELEEQLETLRSKVAQLELQIASL-------NNEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1576 QLQTKAMSFSEqttkLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKs 1655
Cdd:TIGR02168 434 ELKELQAELEE----LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV- 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1656 hAQEEAEKQKLEAERD--------AKKRGKAEEAALK--------------------QKENAEK-----ELDKQRKFAEQ 1702
Cdd:TIGR02168 509 -KALLKNQSGLSGILGvlselisvDEGYEAAIEAALGgrlqavvvenlnaakkaiafLKQNELGrvtflPLDSIKGTEIQ 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1703 IAQQKLSAEQECIRLKAD--FEHAEQQRGLLDNELQRLK--NEVNSTEKQRKQLEDELNKVRSEMDSLLQ---MKINAEK 1775
Cdd:TIGR02168 588 GNDREILKNIEGFLGVAKdlVKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIVTLDGDLVRPggvITGGSAK 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1776 ASMVNTEKSKQLLESEAlKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMAL 1855
Cdd:TIGR02168 668 TNSSILERRREIEELEE-KIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1856 KAKEAENERLKRQAEEEAYQRKLLEdQAAQHKQDIEEKITQLQtssdSELGRQKNIVEETLKQKKVVEEEIHIIKINFHK 1935
Cdd:TIGR02168 747 ERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELE----AQIEQLKEELKALREALDELRAELTLLNEEAAN 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1936 ASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKK 2015
Cdd:TIGR02168 822 LRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2016 KAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKnkedvlAQEKLRDEFENAKKLAQEAEKAKEKAEKEAA 2095
Cdd:TIGR02168 902 ELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER------LSEEYSLTLEEAEALENKIEDDEEEARRRLK 975
|
....*...
gi 1389908286 2096 LLRQKAEE 2103
Cdd:TIGR02168 976 RLENKIKE 983
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1679-2606 |
3.08e-25 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 116.22 E-value: 3.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1679 EEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNK 1758
Cdd:pfam02463 172 KEALKKLIEETENLAELIIDLEELKLQELKLKEQA---KKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1759 VRSEMDSLLQmKINAEKASMvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKL 1838
Cdd:pfam02463 249 EQEEIESSKQ-EIEKEEEKL---AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKK 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1839 AAINEATRLKTEAEMALKAKEaENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQ 1918
Cdd:pfam02463 325 KAEKELKKEKEEIEELEKELK-ELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1919 KKVVEEEIHIIKINFHKASKEKadlESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEE 1998
Cdd:pfam02463 404 EKEAQLLLELARQLEDLLKEEK---KEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLV 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1999 AARQCKaaQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLaqeKLRDEFENAKK 2078
Cdd:pfam02463 481 KLQEQL--ELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA---ISTAVIVEVSA 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2079 LAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMS 2158
Cdd:pfam02463 556 TADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELT 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2159 KHKKEAeqalqqKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIE 2238
Cdd:pfam02463 636 KLKESA------KAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREK 709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2239 EENRRLMQKDKDSTQKLLAEEAEKmkslaeeagrlsvEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAE 2318
Cdd:pfam02463 710 EELKKLKLEAEELLADRVQEAQDK-------------INEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKEL 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2319 AEKLQKQKDQAQETAKRLQEdkqqiqqrldketegfqKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKK 2398
Cdd:pfam02463 777 AEEREKTEKLKVEEEKEEKL-----------------KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2399 QaDEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAE 2478
Cdd:pfam02463 840 L-ELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2479 LQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQER-QRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNK 2557
Cdd:pfam02463 919 IEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRlLLAKEELGKVNLMAIEEFEEKEERYNKDELEKE 998
|
890 900 910 920
....*....|....*....|....*....|....*....|....*....
gi 1389908286 2558 QREMDVLDKKRLEQEkqlaEENKKLREQLQTFEISSKTVSQTKESQTVS 2606
Cdd:pfam02463 999 RLEEEKKKLIRAIIE----ETCQRLKEFLELFVSINKGWNKVFFYLELG 1043
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
141-240 |
4.94e-25 |
|
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: 102.25 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 141 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPE 220
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1389908286 221 D-VDVPHPDEKSIITYVSSLY 240
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1313-2013 |
5.17e-25 |
|
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: 115.54 E-value: 5.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1313 QEYVNLRTRYSEL-MTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELD-KQKQMAEAHAKsVAKAEQEAL 1390
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEeLRLEVSELEEE-IEELQKELY 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1391 ELKMKmkeeaskrqdvAADAEKQKQNIQQELQHLkslsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKS 1470
Cdd:TIGR02168 292 ALANE-----------ISRLEQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESL 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1471 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDEL----KRKSDAEKEAAKQKQRALD--------DLQ 1538
Cdd:TIGR02168 357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIerleARLERLEDRRERLQQEIEEllkkleeaELK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 KYKMQAEEAERRMKQAEEEKIRQIRVVEEV-AQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQK 1617
Cdd:TIGR02168 437 ELQAELEELEEELEELQEELERLEEALEELrEELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQS 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1618 EANTAREEAEQELEI---WRQKANEALRLRLQA-----EEEAQKKSHAQEEAEKQK-----LEAERDAKKRGKAEEAaLK 1684
Cdd:TIGR02168 517 GLSGILGVLSELISVdegYEAAIEAALGGRLQAvvvenLNAAKKAIAFLKQNELGRvtflpLDSIKGTEIQGNDREI-LK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1685 QKENAEKELDKQRKFAEQ---------------------IAQQKLSAEQECI------RLKAD----FEHAEQQRGLL-- 1731
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKlrkalsyllggvlvvddldnaLELAKKLRPGYRIvtldgdLVRPGgvitGGSAKTNSSILer 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1732 DNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM-------------KINAEKASMVNTEKSKQLLESE------- 1791
Cdd:TIGR02168 676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEEleqlrkeleelsrQISALRKDLARLEAEVEQLEERiaqlske 755
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1792 ----ALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEA---EMALKAKEAENER 1864
Cdd:TIGR02168 756 ltelEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAanlRERLESLERRIAA 835
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1865 LKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSelgrqkniVEETLKQKKVVEEEIHIIKINFHKASKEKADLE 1944
Cdd:TIGR02168 836 TERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--------LEALLNERASLEEALALLRSELEELSEELRELE 907
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1945 SELKKLKGIADETQKSKLKAEEEAEKLK--------KLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERL 2013
Cdd:TIGR02168 908 SKRSELRRELEELREKLAQLELRLEGLEvridnlqeRLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
140-240 |
6.90e-25 |
|
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: 101.73 E-value: 6.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 219
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAA-KLGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1389908286 220 EDV---DVphPDEKSIITYVSSLY 240
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
127-240 |
8.58e-25 |
|
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: 102.50 E-value: 8.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 127 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 206
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908286 207 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 240
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1607-2445 |
1.09e-24 |
|
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: 114.38 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1607 EEA---DKLKKQQKEANTAREEAEQEL--------EIWRQKAnealRLRLQAE--EEAQKKSHAQEEAEKQKLEAERDAK 1673
Cdd:TIGR02168 162 EEAagiSKYKERRKETERKLERTRENLdrledilnELERQLK----SLERQAEkaERYKELKAELRELELALLVLRLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1674 KRgKAEEAALKQKENAEKELDKQRKFAEqiAQQKLSaEQECIRLKADFEHAEQQRGLLD--NELQRLKNEVNSTEKQRKQ 1751
Cdd:TIGR02168 238 RE-ELEELQEELKEAEEELEELTAELQE--LEEKLE-ELRLEVSELEEEIEELQKELYAlaNEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1752 LEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLEsealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAE 1831
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDELAEELAELEEKLEELKE----ELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1832 KILKEKLAAINEATRLKTEAEMAlkakEAENERLKRQAEEEayQRKLLEDQAAQHKQDIEEKITQLqtssdselgrqkni 1911
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERL----EDRRERLQQEIEEL--LKKLEEAELKELQAELEELEEEL-------------- 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1912 vEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKR 1991
Cdd:TIGR02168 450 -EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSEL 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1992 ITAAEE---------------------EAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQ 2050
Cdd:TIGR02168 529 ISVDEGyeaaieaalggrlqavvvenlNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV 608
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2051 KAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALL--------------------RQKAEEAEKQKKA 2110
Cdd:TIGR02168 609 KFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2111 AENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDK 2190
Cdd:TIGR02168 689 LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2191 QKVLLDQELQRVKGEVNdafKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQK--DKDSTQKLLAEEAEKMKSLAE 2268
Cdd:TIGR02168 769 RLEEAEEELAEAEAEIE---ELEAQIEQLKEELKALREALDELRAELTLLNEEAANLreRLESLERRIAATERRLEDLEE 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2269 EAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD 2348
Cdd:TIGR02168 846 QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLA 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2349 KETEGFQKsLEAERKRQLEASAEAEKLklrvkELSLAQTKAEDEAKKFKKQADEVKaQLQRTEKHTTEIVVQKLETQRLQ 2428
Cdd:TIGR02168 926 QLELRLEG-LEVRIDNLQERLSEEYSL-----TLEEAEALENKIEDDEEEARRRLK-RLENKIKELGPVNLAAIEEYEEL 998
|
890
....*....|....*..
gi 1389908286 2429 STREaDDLKSAIADLEE 2445
Cdd:TIGR02168 999 KERY-DFLTAQKEDLTE 1014
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
27-124 |
1.54e-24 |
|
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: 100.85 E-value: 1.54e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 27 KTFTKWVNKHLVKA-QRHVTDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKHRQVKLVNIR 102
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1389908286 103 NDDIADGnPKLTLGLIWTIILH 124
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
139-245 |
2.55e-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: 100.44 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 139 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ--ENLEQAFSVAERELGVTK 215
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNKSEFDklENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1389908286 216 -LLDPEDVDvpHPDEKSIITYVSSLYDVMPR 245
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
140-244 |
2.56e-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: 100.25 E-value: 2.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 219
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1389908286 220 EDVDVPHPDEKSIITYVSSLYDVMP 244
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
24-127 |
7.34e-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: 98.90 E-value: 7.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 24 VQKKTFTKWVNKHLVKAQRH--VTDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKHRQ-VKLV 99
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1389908286 100 NIRNDDIADGNPKLTLGLIWTIILHFQI 127
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1743-2542 |
1.05e-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: 111.30 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1743 NSTEKQRKQLEDELNKVRSEMDSLlqmKINAEKAsmvntEKSKQLleSEALKMKQLADEAARMRSvAEEAKKQRQIAEEE 1822
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSL---ERQAEKA-----ERYKEL--KAELRELELALLVLRLEE-LREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1823 AARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssd 1902
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE---- 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1903 sELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIAD---ETQKSKLKAEEEAE-----KLKKL 1974
Cdd:TIGR02168 327 -ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEeqlETLRSKVAQLELQIaslnnEIERL 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1975 AAEEERRRKEAEEKVKRITAAEEEAAR-QCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQ 2053
Cdd:TIGR02168 406 EARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2054 DVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEkeaaLLRQKAEEAEKQKKAAE--------------NEAAKQA 2119
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILG----VLSELISVDEGYEAAIEaalggrlqavvvenLNAAKKA 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2120 KA---QNDTEKQ-----RKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAE-----------------QALQQKSQV 2174
Cdd:TIGR02168 562 IAflkQNELGRVtflplDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvddldNALELAKKL 641
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2175 EKELTVVKLQLD-------------ETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEEL----VKLKLKI 2237
Cdd:TIGR02168 642 RPGYRIVTLDGDlvrpggvitggsaKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELeeelEQLRKEL 721
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2238 EEENRRLmqkdkDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKA 2317
Cdd:TIGR02168 722 EELSRQI-----SALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2318 EAEKLQKQKDQAQETAKRLQEDKQQIQQRLD---KETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAK 2394
Cdd:TIGR02168 797 ELKALREALDELRAELTLLNEEAANLRERLEsleRRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2395 KFKKQADEVKAQLQ--RTEKHTTEIVVQKLETQRLQSTREADDLKSAIADleeerkklkkeaeelqrkskemANAQQEQI 2472
Cdd:TIGR02168 877 ALLNERASLEEALAllRSELEELSEELRELESKRSELRRELEELREKLAQ----------------------LELRLEGL 934
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2473 EQQKAELQQSFLTEKGLLL-----------KREKEVEGEKKRFEKQLE----------DEMKKAKALKDEQERQRKLMEE 2531
Cdd:TIGR02168 935 EVRIDNLQERLSEEYSLTLeeaealenkieDDEEEARRRLKRLENKIKelgpvnlaaiEEYEELKERYDFLTAQKEDLTE 1014
|
890
....*....|.
gi 1389908286 2532 ERKKLQAIMDE 2542
Cdd:TIGR02168 1015 AKETLEEAIEE 1025
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
127-240 |
2.73e-23 |
|
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: 98.22 E-value: 2.73e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 127 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSV 206
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1389908286 207 AERELGVTKLLDPED-VDVPHPDEKSIITYVSSLY 240
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
143-243 |
1.18e-22 |
|
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: 95.22 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 143 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPEDV 222
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1389908286 223 DVPHPDEKSIITYVSSLYDVM 243
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1313-2179 |
1.41e-22 |
|
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: 107.36 E-value: 1.41e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1313 QEYVNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALEL 1392
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1393 -KMKMKEEASKRQDVAADAEKQKQN---------IQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEK 1462
Cdd:pfam02463 246 lRDEQEEIESSKQEIEKEEEKLAQVlkenkeeekEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1463 TTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQ----RALDDLQ 1538
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEeeleLKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 KYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1618
Cdd:pfam02463 406 EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQ 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1619 ANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRK 1698
Cdd:pfam02463 486 LELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQK 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1699 FAEQIAQQKLSAEQECIRLKADFE----HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAE 1774
Cdd:pfam02463 566 LVRALTELPLGARKLRLLIPKLKLplksIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKE 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1775 KASMVNTEKSKQLLESEALKMKQLADeaaRMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEma 1854
Cdd:pfam02463 646 SGLRKGVSLEEGLAEKSEVKASLSEL---TKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAE-- 720
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1855 lkakEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGR---QKNIVEETLKQKKVVEEEIHIIKI 1931
Cdd:pfam02463 721 ----ELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELslkEKELAEEREKTEKLKVEEEKEEKL 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1932 NFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVE 2011
Cdd:pfam02463 797 KAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2012 RLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQ----KAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAK 2087
Cdd:pfam02463 877 EELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKeneiEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKE 956
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2088 EKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADA---EMSKHKKEA 2164
Cdd:pfam02463 957 EEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLElfvSINKGWNKV 1036
|
890
....*....|....*
gi 1389908286 2165 EQALQQKSQVEKELT 2179
Cdd:pfam02463 1037 FFYLELGGSAELRLE 1051
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1846-2412 |
1.84e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 1.84e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1846 RLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdsELGRQKNIVEETLKQKKvveEE 1925
Cdd:COG1196 204 PLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELE-----ELEAELAELEAELEELR---LE 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1926 IHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKlaaeeerRRKEAEEKVKRITAAEEEAARQCKA 2005
Cdd:COG1196 276 LEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE-------ELAELEEELEELEEELEELEEELEE 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2006 AQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEK 2085
Cdd:COG1196 349 AEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2086 AKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQ---KQQADAEMSKHKK 2162
Cdd:COG1196 429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARlllLLEAEADYEGFLE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2163 EAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVR------IQMEELVKLKLK 2236
Cdd:COG1196 509 GVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKagratfLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2237 IEEENRRLMQKDKDSTQKLLAEEAEKMKSL-------------AEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILK 2303
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLgdtllgrtlvaarLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2304 EKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELS 2383
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
570 580
....*....|....*....|....*....
gi 1389908286 2384 LAQTKAEDEAkkfKKQADEVKAQLQRTEK 2412
Cdd:COG1196 749 EEEALEELPE---PPDLEELERELERLER 774
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1943-2542 |
3.44e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.17 E-value: 3.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1943 LESELKKLKGIADETQKSK-LKAEE---EAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAE 2018
Cdd:COG1196 198 LERQLEPLERQAEKAERYReLKEELkelEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2019 DANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLR 2098
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2099 QKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKEL 2178
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2179 TVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDST-QKLLA 2257
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKaALLLA 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2258 EEAEKMKSLAEEAGRLSVE--AEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLkaEAEKLQKQKDQAQETAKR 2335
Cdd:COG1196 518 GLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL--PLDKIRARAALAAALARG 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2336 LQEDKQQIQQRLDKETEGFQKSLEA-------ERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQ 2408
Cdd:COG1196 596 AIGAAVDLVASDLREADARYYVLGDtllgrtlVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2409 RTEKHTTEIVVQKL-ETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEK 2487
Cdd:COG1196 676 EAEAELEELAERLAeEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEE 755
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 2488 GLLLKREKEVEGEKKRFEKQLE----------DEMKKAKALKDEQERQRKLMEEERKKLQAIMDE 2542
Cdd:COG1196 756 LPEPPDLEELERELERLEREIEalgpvnllaiEEYEELEERYDFLSEQREDLEEARETLEEAIEE 820
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
144-242 |
4.57e-22 |
|
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: 93.95 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 144 KLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD-PEDV 222
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1389908286 223 DVPHPDEKSIITYVSSLYDV 242
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1471-2339 |
4.64e-22 |
|
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: 105.82 E-value: 4.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1471 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSdAEKEAAKQKQRALDDLQKYKMQAE----- 1545
Cdd:pfam02463 197 LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL-RDEQEEIESSKQEIEKEEEKLAQVlkenk 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1546 EAERRMKQAEEEKIRQIRvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE 1625
Cdd:pfam02463 276 EEEKEKKLQEEELKLLAK--EEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1626 AEQELEiwrqkanealrlrlQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQrkfaEQIAQ 1705
Cdd:pfam02463 354 EEEEEE--------------ELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLL----LELAR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1706 QKLSAEQECIRLKADFEHAEQQRGLLDnelQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSK 1785
Cdd:pfam02463 416 QLEDLLKEEKKEELEILEEEEESIELK---QGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSR 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1786 QLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEaaRQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERL 1865
Cdd:pfam02463 493 QKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHG--RLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRAL 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1866 KRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLqtssDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLES 1945
Cdd:pfam02463 571 TELPLGARKLRLLIPKLKLPLKSIAVLEIDPI----LNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1946 ELKKLKGIA-DETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQK 2024
Cdd:pfam02463 647 GLRKGVSLEeGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADR 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2025 ekaekeaekqvvlaKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEA 2104
Cdd:pfam02463 727 --------------VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEK 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2105 EKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKqqadAEMSKHKKEAEQALQQKSQVEKELTVVKLQ 2184
Cdd:pfam02463 793 EEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEEL----ALELKEEQKLEKLAEEELERLEEEITKEEL 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2185 LDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMK 2264
Cdd:pfam02463 869 LQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEK 948
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 2265 SLAEEAgRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQED 2339
Cdd:pfam02463 949 EKEENN-KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEF 1022
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
23-128 |
5.01e-22 |
|
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: 94.76 E-value: 5.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 23 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 99
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1389908286 100 NIRNDDIADGNPKLTLGLIWTIILHFQIS 128
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1408-2349 |
7.37e-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: 105.14 E-value: 7.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1408 ADAEKQKQNIQQELQHL-KSLSDQEIKSKNQQLEDALVSRRKIEEeihiiriQLEKTTAHKAKSEAELQELRDRAAEAEK 1486
Cdd:TIGR02168 209 AEKAERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEE-------ELEELTAELQELEEKLEELRLEVSELEE 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1487 LRKAAQDEAERLRKQVAEETQRKKnaedelkrksdaekEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvve 1566
Cdd:TIGR02168 282 EIEELQKELYALANEISRLEQQKQ--------------ILRERLANLERQLEELEAQLEELESKLDELAEE--------- 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1567 evaqksaATQLQTKAMSFSEQTTKLEESLKKEQGnvlKLQEEADKLKKQQKEANTAREEAEQELEiwRQKANEALRLRLQ 1646
Cdd:TIGR02168 339 -------LAELEEKLEELKEELESLEAELEELEA---ELEELESRLEELEEQLETLRSKVAQLEL--QIASLNNEIERLE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1647 AEEEAQKKSHAQEEAEKQKLEaerdakkrgkaEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQ 1726
Cdd:TIGR02168 407 ARLERLEDRRERLQQEIEELL-----------KKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1727 QRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMK-INAEKASMVNTEKSKQLLESEALkmkQLADEAARM 1805
Cdd:TIGR02168 476 ALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSgILGVLSELISVDEGYEAAIEAAL---GGRLQAVVV 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1806 RSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEnerlkrQAEEEAyqRKLLEDQAAQ 1885
Cdd:TIGR02168 553 ENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLV------KFDPKL--RKALSYLLGG 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1886 HK--QDIEEKITQLqtssdSELGRQKNIVeeTLKQKKV---------VEEEIHII---KINFHKASKEKADLESELKKLK 1951
Cdd:TIGR02168 625 VLvvDDLDNALELA-----KKLRPGYRIV--TLDGDLVrpggvitggSAKTNSSIlerRREIEELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1952 GIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKea 2031
Cdd:TIGR02168 698 KALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2032 ekqvvLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAA 2111
Cdd:TIGR02168 776 -----ELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEEL 850
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2112 ENEAAKQAKAQNDTEKQRkeaeeeaARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQ 2191
Cdd:TIGR02168 851 SEDIESLAAEIEELEELI-------EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2192 KVLLDQELQRVKGEVNDAFKQKSqvevelARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLlaeeaekmkslaEEAG 2271
Cdd:TIGR02168 924 LAQLELRLEGLEVRIDNLQERLS------EEYSLTLEEAEALENKIEDDEEEARRRLKRLENKI------------KELG 985
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2272 RLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKlkaeaeklqkqkdqaqETAKRLQEDKQQIQQRLDK 2349
Cdd:TIGR02168 986 PVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDR----------------EARERFKDTFDQVNENFQR 1047
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
23-128 |
8.18e-22 |
|
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: 94.00 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 23 RVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 99
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1389908286 100 NIRNDDIADGNPKLTLGLIWTIILHFQIS 128
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
140-238 |
1.49e-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: 1.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGKLFSAIIHKHRPALIDMN-QVYRQSNQENLEQAFSVAERELGVTKLLD 218
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNeSLDKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1389908286 219 PEDVDVPHPDEKSIITYVSS 238
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1502-2408 |
3.07e-21 |
|
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: 103.13 E-value: 3.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1502 VAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvvEEVAQKSAATQLQTka 1581
Cdd:pfam02463 164 GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKL--------ELEEEYLLYLDYLK-- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1582 msfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEA 1661
Cdd:pfam02463 234 ----LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRK 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1662 EKQKLEAERDAKKRGKAEEAALKQKENAEkELDKQRKFAEQIAQQKLSAEQECIRLKadfEHAEQQRGLLDNELQRLKNE 1741
Cdd:pfam02463 310 VDDEEKLKESEKEKKKAEKELKKEKEEIE-ELEKELKELEIKREAEEEEEEELEKLQ---EKLEQLEEELLAKKKLESER 385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1742 VNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMvNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEE 1821
Cdd:pfam02463 386 LSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK-EEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDE 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1822 EAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKE-AENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTS 1900
Cdd:pfam02463 465 LELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKEsKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1901 SDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLK-----GIADETQKSKLKAEEEAEKLKKLA 1975
Cdd:pfam02463 545 ISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAvleidPILNLAQLDKATLEADEDDKRAKV 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1976 AEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDV 2055
Cdd:pfam02463 625 VEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKK 704
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2056 LSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEE 2135
Cdd:pfam02463 705 EQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2136 AARRAAAEAAALKQKQQADAEMSKHKKEAEQALQqksQVEKELTVVKLQLDETDKQKVLLDQELQrvKGEVNDAFKQKSQ 2215
Cdd:pfam02463 785 KLKVEEEKEEKLKAQEEELRALEEELKEEAELLE---EEQLLIEQEEKIKEEELEELALELKEEQ--KLEKLAEEELERL 859
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2216 VEVELARVRIQMEELVKLKLKIEEENRRLMQK-DKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQ 2294
Cdd:pfam02463 860 EEEITKEELLQELLLKEEELEEQKLKDELESKeEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEE 939
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2295 RALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgfqKSLEAERKRQLEASAEaEK 2374
Cdd:pfam02463 940 LLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEK---ERLEEEKKKLIRAIIE-ET 1015
|
890 900 910
....*....|....*....|....*....|....
gi 1389908286 2375 LKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQ 2408
Cdd:pfam02463 1016 CQRLKEFLELFVSINKGWNKVFFYLELGGSAELR 1049
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
140-239 |
4.42e-21 |
|
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: 91.00 E-value: 4.42e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 219
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFA-SLGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 1389908286 220 ED-VDVPHPDEKSIITYVSSL 239
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
785-851 |
6.89e-21 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 88.86 E-value: 6.89e-21
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 785 QLKPRNptTPLKGKMPIQAVCDFKQMEITVHRGDECALLNNSNPFKWQVLNDTGSEASVPSICFLVP 851
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2096-2586 |
8.10e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 8.10e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2096 LLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVE 2175
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2176 KELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRL------MQKDK 2249
Cdd:COG1196 316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELaeelleALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2250 DSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQA 2329
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2330 QETAKRLQEDKQQIQQRLD------KETEGFQKSLEAERK---------------------RQLEASAEAEKLKLRVKEL 2382
Cdd:COG1196 476 EAALAELLEELAEAAARLLllleaeADYEGFLEGVKAALLlaglrglagavavligveaayEAALEAALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2383 SLAQTKAEDEAKKFKK------QADEVKAQLQRTEKHTT------------EIVVQKLETQRLQSTREADDLKSAIADLE 2444
Cdd:COG1196 556 DEVAAAAIEYLKAAKAgratflPLDKIRARAALAAALARgaigaavdlvasDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2445 EERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALK--DEQ 2522
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAeaEEE 715
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 2523 ERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQL 2586
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
136-243 |
8.56e-21 |
|
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: 90.39 E-value: 8.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 136 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTK 215
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1389908286 216 LLDPEDV-DVPHPDEKSIITYVSSLYDVM 243
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
140-240 |
1.90e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 89.32 E-value: 1.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDP 219
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1389908286 220 EDVDV--PHPDEKSIITYVSSLY 240
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1752-2372 |
2.99e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 99.63 E-value: 2.99e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1752 LEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAK-------KQRQIAEEEAA 1824
Cdd:COG1196 191 LEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEaeleeleAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1825 RQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdsE 1904
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-----E 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1905 LGRQKNIVEETLKQKKVVEEEIhiikinfHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKE 1984
Cdd:COG1196 346 LEEAEEELEEAEAELAEAEEAL-------LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1985 AEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDvlSKNKEDVL 2064
Cdd:COG1196 419 LEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE--AAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2065 AQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAE--------NEAAKQAKAQNDTEKQRKEAEEEA 2136
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALaaalqnivVEDDEVAAAAIEYLKAAKAGRATF 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2137 ARRAAAEAAALKQKQQADAEMSKH-------KKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGE---V 2206
Cdd:COG1196 577 LPLDKIRARAALAAALARGAIGAAvdlvasdLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEgegG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2207 NDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQI 2286
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2287 AESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQ-------AQETAKRLQEDKQQIQQRLD------KETEG 2353
Cdd:COG1196 737 LLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQREdleearETLEE 816
|
650
....*....|....*....
gi 1389908286 2354 FQKSLEAERKRQLEASAEA 2372
Cdd:COG1196 817 AIEEIDRETRERFLETFDA 835
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1352-2053 |
8.83e-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: 98.12 E-value: 8.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1352 KLKEEERRKMAEIQAELDKQKQMA--------EAHAKSVAKAEQEALE--LKMKMKEEASKRQDVAADAEKQKQNIQQEL 1421
Cdd:TIGR00618 159 KAKSKEKKELLMNLFPLDQYTQLAlmefakkkSLHGKAELLTLRSQLLtlCTPCMPDTYHERKQVLEKELKHLREALQQT 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1422 QHLKSLSDQEIKSKNQQLedalvsrrKIEEEIHIIRIQLEKTTAHKAKSEaELQELRDRAAEAEKLrKAAQDEAERLRKQ 1501
Cdd:TIGR00618 239 QQSHAYLTQKREAQEEQL--------KKQQLLKQLRARIEELRAQEAVLE-ETQERINRARKAAPL-AAHIKAVTQIEQQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1502 VAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQirvveevAQKSAATQLQTKA 1581
Cdd:TIGR00618 309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR-------EISCQQHTLTQHI 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1582 MSFSEQTTKLEESLKKEQGNVLKLQEEAdklkkQQKEANTAREEAEQEleiwrQKANEALRLRLQAEEEAQKKSHAQEEA 1661
Cdd:TIGR00618 382 HTLQQQKTTLTQKLQSLCKELDILQREQ-----ATIDTRTSAFRDLQG-----QLAHAKKQQELQQRYAELCAAAITCTA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1662 EKQKLE--AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqkLSAEQECIrLKADFEHAEQQRGLLDN------ 1733
Cdd:TIGR00618 452 QCEKLEkiHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLL--ELQEEPCP-LCGSCIHPNPARQDIDNpgpltr 528
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1734 --------------ELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEaLKMKQLA 1799
Cdd:TIGR00618 529 rmqrgeqtyaqletSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQ-CDNRSKEDIPNLQNITVRLQDL-TEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1800 DEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAineatrLKTEAEMALKAKEAENERLKRQAEEEAYQRKLL 1879
Cdd:TIGR00618 607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTA------LHALQLTLTQERVREHALSIRVLPKELLASRQL 680
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1880 EDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQkkvveeeIHIIKINFHKASKEKADLESELKKLKGIADETQK 1959
Cdd:TIGR00618 681 ALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDRE-------FNEIENASSSLGSDLAAREDALNQSLKELMHQAR 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1960 SKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRitaaeeEAARQCKAAQEEVERLK-KKAEDANKQKEKAEKEAEKQVVLA 2038
Cdd:TIGR00618 754 TVLKARTEAHFNNNEEVTAALQTGAELSHLAA------EIQFFNRLREEDTHLLKtLEAEIGQEIPSDEDILNLQCETLV 827
|
730
....*....|....*
gi 1389908286 2039 KEAAQKCTAAEQKAQ 2053
Cdd:TIGR00618 828 QEEEQFLSRLEEKSA 842
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
143-239 |
9.05e-20 |
|
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: 86.99 E-value: 9.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 143 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ----ENLEQAFSVAERELGVTKLLD 218
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSRfkkiENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1389908286 219 PEDVDVPHPDEKSIITYVSSL 239
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
140-239 |
1.89e-19 |
|
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: 86.44 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 219
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFA-SLGISRLLEP 79
|
90 100
....*....|....*....|.
gi 1389908286 220 ED-VDVPHPDEKSIITYVSSL 239
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2257-2578 |
5.09e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 95.77 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2257 AEEAEKMKSLAEEAGRLsvEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRL 2336
Cdd:COG1196 209 AEKAERYRELKEELKEL--EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2337 QEDKQQIQQRLDKEtegfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTE 2416
Cdd:COG1196 287 QAEEYELLAELARL----EQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2417 IVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQ-QEQIEQQKAELQQSFLTEKGLLLKREK 2495
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErLERLEEELEELEEALAELEEEEEEEEE 442
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2496 EVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQL 2575
Cdd:COG1196 443 ALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGL 522
|
...
gi 1389908286 2576 AEE 2578
Cdd:COG1196 523 AGA 525
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
25-125 |
6.06e-19 |
|
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: 84.94 E-value: 6.06e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 25 QKKTFTKWVNKHLVKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQVKLVN 100
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1389908286 101 IRNDDIADGNPKLTLGLIWTIILHF 125
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1338-2435 |
1.86e-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: 94.09 E-value: 1.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1338 DAQRRLEDDEKASEKLkEEERRKMAEIQAELDKQKQMAEAhAKSVAKAEQEALELKMK-MKEEASKRQDVAADAEKQKQN 1416
Cdd:pfam01576 79 ELESRLEEEEERSQQL-QNEKKKMQQHIQDLEEQLDEEEA-ARQKLQLEKVTTEAKIKkLEEDILLLEDQNSKLSKERKL 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1417 IQQELQHLKS-LSDQEIKSKNqqledalvsrrkieeeihiiriqlekTTAHKAKSEAELQELRDRAAEAEKLRkaaqdea 1495
Cdd:pfam01576 157 LEERISEFTSnLAEEEEKAKS--------------------------LSKLKNKHEAMISDLEERLKKEEKGR------- 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1496 ERLRKqvaeetqrkknaedeLKRKSDAEkeaAKQKQRALDDLQkykMQAEEAERRMKQAEEE-KIRQIRVVEEVAQKSAA 1574
Cdd:pfam01576 204 QELEK---------------AKRKLEGE---STDLQEQIAELQ---AQIAELRAQLAKKEEElQAALARLEEETAQKNNA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1575 tqlqtkamsfseqttklEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRlRLQAEEEAQKK 1654
Cdd:pfam01576 263 -----------------LKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLD-TTAAQQELRSK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1655 SHAQEEAEKQKLEAErdaKKRGKAEEAALKQKENA-----EKELDKQRKFAEQIAQQKLSAEQECIRLKADFE------- 1722
Cdd:pfam01576 325 REQEVTELKKALEEE---TRSHEAQLQEMRQKHTQaleelTEQLEQAKRNKANLEKAKQALESENAELQAELRtlqqakq 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1723 HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASmVNTEKSKQLLESEALKMKQLADEA 1802
Cdd:pfam01576 402 DSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKN-IKLSKDVSSLESQLQDTQELLQEE 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1803 ARMRsvAEEAKKQRQIAEEEAArqrseaekiLKEKLAAINEATRlktEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQ 1882
Cdd:pfam01576 481 TRQK--LNLSTRLRQLEDERNS---------LQEQLEEEEEAKR---NVERQLSTLQAQLSDMKKKLEEDAGTLEALEEG 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1883 AAQHKQDIEEKITQLQTSSDSelgrqkniVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKL 1962
Cdd:pfam01576 547 KKRLQRELEALTQQLEEKAAA--------YDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFDQMLAEEKAISA 618
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1963 KAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLkkkaedankqkekaekeaekqvVLAKEAA 2042
Cdd:pfam01576 619 RYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDL----------------------VSSKDDV 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2043 QKCTAAEQKAQDVLSKNKEDVLAQ-EKLRDEF---ENAKklaqeaekakekaekeaalLRQkaeEAEKQKKAAENEAAKQ 2118
Cdd:pfam01576 677 GKNVHELERSKRALEQQVEEMKTQlEELEDELqatEDAK-------------------LRL---EVNMQALKAQFERDLQ 734
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2119 AKAQNDTEKQRkeaeeeaarraaaeaAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQE 2198
Cdd:pfam01576 735 ARDEQGEEKRR---------------QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQ 799
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2199 LQRVKGEVNDAfkQKSQVEVELARVRI------------QME-ELVKLK--LKIEEENRRLMQKDKDSTQKLLAEEAEKM 2263
Cdd:pfam01576 800 LKKLQAQMKDL--QRELEEARASRDEIlaqskesekklkNLEaELLQLQedLAASERARRQAQQERDELADEIASGASGK 877
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2264 KSLAEEAGRLSveaeetARQRQIAESNLAEQ---RALAEKILKEKMQAIQEATKLKAEAEKLQKQKD-------QAQETA 2333
Cdd:pfam01576 878 SALQDEKRRLE------ARIAQLEEELEEEQsntELLNDRLRKSTLQVEQLTTELAAERSTSQKSESarqqlerQNKELK 951
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2334 KRLQEDKQQIQQR-------LDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQAD----- 2401
Cdd:pfam01576 952 AKLQEMEGTVKSKfkssiaaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEkgnsr 1031
|
1130 1140 1150
....*....|....*....|....*....|....*..
gi 1389908286 2402 --EVKAQLQRTEKHTTEIVVQKLETQR-LQSTREADD 2435
Cdd:pfam01576 1032 mkQLKRQLEEAEEEASRANAARRKLQReLDDATESNE 1068
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1592-2553 |
4.06e-18 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 92.97 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1592 EESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALR------------LRLQAEeeaQKKSHAQE 1659
Cdd:NF041483 7 QESHRADDDHLSRFEAEMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRslasrpaydgadIGYQAE---QLLRNAQI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1660 EAEKQKLEAERdakkrgkaeeaalkqkenaekELDKQRKFAEQIAQqklsaeqecirlkadfEHAEQQrglldnelQRLK 1739
Cdd:NF041483 84 QADQLRADAER---------------------ELRDARAQTQRILQ----------------EHAEHQ--------ARLQ 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1740 NEVNSTEKQRKQ-LEDELNKVRSEMDSLLQMKIN-AEKASMVNTEKSKQLL-ESEALKMKQLADEAARMRSVAEEAKkQR 1816
Cdd:NF041483 119 AELHTEAVQRRQqLDQELAERRQTVESHVNENVAwAEQLRARTESQARRLLdESRAEAEQALAAARAEAERLAEEAR-QR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1817 QIAEEEAARqrSEAEKILK------EKL--AAINEATRLKTEAEMALKAKEAENERLKRQAEEeayqrklLEDQAAQHKQ 1888
Cdd:NF041483 198 LGSEAESAR--AEAEAILRrarkdaERLlnAASTQAQEATDHAEQLRSSTAAESDQARRQAAE-------LSRAAEQRMQ 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1889 DIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEihiikiNFHKASKEKADLESE-LKKLKGIADETQKSKLKAEEE 1967
Cdd:NF041483 269 EAEEALREARAEAEKVVAEAKEAAAKQLASAESANEQ------RTRTAKEEIARLVGEaTKEAEALKAEAEQALADARAE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1968 AEKLkklaaeeerrrKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAekeaekqvvlAKEAAQKCTA 2047
Cdd:NF041483 343 AEKL-----------VAEAAEKARTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAA----------AEEAERIRRE 401
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2048 AEQKAqDVLSKNKEDVLAQEK---LRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQND 2124
Cdd:NF041483 402 AEAEA-DRLRGEAADQAEQLKgaaKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAAR 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2125 TEKQrkeaeeeaarraaaeaaaLKQKQQADAEMSKHKKEAEQALQQKSQVEKElTVVKLQLDETdkqkvlldqeLQRVKG 2204
Cdd:NF041483 481 TAEE------------------LLTKAKADADELRSTATAESERVRTEAIERA-TTLRRQAEET----------LERTRA 531
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2205 EvndAFKQKSQVEVELARVRIQMEELVKlklKIEEENRRLMQkdkdstqkllAEEAEKmkslAEEAGRLSVEAEEtarQR 2284
Cdd:NF041483 532 E---AERLRAEAEEQAEEVRAAAERAAR---ELREETERAIA----------ARQAEA----AEELTRLHTEAEE---RL 588
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2285 QIAESNLAEQRALAEKILKEkmqAIQEATKLKAEA-EKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFqksleAERK 2363
Cdd:NF041483 589 TAAEEALADARAEAERIRRE---AAEETERLRTEAaERIRTLQAQAEQEAERLRTEAAADASAARAEGENV-----AVRL 660
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2364 RQlEASAEAEKLKLRVKEL-----SLAQTKAE---DEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADD 2435
Cdd:NF041483 661 RS-EAAAEAERLKSEAQESadrvrAEAAAAAErvgTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEE 739
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2436 -LKSAIADLEEERKKLKKEAEELQRKSKEMANAqQEQIEQQKAElqqsflTEKGLLLKREKEVEGEKKRFEKQLEDEMKK 2514
Cdd:NF041483 740 lLASARKRVEEAQAEAQRLVEEADRRATELVSA-AEQTAQQVRD------SVAGLQEQAEEEIAGLRSAAEHAAERTRTE 812
|
970 980 990
....*....|....*....|....*....|....*....
gi 1389908286 2515 AkalKDEQERQRKLMEEERKKLQaimDEAVRKQKEAEEE 2553
Cdd:NF041483 813 A---QEEADRVRSDAYAERERAS---EDANRLRREAQEE 845
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1624-2433 |
5.90e-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: 92.44 E-value: 5.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1624 EEAEQELEIWRQKANEalrLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQI 1703
Cdd:TIGR02169 180 EEVEENIERLDLIIDE---KRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1704 AQQKLSAEQECIRLKADFEHAEQQ-RGLLDNELQRLKNEVNSTEKQRKQLEdelnkvRSEMDSLLQMKINAEKASMVNTE 1782
Cdd:TIGR02169 257 TEEISELEKRLEEIEQLLEELNKKiKDLGEEEQLRVKEKIGELEAEIASLE------RSIAEKERELEDAEERLAKLEAE 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1783 KSKQLLESEALKmKQLADEAARMRSVAEEAKKqrqiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMaLKAKEAEN 1862
Cdd:TIGR02169 331 IDKLLAEIEELE-REIEEERKRRDKLTEEYAE----LKEELEDLRAELEEVDKEFAETRDELKDYREKLEK-LKREINEL 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1863 ERLKRQAEEEAYQrklLEDQAAQHKQDI---EEKITQLQTSSDS---ELGRQKNIVEETLKQKKVVEEEIHIIKINFHKA 1936
Cdd:TIGR02169 405 KRELDRLQEELQR---LSEELADLNAAIagiEAKINELEEEKEDkalEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRV 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1937 SKEKADLESELKKLkgiadETQKSKLKAEEE----AEKLKKLAAEEERRRKEAEEKVKR--ITAAEEEAARQCKA----- 2005
Cdd:TIGR02169 482 EKELSKLQRELAEA-----EAQARASEERVRggraVEEVLKASIQGVHGTVAQLGSVGEryATAIEVAAGNRLNNvvved 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2006 ---AQEEVERLK-KKAEDA-----NKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKnkedVLAQEKLRDEFENA 2076
Cdd:TIGR02169 557 davAKEAIELLKrRKAGRAtflplNKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKY----VFGDTLVVEDIEAA 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2077 KKLAQEA-------------------EKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAA 2137
Cdd:TIGR02169 633 RRLMGKYrmvtlegelfeksgamtggSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS 712
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2138 RRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDafkqksqVE 2217
Cdd:TIGR02169 713 DASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALND-------LE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2218 VELARVRIQmeELVKLKLKIEEENRRLMQKDKDSTQKL----LAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESN--L 2291
Cdd:TIGR02169 786 ARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKLnrltLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNgkK 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2292 AEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQ------KSLEAERKRQ 2365
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleeelSEIEDPKGED 943
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2366 LEASAE---AEKLKLRVKELSLA-------QTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIV--VQKLETQRLQSTREA 2433
Cdd:TIGR02169 944 EEIPEEelsLEDVQAELQRVEEEiralepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILerIEEYEKKKREVFMEA 1023
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
142-240 |
8.31e-18 |
|
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: 81.96 E-value: 8.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 142 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 221
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1389908286 222 -VDVPHPDEKSIITYVSSLY 240
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1325-1974 |
9.49e-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: 91.78 E-value: 9.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1325 LMTLTNQYIKFIIDAQRRLEDDEKAS---EKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEAS 1401
Cdd:pfam01576 178 LSKLKNKHEAMISDLEERLKKEEKGRqelEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETA 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1402 KRqdvaadAEKQKQNiqQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTahkaKSEAELQELRD-R 1480
Cdd:pfam01576 258 QK------NNALKKI--RELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSkR 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1481 AAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELkrksdaeKEAAKQKQRALDDLQKYKmQAEEAERRMKQAEEEKIR 1560
Cdd:pfam01576 326 EQEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------TEQLEQAKRNKANLEKAK-QALESENAELQAELRTLQ 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1561 QIRVVEEVAQKSAATQLQTKAMSFSE---QTTKLEESLKKEQG---NVLKLQEEAD-KLKKQQKEANTAREEAE--QEL- 1630
Cdd:pfam01576 398 QAKQDSEHKRKKLEGQLQELQARLSEserQRAELAEKLSKLQSeleSVSSLLNEAEgKNIKLSKDVSSLESQLQdtQELl 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1631 -EIWRQKANEALRLRlQAEEEAQKKSHAQEEAEKQKLEAERdakkrgkaeeaalkQKENAEKELDKQRKFAEQIAQQKLS 1709
Cdd:pfam01576 478 qEETRQKLNLSTRLR-QLEDERNSLQEQLEEEEEAKRNVER--------------QLSTLQAQLSDMKKKLEEDAGTLEA 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1710 AEQECIRLKADFEHAEQQrglldneLQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKasmvNTEKSKQLLE 1789
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQ-------LEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEK----KQKKFDQMLA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1790 SEALKMKQLADEAARMRSVAEEaKKQRQI----AEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERL 1865
Cdd:pfam01576 612 EEKAISARYAEERDRAEAEARE-KETRALslarALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELERSKRAL 690
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1866 KRQAEEEAYQRKLLED--QAAQH-KQDIEEKITQLQTSSDSELGRQKNIVEET----LKQKKVVEEEIHIIKINFHKASK 1938
Cdd:pfam01576 691 EQQVEEMKTQLEELEDelQATEDaKLRLEVNMQALKAQFERDLQARDEQGEEKrrqlVKQVRELEAELEDERKQRAQAVA 770
|
650 660 670
....*....|....*....|....*....|....*.
gi 1389908286 1939 EKADLESELKKLKGIADETQKSKlkaEEEAEKLKKL 1974
Cdd:pfam01576 771 AKKKLELDLKELEAQIDAANKGR---EEAVKQLKKL 803
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
144-242 |
9.79e-18 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 81.47 E-value: 9.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 144 KLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLD-PEDV 222
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1389908286 223 DVPHPDEKSIITYVSSLYDV 242
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
26-123 |
1.59e-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: 80.85 E-value: 1.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 26 KKTFTKWVNKHL-VKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQV-KLVNI 101
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1389908286 102 RNDDI-ADGNPKLTLGLIWTIIL 123
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1266-1953 |
1.99e-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: 90.41 E-value: 1.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1266 DCHKNAKAYIDSVKDyEFQILTYKALQDPIASPLKKPKMEcasddiiQEYVNLRTRYSELMTLTNQYIKFIIDAQRRLED 1345
Cdd:TIGR00618 187 AKKKSLHGKAELLTL-RSQLLTLCTPCMPDTYHERKQVLE-------KELKHLREALQQTQQSHAYLTQKREAQEEQLKK 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1346 DEKASEKLKEEER-----RKMAEIQAELDKQKQMAE--AHAKSVAKAEQEAL----ELKMKMKEEASKRQDVAAdAEKQK 1414
Cdd:TIGR00618 259 QQLLKQLRARIEElraqeAVLEETQERINRARKAAPlaAHIKAVTQIEQQAQrihtELQSKMRSRAKLLMKRAA-HVKQQ 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1415 QNIQQELQHLKSLSDQEIKSKNQQLEDALV----SRRKIEEEIHIIRIQ---------------LEKTTAHKAKSEAELQ 1475
Cdd:TIGR00618 338 SSIEEQRRLLQTLHSQEIHIRDAHEVATSIreisCQQHTLTQHIHTLQQqkttltqklqslckeLDILQREQATIDTRTS 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1476 ELRD---RAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAE---DELKRKSDAEKEAAKQKQRALddLQKYKMQAEEAER 1549
Cdd:TIGR00618 418 AFRDlqgQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKihlQESAQSLKEREQQLQTKEQIH--LQETRKKAVVLAR 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1550 RMKQAEEEKI--RQIRVVEEVAQKSAATQLQTKAMSFSEQT-TKLEESLKKEQGNVLKLQEEADKLKKQQKEAntarEEA 1626
Cdd:TIGR00618 496 LLELQEEPCPlcGSCIHPNPARQDIDNPGPLTRRMQRGEQTyAQLETSEEDVYHQLTSERKQRASLKEQMQEI----QQS 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1627 EQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERdAKKRGKAEEAALKQK----ENAEKELdKQRKFAEQ 1702
Cdd:TIGR00618 572 FSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQH-ALLRKLQPEQDLQDVrlhlQQCSQEL-ALKLTALH 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1703 IAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMV-NT 1781
Cdd:TIGR00618 650 ALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAsSS 729
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1782 EKSKQLLESEAL-----KMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRL--KTEAEMA 1854
Cdd:TIGR00618 730 LGSDLAAREDALnqslkELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLlkTLEAEIG 809
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1855 LKAKEAENERLKRQaeeeayqrKLLEDQAAQHKQDIEEKITQLqtssdSELGRQKNIVEETLKQkkvveeeihiikinFH 1934
Cdd:TIGR00618 810 QEIPSDEDILNLQC--------ETLVQEEEQFLSRLEEKSATL-----GEITHQLLKYEECSKQ--------------LA 862
|
730
....*....|....*....
gi 1389908286 1935 KASKEKADLESELKKLKGI 1953
Cdd:TIGR00618 863 QLTQEQAKIIQLSDKLNGI 881
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
142-241 |
4.50e-17 |
|
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: 79.62 E-value: 4.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 142 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 221
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1389908286 222 VDV--PHPDEKSIITYVSSLYD 241
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
142-245 |
5.79e-17 |
|
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: 79.32 E-value: 5.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 142 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 221
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1389908286 222 VDV--PHPDEKSIITYVSSLYDVMPR 245
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
145-240 |
9.90e-17 |
|
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: 78.94 E-value: 9.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 145 LLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDPED-VD 223
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1389908286 224 VPHPDEKSIITYVSSLY 240
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1098-1973 |
3.26e-16 |
|
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: 86.65 E-value: 3.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1098 ADAEETLKNYEARLRDVSKVPSeQKEVEKHRSQMKSMRSEAEADQVMFDRLQDDLRKATTVHDKMTRIHSERDADLEHYR 1177
Cdd:TIGR02168 209 AEKAERYKELKAELRELELALL-VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQ 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1178 QLVNGLLERWQAVFAQIELRLREldllgrhMNSYRDSYEWLIRWLTEARQRQEKiqavpisdsraLREQLTDEKKLLGEI 1257
Cdd:TIGR02168 288 KELYALANEISRLEQQKQILRER-------LANLERQLEELEAQLEELESKLDE-----------LAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1258 EKNKDKIDDCHKNAKAyidsvkdyefqiltykalqdpiasplKKPKMECASDDIIQEYVNLRTRYSELMTLTNQYIKFII 1337
Cdd:TIGR02168 350 KEELESLEAELEELEA--------------------------ELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1338 DAQRRLEDDEKASEKLKEE--------ERRKMAEIQAELDKQKQMAEAHAKSVAKAEqEALELKMKMKEEASKRQDvaaD 1409
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEieellkklEEAELKELQAELEELEEELEELQEELERLE-EALEELREELEEAEQALD---A 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1410 AEKQKQNIQQELQHLKSLsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTA--HKAKSEA---ELQELRDRAAEA 1484
Cdd:TIGR02168 480 AERELAQLQARLDSLERL--QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyEAAIEAAlggRLQAVVVENLNA 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1485 EKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAkqkQRALDDLQKYKMQAEEAERRMKQaeeekirQIRV 1564
Cdd:TIGR02168 558 AKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGF---LGVAKDLVKFDPKLRKALSYLLG-------GVLV 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1565 VEEVAQksaATQLQtKAMSFSEQTTKLEESLKKEQGNVLklqeeadklkKQQKEANTAREEAEQELEIWRQKANEalrlr 1644
Cdd:TIGR02168 628 VDDLDN---ALELA-KKLRPGYRIVTLDGDLVRPGGVIT----------GGSAKTNSSILERRREIEELEEKIEE----- 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1645 lqAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHA 1724
Cdd:TIGR02168 689 --LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1725 EQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEalkmkqlADEAAR 1804
Cdd:TIGR02168 767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDE-LRAELTLLNEEAANLRERLESLERR-------IAATER 838
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1805 MRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAA 1884
Cdd:TIGR02168 839 RLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1885 QHKQDIEEKITQLQTssdSELGRQKNIveETLKQKKVVEEEIHIIKINFHKASKEKAdlESELKKLKGIADETQKSKLKA 1964
Cdd:TIGR02168 919 ELREKLAQLELRLEG---LEVRIDNLQ--ERLSEEYSLTLEEAEALENKIEDDEEEA--RRRLKRLENKIKELGPVNLAA 991
|
....*....
gi 1389908286 1965 EEEAEKLKK 1973
Cdd:TIGR02168 992 IEEYEELKE 1000
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
142-240 |
3.78e-16 |
|
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: 77.43 E-value: 3.78e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 142 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 221
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1389908286 222 -VDVPHPDEKSIITYVSSLY 240
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2152-2566 |
5.61e-16 |
|
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: 85.89 E-value: 5.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2152 QADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLD--ETDKQKVLLDQELQRVKGEV---------NDAFKQKSQVEVEL 2220
Cdd:TIGR02169 167 EFDRKKEKALEELEEVEENIERLDLIIDEKRQQLErlRREREKAERYQALLKEKREYegyellkekEALERQKEAIERQL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2221 ARVRiqmEELVKLKLKIEEENRRLMQKdkdstQKLLAEEAEKMKSLAEEagrlsveaeetarqrqiaesnlaEQRALAEK 2300
Cdd:TIGR02169 247 ASLE---EELEKLTEEISELEKRLEEI-----EQLLEELNKKIKDLGEE-----------------------EQLRVKEK 295
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2301 ILKekmqaiqeatkLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDK---ETEGFQKSLEAERKRQLEASAEAEKLKl 2377
Cdd:TIGR02169 296 IGE-----------LEAEIASLERSIAEKERELEDAEERLAKLEAEIDKllaEIEELEREIEEERKRRDKLTEEYAELK- 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2378 rvKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQStrEADDLKSAIADleeerkklkkeaeel 2457
Cdd:TIGR02169 364 --EELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQE--ELQRLSEELAD--------------- 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2458 qrkskemANAQQEQIEQQKAELQqsflTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERqrklMEEERKKLQ 2537
Cdd:TIGR02169 425 -------LNAAIAGIEAKINELE----EEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDR----VEKELSKLQ 489
|
410 420
....*....|....*....|....*....
gi 1389908286 2538 AIMDEAVRKQKEAEEEMKNKQREMDVLDK 2566
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKA 518
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
22-121 |
1.11e-15 |
|
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: 75.65 E-value: 1.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 22 DRVQKKTFTKWVNKHLVKAQ-RHVTDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-KHRQV 96
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1389908286 97 KLVNIRNDDIADGNPKLTLGLIWTI 121
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1348-2013 |
1.12e-15 |
|
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: 84.73 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1348 KASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQdvaadaekqkQNIQQELQHLKS- 1426
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ----------LRVKEKIGELEAe 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1427 --LSDQEIKSKNQQLEDALVSRRKieeeihiIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAE 1504
Cdd:TIGR02169 303 iaSLERSIAEKERELEDAEERLAK-------LEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1505 ETQRKKNAEDELK---RKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVaqksaatqLQTKA 1581
Cdd:TIGR02169 376 VDKEFAETRDELKdyrEKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE--------KEDKA 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1582 MSFSEQTTKLE---ESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL------------- 1645
Cdd:TIGR02169 448 LEIKKQEWKLEqlaADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEvlkasiqgvhgtv 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1646 ----QAEEEAQKkshAQEEAEKQKLEA-----ERDAK------KRGKAEEAA---LKQKENAEKELDKQRK--------- 1698
Cdd:TIGR02169 528 aqlgSVGERYAT---AIEVAAGNRLNNvvvedDAVAKeaiellKRRKAGRATflpLNKMRDERRDLSILSEdgvigfavd 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1699 ---FAEQIAqqklSAEQECIRLKADFEHAEQQRGLLDN------------------------------------ELQRLK 1739
Cdd:TIGR02169 605 lveFDPKYE----PAFKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfeksgamtggsraprggilfsrsepaELQRLR 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1740 NEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAK------ 1813
Cdd:TIGR02169 681 ERLEGLKRELSSLQSELRRIENRLDELSQ-ELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIenvkse 759
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1814 ----------KQRQIAEEEAAR---QRSEAEKILKEKLAAIN--EATRLKTEA-----EMALKAKEAENERLKRQAEEEA 1873
Cdd:TIGR02169 760 lkelearieeLEEDLHKLEEALndlEARLSHSRIPEIQAELSklEEEVSRIEArlreiEQKLNRLTLEKEYLEKEIQELQ 839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1874 YQRKLLEDQAAQHKQDIEEKITQLQtSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGI 1953
Cdd:TIGR02169 840 EQRIDLKEQIKSIEKEIENLNGKKE-ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKR 918
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1954 ADETqksKLKAEEEAEKLKKLAAEEERRRKEAEEkvkriTAAEEEAARQCKAAQEEVERL 2013
Cdd:TIGR02169 919 LSEL---KAKLEALEEELSEIEDPKGEDEEIPEE-----ELSLEDVQAELQRVEEEIRAL 970
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1552-2580 |
1.41e-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: 84.46 E-value: 1.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1552 KQAEE--EKIRQIRVVEEVAQKSAA--TQLQTKAMSFSEQTTKLEESLKKEQgnvlKLQEEADKL------KKQQKEANT 1621
Cdd:pfam01576 2 RQEEEmqAKEEELQKVKERQQKAESelKELEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMrarlaaRKQELEEIL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1622 AREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAER-DAKKRGKAEEAALKQKENAEKELDKQRKFA 1700
Cdd:pfam01576 78 HELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKvTTEAKIKKLEEDILLLEDQNSKLSKERKLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1701 EQ-IAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNS---TEKQRKQLEDELNKVRSEMdslLQMKINAEKA 1776
Cdd:pfam01576 158 EErISEFTSNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKGrqeLEKAKRKLEGESTDLQEQI---AELQAQIAEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1777 SMVNTEKSKQLLESEALKMKQLADEAARMRSVAEeakKQRQIAE--EEAARQRSEAEKILKEKLAAINEATRLKTEAEMA 1854
Cdd:pfam01576 235 RAQLAKKEEELQAALARLEEETAQKNNALKKIRE---LEAQISElqEDLESERAARNKAEKQRRDLGEELEALKTELEDT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1855 LKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEkITQLQTSSDSELGRQkniVEETLKQKKVVEEEIHIIKinfh 1934
Cdd:pfam01576 312 LDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQE-MRQKHTQALEELTEQ---LEQAKRNKANLEKAKQALE---- 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1935 kasKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRItaaeeeaarqckaaQEEVERLK 2014
Cdd:pfam01576 384 ---SENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKL--------------QSELESVS 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2015 KKAEDANKQKEKaekeaekqvvLAKEAAQkctaAEQKAQDVLSknkedvLAQEKLRDEFENAKKLAQEAEKAKEkaekea 2094
Cdd:pfam01576 447 SLLNEAEGKNIK----------LSKDVSS----LESQLQDTQE------LLQEETRQKLNLSTRLRQLEDERNS------ 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2095 alLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQV 2174
Cdd:pfam01576 501 --LQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRL 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2175 EKELTVVKLQLDET-------DKQKVLLDQELQRVKGEVNDAFKQKSQVEVElARVRiqmeELVKLKLKIEEENRRLMQK 2247
Cdd:pfam01576 579 QQELDDLLVDLDHQrqlvsnlEKKQKKFDQMLAEEKAISARYAEERDRAEAE-AREK----ETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2248 DKDSTQKLLAEEAEKMKSLAEEAGRlsvEAEETARQRQIAESNLAEQRALAEKiLKEKMQAIQEAtKLKAEAeKLQKQKD 2327
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVGK---NVHELERSKRALEQQVEEMKTQLEE-LEDELQATEDA-KLRLEV-NMQALKA 727
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2328 QAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSL---AQTKAEDEA----KKFKKQA 2400
Cdd:pfam01576 728 QFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAqidAANKGREEAvkqlKKLQAQM 807
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2401 DEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLksaiadleeerkklkkeaeelqRKSKEMANA--QQEQIEQQKAE 2478
Cdd:pfam01576 808 KDLQRELEEARASRDEILAQSKESEKKLKNLEAELL----------------------QLQEDLAASerARRQAQQERDE 865
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2479 LQQ---SFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEE-------ERKKLQAimDEAVRKQK 2548
Cdd:pfam01576 866 LADeiaSGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttelaaERSTSQK--SESARQQL 943
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*
gi 1389908286 2549 EAE-EEMKNKQREMD------------VLDKKRLEQEKQLAEENK 2580
Cdd:pfam01576 944 ERQnKELKAKLQEMEgtvkskfkssiaALEAKIAQLEEQLEQESR 988
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
140-237 |
1.53e-15 |
|
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: 75.11 E-value: 1.53e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGVTKLLD 218
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpDWETWDPNDALENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1389908286 219 PEDVDVPHPDEKSIITYVS 237
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
140-240 |
2.27e-15 |
|
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: 75.11 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 219
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1389908286 220 ED-VDVPHPDEKSIITYVSSLY 240
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1482-2178 |
2.48e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 83.86 E-value: 2.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1482 AEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAA------KQKQRALDDLQKYKMQAEEAERRMKQAE 1555
Cdd:TIGR00618 194 GKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQqshaylTQKREAQEEQLKKQQLLKQLRARIEELR 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1556 ---------EEKIRQIRVVEEVAQKSAAT-----QLQTKAMSFSEQTTKLEESLKKEQGNV---LKLQEEADKLKKQQKE 1618
Cdd:TIGR00618 274 aqeavleetQERINRARKAAPLAAHIKAVtqieqQAQRIHTELQSKMRSRAKLLMKRAAHVkqqSSIEEQRRLLQTLHSQ 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1619 ANTAREEAEQELeIWRQKANEALRLRLQAEEEAQKKSHA------------QEEAEKQKLEAERDAKKRGKAEEAALKQK 1686
Cdd:TIGR00618 354 EIHIRDAHEVAT-SIREISCQQHTLTQHIHTLQQQKTTLtqklqslckeldILQREQATIDTRTSAFRDLQGQLAHAKKQ 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1687 ENAEKE-LDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKnEVNSTEKQRKQLEDELNKVRSEMDS 1765
Cdd:TIGR00618 433 QELQQRyAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQET-RKKAVVLARLLELQEEPCPLCGSCI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1766 LLQMKINAEKASMVNTEKSKQLLEsealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAT 1845
Cdd:TIGR00618 512 HPNPARQDIDNPGPLTRRMQRGEQ----TYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIP 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1846 RLKTEAEMALKAKEAENERLKRQAEEEayQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQkkvvEEE 1925
Cdd:TIGR00618 588 NLQNITVRLQDLTEKLSEAEDMLACEQ--HALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQE----RVR 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1926 IHIIKINFHKASK------EKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEA 1999
Cdd:TIGR00618 662 EHALSIRVLPKELlasrqlALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL 741
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2000 ARQCKAAQEEverlkkkaedankqkekaekeaekqvvlAKEAAQKCTAAEQkaqdvlsKNKEDVLAQEKLRDEFENakkL 2079
Cdd:TIGR00618 742 NQSLKELMHQ----------------------------ARTVLKARTEAHF-------NNNEEVTAALQTGAELSH---L 783
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2080 AQEAEKAKEKAEKEAALLRQKaeEAEKQKKAAENEAAKQakAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSK 2159
Cdd:TIGR00618 784 AAEIQFFNRLREEDTHLLKTL--EAEIGQEIPSDEDILN--LQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSK 859
|
730
....*....|....*....
gi 1389908286 2160 HKKEAEQALQQKSQVEKEL 2178
Cdd:TIGR00618 860 QLAQLTQEQAKIIQLSDKL 878
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1345-1769 |
2.92e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 83.17 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1345 DDEKASEKLKEEERRKmAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHL 1424
Cdd:PRK02224 308 DAEAVEARREELEDRD-EELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEI 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1425 KSLsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQ------------ 1492
Cdd:PRK02224 387 EEL-EEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvegsp 465
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1493 --DEAERLRKQVAEETQRKKNAEDELKRKsDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVaq 1570
Cdd:PRK02224 466 hvETIEEDRERVEELEAELEDLEEEVEEV-EERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEEL-- 542
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1571 KSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANT------AREEAEQELEIWRQkanealRLR 1644
Cdd:PRK02224 543 RERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERirtllaAIADAEDEIERLRE------KRE 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1645 LQAEEEAQKKSHAQEEAE-KQKLEAERDakkrGKAEEAALKQKENAEKELDKqrkfaeqiaqqklsAEQECIRLKADFEH 1723
Cdd:PRK02224 617 ALAELNDERRERLAEKRErKRELEAEFD----EARIEEAREDKERAEEYLEQ--------------VEEKLDELREERDD 678
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1389908286 1724 AEQQRGLLDNELQRLknevNSTEKQRKQLE---DELNKVRSEMDSLLQM 1769
Cdd:PRK02224 679 LQAEIGAVENELEEL----EELRERREALEnrvEALEALYDEAEELESM 723
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1416-1744 |
3.18e-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: 82.86 E-value: 3.18e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1416 NIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQElrdRAAEAEKLRKAAQD-E 1494
Cdd:pfam17380 285 SERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAME---RERELERIRQEERKrE 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1495 AERLRKQ-VAEETQRKKnaedELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkIRQIRVVEEVAQKSA 1573
Cdd:pfam17380 362 LERIRQEeIAMEISRMR----ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVE-MEQIRAEQEEARQRE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1574 ATQLQTKAMSFSEQTtKLEESLKKEQGNVLKLQEEADKLKKQQKEantaREEAEqeleiwRQKANEALRLRLQAEEEAQK 1653
Cdd:pfam17380 437 VRRLEEERAREMERV-RLEEQERQQQVERLRQQEEERKRKKLELE----KEKRD------RKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1654 KSHAQEEAEKQKLEAERDAK--------KRGKAEEAALKQKENAEKeldkqrkfaEQIAQQKLSAEQECIRLKADFEHAE 1725
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERqkaiyeeeRRREAEEERRKQQEMEER---------RRIQEQMRKATEERSRLEAMERERE 576
|
330
....*....|....*....
gi 1389908286 1726 QQRGLLDNELQRLKNEVNS 1744
Cdd:pfam17380 577 MMRQIVESEKARAEYEATT 595
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1522-2541 |
3.19e-15 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 83.56 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1522 AEKEAAKQKQRALDDLQKYkMQAEEAERRMKQAEEEKIRqirvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGN 1601
Cdd:TIGR00606 166 SEGKALKQKFDEIFSATRY-IKALETLRQVRQTQGQKVQ-----EHQMELKYLKQYKEKACEIRDQITSKEAQLESSREI 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1602 VLKLQEEADKLKKQQKEANTARE---EAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEaEKQKLEAERDAKKRGKA 1678
Cdd:TIGR00606 240 VKSYENELDPLKNRLKEIEHNLSkimKLDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDE-QLNDLYHNHQRTVREKE 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1679 EEAALKQKE----NAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEV-------NSTEK 1747
Cdd:TIGR00606 319 RELVDCQREleklNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPfserqikNFHTL 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1748 QRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKK----QRQIAEEEA 1823
Cdd:TIGR00606 399 VIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQ 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1824 ARQRSEAEKILKEKlaaiNEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQhkqdiEEKITQLQTSSDS 1903
Cdd:TIGR00606 479 ELRKAERELSKAEK----NSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ-----MEMLTKDKMDKDE 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1904 ELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKlaaeeerrrk 1983
Cdd:TIGR00606 550 QIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEE---------- 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1984 eaeekvkRITAAEEEAARQCKAAQEEV--ERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTA----------AEQK 2051
Cdd:TIGR00606 620 -------QLSSYEDKLFDVCGSQDEESdlERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAE 692
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2052 AQDVLSK-NKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRK 2130
Cdd:TIGR00606 693 LQEFISDlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQET 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2131 EAEEEAARRAaaeaaaLKQKQQADAEMskhkkeAEQALQQKSQVEKELTVVKLQLDETDkqkvlLDQELQRVKGEVNDaf 2210
Cdd:TIGR00606 773 LLGTIMPEEE------SAKVCLTDVTI------MERFQMELKDVERKIAQQAAKLQGSD-----LDRTVQQVNQEKQE-- 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2211 kqksqvevelarvriQMEELVKLKLKIEEeNRRLMQKDKDSTQKLlaeeaekmKSLAEEAGRLSVEAEETARQRQIAESN 2290
Cdd:TIGR00606 834 ---------------KQHELDTVVSKIEL-NRKLIQDQQEQIQHL--------KSKTNELKSEKLQIGTNLQRRQQFEEQ 889
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2291 LAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQ---AQETAKRLQEDKQQIQQRLDKETEGFQKSLEaerkrqle 2367
Cdd:TIGR00606 890 LVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEElisSKETSNKKAQDKVNDIKEKVKNIHGYMKDIE-------- 961
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2368 asaeaeklklrvkelSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEI------VVQKLETQRLQSTREADDLKSAIA 2441
Cdd:TIGR00606 962 ---------------NKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKInedmrlMRQDIDTQKIQERWLQDNLTLRKR 1026
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2442 DLEEERKKLKKEAEELQrkSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLedemkKAKALKDE 2521
Cdd:TIGR00606 1027 ENELKEVEEELKQHLKE--MGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL-----REPQFRDA 1099
|
1050 1060
....*....|....*....|
gi 1389908286 2522 QERQRKLMEEERKKLQAIMD 2541
Cdd:TIGR00606 1100 EEKYREMMIVMRTTELVNKD 1119
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1780-2544 |
3.19e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 83.48 E-value: 3.19e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1780 NTEKSKQLLEsEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKE 1859
Cdd:TIGR00618 161 KSKEKKELLM-NLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1860 AENERLkRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLqtssdSELGRQKNIVEETLKQKKVVEEEIHIIKINFhKASKE 1939
Cdd:TIGR00618 240 QSHAYL-TQKREAQEEQLKKQQLLKQLRARIEELRAQE-----AVLEETQERINRARKAAPLAAHIKAVTQIEQ-QAQRI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1940 KADLESELKKLKGIADETQKSkLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQckaaQEEVERLKKKAED 2019
Cdd:TIGR00618 313 HTELQSKMRSRAKLLMKRAAH-VKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQ----HTLTQHIHTLQQQ 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2020 ANKQKEKAEKEAEKQVVLAKEAAQkcTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQ 2099
Cdd:TIGR00618 388 KTTLTQKLQSLCKELDILQREQAT--IDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESA 465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2100 KAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELT 2179
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEE 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2180 VVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVEL-------ARVRIQMEELVKLKLKIEEENRRLMQK--DKD 2250
Cdd:TIGR00618 546 DVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIpnlqnitVRLQDLTEKLSEAEDMLACEQHALLRKlqPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2251 STQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQ--------IAESNLAEQRALAEKILKEKMQAI--------QEATK 2314
Cdd:TIGR00618 626 DLQDVRLHLQQCSQELALKLTALHALQLTLTQERVrehalsirVLPKELLASRQLALQKMQSEKEQLtywkemlaQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2315 LKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgFQKSLEAERKRQLEASAEAEK---LKLRVKELSLAQ-TKAE 2390
Cdd:TIGR00618 706 LRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFnnnEEVTAALQTGAElSHLA 784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2391 DEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSaiADLEEERKKLKKEAEELQRKSKEMANAQQE 2470
Cdd:TIGR00618 785 AEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQ--FLSRLEEKSATLGEITHQLLKYEECSKQLA 862
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2471 QIEQQKAELQQsflTEKGLLLKREKEVEGEKKRFEKQLEDEM-KKAKALKDEQERQ---RKLMEEERKKLQAIMDEAV 2544
Cdd:TIGR00618 863 QLTQEQAKIIQ---LSDKLNGINQIKIQFDGDALIKFLHEITlYANVRLANQSEGRfhgRYADSHVNARKYQGLALLV 937
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1524-2018 |
3.89e-15 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 82.80 E-value: 3.89e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1524 KEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQK--------SAATQLQTKAMSFSEQTTKLEESL 1595
Cdd:PRK03918 168 GEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSElpelreelEKLEKEVKELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1596 KKEQGNVLKLQEEADKLKKQQKEANTAREEAEQ---ELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDA 1672
Cdd:PRK03918 248 ESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1673 KKRGKAEEAALKQKENAEKELDKQRKFAEqiAQQKLSAEQECIRLKADFEHAEQQRGllDNELQRLKNEVNSTEKQRKQL 1752
Cdd:PRK03918 328 ERIKELEEKEERLEELKKKLKELEKRLEE--LEERHELYEEAKAKKEELERLKKRLT--GLTPEKLEKELEELEKAKEEI 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1753 EDELNKVRSEMDSLLQMKINAEKASM---------------VNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQ 1817
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEelkkakgkcpvcgreLTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1818 ------IAEEEAARQRSEAEKI--LKEKLAAINeATRLKTEAEMALKAKE------AENERLKRQAEE-EAYQRKLLE-- 1880
Cdd:PRK03918 484 elekvlKKESELIKLKELAEQLkeLEEKLKKYN-LEELEKKAEEYEKLKEkliklkGEIKSLKKELEKlEELKKKLAEle 562
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1881 ---DQAAQHKQDIEEKITQLQTSS----DSELGRQKNIVEETLKQKKVV------EEEIHIIKINFHKASKEKADLESEL 1947
Cdd:PRK03918 563 kklDELEEELAELLKELEELGFESveelEERLKELEPFYNEYLELKDAEkelereEKELKKLEEELDKAFEELAETEKRL 642
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 1948 KKLKGIADETQKSklKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAE 2018
Cdd:PRK03918 643 EELRKELEELEKK--YSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4033-4071 |
4.69e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 4.69e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 4033 LLEAQIATGGIIDPQESHRLPVETAYERGLFDEEMNEIL 4071
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
140-240 |
5.99e-15 |
|
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: 73.91 E-value: 5.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAErELGVTKLLDP 219
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1389908286 220 ED-VDVPHPDEKSIITYVSSLY 240
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
25-125 |
7.68e-15 |
|
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: 73.10 E-value: 7.68e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 25 QKKTFTKWVNKHLVK--AQRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKHRQV 96
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1389908286 97 KLVNIRNDDIADGNPKLTLGLIWTIILHF 125
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1338-1916 |
8.00e-15 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 82.01 E-value: 8.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1338 DAQRRLEDDEKASEKLKEEE--------RRKMAEIQAELDK---QKQMAEA---HAKSVAKAEQEALELKMKMKEEASKR 1403
Cdd:PRK02224 184 DQRGSLDQLKAQIEEKEEKDlherlnglESELAELDEEIERyeeQREQAREtrdEADEVLEEHEERREELETLEAEIEDL 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1404 QDVAADAEKQKQNIQQELQHLKslsdqeiksknQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAE 1483
Cdd:PRK02224 264 RETIAETEREREELAEEVRDLR-----------ERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEE 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1484 AEKLRKAAQDEAERLRKQVA---EETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKykmQAEEAERRMKQAEEEKIR 1560
Cdd:PRK02224 333 CRVAAQAHNEEAESLREDADdleERAEELREEAAELESELEEAREAVEDRREEIEELEE---EIEELRERFGDAPVDLGN 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1561 QIRVVEEVAQKSAATQlqtkamsfsEQTTKLEESLKKEQGNVlklqEEADKLKKQQK--EANTAREEAE--QELEIWRQK 1636
Cdd:PRK02224 410 AEDFLEELREERDELR---------EREAELEATLRTARERV----EEAEALLEAGKcpECGQPVEGSPhvETIEEDRER 476
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1637 ANEALRLRLQAEEEaqkkshaqEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIR 1716
Cdd:PRK02224 477 VEELEAELEDLEEE--------VEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAE 548
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1717 LKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNtEKSKQLLESEALKMK 1796
Cdd:PRK02224 549 LEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLR-EKREALAELNDERRE 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1797 QLADEAARMRSVAEEAKKQRQiaeEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEeayqR 1876
Cdd:PRK02224 628 RLAEKRERKRELEAEFDEARI---EEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRER----R 700
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1389908286 1877 KLLEDQaAQHKQDIEEKITQLQTSS---DSELgRQKNIveETL 1916
Cdd:PRK02224 701 EALENR-VEALEALYDEAEELESMYgdlRAEL-RQRNV--ETL 739
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1380-2208 |
1.74e-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: 80.54 E-value: 1.74e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1380 KSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKS--KNQQLEDALVSRRkieeEIHIIR 1457
Cdd:pfam05483 9 KSFNKCTEDDFEFPFAKSNLSKNGENIDSDPAFQKLNFLPMLEQVANSGDCHYQEglKDSDFENSEGLSR----LYSKLY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1458 IQLEKTTAHKAKSEAELQELRDRAAEAEKL----RKAAQD---EAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQK 1530
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIieaqRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1531 QRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEE--VAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVlklQEE 1608
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEElrVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDK---EKQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1609 ADKLKKQQKEANTAREEAEQELEIWRQKANE-ALRLRLQAE---EEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALK 1684
Cdd:pfam05483 242 VSLLLIQITEKENKMKDLTFLLEESRDKANQlEEKTKLQDEnlkELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1685 QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQqrgLLDNELQRLKNevnsTEKQRKQLEDELNKVRSEMD 1764
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE---LLRTEQQRLEK----NEDQLKIITMELQKKSSELE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1765 SLLQMKINAEkasmVNTEKSKQLLESEalkmKQLADEAARMRSVAEEAK-KQRQIAEEEAARQRSEAEKILKEKLAAINE 1843
Cdd:pfam05483 395 EMTKFKNNKE----VELEELKKILAED----EKLLDEKKQFEKIAEELKgKEQELIFLLQAREKEIHDLEIQLTAIKTSE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1844 ATRLKTEAEMAlkaKEAENERLKRQAEEEAYQRKLLEDQaaqhkqdieeKITQLQTSSDSELGRQKNIVEETLKQKKVVE 1923
Cdd:pfam05483 467 EHYLKEVEDLK---TELEKEKLKNIELTAHCDKLLLENK----------ELTQEASDMTLELKKHQEDIINCKKQEERML 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1924 EEIHIIKinfHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQC 2003
Cdd:pfam05483 534 KQIENLE---EKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNI 610
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2004 KAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKedvLAQEKLRDEFENAKKLAQEA 2083
Cdd:pfam05483 611 EELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKK---ISEEKLLEEVEKAKAIADEA 687
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2084 EKAkekaekeaallrQKAEEAEKQKKAAENEA-AKQAKAQNDtekqrkeaeeeaarraaaeaaalKQKQQADAEMSKHKK 2162
Cdd:pfam05483 688 VKL------------QKEIDKRCQHKIAEMVAlMEKHKHQYD-----------------------KIIEERDSELGLYKN 732
|
810 820 830 840
....*....|....*....|....*....|....*....|....*.
gi 1389908286 2163 EAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVND 2208
Cdd:pfam05483 733 KEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2320-2610 |
1.78e-14 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 80.75 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2320 EKLQKQKDQAQEtAKRLQEDKQQIQQRL--------DKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAED 2391
Cdd:COG1196 203 EPLERQAEKAER-YRELKEELKELEAELlllklrelEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELEL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2392 EAKKFKKQADEVKAQLQRTEKhttEIVVQKLETQRLQSTREADDLKsaiADLEEERKKLKKEAEELQRKSKEMANAQQEQ 2471
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQ---DIARLEERRRELEERLEELEEE---LAELEEELEELEEELEELEEELEEAEEELEE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2472 IEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAE 2551
Cdd:COG1196 356 AEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE 435
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2552 EEMKNKQREMDVLDKK-RLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL 2610
Cdd:COG1196 436 EEEEEEEALEEAAEEEaELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLL 495
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
142-237 |
1.90e-14 |
|
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: 72.03 E-value: 1.90e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 142 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGVTKLLDPE 220
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1389908286 221 DVDVPHPDEKSIITYVS 237
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
609-799 |
2.08e-14 |
|
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: 75.17 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 609 QLHAFVVAATKELMWLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAVQTTGDKLLRDGHPARKTIEAF 688
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 689 TAALQTQWSWLLQLCCCIETHLKENTAHFQFFTDVKEAEEKLKKMQDTMKRKYTCDrsiTVTRLEDLLQDAADEKEQLAE 768
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1389908286 769 FKTNLEALKRRAKTVIQLKPRNPTTPLKGKM 799
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1474-1974 |
2.82e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.08 E-value: 2.82e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1474 LQELRDRAAEA----EKLRKAAQDEAERLRKQVAEetqrkKNAEDELKRKSDAEKEAAKQKqralDDLQKYKMQAEEAER 1549
Cdd:PRK02224 164 LEEYRERASDArlgvERVLSDQRGSLDQLKAQIEE-----KEEKDLHERLNGLESELAELD----EEIERYEEQREQARE 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1550 RMKQAE------EEKIRQIRVVEEVAQKSAAtqlqTKAMSFSEQTTkLEESLKKEQGNVLKLQEE--------------A 1609
Cdd:PRK02224 235 TRDEADevleehEERREELETLEAEIEDLRE----TIAETEREREE-LAEEVRDLRERLEELEEErddllaeaglddadA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1610 DKLKKQQKEANTAREEAEQELEIWRQKA----NEALRLR---LQAEEEAQKKSHAQEEAEKQKLEAERDAKKRG------ 1676
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAqahnEEAESLRedaDDLEERAEELREEAAELESELEEAREAVEDRReeieel 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1677 -KAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAE------------------------------ 1725
Cdd:PRK02224 390 eEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARerveeaealleagkcpecgqpvegsphvet 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1726 -----QQRGLLDNELQRLKNEVNSTEKQRKQLEDeLNKVRSEMDSLLQMKINAEKAsmvnTEKSKQLLESEALKMKQLAD 1800
Cdd:PRK02224 470 ieedrERVEELEAELEDLEEEVEEVEERLERAED-LVEAEDRIERLEERREDLEEL----IAERRETIEEKRERAEELRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1801 EAARMRSVAEEAKKQRQIAEEEAARQRSEAeKILKEKLAAINEA-TRLKTEAEMALKAKEAENERLKRQAEEEAYQRKll 1879
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEV-AELNSKLAELKERiESLERIRTLLAAIADAEDEIERLREKREALAEL-- 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1880 EDQAAQHKQDIEEKITQLQTSSDSELgrqkniVEETLKQKKVVEEEIhiikinfhkaskekADLESELKKLKGIADETQK 1959
Cdd:PRK02224 622 NDERRERLAEKRERKRELEAEFDEAR------IEEAREDKERAEEYL--------------EQVEEKLDELREERDDLQA 681
|
570
....*....|....*
gi 1389908286 1960 SKLKAEEEAEKLKKL 1974
Cdd:PRK02224 682 EIGAVENELEELEEL 696
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3050-3088 |
2.97e-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: 2.97e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 3050 FLEAQAATGFVIDPIKNERVPVDEAVKSGLVGPEIHERL 3088
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1605-2428 |
1.08e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 78.24 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1605 LQEEADKLKKQQKEANTAREEAEQELEIWRQKANEaLRLRLQaeeEAQKKSHAQEEAEKQKLEAERDAKKRGKAE----E 1680
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVID-LQTKLQ---EMQMERDAMADIRRRESQSQEDLRNQLQNTvhelE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1681 AALKQKENAEKELDKQrkfAEQIAQQKLSAE---QECIRLKADFEHAEQQR----------------GLLDNELQRLKNE 1741
Cdd:pfam15921 156 AAKCLKEDMLEDSNTQ---IEQLRKMMLSHEgvlQEIRSILVDFEEASGKKiyehdsmstmhfrslgSAISKILRELDTE 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1742 VNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKasmvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEE 1821
Cdd:pfam15921 233 ISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQ------DRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1822 EAARQRSEAEKILKEKLAAINEatrLKTEAEMALKAKEAENERLKRQ---AEEEAYQRKLLEDQAAQHKQDIEEKITQLQ 1898
Cdd:pfam15921 307 QARNQNSMYMRQLSDLESTVSQ---LRSELREAKRMYEDKIEELEKQlvlANSELTEARTERDQFSQESGNLDDQLQKLL 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1899 TSSDSelgRQKNIVEETLKQKKVVEEEIHiIKINFHKASKEKADLESELKKLKGIAdETQKSKLKAEEEAEklkklaAEE 1978
Cdd:pfam15921 384 ADLHK---REKELSLEKEQNKRLWDRDTG-NSITIDHLRRELDDRNMEVQRLEALL-KAMKSECQGQMERQ------MAA 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1979 ERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANkqkekaekeaekqvvlaKEAAQKCTAAEQKAQDVLSK 2058
Cdd:pfam15921 453 IQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSE-----------------RTVSDLTASLQEKERAIEAT 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2059 NKEDVlaqeKLRDEFEnakklaqeaekakekaEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDtekqrkeaeeeaar 2138
Cdd:pfam15921 516 NAEIT----KLRSRVD----------------LKLQELQHLKNEGDHLRNVQTECEALKLQMAEKD-------------- 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2139 raaAEAAALKQKQQADAEM-SKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDafkqksqVE 2217
Cdd:pfam15921 562 ---KVIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD-------LE 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2218 VELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKL--LAEEAEKMK-SLAEEAGRLSVEAEETARQRQIAESNLAEQ 2294
Cdd:pfam15921 632 LEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKrNFRNKSEEMETTTNKLKMQLKSAQSELEQT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2295 RALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE---DKQQIQQRLDKETEGFQKSLEAERKRQLEASAE 2371
Cdd:pfam15921 712 RNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEamtNANKEKHFLKEEKNKLSQELSTVATEKNKMAGE 791
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2372 AEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQ-KLETQRLQ 2428
Cdd:pfam15921 792 LEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQhTLDVKELQ 849
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1684-2550 |
1.40e-13 |
|
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: 77.80 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1684 KQKENAEKELDKQRKFAE----QIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKV 1759
Cdd:TIGR02169 205 REREKAERYQALLKEKREyegyELLKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1760 RSEMDSLLQMKINAEKASMVNTEKSKQLLESEAlkmkqladeaarmrsvaEEAKKQRQIAEEEAARQRSEAEKILKEkla 1839
Cdd:TIGR02169 285 GEEEQLRVKEKIGELEAEIASLERSIAEKEREL-----------------EDAEERLAKLEAEIDKLLAEIEELERE--- 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1840 aINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdsELGRQKNIVEETLKQK 1919
Cdd:TIGR02169 345 -IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREIN-----ELKRELDRLQEELQRL 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1920 kvvEEEIHIIKINFHKASKEKADLESELKKLkgiADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEA 1999
Cdd:TIGR02169 419 ---SEELADLNAAIAGIEAKINELEEEKEDK---ALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQREL 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2000 AR---QCKAAQEEVeRLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKC--TAAEQKAQDVLSKNkeDVLAQEKLrdEFE 2074
Cdd:TIGR02169 493 AEaeaQARASEERV-RGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAieVAAGNRLNNVVVED--DAVAKEAI--ELL 567
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2075 NAKKLAQEAEKAKEKAEKEAALLRQKAE-----------EAEKQKKAA-----------EN-EAAKQAKAQN-----DTE 2126
Cdd:TIGR02169 568 KRRKAGRATFLPLNKMRDERRDLSILSEdgvigfavdlvEFDPKYEPAfkyvfgdtlvvEDiEAARRLMGKYrmvtlEGE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2127 KQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAeqalqqksqVEKELTVVKLQLDETDKQKVLLDQELQRVKGEV 2206
Cdd:TIGR02169 648 LFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEG---------LKRELSSLQSELRRIENRLDELSQELSDASRKI 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2207 NDAFKQKSQVEVELARVRIQMEELVKLKLKIEEEnrrlMQKDKDSTQKLLAEEAEKMKSLAEeagrlsVEAEETARQRQI 2286
Cdd:TIGR02169 719 GEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQE----IENVKSELKELEARIEELEEDLHK------LEEALNDLEARL 788
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2287 AESNLAEQRALAEKILKEkmqaIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQL 2366
Cdd:TIGR02169 789 SHSRIPEIQAELSKLEEE----VSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2367 EASAEAEKLKLRVKELslaqtkaEDEAKKFKKQADEVKAQLQRTEKHtteivVQKLETQRLQSTREADDLKSAIADLEEE 2446
Cdd:TIGR02169 865 ELEEELEELEAALRDL-------ESRLGDLKKERDELEAQLRELERK-----IEELEAQIEKKRKRLSELKAKLEALEEE 932
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2447 RKKLKKEAEELQRKSKEMANAqqEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFekqledemkkakalkDEQERQR 2526
Cdd:TIGR02169 933 LSEIEDPKGEDEEIPEEELSL--EDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL---------------DELKEKR 995
|
890 900
....*....|....*....|....
gi 1389908286 2527 KLMEEERKKLQAIMDEAVRKQKEA 2550
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKKKREV 1019
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1760-2601 |
1.68e-13 |
|
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: 77.80 E-value: 1.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1760 RSEMDSLL-QMKINAEKASMVNTEKSKQLLESEALKMKQLADEAArmrSVAE-EAKKQRQIAEEEAARQRSE-AEKILKE 1836
Cdd:TIGR02169 119 LSEIHDFLaAAGIYPEGYNVVLQGDVTDFISMSPVERRKIIDEIA---GVAEfDRKKEKALEELEEVEENIErLDLIIDE 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1837 KlaaINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQ---HKQDIEEKITQLqTSSDSELGRQKNIVE 1913
Cdd:TIGR02169 196 K---RQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAierQLASLEEELEKL-TEEISELEKRLEEIE 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1914 ETLKQ-----KKVVEEEIHIIKinfhkasKEKADLESELKKLKGIADEtqkSKLKAEEEAEKLKKLAAEEERRRKEAEEK 1988
Cdd:TIGR02169 272 QLLEElnkkiKDLGEEEQLRVK-------EKIGELEAEIASLERSIAE---KERELEDAEERLAKLEAEIDKLLAEIEEL 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1989 VKRItaaeEEAARQCKAAQEEVERLKKKAEDAnkqkekaekeaekqvvlakeaaqkctaaEQKAQDVLSKNKEDVLAQEK 2068
Cdd:TIGR02169 342 EREI----EEERKRRDKLTEEYAELKEELEDL----------------------------RAELEEVDKEFAETRDELKD 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2069 LRDEFEnakKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAArraaaeaaalk 2148
Cdd:TIGR02169 390 YREKLE---KLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEW----------- 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2149 QKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQElQRVKGEVNDAFKQKSQVEVELARVRIQME 2228
Cdd:TIGR02169 456 KLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER-VRGGRAVEEVLKASIQGVHGTVAQLGSVG 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2229 ELVKLKLKIEEENRR---LMQKDKDSTQ--KLLAEEA---------EKMKSLAEEAGRLS-----------VEAEETAR- 2282
Cdd:TIGR02169 535 ERYATAIEVAAGNRLnnvVVEDDAVAKEaiELLKRRKagratflplNKMRDERRDLSILSedgvigfavdlVEFDPKYEp 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2283 ------QRQIAESNLAEQRALAEKI--------LKEKMQAIQE-ATKLKAEAEKLQKQKDQAQETAKRLQEdkqqiqqrL 2347
Cdd:TIGR02169 615 afkyvfGDTLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGgSRAPRGGILFSRSEPAELQRLRERLEG--------L 686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2348 DKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEkhtteivvQKLETQRl 2427
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLE--------QEIENVK- 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2428 qstREADDLKSAIADLeeerkklkkeaeelqrksKEMANAQQEQIEQQKAELQQSFLTEKGLLLK-------------RE 2494
Cdd:TIGR02169 758 ---SELKELEARIEEL------------------EEDLHKLEEALNDLEARLSHSRIPEIQAELSkleeevsriearlRE 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2495 KEVEGEKKRFEKQ-LEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEK 2573
Cdd:TIGR02169 817 IEQKLNRLTLEKEyLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896
|
890 900
....*....|....*....|....*...
gi 1389908286 2574 QLAEENKKLREQLQTFEISSKTVSQTKE 2601
Cdd:TIGR02169 897 QLRELERKIEELEAQIEKKRKRLSELKA 924
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
43-122 |
1.76e-13 |
|
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: 69.54 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 43 HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKHRQV----KLVNIRNDDIADGNPKLT 114
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1389908286 115 LGLIWTII 122
Cdd:cd21223 105 LALLWRII 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3714-3752 |
2.17e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.97 E-value: 2.17e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 3714 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPELHDKL 3752
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
27-128 |
2.73e-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: 69.19 E-value: 2.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 27 KTFTKWVNKHLVKAqrHVTDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLV 99
Cdd:cd21298 9 KTYRNWMNSLGVNP--FVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1389908286 100 NIRNDDIADGNPKLTLGLIWTIILHFQIS 128
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
19-124 |
2.93e-13 |
|
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: 68.85 E-value: 2.93e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 19 DERDrvqKKTFTKWVNKHLVKAQRHvtDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALDF 90
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPLIN--NLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVDL 73
|
90 100 110
....*....|....*....|....*....|....
gi 1389908286 91 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 124
Cdd:cd21219 74 AKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1313-1897 |
3.08e-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: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1313 QEYVNLRTRYSELMTLtnqyikfiiDAQRRLEDDEKASEKLKEEERRkmaeIQAELDKQKQMAEAHAKSVAKAEQEALEL 1392
Cdd:COG4913 262 ERYAAARERLAELEYL---------RAALRLWFAQRRLELLEAELEE----LRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1393 kmkmkeeaskRQDVAADAEKQKQNIQQELQHLKSLSDqEIKSKNQQLEDALVS-RRKIEEEIHIIRIQLEKTTAHKAKSE 1471
Cdd:COG4913 329 ----------EAQIRGNGGDRLEQLEREIERLERELE-ERERRRARLEALLAAlGLPLPASAEEFAALRAEAAALLEALE 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1472 AELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALD---DLqkykMQAEEAE 1548
Cdd:COG4913 398 EELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLDEAELPfvgEL----IEVRPEE 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1549 RRMKQAEEEKIRQIR---VVEEVAQKSAA-----TQLQTKAmsfseQTTKLEESLKKEQGNVLKLQEEADKLkkqQKEAN 1620
Cdd:COG4913 474 ERWRGAIERVLGGFAltlLVPPEHYAAALrwvnrLHLRGRL-----VYERVRTGLPDPERPRLDPDSLAGKL---DFKPH 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1621 TAREEAEQEL-----------------------------------EIWRQKA----------NEALRLRLQAEEEAQKKS 1655
Cdd:COG4913 546 PFRAWLEAELgrrfdyvcvdspeelrrhpraitragqvkgngtrhEKDDRRRirsryvlgfdNRAKLAALEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1656 HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlKADFEHAEQQRGLLDNEL 1735
Cdd:COG4913 626 LAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDAS----SDDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1736 QRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEkasmvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQ 1815
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAE-------DLARLELRALLEERFAAALGDAVERELRENLEER 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1816 RQIAEEEAARQRSEAEKILKE--------------KLAAINEA----TRLKTEaemALKAKEAE-NERLKRQAEEEayqR 1876
Cdd:COG4913 775 IDALRARLNRAEEELERAMRAfnrewpaetadldaDLESLPEYlallDRLEED---GLPEYEERfKELLNENSIEF---V 848
|
650 660
....*....|....*....|.
gi 1389908286 1877 KLLEDQAAQHKQDIEEKITQL 1897
Cdd:COG4913 849 ADLLSKLRRAIREIKERIDPL 869
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1331-2021 |
4.27e-13 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 76.31 E-value: 4.27e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1331 QYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKE-----EASK--R 1403
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNtvhelEAAKclK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1404 QDVAADAEKQKQNIQQ-ELQHLKSLsdQEIKSKNQQLEDAlvSRRKIEEEIHIIRIQLEKTTAHKAKS----EAELQELR 1478
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmMLSHEGVL--QEIRSILVDFEEA--SGKKIYEHDSMSTMHFRSLGSAISKIlrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1479 DR----AAEAEKLRKAAQDEAERLRKQ------------------VAEETQRKKNAEDELKRKSDAEKEAAKQKQ----R 1532
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQhqdrieqliseheveitgLTEKASSARSQANSIQSQLEIIQEQARNQNsmymR 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1533 ALDDLQKYKMQAEEAERRMKQAEEEKIRQIRvVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKL 1612
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELE-KQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1613 KKQQKEA------------NTAREEAEQELEIWRQkanEALRLRLqaeeeaqkKSHAQEEAEKQKleaerdAKKRGKAEE 1680
Cdd:pfam15921 397 KEQNKRLwdrdtgnsitidHLRRELDDRNMEVQRL---EALLKAM--------KSECQGQMERQM------AAIQGKNES 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1681 AALKQKENAEKELDKQ--RKFAEQIAQQKL---SAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDE 1755
Cdd:pfam15921 460 LEKVSSLTAQLESTKEmlRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1756 LNKVRSemdslLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQrqiAEEEAARQRSEAE--KI 1833
Cdd:pfam15921 540 GDHLRN-----VQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQ---LEKEINDRRLELQefKI 611
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1834 LKEKL-AAINEATRLKTEAEM-ALKAKEAENERLKRQaeeeayqrklledqaaqhkQDIEEKITQLQtssdselgrqkNI 1911
Cdd:pfam15921 612 LKDKKdAKIRELEARVSDLELeKVKLVNAGSERLRAV-------------------KDIKQERDQLL-----------NE 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1912 VEETLKQKKVVEEEIHIIKINFHKASKEkadLESELKKLKGiadETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKR 1991
Cdd:pfam15921 662 VKTSRNELNSLSEDYEVLKRNFRNKSEE---METTTNKLKM---QLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQ 735
|
730 740 750
....*....|....*....|....*....|
gi 1389908286 1992 ITAAEEeaarQCKAAQEEVERLKKKAEDAN 2021
Cdd:pfam15921 736 ITAKRG----QIDALQSKIQFLEEAMTNAN 761
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1876-2591 |
4.59e-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: 76.25 E-value: 4.59e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1876 RKLLEDQA--AQHKQDIEEKITQLQTSSDSeLGRQKNIVEETLKQKKVVEEEIHI-IKINFHKASKEKADLESELKKLKG 1952
Cdd:TIGR02168 158 RAIFEEAAgiSKYKERRKETERKLERTREN-LDRLEDILNELERQLKSLERQAEKaERYKELKAELRELELALLVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1953 IADETQKSKLKAEEEAEKLKKLAAEEERrrkeAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAE 2032
Cdd:TIGR02168 237 LREELEELQEELKEAEEELEELTAELQE----LEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2033 KQVVLAKEAAQKCTAAEQKAQDVL-----SKNKEDVLAQEK--LRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAE 2105
Cdd:TIGR02168 313 NLERQLEELEAQLEELESKLDELAeelaeLEEKLEELKEELesLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2106 KQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQadAEMSKHKKEAEQALQQKSQVEKELTVVKLQL 2185
Cdd:TIGR02168 393 LQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQ--AELEELEEELEELQEELERLEEALEELREEL 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2186 DETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKL---------KLKIEEENRRLMQKD-KDSTQKL 2255
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLsgilgvlseLISVDEGYEAAIEAAlGGRLQAV 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2256 LAEEAEKMKSLAE-----EAGRLSVEAEETARQRQIaESNLAEQRALAEKILKEKMQAIQEATKLK-------------- 2316
Cdd:TIGR02168 551 VVENLNAAKKAIAflkqnELGRVTFLPLDSIKGTEI-QGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvd 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2317 --AEAEKLQKQKD----------------------------QAQETAKRLQEDKQQIQQRLDKETEGfQKSLEAERKRQL 2366
Cdd:TIGR02168 630 dlDNALELAKKLRpgyrivtldgdlvrpggvitggsaktnsSILERRREIEELEEKIEELEEKIAEL-EKALAELRKELE 708
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2367 EASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQklETQRLQSTREADDLKSAIADLEEE 2446
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE--IEELEERLEEAEEELAEAEAEIEE 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2447 RKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKR---EKEVEGEKKRFEKQLEDEMKKAKALKDEQE 2523
Cdd:TIGR02168 787 LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIaatERRLEDLEEQIEELSEDIESLAAEIEELEE 866
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 2524 RQRKLmEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKL---REQLQTFEI 2591
Cdd:TIGR02168 867 LIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLaqlELRLEGLEV 936
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1243-1892 |
5.12e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 75.98 E-value: 5.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1243 LREQLTDEKKLLGEIEKNKDkiddchknakayidsvkdyefqiltykalqdpiasplkkpKMECASDDIIQEYVNLRTRY 1322
Cdd:pfam01576 192 LEERLKKEEKGRQELEKAKR----------------------------------------KLEGESTDLQEQIAELQAQI 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1323 SELMTLTNQYIKFIIDAQRRLEDDEKAseklKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMK---MKEE 1399
Cdd:pfam01576 232 AELRAQLAKKEEELQAALARLEEETAQ----KNNALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGEEleaLKTE 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1400 ASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDAlvsRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELrd 1479
Cdd:pfam01576 308 LEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEM---RQKHTQALEELTEQLEQAKRNKANLEKAKQAL-- 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1480 raaeaEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEeki 1559
Cdd:pfam01576 383 -----ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEG--- 454
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1560 RQIRVVEEVAqkSAATQLQTKAMSFSEQT-TKLEESLKKEQgnvlkLQEEADKLKKQQKEANTAREEAEQELEIWRQ--- 1635
Cdd:pfam01576 455 KNIKLSKDVS--SLESQLQDTQELLQEETrQKLNLSTRLRQ-----LEDERNSLQEQLEEEEEAKRNVERQLSTLQAqls 527
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1636 ---KANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQK-ENAEKELD-----------KQRKFA 1700
Cdd:pfam01576 528 dmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElDDLLVDLDhqrqlvsnlekKQKKFD 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1701 EQIAQQKLSAEQ---ECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLedelnkvRSEMDSLLQMKINAEKaS 1777
Cdd:pfam01576 608 QMLAEEKAISARyaeERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQL-------RAEMEDLVSSKDDVGK-N 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1778 MVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAK---------------KQRQIAEEEAARQRSEAEKILKEKLAAIN 1842
Cdd:pfam01576 680 VHELERSKRALEQQVEEMKTQLEELEDELQATEDAKlrlevnmqalkaqfeRDLQARDEQGEEKRRQLVKQVRELEAELE 759
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1843 EATRLKTEA-------EMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEE 1892
Cdd:pfam01576 760 DERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEE 816
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1331-1627 |
5.49e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 75.55 E-value: 5.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1331 QYIKFIIDAQRRLEDDEKasEKLKE-EERRKMAEI----QAELDKQKQMAEAHAKSVAKAEQEALELKM---KMKEEASK 1402
Cdd:pfam17380 289 QQEKFEKMEQERLRQEKE--EKAREvERRRKLEEAekarQAEMDRQAAIYAEQERMAMERERELERIRQeerKRELERIR 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1403 RQDVAADAEKQKqniqqELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELR---- 1478
Cdd:pfam17380 367 QEEIAMEISRMR-----ELERLQ----MERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARqrev 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1479 -----DRAAEAEKLRKAA-----------QDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKM 1542
Cdd:pfam17380 438 rrleeERAREMERVRLEEqerqqqverlrQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKL 517
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1543 QAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT--QLQTKAMSFSEQTTKLeESLKKEQgnvlklqeeadKLKKQQKEAN 1620
Cdd:pfam17380 518 LEKEMEERQKAIYEEERRREAEEERRKQQEMEErrRIQEQMRKATEERSRL-EAMERER-----------EMMRQIVESE 585
|
....*..
gi 1389908286 1621 TAREEAE 1627
Cdd:pfam17380 586 KARAEYE 592
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3457-3493 |
7.22e-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: 7.22e-13
10 20 30
....*....|....*....|....*....|....*..
gi 1389908286 3457 LLEAQLATGGIIDPASSHRVPTDVAIQRGYFSKQMAK 3493
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1241-1898 |
9.64e-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: 75.09 E-value: 9.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1241 RALREQLTDEKK--LLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDpiASPLKKPKMECASDDIIQEYVNL 1318
Cdd:TIGR02168 216 KELKAELRELELalLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE--ELRLEVSELEEEIEELQKELYAL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1319 RTRYSELmtltNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKE 1398
Cdd:TIGR02168 294 ANEISRL----EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1399 EASKRQDVAADAEKQKQNIQQELQHLKSLSDQeIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKttAHKAKSEAELQELR 1478
Cdd:TIGR02168 370 LESRLEELEEQLETLRSKVAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1479 DRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKS-----------------DAEKEAAKQKQR--------- 1532
Cdd:TIGR02168 447 EELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslerlqenlegfsEGVKALLKNQSGlsgilgvls 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1533 --------------------------------------------------ALDDLQKYKMQAEEAERRMKQAE------- 1555
Cdd:TIGR02168 527 elisvdegyeaaieaalggrlqavvvenlnaakkaiaflkqnelgrvtflPLDSIKGTEIQGNDREILKNIEGflgvakd 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1556 ----EEKIR--------QIRVVEEVAQksaATQLQTK-------------------AMSFSEQTT------------KLE 1592
Cdd:TIGR02168 607 lvkfDPKLRkalsyllgGVLVVDDLDN---ALELAKKlrpgyrivtldgdlvrpggVITGGSAKTnssilerrreieELE 683
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1593 ESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEA-------------LRLRLQAEEEAQKKSHAQE 1659
Cdd:TIGR02168 684 EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALrkdlarleaeveqLEERIAQLSKELTELEAEI 763
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1660 EAEKQKLEAERDAKKRGKAEEAALKQK---------------ENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHA 1724
Cdd:TIGR02168 764 EELEERLEEAEEELAEAEAEIEELEAQieqlkeelkalrealDELRAELTLLNEEAANLRERLESLERRIAATERRLEDL 843
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1725 EQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEA-- 1802
Cdd:TIGR02168 844 EEQIEELSEDIESLAAEIEELEELIEELESELEALLNERAS-LEEALALLRSELEELSEELRELESKRSELRRELEELre 922
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1803 --ARMRSVAEEAKKQR-QIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEmALKAKEAENERLKRQAEEEAYQRKLL 1879
Cdd:TIGR02168 923 klAQLELRLEGLEVRIdNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLK-RLENKIKELGPVNLAAIEEYEELKER 1001
|
810
....*....|....*....
gi 1389908286 1880 EDQAAQHKQDIEEKITQLQ 1898
Cdd:TIGR02168 1002 YDFLTAQKEDLTEAKETLE 1020
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1904-2610 |
1.01e-12 |
|
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: 75.09 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1904 ELGRQKNIVEETLKQKKVVEEE---IHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLaaeeer 1980
Cdd:TIGR02168 142 EQGKISEIIEAKPEERRAIFEEaagISKYKERRKETERKLERTRENLDRLEDILNELERQLKSLERQAEKAERY------ 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1981 rrkeaeekvKRITAAEEEA-----ARQCKAAQEEVERLKKKAedankqkekaekeaekqvvlaKEAAQKCTAAEQKAQDV 2055
Cdd:TIGR02168 216 ---------KELKAELRELelallVLRLEELREELEELQEEL---------------------KEAEEELEELTAELQEL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2056 LSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQakaqndtekqrkeaeee 2135
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEEL----------------- 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2136 aarraaaeaaaLKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQ 2215
Cdd:TIGR02168 329 -----------ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIAS 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2216 VEVELARVRIQMEELvklklkiEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQR 2295
Cdd:TIGR02168 398 LNNEIERLEARLERL-------EDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREEL 470
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2296 ALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD------KETEGFQKSLEA--------- 2360
Cdd:TIGR02168 471 EEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGvlseliSVDEGYEAAIEAalggrlqav 550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2361 ------ERKRQLEASAEAEKLKLRVKELSLAQ-TKAEDEAKKFKKQADEVKAQLQRTEKHTTEIvvQKLETQRLQSTREA 2433
Cdd:TIGR02168 551 vvenlnAAKKAIAFLKQNELGRVTFLPLDSIKgTEIQGNDREILKNIEGFLGVAKDLVKFDPKL--RKALSYLLGGVLVV 628
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2434 DDLKSAIADLEEERKKL--------------------KKEAEELQRKSKEMANAQQE-----------QIEQQKAELQQS 2482
Cdd:TIGR02168 629 DDLDNALELAKKLRPGYrivtldgdlvrpggvitggsAKTNSSILERRREIEELEEKieeleekiaelEKALAELRKELE 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2483 FLTEKGLLLKREKE--------VEGEKKRFEK---QLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAE 2551
Cdd:TIGR02168 709 ELEEELEQLRKELEelsrqisaLRKDLARLEAeveQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2552 EEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL 2610
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1332-1968 |
1.09e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 74.72 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1332 YIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmkmkeeaskrqdvaadae 1411
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELE------------------ 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1412 kqkqniqqelqhlkslsdqEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKaksEAELQELRDRAAEAEKLRKAA 1491
Cdd:PRK03918 235 -------------------ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEEL---KKEIEELEEKVKELKELKEKA 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1492 qDEAERLRKQVAEETQRKKNAEDELKRKSdaekEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRqirvveevaqk 1571
Cdd:PRK03918 293 -EEYIKLSEFYEEYLDELREIEKRLSRLE----EEINGIEERIKELEEKEERLEELKKKLKELEKRLEE----------- 356
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1572 saatqLQTKAMSFSEQTTKLE--ESLKKEQGNvlklqEEADKLKKQQKEANTAREEAEQELEIWRQKANE------ALRL 1643
Cdd:PRK03918 357 -----LEERHELYEEAKAKKEelERLKKRLTG-----LTPEKLEKELEELEKAKEEIEEEISKITARIGElkkeikELKK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1644 RLQAEEEAQKK----------SHAQEEAEKQKLEAERDAKKRGKAEEA---ALKQKENAEKELDKQRKFA--EQIAQQKL 1708
Cdd:PRK03918 427 AIEELKKAKGKcpvcgrelteEHRKELLEEYTAELKRIEKELKEIEEKerkLRKELRELEKVLKKESELIklKELAEQLK 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1709 SAEQECirLKADFEHAEQQRglldNELQRLKNEVNSTEKQRKQLEDELNkvrsemdsllqmKINAEKASMVNTEKSKQLL 1788
Cdd:PRK03918 507 ELEEKL--KKYNLEELEKKA----EEYEKLKEKLIKLKGEIKSLKKELE------------KLEELKKKLAELEKKLDEL 568
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1789 ESEalkMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQ 1868
Cdd:PRK03918 569 EEE---LAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1869 AEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKinfhKASKEKADLESELK 1948
Cdd:PRK03918 646 RKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEERE----KAKKELEKLEKALE 721
|
650 660
....*....|....*....|
gi 1389908286 1949 KLKGIADETQKSKLKAEEEA 1968
Cdd:PRK03918 722 RVEELREKVKKYKALLKERA 741
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1591-2019 |
1.17e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 74.42 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1591 LEESLKKEQGNVLKLQEEADKLKKQQ-KEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEK-QKLEA 1668
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKElKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKlEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1669 ERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLD-NELQRLKNEVNSTEK 1747
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATeEELQDLAEELEELQQ 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1748 QRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEAL---------------------------------- 1793
Cdd:COG4717 207 RLAELEEELEEAQEELEELEE-ELEQLENELEAAALEERLKEARLLlliaaallallglggsllsliltiagvlflvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1794 -------KMKQLADEAARMRSVAEEAKKQRqIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLK 1866
Cdd:COG4717 286 lallfllLAREKASLGKEAEELQALPALEE-LEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1867 RQAEEEAYQRKLLEDQA------------AQHKQDIEEKITQLQTSSDSELGRQKNIVEETlkQKKVVEEEIHIIKINFH 1934
Cdd:COG4717 365 LEELEQEIAALLAEAGVedeeelraaleqAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELE 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1935 KASKEKADLESELKKLkgiadETQKSKLKAEEEAEKLKklaaeeerrrKEAEEKVKRITAAEEEAARqCKAAQEEVERLK 2014
Cdd:COG4717 443 ELEEELEELREELAEL-----EAELEQLEEDGELAELL----------QELEELKAELRELAEEWAA-LKLALELLEEAR 506
|
....*
gi 1389908286 2015 KKAED 2019
Cdd:COG4717 507 EEYRE 511
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3381-3419 |
1.50e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.27 E-value: 1.50e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 3381 LLEAQAATGFITDPVKDKKCSVDDAVKEGIVGPELHEKL 3419
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1317-1919 |
1.65e-12 |
|
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: 74.02 E-value: 1.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1317 NLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDkqkqmAEAHAKSVAKAEQEALELKMKM 1396
Cdd:pfam07111 52 SLELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELD-----ALAVAEKAGQAEAEGLRAALAG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1397 KEEASKRQDVAAdaekqkqniQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAElqe 1476
Cdd:pfam07111 127 AEMVRKNLEEGS---------QRELEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAE--- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1477 lrdraaeaeklrkaAQDEAERLRKQVAE------------ETQRKKNAEDELKRKSDAEKEAAKQK--------QRALDD 1536
Cdd:pfam07111 195 --------------AQKEAELLRKQLSKtqeeleaqvtlvESLRKYVGEQVPPEVHSQTWELERQElldtmqhlQEDRAD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1537 LQK---------------YKMQAEEAERRMKQA---EEEKIRQIR-VVEEVAQKSAATQLQTKAmsfseQTTKLEESLKK 1597
Cdd:pfam07111 261 LQAtvellqvrvqslthmLALQEEELTRKIQPSdslEPEFPKKCRsLLNRWREKVFALMVQLKA-----QDLEHRDSVKQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1598 EQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKAnEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGK 1677
Cdd:pfam07111 336 LRGQVAELQEQVTSQSQEQAILQRALQDKAAEVEVERMSA-KGLQMELSRAQEARRRQQQQTASAEEQLKFVVNAMSSTQ 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1678 A---------EEAALK------------QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKAD----FEHAEQQRGLLD 1732
Cdd:pfam07111 415 IwlettmtrvEQAVARipslsnrlsyavRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADlsleLEQLREERNRLD 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1733 NELQR----LKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKinaeKASMVNTeksKQLLESEALKMKQLADEAARMRsv 1808
Cdd:pfam07111 495 AELQLsahlIQQEVGRAREQGEAERQQLSEVAQQLEQELQRA----QESLASV---GQQLEVARQGQQESTEEAASLR-- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1809 aEEAKKQRQIAEEEAARQRSEAEKILKEKLA----AINEATRLKTEAEMALKAKEAENERLKRQAEEeayQRKLLEDQAA 1884
Cdd:pfam07111 566 -QELTQQQEIYGQALQEKVAEVETRLREQLSdtkrRLNEARREQAKAVVSLRQIQHRATQEKERNQE---LRRLQDEARK 641
|
650 660 670
....*....|....*....|....*....|....*
gi 1389908286 1885 QHKQDIEEKItqlqtssdSELGRQKNIVEETLKQK 1919
Cdd:pfam07111 642 EEGQRLARRV--------QELERDKNLMLATLQQE 668
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2294-2587 |
1.73e-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: 74.00 E-value: 1.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2294 QRALAEKILKEKMQaiqeatklKAEAEKLQKQKDQ-AQETAKR--LQEDKQQIQQRLDKetegfQKSLEAERKR-QLEAS 2369
Cdd:pfam17380 281 QKAVSERQQQEKFE--------KMEQERLRQEKEEkAREVERRrkLEEAEKARQAEMDR-----QAAIYAEQERmAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2370 AEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHttEIVVQKLETQRLQSTREADdlksaiadleeERKK 2449
Cdd:pfam17380 348 RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKN--ERVRQELEAARKVKILEEE-----------RQRK 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2450 LKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgekkRFEKQLEDEMKKAKALKDEQERQRKLM 2529
Cdd:pfam17380 415 IQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVE----RLRQQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 2530 EEERKKLQAIMDEavRKQKEAEEEMKNKQREMDVLDKKRL---EQEKQLAEENKKLREQLQ 2587
Cdd:pfam17380 491 EQRRKILEKELEE--RKQAMIEEERKRKLLEKEMEERQKAiyeEERRREAEEERRKQQEME 549
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2724-2762 |
1.88e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.27 E-value: 1.88e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 2724 LLEAQAASGFIVDPVKNKFLSVDEAVKDKVIGPELHDRL 2762
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1348-1973 |
3.10e-12 |
|
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: 73.22 E-value: 3.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1348 KASEKLK--EEERRKMAEIQAELDKQ-KQMAEAHAKSVAKAEQEALELKMKMKEEASKrqdvaadaekqkqniqqeLQHL 1424
Cdd:pfam05483 166 RSAEKTKkyEYEREETRQVYMDLNNNiEKMILAFEELRVQAENARLEMHFKLKEDHEK------------------IQHL 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1425 KSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEkttahkakseaelqELRDRAAEAEKLRKAAQDEAERLRKQVAE 1504
Cdd:pfam05483 228 EEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLE--------------ESRDKANQLEEKTKLQDENLKELIEKKDH 293
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1505 ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYkmqAEEAERRMKQAEEEKIRQIRVVEEVaqKSAATQLQTKAMSF 1584
Cdd:pfam05483 294 LTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQL---TEEKEAQMEELNKAKAAHSFVVTEF--EATTCSLEELLRTE 368
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1585 SEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE-----AEQELEIWRQKANEALRLRLQAEEEAQKKSHAQE 1659
Cdd:pfam05483 369 QQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEElkkilAEDEKLLDEKKQFEKIAEELKGKEQELIFLLQAR 448
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1660 EAEKQKLEAERDAKKrgKAEEAALKQKENAEKELDKQR-KFAEQIAQ-QKLSAEQECIRLKAD---FEHAEQQRGLLDNE 1734
Cdd:pfam05483 449 EKEIHDLEIQLTAIK--TSEEHYLKEVEDLKTELEKEKlKNIELTAHcDKLLLENKELTQEASdmtLELKKHQEDIINCK 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1735 LQ--RLKNEVNSTEKQRKQLEDELNKVRSEmdslLQMKINAEKASMVNTEKSKQLLESEALK----MKQLADEAARMRSV 1808
Cdd:pfam05483 527 KQeeRMLKQIENLEEKEMNLRDELESVREE----FIQKGDEVKCKLDKSEENARSIEYEVLKkekqMKILENKCNNLKKQ 602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1809 AEEAKKQRQIAEEE--AARQRSEAE-------KILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQA-EEEAYQRKL 1878
Cdd:pfam05483 603 IENKNKNIEELHQEnkALKKKGSAEnkqlnayEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKlLEEVEKAKA 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1879 LEDQAAQHKQDI----EEKITQLQTSSDSELGRQKNIVEETlkqkkvvEEEIHIIKINFHKASKEKADLESELKKLKGIA 1954
Cdd:pfam05483 683 IADEAVKLQKEIdkrcQHKIAEMVALMEKHKHQYDKIIEER-------DSELGLYKNKEQEQSSAKAALEIELSNIKAEL 755
|
650
....*....|....*....
gi 1389908286 1955 DETQKSKLKAEEEAEKLKK 1973
Cdd:pfam05483 756 LSLKKQLEIEKEEKEKLKM 774
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2068-2613 |
3.43e-12 |
|
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: 73.22 E-value: 3.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2068 KLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEaarraaaeaaaL 2147
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDEN-----------L 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2148 KQKQQADAEMSKHKKEAEQALQQKSQVEKELtvvKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQM 2227
Cdd:pfam05483 285 KELIEKKDHLTKELEDIKMSLQRSMSTQKAL---EEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSL 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2228 EELVKlklkieeenrrlmqkdkdSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRalaeKILKEKMQ 2307
Cdd:pfam05483 362 EELLR------------------TEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK----KILAEDEK 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2308 AIQEATKLKAEAEKLQKQKdqaQETAKRLQEDKQQI-------------QQRLDKETEGFQKSLEAERKRQLEASAEAEK 2374
Cdd:pfam05483 420 LLDEKKQFEKIAEELKGKE---QELIFLLQAREKEIhdleiqltaiktsEEHYLKEVEDLKTELEKEKLKNIELTAHCDK 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2375 LKLRVKELS-------LAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVvQKLETQRLQSTREADDLKSAIADLEEER 2447
Cdd:pfam05483 497 LLLENKELTqeasdmtLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLR-DELESVREEFIQKGDEVKCKLDKSEENA 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2448 KKLKKEAEELQ-------------RKSKEMANAQQEQIEQQKAELQQSFLTEKGLLL-------KREKEVEGEKKRFEKQ 2507
Cdd:pfam05483 576 RSIEYEVLKKEkqmkilenkcnnlKKQIENKNKNIEELHQENKALKKKGSAENKQLNayeikvnKLELELASAKQKFEEI 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2508 LEDEMKKAKALKDEQERqrklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENK------K 2581
Cdd:pfam05483 656 IDNYQKEIEDKKISEEK----LLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDselglyK 731
|
570 580 590
....*....|....*....|....*....|...
gi 1389908286 2582 LREQLQ-TFEISSKTVSQTKESQTVSVEKLVAV 2613
Cdd:pfam05483 732 NKEQEQsSAKAALEIELSNIKAELLSLKKQLEI 764
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
142-241 |
4.30e-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: 65.44 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 142 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSN---QENLEQAFSVAERE-LGVTKLL 217
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKLgLPELDLF 80
|
90 100
....*....|....*....|....
gi 1389908286 218 DPEDVdVPHPDEKSIITYVSSLYD 241
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
20-119 |
4.34e-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: 65.91 E-value: 4.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 20 ERDRvQKKTFTKWVNKHLVKAQrhVTDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 91
Cdd:cd21300 4 EGER-EARVFTLWLNSLDVEPA--VNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1389908286 92 KHRQVKLVNIRNDDIADGNPKLTLGLIW 119
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4303-4341 |
4.80e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 4.80e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 4303 LLEAQACTGGIIDPNTGEKFSVVDAMNKGLVDKIMVDRI 4341
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1362-1822 |
5.25e-12 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 72.49 E-value: 5.25e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1362 AEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAAdAEKQKQNIQQELQHLKSLSDQeiKSKNQQLED 1441
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEE-LEEELEELEAELEELREELEK--LEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1442 ALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSD 1521
Cdd:COG4717 130 LYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1522 AEKEAAKQKQRALDDLQKYKMQAEEAERRmkQAEEEKIRQIRVV------------EEVAQKSAATQLQTKAMSFSEQTT 1589
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEA--AALEERLKEARLLlliaaallallgLGGSLLSLILTIAGVLFLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1590 KLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAE 1669
Cdd:COG4717 288 LLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1670 RDAKKRGKAEEAALKQKENAEKELDKQRKFaEQIAQQKLSAEQECIRLKADFEHAEQQRGL--LDNELQRLKNEVNSTEK 1747
Cdd:COG4717 368 LEQEIAALLAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEeeLEEELEELEEELEELEE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 1748 QRKQLEDELNKVRSEMDSLLQMKINAEKasmvnteksKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEE 1822
Cdd:COG4717 447 ELEELREELAELEAELEQLEEDGELAEL---------LQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
142-240 |
1.34e-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: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 142 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSVAERELGVTKLLDPED 221
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1389908286 222 VdVPHPDEKSIITYVSSLY 240
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2800-2838 |
1.53e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.53e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 2800 FLDVQLATGGIIDPVNSHRVPLQTAYSQGQFDADMNKKL 2838
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1489-1713 |
1.54e-11 |
|
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: 69.10 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1489 KAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLqKYKMQAEEAERRMKQAEEEKIRQIRVVEEV 1568
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL-EQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1569 AQKSAAtqlqtkamsfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEqeleiwRQKANEAlrlrlQAE 1648
Cdd:TIGR02794 125 KAKQAA-----------EAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAK------KKAEAEA-----KAK 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908286 1649 EEAQKKshAQEEAEKQKLEAerdAKKRGKAEEAALKQKENAEK-ELDKQRKFAEQIAQQKLSAEQE 1713
Cdd:TIGR02794 183 AEAEAK--AKAEEAKAKAEA---AKAKAAAEAAAKAEAEAAAAaAAEAERKADEAELGDIFGLASG 243
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3790-3828 |
1.63e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.57 E-value: 1.63e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 3790 LLEAQNATGGYMDPEYYFRLPIDVAMQRGYINKETHERL 3828
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1472-1907 |
1.70e-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: 71.14 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1472 AELQELRDRAAEAEKLRKAAqdeaerlRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYkMQAeeaerrM 1551
Cdd:COG3096 278 NERRELSERALELRRELFGA-------RRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLV-QTA------L 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1552 KQAEeeKIrqIRVVEEVAQKSAATQLQtkamsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQ----------QKEANT 1621
Cdd:COG3096 344 RQQE--KI--ERYQEDLEELTERLEEQ------EEVVEEAAEQLAEAEARLEAAEEEVDSLKSQladyqqaldvQQTRAI 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1622 AREEAEQELEiwrqKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELdkqRKFAE 1701
Cdd:COG3096 414 QYQQAVQALE----KARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELV---CKIAG 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1702 QI-AQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEdELNKvrsemdsllQMKINAEKASMVN 1780
Cdd:COG3096 487 EVeRSQAWQTARELLRRYRSQQALAQRLQQLRAQLAELEQRLRQQQNAERLLE-EFCQ---------RIGQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1781 TEKSKQllesEAlkmkQLADEAARMRSVAEEAKKQRQiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEA 1860
Cdd:COG3096 557 ELLAEL----EA----QLEELEEQAAEAVEQRSELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQE 627
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1389908286 1861 ENERLKRQAEEEAyQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGR 1907
Cdd:COG3096 628 VTAAMQQLLERER-EATVERDELAARKQALESQIERLSQPGGAEDPR 673
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
8-125 |
1.96e-11 |
|
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: 64.15 E-value: 1.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 8 DFMETLIQRGQDERDRVqKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQN 83
Cdd:cd21222 1 DAFDDLFDEAPEKLAEV-KELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHN 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908286 84 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 125
Cdd:cd21222 80 VKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2148-2378 |
2.25e-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: 69.02 E-value: 2.25e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2148 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQM 2227
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2228 EELVKLKLKIEEENR---RLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQiaesNLAEQRALAEKILKE 2304
Cdd:COG4942 107 AELLRALYRLGRQPPlalLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRA----ELEAERAELEALLAE 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 2305 KMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLR 2378
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAALKGKLP 256
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1910-2578 |
3.40e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 70.09 E-value: 3.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1910 NIVEETLKQKKVVEEEIHIIKinFHKASKEKADLESELKKLKgiadETQKSKLKAEEEAEKLKKlaaEEERRRKEAEEKV 1989
Cdd:PRK03918 139 AILESDESREKVVRQILGLDD--YENAYKNLGEVIKEIKRRI----ERLEKFIKRTENIEELIK---EKEKELEEVLREI 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1990 KRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDV--LSKNKEDVLAQE 2067
Cdd:PRK03918 210 NEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIeeLEEKVKELKELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2068 KLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKeaEEEAARRAAAEAAAL 2147
Cdd:PRK03918 290 EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEK--RLEELEERHELYEEA 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2148 KQKQqadAEMSKHKKEAEqalqqksqvEKELTVVKLQLDETDKQKVLLDQELQRVKGEvndafkqKSQVEVELARVRIQM 2227
Cdd:PRK03918 368 KAKK---EELERLKKRLT---------GLTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELKKAI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2228 EELVKLKLKIEEENRRLMQKDKdstQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRAL-AEKILKEKM 2306
Cdd:PRK03918 429 EELKKAKGKCPVCGRELTEEHR---KELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESELiKLKELAEQL 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2307 QAIQEATKlKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDketegfqkslEAERKRQLEASAEAEKLKLRVKELSLAQ 2386
Cdd:PRK03918 506 KELEEKLK-KYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKK----------ELEKLEELKKKLAELEKKLDELEEELAE 574
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2387 TKAEDEAKKFkKQADEVKAQLQRTEKHTTEIVVQKLETQRLQST-READDLKSAIADLeeerkklkkeaeelqRKSKEMA 2465
Cdd:PRK03918 575 LLKELEELGF-ESVEELEERLKELEPFYNEYLELKDAEKELEREeKELKKLEEELDKA---------------FEELAET 638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2466 NAQQEQIEQQKAELQQSFLTE-----KGLLLKREKEVEGEKKRFEkQLEDEMKKAKALKDEQERQRKLMEEERKKLqaim 2540
Cdd:PRK03918 639 EKRLEELRKELEELEKKYSEEeyeelREEYLELSRELAGLRAELE-ELEKRREEIKKTLEKLKEELEEREKAKKEL---- 713
|
650 660 670
....*....|....*....|....*....|....*....
gi 1389908286 2541 dEAVRKQKEAEEEMKNKQREMDVLDKKR-LEQEKQLAEE 2578
Cdd:PRK03918 714 -EKLEKALERVEELREKVKKYKALLKERaLSKVGEIASE 751
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1333-1893 |
3.72e-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: 69.75 E-value: 3.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1333 IKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQ---MAEAHAKSVAKAEQEALELKMK----MKEEASKRQD 1405
Cdd:pfam05483 259 LTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEdikMSLQRSMSTQKALEEDLQIATKticqLTEEKEAQME 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1406 VAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAE 1485
Cdd:pfam05483 339 ELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDE 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1486 KLrkaaQDEAERLRKqVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQaeEAERRMKQAEEEKIRQIrvv 1565
Cdd:pfam05483 419 KL----LDEKKQFEK-IAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLK--EVEDLKTELEKEKLKNI--- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1566 eEVAQKSAATQLQTKAMsfSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKanealrLRL 1645
Cdd:pfam05483 489 -ELTAHCDKLLLENKEL--TQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREE------FIQ 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1646 QAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAAlkqkENAEKELDKQRKFAEQIAQqklsaeqecirlkadfehae 1725
Cdd:pfam05483 560 KGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC----NNLKKQIENKNKNIEELHQ-------------------- 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1726 qqrglldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM---KINAEKASMVNTEKSKQLLESEALKMKQLADEA 1802
Cdd:pfam05483 616 --------ENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKfeeIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEA 687
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1803 ARMRSVAEEaKKQRQIAEEEA--ARQRSEAEKILKEKLAAI-------NEATRLKTEAEMALKAKEAENERLKRQAEEEA 1873
Cdd:pfam05483 688 VKLQKEIDK-RCQHKIAEMVAlmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEK 766
|
570 580
....*....|....*....|
gi 1389908286 1874 YQRKLLEDQAAQHKQDIEEK 1893
Cdd:pfam05483 767 EEKEKLKMEAKENTAILKDK 786
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2253-2593 |
3.76e-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: 69.77 E-value: 3.76e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2253 QKLLAEEAEKMKSLAEEAGRLSVEAEETARQ----RQIAESNLAEQRALAEKilkEKMQAIQE--ATKLKAEAEKLQKQK 2326
Cdd:pfam17380 281 QKAVSERQQQEKFEKMEQERLRQEKEEKAREverrRKLEEAEKARQAEMDRQ---AAIYAEQErmAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2327 DQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQ-LEAsaeAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKA 2405
Cdd:pfam17380 358 RKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeLEA---ARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2406 QLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEerkklkkeaeelqrKSKEManaQQEQIEQQKAELQQSFLT 2485
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKR--------------KKLEL---EKEKRDRKRAEEQRRKIL 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2486 EKGLLLKREKEVEGEKKRfeKQLEDEMKKAKALKDEQERQRKLMEEERKKLQaiMDEAVRKQKEAEEEMKNKQReMDVLD 2565
Cdd:pfam17380 498 EKELEERKQAMIEEERKR--KLLEKEMEERQKAIYEEERRREAEEERRKQQE--MEERRRIQEQMRKATEERSR-LEAME 572
|
330 340
....*....|....*....|....*...
gi 1389908286 2566 KKRlEQEKQLAEENKKLREQLQTFEISS 2593
Cdd:pfam17380 573 RER-EMMRQIVESEKARAEYEATTPITT 599
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1467-1716 |
4.74e-11 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 67.95 E-value: 4.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1467 KAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEEtQRKKNAEDELKRKSDAEKEAAKQKQRALDDlqkyKMQAEE 1546
Cdd:TIGR02794 63 AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE-KAAKQAEQAAKQAEEKQKQAEEAKAKQAAE----AKAKAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1547 AERRMKQAEEEKIRQirvvEEVAQKSAATQLQTKAmsfseqttklEESLKKEqgnvlklqeEADKLKKQQKEANTAREEA 1626
Cdd:TIGR02794 138 AEAERKAKEEAAKQA----EEEAKAKAAAEAKKKA----------EEAKKKA---------EAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1627 EQELEIWRQKanealrlrlqAEEEAQKKShAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQ 1706
Cdd:TIGR02794 195 KAKAEAAKAK----------AAAEAAAKA-EAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
250
....*....|
gi 1389908286 1707 KLSAEQECIR 1716
Cdd:TIGR02794 264 YAAIIQQAIQ 273
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2147-2586 |
5.94e-11 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 69.32 E-value: 5.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2147 LKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKvlldQELQRVKGEVNDAFKQKSQVEVELARVRIQ 2226
Cdd:PRK03918 185 IKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2227 MEELVKLKLKIEEENRRLMQKDKDSTQ------------KLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQ 2294
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKElkekaeeyiklsEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERL 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2295 RALAEKI---------LKEKMQAIQEATKLKAEAEKLQKQK-----DQAQETAKRLQEDKQQIQQRLDKETE--GFQKSL 2358
Cdd:PRK03918 341 EELKKKLkelekrleeLEERHELYEEAKAKKEELERLKKRLtgltpEKLEKELEELEKAKEEIEEEISKITAriGELKKE 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2359 EAERKRQLEASAEA--------------------EKLKLRVKELSLAQTKAEDEAKKFKKQADEVKA------------- 2405
Cdd:PRK03918 421 IKELKKAIEELKKAkgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKvlkkeseliklke 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2406 ---QLQRTEKHTTEIVVQKLEtqrlQSTREADDLKSAIADLEEERKKLKKEAEELQ--RKSKEMANAQQEQIEQQKAELQ 2480
Cdd:PRK03918 501 laeQLKELEEKLKKYNLEELE----KKAEEYEKLKEKLIKLKGEIKSLKKELEKLEelKKKLAELEKKLDELEEELAELL 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2481 QSfLTEKGL-----LLKREKEVEGEKKRF------EKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKE 2549
Cdd:PRK03918 577 KE-LEELGFesveeLEERLKELEPFYNEYlelkdaEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKK 655
|
490 500 510
....*....|....*....|....*....|....*...
gi 1389908286 2550 -AEEEMKNKQREMDVLDKKRLEQEKQLaEENKKLREQL 2586
Cdd:PRK03918 656 ySEEEYEELREEYLELSRELAGLRAEL-EELEKRREEI 692
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3126-3164 |
7.11e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 59.65 E-value: 7.11e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 3126 LLEAQLSTGGIVDPVKSYRIPHEVACKRGYFDDKMSKTL 3164
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1821-2603 |
7.39e-11 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 68.93 E-value: 7.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1821 EEAA------RQRSEAEKilkeKLAAINEA-TRLkteaEMALKAKEAENERLKRQAEE-EAYQRKLLEDQAAQH---KQD 1889
Cdd:TIGR02168 162 EEAAgiskykERRKETER----KLERTRENlDRL----EDILNELERQLKSLERQAEKaERYKELKAELRELELallVLR 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1890 IEEKITQLQTSsDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAE 1969
Cdd:TIGR02168 234 LEELREELEEL-QEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1970 KLKKlaaeeerrrkeaeeKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAE 2049
Cdd:TIGR02168 313 NLER--------------QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELE 378
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2050 QKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQR 2129
Cdd:TIGR02168 379 EQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELER 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2130 KeaeeeaarraaaeaaalkqkQQADAEMSKHKKEAEQALQQKSQvekeltvvklQLDETDKQKVLLDQELQRVKGE---V 2206
Cdd:TIGR02168 459 L--------------------EEALEELREELEEAEQALDAAER----------ELAQLQARLDSLERLQENLEGFsegV 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2207 NDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQK--DKDSTQKLLAEEAEKMKSLaeeaGRLSVEAEETARQR 2284
Cdd:TIGR02168 509 KALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvVENLNAAKKAIAFLKQNEL----GRVTFLPLDSIKGT 584
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2285 QIaESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQ------KDQAQETAKRLQEDKQQIQQRLDKETEGFQKSL 2358
Cdd:TIGR02168 585 EI-QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGvlvvddLDNALELAKKLRPGYRIVTLDGDLVRPGGVITG 663
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2359 EAERKRQ--LEASAEAEKLKLRVKELslaqtkaEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQStreaddl 2436
Cdd:TIGR02168 664 GSAKTNSsiLERRREIEELEEKIEEL-------EEKIAELEKALAELRKELEELEEELEQLRKELEELSRQIS------- 729
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2437 ksaiadleeerkklkkeaeeLQRKSKEMANAQQEQIEQQKAELQqsfltekglllKREKEVEGEKKRFEKQLEDEMKKAK 2516
Cdd:TIGR02168 730 --------------------ALRKDLARLEAEVEQLEERIAQLS-----------KELTELEAEIEELEERLEEAEEELA 778
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2517 ALkdeqerqrklmEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTV 2596
Cdd:TIGR02168 779 EA-----------EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
....*..
gi 1389908286 2597 SQTKESQ 2603
Cdd:TIGR02168 848 EELSEDI 854
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1722-2418 |
8.37e-11 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 68.51 E-value: 8.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1722 EHAEQQrglLDNELQRLKNEVNSTEKQRKQLEDELNKvRSEMDSLLQMKINAEKASmVNTEKSKQLLESEalKMKQLADE 1801
Cdd:TIGR04523 32 DTEEKQ---LEKKLKTIKNELKNKEKELKNLDKNLNK-DEEKINNSNNKIKILEQQ-IKDLNDKLKKNKD--KINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1802 AARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEaemaLKAKEAENERLKRQAEEEAYQRKLLED 1881
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKE----LEKLNNKYNDLKKQKEELENELNLLEK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1882 QaaqhKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfHKASKEKADLESELKKLKGIADETQKSK 1961
Cdd:TIGR04523 181 E----KLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLESQISELKKQN-NQLKDNIEKKQQEINEKTTEISNTQTQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1962 LKAEEEAEKLKKlaaeeerrrkeaeekvkritaaeeeaarQCKAAQEEVERLKKKAEDANKQkekaekeaekqvvLAKEA 2041
Cdd:TIGR04523 256 NQLKDEQNKIKK----------------------------QLSEKQKELEQNNKKIKELEKQ-------------LNQLK 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2042 AQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENA---------------KKLAQEAEKAKEKAEKEAALLRQKAEEAEK 2106
Cdd:TIGR04523 295 SEISDLNNQKEQDWNKELKSELKNQEKKLEEIQNQisqnnkiisqlneqiSQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2107 QKKaaENEAAKQAKAQ-----NDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVV 2181
Cdd:TIGR04523 375 LKK--ENQSYKQEIKNlesqiNDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVK 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2182 KLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAE 2261
Cdd:TIGR04523 453 ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESE 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2262 KMKslaeeagrlsVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEatkLKAEAEKLQKQKDQAQETAKRLQEDKQ 2341
Cdd:TIGR04523 533 KKE----------KESKISDLEDELNKDDFELKKENLEKEIDEKNKEIEE---LKQTQKSLKKKQEEKQELIDQKEKEKK 599
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2342 QIQQRLDKETEgfqksLEAERKRQLE-ASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIV 2418
Cdd:TIGR04523 600 DLIKEIEEKEK-----KISSLEKELEkAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESK 672
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1459-1881 |
9.95e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 68.26 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1459 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRK--QVAEETQRKKNAEDELKRKsDAEKEAAKQKQRALDD 1536
Cdd:COG4717 82 EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAEL-PERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1537 LQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQtkamSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQ 1616
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE----ELQQRLAELEEELEEAQEELEELEEELEQLENEL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1617 KEANTAREEAEQE--------------------------------------LEIWRQKANEALRLRLQAEEEAQKKSHAQ 1658
Cdd:COG4717 237 EAAALEERLKEARlllliaaallallglggsllsliltiagvlflvlgllaLLFLLLAREKASLGKEAEELQALPALEEL 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1659 EEAEKQKLEAERDAKKRGKAEEA--ALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNelq 1736
Cdd:COG4717 317 EEEELEELLAALGLPPDLSPEELleLLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQ--- 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1737 rlKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMkinaekasmVNTEKSKQLLESEALKMKQLADEAARMRsvAEEAKKQR 1816
Cdd:COG4717 394 --AEEYQELKEELEELEEQLEELLGELEELLEA---------LDEEELEEELEELEEELEELEEELEELR--EELAELEA 460
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 1817 QIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKeaenERLKRQAEEEaYQRKLLED 1881
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELL----EEAREEYREE-RLPPVLER 520
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1459-1767 |
1.01e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 68.56 E-value: 1.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1459 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDaEKEAAKQKQRALD--- 1535
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQ-EIENVKSELKELEari 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1536 -----DLQKYKMQAEEAERRMKQAEEEKI-RQIRVVEEVAQK--SAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQE 1607
Cdd:TIGR02169 768 eeleeDLHKLEEALNDLEARLSHSRIPEIqAELSKLEEEVSRieARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1608 EADKLKKQQKEANTAREEAEQELEiwrqkanealrlRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEeaaLKQKE 1687
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELE------------ELEAALRDLESRLGDLKKERDELEAQLRELERKIEE---LEAQI 912
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1688 NAEKELDKQRKFAEQIAQQKLS-------AEQECIRLKADFEHAEQQRGLLDNELQRLK-------NEVNSTEKQRKQLE 1753
Cdd:TIGR02169 913 EKKRKRLSELKAKLEALEEELSeiedpkgEDEEIPEEELSLEDVQAELQRVEEEIRALEpvnmlaiQEYEEVLKRLDELK 992
|
330
....*....|....
gi 1389908286 1754 DELNKVRSEMDSLL 1767
Cdd:TIGR02169 993 EKRAKLEEERKAIL 1006
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1236-1973 |
1.17e-10 |
|
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: 68.53 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1236 PISDSRALREQLTD---EKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIASplkKPKMECASDDII 1312
Cdd:TIGR00606 164 PLSEGKALKQKFDEifsATRYIKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITS---KEAQLESSREIV 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1313 QEYVN----LRTRYSELMTLTNQYIKfIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQ-KQMAEAHAKSVAKAEQ 1387
Cdd:TIGR00606 241 KSYENeldpLKNRLKEIEHNLSKIMK-LDNEIKALKSRKKQMEKDNSELELKMEKVFQGTDEQlNDLYHNHQRTVREKER 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1388 EALELKMKMKEEASKRQDVaaDAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHK 1467
Cdd:TIGR00606 320 ELVDCQRELEKLNKERRLL--NQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHT 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1468 AKSEAElqelRDRAAEAEKLRKAAQDEaERLRKQVAEETQRKKNAedeLKRKSDAEKEAAKQKQRALDDLQKYKMQAEEA 1547
Cdd:TIGR00606 398 LVIERQ----EDEAKTAAQLCADLQSK-ERLKQEQADEIRDEKKG---LGRTIELKKEILEKKQEELKFVIKELQQLEGS 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1548 ERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQkeaNTAREEAE 1627
Cdd:TIGR00606 470 SDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQME---MLTKDKMD 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1628 QELEIWRQKANEALRLRLQAEEEAQKKS-----HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR-KFAE 1701
Cdd:TIGR00606 547 KDEQIRKIKSRHSDELTSLLGYFPNKKQledwlHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLsSYED 626
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1702 QIAQQKLSAEQECI--RLKADFEHAEQQRGLL-------------------------------DNELQ----RLKNEVNS 1744
Cdd:TIGR00606 627 KLFDVCGSQDEESDleRLKEEIEKSSKQRAMLagatavysqfitqltdenqsccpvcqrvfqtEAELQefisDLQSKLRL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1745 TEKQRKQLEDELNKVRSEMDSLLqmkINAEKASMVNTEKSKQLLESEAlKMKQLADEAARMRSVAEEAKKQRQ--IAEEE 1822
Cdd:TIGR00606 707 APDKLKSTESELKKKEKRRDEML---GLAPGRQSIIDLKEKEIPELRN-KLQKVNRDIQRLKNDIEEQETLLGtiMPEEE 782
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1823 AAR--------------QRSEAEKILkEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQhKQ 1888
Cdd:TIGR00606 783 SAKvcltdvtimerfqmELKDVERKI-AQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQ-IQ 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1889 DIEEKITQLQT---SSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAE 1965
Cdd:TIGR00606 861 HLKSKTNELKSeklQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQ 940
|
....*...
gi 1389908286 1966 EEAEKLKK 1973
Cdd:TIGR00606 941 DKVNDIKE 948
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1512-1771 |
1.24e-10 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 66.41 E-value: 1.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1512 AEDELKRKSDAEKEAAKQKQRALDDLQKykmQAEEAERRmKQAEEEKIRQIRvveevaQKSAAtqlqtkamsfsEQTTKL 1591
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQ---QAEEAEKQ-RAAEQARQKELE------QRAAA-----------EKAAKQ 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1592 EESLKKEQgnvLKLQEEADKLKKQQKEANTAREEAEQEleiwRQKANEALRlrlQAEEEAQKKshAQEEAEKQKLEAERD 1671
Cdd:TIGR02794 107 AEQAAKQA---EEKQKQAEEAKAKQAAEAKAKAEAEAE----RKAKEEAAK---QAEEEAKAK--AAAEAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1672 AKKRGKAEEAALKQK--ENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1749
Cdd:TIGR02794 175 AEAEAKAKAEAEAKAkaEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARG 254
|
250 260
....*....|....*....|..
gi 1389908286 1750 KQLEDELNKVRSEMDSLLQMKI 1771
Cdd:TIGR02794 255 AAAGSEVDKYAAIIQQAIQQNL 276
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1668-1901 |
1.38e-10 |
|
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: 66.71 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1668 AERDAKKRGKAE-EAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTE 1746
Cdd:COG4942 17 AQADAAAEAEAElEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1747 KQRKQLEDELNKVrseMDSLLQMKINAEKASMVNTEKSKQLLESEALkMKQLADeaARMRSVAEEAKKQRQIAE--EEAA 1824
Cdd:COG4942 97 AELEAQKEELAEL---LRALYRLGRQPPLALLLSPEDFLDAVRRLQY-LKYLAP--ARREQAEELRADLAELAAlrAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1825 RQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSS 1901
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2156-2584 |
1.46e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 67.78 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2156 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSqvevELARVRIQMEELVKLKL 2235
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVK----ELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2236 KIEEENRRLMQKDKDsTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAEsnlaeqraLAEKILKEKMQAIQEATKL 2315
Cdd:PRK03918 249 SLEGSKRKLEEKIRE-LEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSE--------FYEEYLDELREIEKRLSRL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2316 KAEAEKLQKQKDQAQETAKRLQEDKQQIQQrLDKETEGFQKSLEA-ERKRQLEAsaEAEKLKLRVKELSLAQTKAE-DEA 2393
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEELKKKLKE-LEKRLEELEERHELyEEAKAKKE--ELERLKKRLTGLTPEKLEKElEEL 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2394 KKFKKQ-ADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQqEQI 2472
Cdd:PRK03918 397 EKAKEEiEEEISKITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKELLEEYTAELKRIEKELKEIE-EKE 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2473 EQQKAELqqsflTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAE- 2551
Cdd:PRK03918 476 RKLRKEL-----RELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEk 550
|
410 420 430
....*....|....*....|....*....|....
gi 1389908286 2552 -EEMKNKQREmdvLDKKRLEQEKQLAEENKKLRE 2584
Cdd:PRK03918 551 lEELKKKLAE---LEKKLDELEEELAELLKELEE 581
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2171-2601 |
1.47e-10 |
|
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: 67.82 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2171 KSQVEKELTVVKLQLDETDKQKVLLDQELQRvkgEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKD 2250
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLEESRDKANQLEEKTKL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2251 STQKLlAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQkdqAQ 2330
Cdd:pfam05483 280 QDENL-KELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTE---FE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2331 ETAKRLQEDKQQIQQRLDKETEGFQ--------KSLEAERKRQLEASAEAEKLKLrvKELSLAQTKAEDEAKKFKKQADE 2402
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKiitmelqkKSSELEEMTKFKNNKEVELEEL--KKILAEDEKLLDEKKQFEKIAEE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2403 VKA---------QLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEerkklkkeaeelqRKSKEMANAQQEQIE 2473
Cdd:pfam05483 434 LKGkeqelifllQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKL-------------KNIELTAHCDKLLLE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2474 QQKAELQQSFLTekgLLLKREKE----VEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKE 2549
Cdd:pfam05483 501 NKELTQEASDMT---LELKKHQEdiinCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARS 577
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 2550 AEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLRE-QLQTFEISSKTVSQTKE 2601
Cdd:pfam05483 578 IEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEElHQENKALKKKGSAENKQ 630
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4301-4338 |
1.49e-10 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 58.65 E-value: 1.49e-10
10 20 30
....*....|....*....|....*....|....*...
gi 1389908286 4301 QRLLEAQACTGGIIDPNTGEKFSVVDAMNKGLVDKIMV 4338
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1937-2588 |
1.57e-10 |
|
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: 68.07 E-value: 1.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1937 SKEKADLESELKKL---KGIADETQKSKLKAEEEAEKLKK---LAAEEERRRKEAEEKVKRITAAE----EEAARQCKAA 2006
Cdd:TIGR00618 162 SKEKKELLMNLFPLdqyTQLALMEFAKKKSLHGKAELLTLrsqLLTLCTPCMPDTYHERKQVLEKElkhlREALQQTQQS 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2007 QEEVERLKKKAEDANKQKEkaekeaekqvvLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRdEFENAKKLAQEAEKA 2086
Cdd:TIGR00618 242 HAYLTQKREAQEEQLKKQQ-----------LLKQLRARIEELRAQEAVLEETQERINRARKAAP-LAAHIKAVTQIEQQA 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2087 KEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQ 2166
Cdd:TIGR00618 310 QRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2167 ALQQKSQVEKELTvvkLQLDETDKQKVLLDQELQRVKGEVNDAFKQK--SQVEVELARVRIQmEELVKLKLKIEEENRrL 2244
Cdd:TIGR00618 390 TLTQKLQSLCKEL---DILQREQATIDTRTSAFRDLQGQLAHAKKQQelQQRYAELCAAAIT-CTAQCEKLEKIHLQE-S 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2245 MQKDKDSTQKLLAEEA----EKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQA-IQEATKLKAEA 2319
Cdd:TIGR00618 465 AQSLKEREQQLQTKEQihlqETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRgEQTYAQLETSE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2320 EKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLE-AERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKK 2398
Cdd:TIGR00618 545 EDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEdIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2399 QADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAiadleEERKKLKKEAEELQRKSKEMANaQQEQIEQQKAE 2478
Cdd:TIGR00618 625 QDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHAL-----SIRVLPKELLASRQLALQKMQS-EKEQLTYWKEM 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2479 LQQsflteKGLLLKREKEVEGEKKRFEKQLEDEMKKAKA-----LKDEQERQRKLMEEERKKLQAimdeavrkqKEAEEE 2553
Cdd:TIGR00618 699 LAQ-----CQTLLRELETHIEEYDREFNEIENASSSLGSdlaarEDALNQSLKELMHQARTVLKA---------RTEAHF 764
|
650 660 670
....*....|....*....|....*....|....*
gi 1389908286 2554 MKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQT 2588
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTH 799
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1461-1712 |
1.87e-10 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 67.28 E-value: 1.87e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1461 EKTTAHKAKS--EAELQEL-RDRAAEAEKLRKAAQDEAERLRKQVAEetqrkknAEDELKRKSDAEKEAAKQKQRALDDl 1537
Cdd:PRK05035 444 EKKKAEEAKArfEARQARLeREKAAREARHKKAAEARAAKDKDAVAA-------ALARVKAKKAAATQPIVIKAGARPD- 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1538 QKYKMQAEEAERRMKQAEEEKIRQirvVEEVAQKSAA-------TQLQTKAMSFSEQTTKLEESLKKEQgnVLKLQEEAd 1610
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQA---AAAADPKKAAvaaaiarAKAKKAAQQAANAEAEEEVDPKKAA--VAAAIARA- 589
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1611 KLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAE 1690
Cdd:PRK05035 590 KAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEP 669
|
250 260
....*....|....*....|....*.
gi 1389908286 1691 KELDKQRK--FAEQIA--QQKLSAEQ 1712
Cdd:PRK05035 670 EEAEDPKKaaVAAAIAraKAKKAAQQ 695
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1475-1920 |
2.01e-10 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 67.77 E-value: 2.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1475 QELRDraAEAEKlrKAAQDEaerlrkqVAEETQRKKNAEDElkRKSDAEKeaAKQKQRALDDLQKYKMQAeeaeRRMKQA 1554
Cdd:PRK10929 30 QELEQ--AKAAK--TPAQAE-------IVEALQSALNWLEE--RKGSLER--AKQYQQVIDNFPKLSAEL----RQQLNN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1555 EEEKIRQIRvveevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQeleiwr 1634
Cdd:PRK10929 91 ERDEPRSVP------PNMSTDALEQEILQVSSQLLEKSRQAQQEQDRAREISDSLSQLPQQQTEARRQLNEIER------ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1635 qkanealrlRLQAeeeAQKKSHAQEEAEKQKLeaerdakkrgKAEEAALKQKENaekELDkqrkfaeqIAQqkLSA--EQ 1712
Cdd:PRK10929 159 ---------RLQT---LGTPNTPLAQAQLTAL----------QAESAALKALVD---ELE--------LAQ--LSAnnRQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1713 ECIRLKADFEHAEQQRglLDNELQRLKNEVNStekQRKQledelnkvrsemdsllqmkiNAEKAsmvnTEKSKQLLESEA 1792
Cdd:PRK10929 204 ELARLRSELAKKRSQQ--LDAYLQALRNQLNS---QRQR--------------------EAERA----LESTELLAEQSG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1793 LKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKIL--KEKLAAINEATRLKTEAEM---ALKAKEA------E 1861
Cdd:PRK10929 255 DLPKSIVAQFKINRELSQALNQQAQRMDLIASQQRQAASQTLqvRQALNTLREQSQWLGVSNAlgeALRAQVArlpempK 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1862 NERLKRQAEEEAYQRKLLEDQAAQHKQDieekiTQLQTSSDSEL-GRQKNIVEETLKQKK 1920
Cdd:PRK10929 335 PQQLDTEMAQLRVQRLRYEDLLNKQPQL-----RQIRQADGQPLtAEQNRILDAQLRTQR 389
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3957-3995 |
2.15e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 2.15e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 3957 LLEAQAATGYVIDPIKNLKLNVTEAVKMGIVGTEFKDKL 3995
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1474-1694 |
2.15e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.98 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1474 LQELRDRAAEAEKLR-KAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDlQKykmQAEEAERRMK 1552
Cdd:PRK09510 67 QQQQQKSAKRAEEQRkKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALK-QK---QAEEAAAKAA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1553 QAEEEKIRQIRVVEEVAQKSAAtqlqtkamsfseqttklEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEqelei 1632
Cdd:PRK09510 143 AAAKAKAEAEAKRAAAAAKKAA-----------------AEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK----- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 1633 wrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELD 1694
Cdd:PRK09510 201 --KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
514-703 |
2.86e-10 |
|
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: 63.23 E-value: 2.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 514 LRYTQDLLGWVEENQRRVDEGEWGSDLPTVESLLGSHRGLHQCVEEFRSKIERAKADESQV---SPASKAAYRDYLGKLE 590
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLieeGHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 591 LQYGKLLTSSKARLRYLD---QLHAFVVAATKELMWLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAV 667
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1389908286 668 QTTGDKLLRDGHP-ARKTIEAFTAALQTQWSWLLQLC 703
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2147-2590 |
3.01e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.71 E-value: 3.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2147 LKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVkgevnDAFKQKSQVEVELARVRIQ 2226
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2227 MEELvklKLKIEEENRRLMQKDKdstqkLLAEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRalaEKILKEKM 2306
Cdd:COG4717 148 LEEL---EERLEELRELEEELEE-----LEAELAELQEELEELLEQLSLATEEELQD-------LAEEL---EELQQRLA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2307 QAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAE-AEKLKLRVKELSLA 2385
Cdd:COG4717 210 ELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALL 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2386 QTKAEDEAKKFKKQADEVKAQLQRtekhtteivvQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMA 2465
Cdd:COG4717 290 FLLLAREKASLGKEAEELQALPAL----------EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2466 NAQ--QEQIEQQKAELQQSF-------LTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRklmeeerkkL 2536
Cdd:COG4717 360 EEElqLEELEQEIAALLAEAgvedeeeLRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE---------L 430
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 2537 QAIMDEAVRKQKEAEEEMKNKQREmdvldKKRLEQEKQLAEENKKLREQLQTFE 2590
Cdd:COG4717 431 EEELEELEEELEELEEELEELREE-----LAELEAELEQLEEDGELAELLQELE 479
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1508-2130 |
3.07e-10 |
|
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: 66.58 E-value: 3.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1508 RKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEaerrMKQAEEEKIRQIRvVEEVAQKSAATQLQTKAMSFSEQ 1587
Cdd:TIGR04523 30 KQDTEEKQLEKKLKTIKNELKNKEKELKNLDKNLNKDEE----KINNSNNKIKILE-QQIKDLNDKLKKNKDKINKLNSD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1588 TTKLEESLKKEQGNVLKLQEEADKLKKQQKEANtareeaEQELEIwrqkANEALRLrlqaEEEAQKKSHAQEEAEKQKLE 1667
Cdd:TIGR04523 105 LSKINSEIKNDKEQKNKLEVELNKLEKQKKENK------KNIDKF----LTEIKKK----EKELEKLNNKYNDLKKQKEE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1668 AERDAKKrgkaeeaALKQKENAEKELDKQRKfAEQIAQQKLSAEQECIR----LKADFEHAEQQRGLLDN-------ELQ 1736
Cdd:TIGR04523 171 LENELNL-------LEKEKLNIQKNIDKIKN-KLLKLELLLSNLKKKIQknksLESQISELKKQNNQLKDniekkqqEIN 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1737 RLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEALKMKQLAdEAARMRSVAEEAKKQR 1816
Cdd:TIGR04523 243 EKTTEISNTQTQLNQLKDEQNKIKKQLSE-KQKELEQNNKKIKELEKQLNQLKSEISDLNNQK-EQDWNKELKSELKNQE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1817 qiaeeeaaRQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQ 1896
Cdd:TIGR04523 321 --------KKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1897 -----LQTSSDSELGRQKNIVEETLKQ-KKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEK 1970
Cdd:TIGR04523 393 indleSKIQNQEKLNQQKDEQIKKLQQeKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1971 LKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKaekeaekqvvLAKEAAQKCTAAEQ 2050
Cdd:TIGR04523 473 LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEK----------LESEKKEKESKISD 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2051 KAQDVLSKNkeDVLAQEKLRDEF----ENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTE 2126
Cdd:TIGR04523 543 LEDELNKDD--FELKKENLEKEIdeknKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELE 620
|
....
gi 1389908286 2127 KQRK 2130
Cdd:TIGR04523 621 KAKK 624
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2148-2598 |
3.12e-10 |
|
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: 66.58 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2148 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVevelarvriqM 2227
Cdd:TIGR04523 239 QEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSEISDLNNQKEQD----------W 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2228 EELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRALAEKILKEKMQ 2307
Cdd:TIGR04523 309 NKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRE-------LEEKQNEIEKLKKENQS 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2308 AIQEATKLKAEAEKLQKQKDQAQETAkrlqedkqqiqQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2387
Cdd:TIGR04523 382 YKQEIKNLESQINDLESKIQNQEKLN-----------QQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2388 KAEDEAKKFKKQADEVKAQLQrtekhTTEIVVQKLETQRLQSTREADDLKSAIadleeerkklkkeaeelqrkskEMANA 2467
Cdd:TIGR04523 451 VKELIIKNLDNTRESLETQLK-----VLSRSINKIKQNLEQKQKELKSKEKEL----------------------KKLNE 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2468 QQEQIEQQKAELQQsfltEKGLLLKREKEVEGEKKRFEKQLEDemKKAKALKDEQERQRKLMEEERKKLQaimdEAVRKQ 2547
Cdd:TIGR04523 504 EKKELEEKVKDLTK----KISSLKEKIEKLESEKKEKESKISD--LEDELNKDDFELKKENLEKEIDEKN----KEIEEL 573
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 2548 KEAEEEMKNKQREMDvldkkrlEQEKQLAEENKKLREQLQTFEISSKTVSQ 2598
Cdd:TIGR04523 574 KQTQKSLKKKQEEKQ-------ELIDQKEKEKKDLIKEIEEKEKKISSLEK 617
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2175-2594 |
3.57e-10 |
|
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: 66.58 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2175 EKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLmqkdkdstQK 2254
Cdd:TIGR04523 81 EQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKK--------EK 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2255 LLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAE---QRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQE 2331
Cdd:TIGR04523 153 ELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKiknKLLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKD 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2332 TAKRLQEDKQQIQQRLDKETEGFQ--KSLEAERKRQLEA-SAEAEKLKLRVKELS--LAQTKAEDEAKKFKKQAD---EV 2403
Cdd:TIGR04523 233 NIEKKQQEINEKTTEISNTQTQLNqlKDEQNKIKKQLSEkQKELEQNNKKIKELEkqLNQLKSEISDLNNQKEQDwnkEL 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2404 KAQLQRTEKHTTEIvvqklETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEmanaQQEQIEQQKAElQQSF 2483
Cdd:TIGR04523 313 KSELKNQEKKLEEI-----QNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEE----KQNEIEKLKKE-NQSY 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2484 LTEKGLLLKREKEVEGE---KKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNkqre 2560
Cdd:TIGR04523 383 KQEIKNLESQINDLESKiqnQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKN---- 458
|
410 420 430
....*....|....*....|....*....|....
gi 1389908286 2561 mdvLDKKRLEQEKQLAEENKKLREQLQTFEISSK 2594
Cdd:TIGR04523 459 ---LDNTRESLETQLKVLSRSINKIKQNLEQKQK 489
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1518-1962 |
3.92e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 66.33 E-value: 3.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1518 RKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKK 1597
Cdd:COG4717 64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1598 EQGNVLKLQEEADKLKKQQKEantaREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGK 1677
Cdd:COG4717 144 LPERLEELEERLEELRELEEE----LEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1678 AEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRL------KADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQ 1751
Cdd:COG4717 220 EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1752 LEDELNKVR--SEMDSLLQMKINAEKAS-MVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEA--ARQ 1826
Cdd:COG4717 300 LGKEAEELQalPALEELEEEELEELLAAlGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAllAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1827 RSEAEKILKEKLAAINEATRLK---TEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQhkQDIEEKITQLQTssds 1903
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKeelEELEEQLEELLGELEELLEALDEEELEEELEELEEEL--EELEEELEELRE---- 453
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 1904 ELGRQKNIVEETLKQKKVVE--EEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKL 1962
Cdd:COG4717 454 ELAELEAELEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
140-239 |
5.51e-10 |
|
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: 59.70 E-value: 5.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYrQSNQ--ENLEQAFSVAERELGVTKLL 217
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCPDWESW-DPNQpvQNAREAMQQADDWLGVPQVI 86
|
90 100
....*....|....*....|..
gi 1389908286 218 DPEDVDVPHPDEKSIITYVSSL 239
Cdd:cd21314 87 APEEIVDPNVDEHSVMTYLSQF 108
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
26-122 |
5.86e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 59.51 E-value: 5.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 26 KKTFTKWVNKHLVKAQ---------RHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDFL 91
Cdd:cd21217 3 KEAFVEHINSLLADDPdlkhllpidPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 1389908286 92 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 122
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1902-2590 |
6.31e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 65.86 E-value: 6.31e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1902 DSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLEsELKKLKGIADETQ-----KSKLKAEEEAEKLKK--- 1973
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEgyellKEKEALERQKEAIERqla 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1974 -LAAEEERRRKEAEEKVKRITAAE----EEAARQCKAAQEEVERLKKKAEDankqKEKAEKEAEKQVVLAKEAAQKCTAA 2048
Cdd:TIGR02169 248 sLEEELEKLTEEISELEKRLEEIEqlleELNKKIKDLGEEEQLRVKEKIGE----LEAEIASLERSIAEKERELEDAEER 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2049 EQKAQDVLSKNKEDVlaqEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQ 2128
Cdd:TIGR02169 324 LAKLEAEIDKLLAEI---EELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKRE 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2129 RkeaeeeaARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKL-------QLDETDKQKVLLDQELQR 2201
Cdd:TIGR02169 401 I-------NELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALeikkqewKLEQLAADLSKYEQELYD 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2202 VKGEVNDAFKQKSQVEVELARV---RIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAG-RLS--- 2274
Cdd:TIGR02169 474 LKEEYDRVEKELSKLQRELAEAeaqARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGnRLNnvv 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2275 VEAEETA-------RQRQIAE----------------------------------------------------SNLAEQR 2295
Cdd:TIGR02169 554 VEDDAVAkeaiellKRRKAGRatflplnkmrderrdlsilsedgvigfavdlvefdpkyepafkyvfgdtlvvEDIEAAR 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2296 ALAEKI--------LKEKMQAI-----------QEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD-------- 2348
Cdd:TIGR02169 634 RLMGKYrmvtlegeLFEKSGAMtggsraprggiLFSRSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDelsqelsd 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2349 --KETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQR 2426
Cdd:TIGR02169 714 asRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2427 LQSTREADDLK------SAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgE 2500
Cdd:TIGR02169 794 PEIQAELSKLEeevsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELE-E 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2501 KKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQE-------- 2572
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEeipeeels 952
|
810
....*....|....*....
gi 1389908286 2573 -KQLAEENKKLREQLQTFE 2590
Cdd:TIGR02169 953 lEDVQAELQRVEEEIRALE 971
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1344-1698 |
8.54e-10 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 64.89 E-value: 8.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1344 EDDEKASEKLKE----EERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQN-IQ 1418
Cdd:pfam02029 1 IEDEEEAARERRrrarEERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKrLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1419 QELQHLK---------SLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRK 1489
Cdd:pfam02029 81 EALERQKefdptiadeKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1490 AAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRalddLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVA 1569
Cdd:pfam02029 161 DKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRG----HPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1570 QKSAATQLQTkamsfsEQttKLEESLKKEQGnvlKLQEEADKLKKQQkeantarEEAEQELEIWRQKANEalRLRLQAEE 1649
Cdd:pfam02029 237 EEEAEVFLEA------EQ--KLEELRRRRQE---KESEEFEKLRQKQ-------QEAELELEELKKKREE--RRKLLEEE 296
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 1650 EAQKKshaQEEAEKQKLEAERdaKKRGKAE------EAALKQKENAEKELDKQRK 1698
Cdd:pfam02029 297 EQRRK---QEEAERKLREEEE--KRRMKEEierrraEAAEKRQKLPEDSSSEGKK 346
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2156-2587 |
8.55e-10 |
|
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: 65.38 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2156 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKL 2235
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQ 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2236 KIEEENRRL--MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAEsnLAEQRALAEKILKEKMQAIQEAT 2313
Cdd:TIGR00618 240 QSHAYLTQKreAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAP--LAAHIKAVTQIEQQAQRIHTELQ 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2314 KLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRqlEASAEAEKLKLRVKELSLAQTKAEDE- 2392
Cdd:TIGR00618 318 SKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIR--EISCQQHTLTQHIHTLQQQKTTLTQKl 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2393 ----AKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMAN-- 2466
Cdd:TIGR00618 396 qslcKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQql 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2467 AQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFE-----------------------KQLEDEMKKAKALKDEQE 2523
Cdd:TIGR00618 476 QTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNparqdidnpgpltrrmqrgeqtyAQLETSEEDVYHQLTSER 555
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 2524 RQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDK---KRLEQEKQLAEENKKLREQLQ 2587
Cdd:TIGR00618 556 KQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQ 622
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1528-1951 |
1.11e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 1.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1528 KQKQRALDDL------QKYKMQAEEAE---RRMKQAEEEKIRQIRvvEEVAQKSAA------TQLQTKAMSFSEQTTKLE 1592
Cdd:PRK02224 149 SDRQDMIDDLlqlgklEEYRERASDARlgvERVLSDQRGSLDQLK--AQIEEKEEKdlherlNGLESELAELDEEIERYE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1593 EslKKEQGNVLKlqEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDA 1672
Cdd:PRK02224 227 E--QREQARETR--DEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEA 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1673 KKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQL 1752
Cdd:PRK02224 303 GLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDR 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1753 EDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEE----------- 1821
Cdd:PRK02224 383 REEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpve 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1822 -----EAARQRSEAEKILKEKLAAINEA-TRLKTEAEMALKAKEAEnerlkRQAEEEAYQRKLLEDQAAQHKQDIEEKIT 1895
Cdd:PRK02224 463 gsphvETIEEDRERVEELEAELEDLEEEvEEVEERLERAEDLVEAE-----DRIERLEERREDLEELIAERRETIEEKRE 537
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908286 1896 QLQtssdsELGRQKNIVEETLKQKKVVEEEIHiikINFHKASKEKADLESELKKLK 1951
Cdd:PRK02224 538 RAE-----ELRERAAELEAEAEEKREAAAEAE---EEAEEAREEVAELNSKLAELK 585
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1487-1898 |
1.13e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 64.79 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1487 LRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVE 1566
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1567 EVAQKSAATQLQTKAMSFSEQTTKLEESLKKeqgnvlkLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRlRLQ 1646
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEERLEE-------LRELEEELEELEAELAELQEELEELLEQLSLATEEELQ-DLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1647 AEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIA---------------------- 1704
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAallallglggsllsliltiagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1705 ------------QQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVN-STEKQRKQLEDELNKVRSEMDSLLQMKI 1771
Cdd:COG4717 279 lflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGlPPDLSPEELLELLDRIEELQELLREAEE 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1772 NAEKASMVNTEKSKQLLeseaLKMKQLADEAArMRSVAEEAKKQRQIAEE--EAARQRSEAEKILKEKLAAINEATRLKT 1849
Cdd:COG4717 359 LEEELQLEELEQEIAAL----LAEAGVEDEEE-LRAALEQAEEYQELKEEleELEEQLEELLGELEELLEALDEEELEEE 433
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 1850 EAEMALKAKEAENER---LKRQAEEEAYQRKLLEDQAAQH-KQDIEEKITQLQ 1898
Cdd:COG4717 434 LEELEEELEELEEELeelREELAELEAELEQLEEDGELAElLQELEELKAELR 486
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1460-1881 |
1.16e-09 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 64.65 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1460 LEKTTAHKAKSEAELqelrdraaeAEKLRKAAQDEAERLRKQVAEETqrKKNAEDElKRKSDAEKEAAKQKQralDDLQK 1539
Cdd:NF033838 101 LYELNVLKEKSEAEL---------TSKTKKELDAAFEQFKKDTLEPG--KKVAEAT-KKVEEAEKKAKDQKE---EDRRN 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1540 Y--------KMQAEEAERRMKQAEEEkirqirVVEEVAQKSaatqlqtkamsfseqttKLEESLKKEQGNVLKLQEEADK 1611
Cdd:NF033838 166 YptntyktlELEIAESDVEVKKAELE------LVKEEAKEP-----------------RDEEKIKQAKAKVESKKAEATR 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1612 LKKQQkeanTAREEAEQeleiwrqkanEALRLRLQAEEEAQKKSHAQEEAEKQKleaeRDAKKRGKAEEAALKQKENAEK 1691
Cdd:NF033838 223 LEKIK----TDREKAEE----------EAKRRADAKLKEAVEKNVATSEQDKPK----RRAKRGVLGEPATPDKKENDAK 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1692 ELDKQRKfAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRlknevNSTEKQRKQLEDELNKVRSEMDSLLQMKI 1771
Cdd:NF033838 285 SSDSSVG-EETLPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRR-----NYPTNTYKTLELEIAESDVKVKEAELELV 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1772 NAEKASMVNTEKSKQLLESEALKMKqladEAARMrsvaEEAKKQRQIAEEEAARQRSEAEKIlKEKLAAINEATRLKTEA 1851
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVESKKA----EATRL----EKIKTDRKKAEEEAKRKAAEEDKV-KEKPAEQPQPAPAPQPE 429
|
410 420 430
....*....|....*....|....*....|....
gi 1389908286 1852 EMALK----AKEAENERLKRQAEEEAYQRKLLED 1881
Cdd:NF033838 430 KPAPKpekpAEQPKAEKPADQQAEEDYARRSEEE 463
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2253-2574 |
1.17e-09 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 63.40 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2253 QKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQET 2332
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2333 AKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEklkLRVKELSLAQTKAEDEAKKFKKQADEVKaqlqrtEK 2412
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREED---ERILEYLKEKAEREEEREAEREEIEEEK------ER 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2413 HTTEIVVQKLETQRLQSTREADDLKSAIADLeeerkklkkeaeelQRKSKEMANAQQEQIEQQKAELQQSFLTEKGL-LL 2491
Cdd:pfam13868 185 EIARLRAQQEKAQDEKAERDELRAKLYQEEQ--------------ERKERQKEREEAEKKARQRQELQQAREEQIELkER 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2492 KREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDE---AVRKQKEAEEEMKNKQREMDVLDKKR 2568
Cdd:pfam13868 251 RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEreeQRAAEREEELEEGERLREEEAERRER 330
|
....*.
gi 1389908286 2569 LEQEKQ 2574
Cdd:pfam13868 331 IEEERQ 336
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2224-2638 |
1.26e-09 |
|
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: 64.99 E-value: 1.26e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2224 RIQMEELV---KLKLKIEEENRRLMQKdKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEK 2300
Cdd:pfam02463 155 RLEIEEEAagsRLKRKKKEALKKLIEE-TENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLK 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2301 ILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAErkrqlEASAEAEKLKLRVK 2380
Cdd:pfam02463 234 LNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKE-----EEELKSELLKLERR 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2381 ELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKhttEIVVQKLETQRLQSTREADDLksaiADLEEERKKLKKEAEELQRK 2460
Cdd:pfam02463 309 KVDDEEKLKESEKEKKKAEKELKKEKEEIEEL---EKELKELEIKREAEEEEEEEL----EKLQEKLEQLEEELLAKKKL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2461 SKEMANAQQEQIEQQKAELqqsfltekgllLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQaim 2540
Cdd:pfam02463 382 ESERLSSAAKLKEEELELK-----------SEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLT--- 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2541 deaVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVAVTTVGTSK 2620
Cdd:pfam02463 448 ---EEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
410
....*....|....*...
gi 1389908286 2621 GVLNGSTEVDGVKKEGDS 2638
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYK 542
|
|
| COG5281 |
COG5281 |
Phage-related minor tail protein [Mobilome: prophages, transposons]; |
2064-2477 |
1.42e-09 |
|
Phage-related minor tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444092 [Multi-domain] Cd Length: 603 Bit Score: 64.25 E-value: 1.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2064 LAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAE 2143
Cdd:COG5281 15 AAAAASAAAAAAAAALAAAAAAAAAAAGLAAAAAAAAAASLAAAAAAAALAAAAAAAAAAAAADALAAALAEDAAAAAAA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2144 AAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARV 2223
Cdd:COG5281 95 AEAALAALAAAALALAAAALAEAALAAAAAAAAAAAAAAAAAAAAAAAAAEAAKAAAAAAAAAALAAAAAAAAAAAAAAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2224 RIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILK 2303
Cdd:COG5281 175 AAAALAAASAAAAAAAAKAAAEAAAEAAAAAEAAAAAAAAAAEAAAAEAQALAAAALAEQAALAAASAAAQALAALAAAA 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2304 EKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRvKELS 2383
Cdd:COG5281 255 AAAALALAAAAELALTAQAEAAAAAAAAAAAAAQAAEAAAAAAEAQALAAAAAAAAAQLAAAAAAAAQALRAAAQ-ALAA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2384 LAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKE 2463
Cdd:COG5281 334 LAQRALAAAALAAAAQEAALAAAAAALQAALEAAAAAAAAELAAAGDWAAGAKAALAEYADSATNVAAQVAQAATSAFSG 413
|
410
....*....|....
gi 1389908286 2464 MANAQQEQIEQQKA 2477
Cdd:COG5281 414 LTDALAGAVTTGKL 427
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1356-1720 |
1.79e-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: 64.32 E-value: 1.79e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1356 EERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKeeaskrqdvaaDAEKQKQNIQQELQHLkslsDQEIKSK 1435
Cdd:TIGR02169 671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELS-----------DASRKIGEIEKEIEQL----EQEEEKL 735
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1436 NQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAE-KLR----KAAQDEAERLRKQVAEETQRKK 1510
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEaRLShsriPEIQAELSKLEEEVSRIEARLR 815
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1511 NAEDELKRKSDAEKEAAKQKQraldDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT--QLQTKAMSFSEQT 1588
Cdd:TIGR02169 816 EIEQKLNRLTLEKEYLEKEIQ----ELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAAlrDLESRLGDLKKER 891
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1589 TKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELeiwrqkanEALRLRLQAEEEAQKKSHAQEEAEKQKLEA 1668
Cdd:TIGR02169 892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEEL--------SEIEDPKGEDEEIPEEELSLEDVQAELQRV 963
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 1669 ERDAKKRGKAEEAALKQKENAEKELDKQRKfaeqiAQQKLSAEQECIRLKAD 1720
Cdd:TIGR02169 964 EEEIRALEPVNMLAIQEYEEVLKRLDELKE-----KRAKLEEERKAILERIE 1010
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1338-1628 |
1.92e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 64.31 E-value: 1.92e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1338 DAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEAS--------------KR 1403
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEErleeaeeelaeaeaEI 784
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1404 QDVAADAEKQKQNIQQELQHLKSLSDQ------EIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQEL 1477
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAEltllneEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1478 RDRAAEAEKLRKAAQDEaerlRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEE 1557
Cdd:TIGR02168 865 EELIEELESELEALLNE----RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDN 940
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1558 KIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLE--ESLKKEQGNV--------LKLQEEADKLKKQQKEANTAREEAE 1627
Cdd:TIGR02168 941 LQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKrlENKIKELGPVnlaaieeyEELKERYDFLTAQKEDLTEAKETLE 1020
|
.
gi 1389908286 1628 Q 1628
Cdd:TIGR02168 1021 E 1021
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
18-124 |
2.93e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 57.51 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 18 QDERDrvqKKTFTKWVNKhlVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLK 92
Cdd:cd21299 1 ETSRE---ERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGK 75
|
90 100 110
....*....|....*....|....*....|..
gi 1389908286 93 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 124
Cdd:cd21299 76 QLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1248-1956 |
3.32e-09 |
|
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: 63.50 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1248 TDEKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKalqdpiaSPLKKPKMECASDDIIQEYVNLR-TRYSELM 1326
Cdd:TIGR04523 82 QQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLE-------VELNKLEKQKKENKKNIDKFLTEiKKKEKEL 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1327 TLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMaeahAKSVAKAEQEALELKMKMKEEASKRQDV 1406
Cdd:TIGR04523 155 EKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL----LSNLKKKIQKNKSLESQISELKKQNNQL 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1407 aadaEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRdraAEAEK 1486
Cdd:TIGR04523 231 ----KDNIEKKQQEINEKT----TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLK---SEISD 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1487 LRKAAQDEaerLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVE 1566
Cdd:TIGR04523 300 LNNQKEQD---WNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLK 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1567 EVAQ--KSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEalrLR 1644
Cdd:TIGR04523 377 KENQsyKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSV---KE 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1645 LQAEEEAQKKSHAQEEAEKQKLEAerdakkrgKAEEAALKQKenaEKELDKQRKFAEQIAQQKLSAEQECIRLKadfeha 1724
Cdd:TIGR04523 454 LIIKNLDNTRESLETQLKVLSRSI--------NKIKQNLEQK---QKELKSKEKELKKLNEEKKELEEKVKDLT------ 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1725 eQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSllqmkinaekasmVNTEKSKQLLESEALKMKQLADEAar 1804
Cdd:TIGR04523 517 -KKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFELKK-------------ENLEKEIDEKNKEIEELKQTQKSL-- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1805 mrsvaeeAKKQRQiAEEEAARQRSEAEKILKEklaaINEATRLKTEAEMALKAKEAENERL----------KRQAEEEAY 1874
Cdd:TIGR04523 581 -------KKKQEE-KQELIDQKEKEKKDLIKE----IEEKEKKISSLEKELEKAKKENEKLssiiknikskKNKLKQEVK 648
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1875 QRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEiHIIKINFHKASKEKADLESELKKLKGIA 1954
Cdd:TIGR04523 649 QIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITR-MIRIKDLPKLEEKYKEIEKELKKLDEFS 727
|
..
gi 1389908286 1955 DE 1956
Cdd:TIGR04523 728 KE 729
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2231-2591 |
3.44e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 63.54 E-value: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2231 VKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQ 2310
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELES 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2311 EATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQ--RLDKETEGFQKsLEAERKRQLEASAEAEKLKLRVKELSLAQTK 2388
Cdd:PRK03918 250 LEGSKRKLEEKIRELEERIEELKKEIEELEEKVKElkELKEKAEEYIK-LSEFYEEYLDELREIEKRLSRLEEEINGIEE 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2389 AEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTR-EADDLKSAIADleeerkklkkeaeelqrKSKEMANA 2467
Cdd:PRK03918 329 RIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKeELERLKKRLTG-----------------LTPEKLEK 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2468 QQEQIEQQKAELQQSFLTekglLLKREKEVEGEKKRFEKQLEdEMKKAK-------ALKDEQERQRkLMEEERKKLQAIM 2540
Cdd:PRK03918 392 ELEELEKAKEEIEEEISK----ITARIGELKKEIKELKKAIE-ELKKAKgkcpvcgRELTEEHRKE-LLEEYTAELKRIE 465
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 2541 DEaVRKQKEAEEEMKNKQREMD--VLDKKRLEQEKQLAEENKKLREQLQTFEI 2591
Cdd:PRK03918 466 KE-LKEIEEKERKLRKELRELEkvLKKESELIKLKELAEQLKELEEKLKKYNL 517
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1477-1852 |
3.91e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 63.44 E-value: 3.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1477 LRDRAAEAEKLRKAAQDEAERL--RKQVAEETQRKKNAEDELKRKSDAEKE--------------------AAKQKQRAL 1534
Cdd:PRK04863 275 MRHANERRVHLEEALELRRELYtsRRQLAAEQYRLVEMARELAELNEAESDleqdyqaasdhlnlvqtalrQQEKIERYQ 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1535 DDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQ--KSAATQL----------QTKAMSFSEQTTKLEESLKKEQGNV 1602
Cdd:PRK04863 355 ADLEELEERLEEQNEVVEEADEQQEENEARAEAAEEevDELKSQLadyqqaldvqQTRAIQYQQAVQALERAKQLCGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1603 L---KLQEEADKLKKQQKEANTAREEAEQEL----EIWRQ--KANEALRlRLQAE-EEAQKKSHAQE---EAEKQKLEAE 1669
Cdd:PRK04863 435 LtadNAEDWLEEFQAKEQEATEELLSLEQKLsvaqAAHSQfeQAYQLVR-KIAGEvSRSEAWDVAREllrRLREQRHLAE 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1670 RDAKKRGKAEEaaLKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1749
Cdd:PRK04863 514 QLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDE---LEQLQEELEARLESLSESVSEARERRMALRQQL 588
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1750 KQLEDELNKVRSEMDSLLQMKinaEKASMVNTEKSKQLLESEALkmkqlaDEAarMRSVAEEAKKQRQIAEEEAARQRSE 1829
Cdd:PRK04863 589 EQLQARIQRLAARAPAWLAAQ---DALARLREQSGEEFEDSQDV------TEY--MQQLLERERELTVERDELAARKQAL 657
|
410 420
....*....|....*....|...
gi 1389908286 1830 AEKILKEKLAAINEATRLKTEAE 1852
Cdd:PRK04863 658 DEEIERLSQPGGSEDPRLNALAE 680
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
27-121 |
4.62e-09 |
|
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: 56.96 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 27 KTFTKWVNKHLVKA--QRHVTDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKHRQVKL 98
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1389908286 99 VNIRNDDIADGNPKLTLGLIWTI 121
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1545-1954 |
5.49e-09 |
|
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: 62.47 E-value: 5.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1545 EEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTARE 1624
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1625 EAEQELEiwrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAK------KRGKAEEAALKQKENAEKELDKQRK 1698
Cdd:pfam09731 132 EVLKEAI---SKAESATAVAKEAKDDAIQAVKAHTDSLKEASDTAEISRekatdsALQKAEALAEKLKEVINLAKQSEEE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1699 FA-EQIAQQKLSAEQECIRLKADFEhaeqqrglldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL-QMKINAEKA 1776
Cdd:pfam09731 209 AApPLLDAAPETPPKLPEHLDNVEE-----------KVEKAQSLAKLVDQYKELVASERIVFQQELVSIFpDIIPVLKED 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1777 SMVNTEKSKQLLESEALKMKQLADEAARMRsVAEEAKKQRQIAEEEAARQRSEAEKI--LKEKLAAINEATRLKTEAEMA 1854
Cdd:pfam09731 278 NLLSNDDLNSLIAHAHREIDQLSKKLAELK-KREEKHIERALEKQKEELDKLAEELSarLEEVRAADEAQLRLEFERERE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1855 LKAKEAENE---RLKRQAEE-EAYQRKLLEDQAAQ----HKQDIEEKITQLQTSSDSELGRQK---NIVEETLKQKKVVE 1923
Cdd:pfam09731 357 EIRESYEEKlrtELERQAEAhEEHLKDVLVEQEIElqreFLQDIKEKVEEERAGRLLKLNELLanlKGLEKATSSHSEVE 436
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1389908286 1924 EE----------IHIIKINFHKAS--KEKADLESELKKLKGIA 1954
Cdd:pfam09731 437 DEnrkaqqlwlaVEALRSTLEDGSadSRPRPLVRELKALKELA 479
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1345-1591 |
5.54e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.70 E-value: 5.54e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1345 DDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEeaskRQDVAADAEKQKQNIQQELQHL 1424
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRA----LEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1425 KslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQEL-RDRAAEAEKLRkAAQDEAERLRKQVA 1503
Cdd:COG4942 96 R----AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaPARREQAEELR-ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1504 EETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKyKMQAEEAERRMKQAEEEKIRqiRVVEEVAQKSAATQLQTKAMS 1583
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEK-ELAELAAELAELQQEAEELE--ALIARLEAEAAAAAERTPAAG 247
|
....*...
gi 1389908286 1584 FSEQTTKL 1591
Cdd:COG4942 248 FAALKGKL 255
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1691-2582 |
6.18e-09 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 62.76 E-value: 6.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1691 KELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLL---DNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL 1767
Cdd:TIGR00606 186 KALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQItskEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIM 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1768 QM--KINAEKASMVNTEKSKQLLESEALKMKQLADEaaRMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAT 1845
Cdd:TIGR00606 266 KLdnEIKALKSRKKQMEKDNSELELKMEKVFQGTDE--QLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1846 RLKTE-AEMALKAKEAENERLKRQAEEEAYQRKLlEDQAAQHKQDIEEKITQLQT-----SSDSELGRQKNIVE----ET 1915
Cdd:TIGR00606 344 ELLVEqGRLQLQADRHQEHIRARDSLIQSLATRL-ELDGFERGPFSERQIKNFHTlvierQEDEAKTAAQLCADlqskER 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1916 LKQKKVVEEEIHIiKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAA 1995
Cdd:TIGR00606 423 LKQEQADEIRDEK-KGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKK 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1996 EEEAARQCKAaqeEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKctaaEQKAQDVLSKNKEDVLAQEKlrdEFEN 2075
Cdd:TIGR00606 502 EVKSLQNEKA---DLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK----DEQIRKIKSRHSDELTSLLG---YFPN 571
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2076 AKKLAQEAEKakekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQkQQADA 2155
Cdd:TIGR00606 572 KKQLEDWLHS-----------KSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS-QDEES 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2156 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVkgevndaFKQKSQVEvELARVRIQMEELVKLKL 2235
Cdd:TIGR00606 640 DLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRV-------FQTEAELQ-EFISDLQSKLRLAPDKL 711
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2236 KIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQralaEKILKEKMQAIQEATKL 2315
Cdd:TIGR00606 712 KSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQ----ETLLGTIMPEEESAKVC 787
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2316 KAEAEKLQKQKDQAQETAKRLQedkqqiQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKK 2395
Cdd:TIGR00606 788 LTDVTIMERFQMELKDVERKIA------QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQH 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2396 FKKQADEVKAQlqRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEqiEQQ 2475
Cdd:TIGR00606 862 LKSKTNELKSE--KLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKET--SNK 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2476 KAELQQSFLTEK-----GLLLKREKEVEGEKKRFEKQLEDEMKKAKA-LKDEQERQRKLMEEERKKLQAIMDEAVR---- 2545
Cdd:TIGR00606 938 KAQDKVNDIKEKvknihGYMKDIENKIQDGKDDYLKQKETELNTVNAqLEECEKHQEKINEDMRLMRQDIDTQKIQerwl 1017
|
890 900 910 920
....*....|....*....|....*....|....*....|....*...
gi 1389908286 2546 -----------KQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKL 2582
Cdd:TIGR00606 1018 qdnltlrkrenELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL 1065
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2162-2400 |
6.44e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 6.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2162 KEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRiqmEELVKLKLKIEEen 2241
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALE---AELAELEKEIAE-- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2242 rrlMQKDKDSTQKLLAE---EAEKMKSLAEEAGRLSVE-AEETARQRQIAESNLAEQRALAEKILKEKmqaiqeatklkA 2317
Cdd:COG4942 95 ---LRAELEAQKEELAEllrALYRLGRQPPLALLLSPEdFLDAVRRLQYLKYLAPARREQAEELRADL-----------A 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2318 EAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFK 2397
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
...
gi 1389908286 2398 KQA 2400
Cdd:COG4942 241 ERT 243
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1318-1672 |
6.84e-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: 6.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1318 LRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMaeahaksvakaEQEALELKMKMK 1397
Cdd:TIGR02169 693 LQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL-----------EQEIENVKSELK 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1398 EEASKRQDVAADAEKqkqnIQQELQHLK-SLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQE 1476
Cdd:TIGR02169 762 ELEARIEELEEDLHK----LEEALNDLEaRLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQE 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1477 LRDRAAEAEKLRKAAQDEAERLRKQVAEetqrkknAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEE 1556
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEE-------LEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEA 910
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1557 EkirqirvVEEvaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVlklqEEADKLKKQQKEantaREEAEQELEiwrqk 1636
Cdd:TIGR02169 911 Q-------IEK--KRKRLSELKAKLEALEEELSEIEDPKGEDEEIP----EEELSLEDVQAE----LQRVEEEIR----- 968
|
330 340 350
....*....|....*....|....*....|....*.
gi 1389908286 1637 ANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDA 1672
Cdd:TIGR02169 969 ALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKA 1004
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2187-2590 |
7.00e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 62.36 E-value: 7.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2187 ETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELvklklkieEENRRLMQKDKDSTQKLLAEEAEK---M 2263
Cdd:PRK02224 182 LSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERY--------EEQREQARETRDEADEVLEEHEERreeL 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2264 KSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKD----QAQETAKRLQED 2339
Cdd:PRK02224 254 ETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeledRDEELRDRLEEC 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2340 KQQIQQrldketegFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVV 2419
Cdd:PRK02224 334 RVAAQA--------HNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPV 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2420 Q--KLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQR--------------KSKEMANA---QQEQIEQQKAEL- 2479
Cdd:PRK02224 406 DlgNAEDFLEELREERDELREREAELEATLRTARERVEEAEAlleagkcpecgqpvEGSPHVETieeDRERVEELEAELe 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2480 ----QQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMK 2555
Cdd:PRK02224 486 dleeEVEEVEERLERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430
....*....|....*....|....*....|....*
gi 1389908286 2556 NKQREMDVLdkKRLEQEKQlaeENKKLREQLQTFE 2590
Cdd:PRK02224 566 EAEEAREEV--AELNSKLA---ELKERIESLERIR 595
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1338-1537 |
7.16e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.36 E-value: 7.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1338 DAQRRLEDDEKASEKLKEEERRKMAEIQ---AELDKQKQMAEAHAKSVAKAEQEALElKMKMKEEASKRQDVAADAEKQK 1414
Cdd:PRK09510 73 SAKRAEEQRKKKEQQQAEELQQKQAAEQerlKQLEKERLAAQEQKKQAEEAAKQAAL-KQKQAEEAAAKAAAAAKAKAEA 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1415 QNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKieeeihiiriQLEKTTAHKAKSEAElqelrdRAAEAEKLRKAAQD- 1493
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKK----------KAEAEAAAKAAAEAK------KKAEAEAKKKAAAEa 215
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1389908286 1494 --EAERLRKQVAEETQRKKNAEDELKRKSDA-EKEAAKQKQRALDDL 1537
Cdd:PRK09510 216 kkKAAAEAKAAAAKAAAEAKAAAEKAAAAKAaEKAAAAKAAAEVDDL 262
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4379-4417 |
7.62e-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: 7.62e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 4379 FLEVQYLTGGLIEPDATNRVAIDEAVKKGTLDARTAQKL 4417
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1998-2376 |
8.60e-09 |
|
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: 62.06 E-value: 8.60e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1998 EAARQCKAAQEEVERLKK-KAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENA 2076
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQeKEEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKRELERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2077 KKLAQEAEKAKEKAEKEAALLRQKAEEAEKQkkaaENEAAKQAKAQnDTEKQRKEaeeeaarraaaeaaalkqkQQADAE 2156
Cdd:pfam17380 366 RQEEIAMEISRMRELERLQMERQQKNERVRQ----ELEAARKVKIL-EEERQRKI-------------------QQQKVE 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2157 MSKHKKEAEQALQQKSQV---EKELTVVKLQLDETDKQkvlldQELQRVKgevndafkqksQVEVELARVRIQMEELVKL 2233
Cdd:pfam17380 422 MEQIRAEQEEARQREVRRleeERAREMERVRLEEQERQ-----QQVERLR-----------QQEEERKRKKLELEKEKRD 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2234 KLKIEEENRRLMQKDKdstqkllaeEAEKMKSLAEEAGRLSVEAEETARQRQIAESnlaEQRALAEKiLKEKMQAIQeat 2313
Cdd:pfam17380 486 RKRAEEQRRKILEKEL---------EERKQAMIEEERKRKLLEKEMEERQKAIYEE---ERRREAEE-ERRKQQEME--- 549
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 2314 klkaEAEKLQKQKDQAQETAKRLQEdkqqiqqrLDKETEGFQKSLEAERKRQ-LEASAEAEKLK 2376
Cdd:pfam17380 550 ----ERRRIQEQMRKATEERSRLEA--------MEREREMMRQIVESEKARAeYEATTPITTIK 601
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
135-239 |
8.61e-09 |
|
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: 56.25 E-value: 8.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 135 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGV 213
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*.
gi 1389908286 214 TKLLDPEDVDVPHPDEKSIITYVSSL 239
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQF 105
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1533-1763 |
9.28e-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: 9.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1533 ALDDLQKYKMQAEEAERRMKQAEEeKIRQIRVVEEVAQKSAATQlqtkamsfsEQTTKLEESlkKEQGNVLKLQEEADKL 1612
Cdd:COG4913 226 AADALVEHFDDLERAHEALEDARE-QIELLEPIRELAERYAAAR---------ERLAELEYL--RAALRLWFAQRRLELL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1613 KKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQK------ 1686
Cdd:COG4913 294 EAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALlaalgl 373
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 1687 --ENAEKELDKQRkfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEM 1763
Cdd:COG4913 374 plPASAEEFAALR---AEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDAL 449
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1351-1803 |
9.96e-09 |
|
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: 61.76 E-value: 9.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1351 EKLKEEERRKMAEIQA------ELDKQ----KQMAEAHAKSVAKAEQ---------EALELKMKMKEEA-SKRQDVAADA 1410
Cdd:pfam10174 292 DQLKQELSKKESELLAlqtkleTLTNQnsdcKQHIEVLKESLTAKEQraailqtevDALRLRLEEKESFlNKKTKQLQDL 371
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1411 EKQKQNIQQELQHLKSLSDQE------IKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHkakSEAELQELRDRAAEA 1484
Cdd:pfam10174 372 TEEKSTLAGEIRDLKDMLDVKerkinvLQKKIENLQEQLRDKDKQLAGLKERVKSLQTDSSN---TDTALTTLEEALSEK 448
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1485 EKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAekeaakqkqralddlqkykMQAEEAERrmkqaeeekirqirv 1564
Cdd:pfam10174 449 ERIIERLKEQREREDRERLEELESLKKENKDLKEKVSA-------------------LQPELTEK--------------- 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1565 veevaqKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIwrqkaneALRLR 1644
Cdd:pfam10174 495 ------ESSLIDLKEHASSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEI-------NDRIR 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1645 LQAEEEAQKKshaqEEAEKQKLEAERDAKKRGKAE-EAALKQKENAEKELDKQRKFAEQ-IAQQKLSAEQECIRLKAdfe 1722
Cdd:pfam10174 562 LLEQEVARYK----EESGKAQAEVERLLGILREVEnEKNDKDKKIAELESLTLRQMKEQnKKVANIKHGQQEMKKKG--- 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1723 haeqqRGLLDNELQRLKNEV-NSTEKQRKQLEDELNKVRSEMDSlLQMKIN------AEKASMVNT---EKSKQLleSEA 1792
Cdd:pfam10174 635 -----AQLLEEARRREDNLAdNSQQLQLEELMGALEKTRQELDA-TKARLSstqqslAEKDGHLTNlraERRKQL--EEI 706
|
490
....*....|.
gi 1389908286 1793 LKMKQLADEAA 1803
Cdd:pfam10174 707 LEMKQEALLAA 717
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2308-2581 |
1.16e-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: 60.55 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2308 AIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2387
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2388 KAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVqkletqrLQSTREADDLKSAIAdleeerkklkkeaeelqrkSKEMANA 2467
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALL-------LSPEDFLDAVRRLQY-------------------LKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2468 QQEQIEQQKAELQQsfLTEKglllkrekevegekkrfEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQ 2547
Cdd:COG4942 148 RREQAEELRADLAE--LAAL-----------------RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKEL 208
|
250 260 270
....*....|....*....|....*....|....
gi 1389908286 2548 KEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKK 2581
Cdd:COG4942 209 AELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2196-2406 |
1.56e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 60.23 E-value: 1.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2196 DQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLmQKDKDSTQKLLAEEAEKMKSLAEEAGRLSV 2275
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL-QAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2276 EAEETARQRQIAE--------SNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRL 2347
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2348 DKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQ 2406
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
140-237 |
1.69e-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: 55.56 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 140 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVAERELGVTKLLD 218
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1389908286 219 PEDVDVPHPDEKSIITYVS 237
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
144-239 |
1.70e-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: 56.16 E-value: 1.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 144 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQ-----------------------EN 199
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 200 LEQAFSVAER-----------ELG-VTKLLDPEDVDVPHPDEKSIITYVSSL 239
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1664-2129 |
1.74e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.94 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1664 QKLEAERDA--KKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqklsAEQECIRLKADFEHAEQQRGLLDNELQRLKNE 1741
Cdd:COG4717 49 ERLEKEADElfKPQGRKPELNLKELKELEEELKEAEEKEEEYAE----LQEELEELEEELEELEAELEELREELEKLEKL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1742 VN--STEKQRKQLEDELNKVRSEMDSLLQmkinaekasmvntekskqllesealKMKQLADEAARMRSVAEEAKKQRQIA 1819
Cdd:COG4717 125 LQllPLYQELEALEAELAELPERLEELEE-------------------------RLEELRELEEELEELEAELAELQEEL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1820 EEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEayqRKLLEDQAAQHKQDIEEKITQLQT 1899
Cdd:COG4717 180 EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQL---ENELEAAALEERLKEARLLLLIAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1900 SSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIAdetQKSKLKAEEEAEKLKKLAAEEE 1979
Cdd:COG4717 257 ALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALP---ALEELEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1980 RRRKEAEEKVKRITAAEEEAARQCKAAQE-EVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSK 2058
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEElQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEE 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 2059 NKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQR 2129
Cdd:COG4717 414 LLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAE 484
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1528-1710 |
1.74e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 60.27 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1528 KQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIrvveevaQKSAATQLQTKAmsfseqttklEESLKKEQGNVLKLQE 1607
Cdd:COG2268 180 EDENNYLDALGRRKIAEIIRDARIAEAEAERETEI-------AIAQANREAEEA----------ELEQEREIETARIAEA 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1608 EADKLKKQ---QKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALK 1684
Cdd:COG2268 243 EAELAKKKaeeRREAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAE 322
|
170 180
....*....|....*....|....*.
gi 1389908286 1685 QKENAEKELDKQRKFAEQIAQQKLSA 1710
Cdd:COG2268 323 AEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1390-1949 |
1.86e-08 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 60.81 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1390 LELKmKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQ-EIKSKNQQLEDAlvSRRKIEEEIHIIRIQLEKTTAHKA 1468
Cdd:pfam05701 42 LELE-KVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEElKLNLERAQTEEA--QAKQDSELAKLRVEEMEQGIADEA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1469 K--SEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEE 1546
Cdd:pfam05701 119 SvaAKAQLEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELIATKESLES 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1547 AERRMKQAEEEKIRQirvveevaqksaatqlqtkAMSFSEQTTKLEESLKkeqgnvlKLQEEADKLKKQQkeanTAREEA 1626
Cdd:pfam05701 199 AHAAHLEAEEHRIGA-------------------ALAREQDKLNWEKELK-------QAEEELQRLNQQL----LSAKDL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1627 EQELEiwrqkANEALRLRLQAEEEAQKKSHAQEEAEKQKLEaerdaKKRGKAEEAALKQkenAEKELDKQRKFAEqiaqq 1706
Cdd:pfam05701 249 KSKLE-----TASALLLDLKAELAAYMESKLKEEADGEGNE-----KKTSTSIQAALAS---AKKELEEVKANIE----- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1707 KLSAEQECIRLKAdfehaeqqrGLLDNELQRLKNEVNSTeKQRK--------QLEDELNKVRSEMdSLLQMKINAEKASM 1778
Cdd:pfam05701 311 KAKDEVNCLRVAA---------ASLRSELEKEKAELASL-RQREgmasiavsSLEAELNRTKSEI-ALVQAKEKEAREKM 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1779 VNTEKSKQLLESEALKMKQLAdEAARmrsvaEEAKKQRQIAEE-EAARQRSEA--EKILKEKLAAiNEATRLKTEAEMAL 1855
Cdd:pfam05701 380 VELPKQLQQAAQEAEEAKSLA-QAAR-----EELRKAKEEAEQaKAAASTVESrlEAVLKEIEAA-KASEKLALAAIKAL 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1856 KAKEAENE----------------------RLKRQAEEEAYQRklledqaaqhkqdIEEKITQLQTSSDSELgRQKNIVE 1913
Cdd:pfam05701 453 QESESSAEstnqedsprgvtlsleeyyelsKRAHEAEELANKR-------------VAEAVSQIEEAKESEL-RSLEKLE 518
|
570 580 590
....*....|....*....|....*....|....*.
gi 1389908286 1914 ETLKQKKVVEEEIHIIKINFHKASKEKADLESELKK 1949
Cdd:pfam05701 519 EVNREMEERKEALKIALEKAEKAKEGKLAAEQELRK 554
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1566-2355 |
2.57e-08 |
|
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: 60.62 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1566 EEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQ-----------EEADKLKKQQKEANTAREEAEQELEIWR 1634
Cdd:pfam12128 221 QQVEHWIRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLShlhfgyksdetLIASRQEERQETSAELNQLLRTLDDQWK 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1635 QKANEaLRLRLQAEEEA-QKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQiAQQKLSAEQE 1713
Cdd:pfam12128 301 EKRDE-LNGELSAADAAvAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTG-KHQDVTAKYN 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1714 CIRLKADFEHAeqqRGLLDNElQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINaekasmvNTEKSKQLLESEAL 1793
Cdd:pfam12128 379 RRRSKIKEQNN---RDIAGIK-DKLAKIREARDRQLAVAEDDLQALESELREQLEAGKL-------EFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1794 KMKQLADEAarmrSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERL--KRQAEE 1871
Cdd:pfam12128 448 ELKLRLNQA----TATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLeeRQSALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1872 EAYQR---------KLLEDQAAQHKQDIEEKITQ---LQTSSDSELGRQKNIVEETLKQKKVVEEEIHIikinfhkasKE 1939
Cdd:pfam12128 524 ELELQlfpqagtllHFLRKEAPDWEQSIGKVISPellHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDV---------PE 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1940 KADLESELKKLKGIADETqkskLKAEEEaeklkklaaeeerrrkeaeekvkRITAAEEEAArqckAAQEEVERLKKKAED 2019
Cdd:pfam12128 595 WAASEEELRERLDKAEEA----LQSARE-----------------------KQAAAEEQLV----QANGELEKASREETF 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2020 ANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLrdefeNAKKLAQEAEKAKEKAEKEAALLRQ 2099
Cdd:pfam12128 644 ARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQ-----LDKKHQAWLEEQKEQKREARTEKQA 718
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2100 KAEEAEKQKKAAEnEAAKQAKAQndTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELT 2179
Cdd:pfam12128 719 YWQVVEGALDAQL-ALLKAAIAA--RRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVL 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2180 VVKLQLDETdkqkvlLDQELQRVKGEVNDAFKQKSQVEVELARvriqMEELVKLKLKIEEENRrlmqKDKDSTQKLLAEE 2259
Cdd:pfam12128 796 RYFDWYQET------WLQRRPRLATQLSNIERAISELQQQLAR----LIADTKLRRAKLEMER----KASEKQQVRLSEN 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2260 AEKMKSLAEEAGRLSVEAEETARQRQIAESNlaeqRALAEkiLKEKMQAIQEATKLKAEAEKLQKQKDQAQ---ETAKRL 2336
Cdd:pfam12128 862 LRGLRCEMSKLATLKEDANSEQAQGSIGERL----AQLED--LKLKRDYLSESVKKYVEHFKNVIADHSGSglaETWESL 935
|
810 820
....*....|....*....|..
gi 1389908286 2337 QEDKQQI---QQRLDKETEGFQ 2355
Cdd:pfam12128 936 REEDHYQndkGIRLLDYRKLVP 957
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2152-2393 |
2.69e-08 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 59.46 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2152 QADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELV 2231
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2232 klklkieeenrRLMQKDKDSTQKLLA-EEAEkmkSLAEEAGRLSVEAEETARQRQIAESnLAEQRALAEKILKEKMQAIQ 2310
Cdd:COG3883 93 -----------RALYRSGGSVSYLDVlLGSE---SFSDFLDRLSALSKIADADADLLEE-LKADKAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2311 EATKLKAEAEK----LQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQ 2386
Cdd:COG3883 158 ELEALKAELEAakaeLEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAA 237
|
....*..
gi 1389908286 2387 TKAEDEA 2393
Cdd:COG3883 238 AAAAAAA 244
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1488-1706 |
2.70e-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: 59.97 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1488 RKAAQDEAERLRKQVAE----ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKmqAEEAERRMKQAEEEKIRQir 1563
Cdd:pfam15709 328 REQEKASRDRLRAERAEmrrlEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRR--FEEIRLRKQRLEEERQRQ-- 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1564 vveEVAQKSAATQLQTKamsfSEQTTKLEESLKKeqgnvlKLQEEadKLKKQQKEANTAREEAEQELEIWRQKANEALRL 1643
Cdd:pfam15709 404 ---EEEERKQRLQLQAA----QERARQQQEEFRR------KLQEL--QRKKQQEEAERAEAEKQRQKELEMQLAEEQKRL 468
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 1644 RLQAEEEaqkkshaQEEAEKQKLEAErdAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQ 1706
Cdd:pfam15709 469 MEMAEEE-------RLEYQRQKQEAE--EKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1673-1874 |
2.78e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 59.79 E-value: 2.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1673 KKRGKAEEAALKQKENAEKEldkqrkfAEQIAQQKLS-AEQECIRLKADFEhaeqqrglldNELQRLKNEVNSTEKQRKQ 1751
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-------AEAIKKEALLeAKEEIHKLRNEFE----------KELRERRNELQKLEKRLLQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1752 LEDELNKvrsEMDSLlqmkinaekasmvntEKSKQLLESEALKMKQLADEAARMRSVAEEA-KKQRQIAEEEAARQRSEA 1830
Cdd:PRK12704 94 KEENLDR---KLELL---------------EKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1389908286 1831 EKILKEKLaaineatRLKTEAEMALKAKEAENErLKRQAEEEAY 1874
Cdd:PRK12704 156 KEILLEKV-------EEEARHEAAVLIKEIEEE-AKEEADKKAK 191
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1701-2427 |
2.90e-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: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1701 EQIAQQKLSAEQECIRlKADFEHAEQQRGL---LDNELQRLKNEVNSTEKQRKQLEDELNKVRSemdsLLQMKINAEKAS 1777
Cdd:pfam05483 51 EQVANSGDCHYQEGLK-DSDFENSEGLSRLyskLYKEAEKIKKWKVSIEAELKQKENKLQENRK----IIEAQRKAIQEL 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1778 MVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEmALKA 1857
Cdd:pfam05483 126 QFENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFE-ELRV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1858 kEAENERLKR--QAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNI---VEETLKQKKVVEEEIHIIKIN 1932
Cdd:pfam05483 205 -QAENARLEMhfKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLtflLEESRDKANQLEEKTKLQDEN 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1933 FHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVER 2012
Cdd:pfam05483 284 LKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2013 LKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEK 2092
Cdd:pfam05483 364 LLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIF 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2093 EAALLRQKAEEAEKQ---KKAAENEAAKQA---KAQNDTEKQRKEAEEEAARRAAAEAAALKQ----------KQQADae 2156
Cdd:pfam05483 444 LLQAREKEIHDLEIQltaIKTSEEHYLKEVedlKTELEKEKLKNIELTAHCDKLLLENKELTQeasdmtlelkKHQED-- 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2157 MSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQkvlLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVK---- 2232
Cdd:pfam05483 522 IINCKKQEERMLKQIENLEEKEMNLRDELESVREE---FIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENkcnn 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2233 LKLKIEEENRRL--MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEeTARQRQIAESNLAEQRALAEKILKEKM-QAI 2309
Cdd:pfam05483 599 LKKQIENKNKNIeeLHQENKALKKKGSAENKQLNAYEIKVNKLELELA-SAKQKFEEIIDNYQKEIEDKKISEEKLlEEV 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2310 QEATKLKAEAEKLQKQKDqaqetaKRLQEDKQQIQQRLDKETEGFQKSLEaerkrqlEASAEAEKLKLRVKELSLAQTKA 2389
Cdd:pfam05483 678 EKAKAIADEAVKLQKEID------KRCQHKIAEMVALMEKHKHQYDKIIE-------ERDSELGLYKNKEQEQSSAKAAL 744
|
730 740 750
....*....|....*....|....*....|....*...
gi 1389908286 2390 EDEAKKFKKQADEVKAQLQrtekhtteivVQKLETQRL 2427
Cdd:pfam05483 745 EIELSNIKAELLSLKKQLE----------IEKEEKEKL 772
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1466-1674 |
3.03e-08 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 59.79 E-value: 3.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1466 HKAKSEAELQELRdraAEAEKLRKAAQDEAERLRKQVAEETQrkknaEDELKRKSDAEKEAaKQKQRALDDLqkykmqae 1545
Cdd:PRK12704 25 RKKIAEAKIKEAE---EEAKRILEEAKKEAEAIKKEALLEAK-----EEIHKLRNEFEKEL-RERRNELQKL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1546 eaERRMKQAEEekirqirvveevaqksaatQLQTKamsfSEQTTKLEESLKKEQGNVLKLQEEadkLKKQQKEANTAREE 1625
Cdd:PRK12704 88 --EKRLLQKEE-------------------NLDRK----LELLEKREEELEKKEKELEQKQQE---LEKKEEELEELIEE 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 1626 AEQELE----IWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKK 1674
Cdd:PRK12704 140 QLQELErisgLTAEEAKEILLEKVEEEARHEAAVLIKEIEEEAKEEADKKAKE 192
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2055-2603 |
3.57e-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: 60.08 E-value: 3.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2055 VLSKNKEDVLAQ-EKLRDEFENAKK-LAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEA 2132
Cdd:TIGR02169 227 ELLKEKEALERQkEAIERQLASLEEeLEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2133 EEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQ 2212
Cdd:TIGR02169 307 ERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDE 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2213 KSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKL------LAEEAEKMKSLAEEAGRLSVEAEETARQRQI 2286
Cdd:TIGR02169 387 LKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIagieakINELEEEKEDKALEIKKQEWKLEQLAADLSK 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2287 AESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQ---QRLDKETEGFQKSLEAERK 2363
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHgtvAQLGSVGERYATAIEVAAG 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2364 RQLEA--------SAEAEKLKLRVK--------------ELSLAQTKAEDEAKKF--------KKQADEVKAQLQRTekh 2413
Cdd:TIGR02169 547 NRLNNvvveddavAKEAIELLKRRKagratflplnkmrdERRDLSILSEDGVIGFavdlvefdPKYEPAFKYVFGDT--- 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2414 tteIVVQKLETQRLQS-------------------TREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQ--I 2472
Cdd:TIGR02169 624 ---LVVEDIEAARRLMgkyrmvtlegelfeksgamTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELrrI 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2473 EQQKAELQQSFLTEKGLLLKREKEVE---GEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVR---- 2545
Cdd:TIGR02169 701 ENRLDELSQELSDASRKIGEIEKEIEqleQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKleea 780
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 2546 ----KQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVsQTKESQ 2603
Cdd:TIGR02169 781 lndlEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEI-QELQEQ 841
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
20-127 |
3.98e-08 |
|
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin-3 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409180 Cd Length: 134 Bit Score: 55.01 E-value: 3.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 20 ERDRVQKKTFTKWVNKHLVKAqrHVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 90
Cdd:cd21331 18 EGETREERTFRNWMNSLGVNP--HVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1389908286 91 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 127
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1346-1587 |
4.36e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 58.66 E-value: 4.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1346 DEKASEKLKEEERRKMAEIQAELDKQKQMAEahaksvakaeQEalelkmKMKEEASKRQdvaADAEKQKQNIQQElqhlk 1425
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAE----------QE------RLKQLEKERL---AAQEQKKQAEEAA----- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1426 slsdQEIKSKNQQLEDAlvsrrkieeeihiiriqlEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEE 1505
Cdd:PRK09510 125 ----KQAALKQKQAEEA------------------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1506 TQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRqirvveevAQKSAATQLQTKAMSFS 1585
Cdd:PRK09510 183 AKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAA--------AEKAAAAKAAEKAAAAK 254
|
..
gi 1389908286 1586 EQ 1587
Cdd:PRK09510 255 AA 256
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4031-4067 |
4.65e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 51.71 E-value: 4.65e-08
10 20 30
....*....|....*....|....*....|....*..
gi 1389908286 4031 IRLLEAQIATGGIIDPQESHRLPVETAYERGLFDEEM 4067
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1460-1965 |
4.67e-08 |
|
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: 59.85 E-value: 4.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1460 LEKTTAHKAKSEAELQElrdraaeaEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQK 1539
Cdd:pfam12128 258 LRLSHLHFGYKSDETLI--------ASRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALED 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1540 YKMQAEEAERRMKQAEEEKIRQIRvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQgNVLKLQEEADKLKKQQKEA 1619
Cdd:pfam12128 330 QHGAFLDADIETAAADQEQLPSWQ--SELENLEERLKALTGKHQDVTAKYNRRRSKIKEQ-NNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1620 NTAREEAEQELEiwrqkaneALRLRLQAEEEAQKKShAQEEAEKQKLEAErDAKKR---GKAEEAALKQKENAEKELDKQ 1696
Cdd:pfam12128 407 DRQLAVAEDDLQ--------ALESELREQLEAGKLE-FNEEEYRLKSRLG-ELKLRlnqATATPELLLQLENFDERIERA 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1697 RKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQ------------RKQL---EDELNKV-- 1759
Cdd:pfam12128 477 REEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQlfpqagtllhflRKEApdwEQSIGKVis 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1760 -----RSEMD------------SLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAarmRSVAEEAKKQ------- 1815
Cdd:pfam12128 557 pellhRTDLDpevwdgsvggelNLYGVKLDLKRIDVPEWAASEEELRERLDKAEEALQSA---REKQAAAEEQlvqange 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1816 --RQIAEEEAARQrseAEKILKEKLAaineatRLKTEAEMALKAKEAENERLKRQAEEE----AYQRKLLEDqaaQHKQD 1889
Cdd:pfam12128 634 leKASREETFART---ALKNARLDLR------RLFDEKQSEKDKKNKALAERKDSANERlnslEAQLKQLDK---KHQAW 701
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1890 IEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfHKA--SKEKADLESELKKLkGIaDETQKSKLKAE 1965
Cdd:pfam12128 702 LEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG-AKAelKALETWYKRDLASL-GV-DPDVIAKLKRE 776
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2220-2590 |
4.78e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.40 E-value: 4.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2220 LARVRIQMEELVKLKLKIEEENRRLMQKdkdsTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQiAESNLAEQRALAE 2299
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKE----LEEELKEAEEKEEEYAELQEELEELEEELEELEA-ELEELREELEKLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2300 KIL------KEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAE 2373
Cdd:COG4717 123 KLLqllplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2374 KLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKhtteivVQKLETQR------------LQSTREADDLKSAIA 2441
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAAL------EERLKEARlllliaaallalLGLGGSLLSLILTIA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2442 DLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKA------ELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKA 2515
Cdd:COG4717 277 GVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAleeleeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2516 KALkdEQERQRKLMEEERKKL----QAIMDEAVRKQKEAEEEMKNKQREMDVLdkkrleqEKQLAEENKKLREQLQTFE 2590
Cdd:COG4717 357 EEL--EEELQLEELEQEIAALlaeaGVEDEEELRAALEQAEEYQELKEELEEL-------EEQLEELLGELEELLEALD 426
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1521-1838 |
4.96e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 59.11 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1521 DAEKEAAKQKQRalddlqkykmQAEEAERRMKQaEEEKIRQIRVVEEVAQKSAATQLQTKAMS----------FSEQTTK 1590
Cdd:pfam02029 2 EDEEEAARERRR----------RAREERRRQKE-EEEPSGQVTESVEPNEHNSYEEDSELKPSgqggldeeeaFLDRTAK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1591 LEESLKKEQGNVLKLQEEADKLKKQQKE--ANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKShaQEEAEKQKLEA 1668
Cdd:pfam02029 71 REERRQKRLQEALERQKEFDPTIADEKEsvAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIRE--KEYQENKWSTE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1669 ERDAKKRGKAEEaalkQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRglldnelqRLKNEVNSTEKQ 1748
Cdd:pfam02029 149 VRQAEEEGEEEE----DKSEEAEEVPTENFAKEEVKDEKIKKEKK---VKYESKVFLDQK--------RGHPEVKSQNGE 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1749 RKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEK-------SKQLLESEAL-KMKQLADEAA-----------RMRSVA 1809
Cdd:pfam02029 214 EEVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEQkleelrrRRQEKESEEFeKLRQKQQEAEleleelkkkreERRKLL 293
|
330 340
....*....|....*....|....*....
gi 1389908286 1810 EEAKKQRQIAEEEAARQRSEAEKILKEKL 1838
Cdd:pfam02029 294 EEEEQRRKQEEAERKLREEEEKRRMKEEI 322
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1358-1626 |
5.05e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.73 E-value: 5.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1358 RRKMAEIQAELDKQKQMAEAHA-KSVAKAEQEALELKMKMKEEASKRQDVAADAEKQ--KQNIQQELQHLKSLSDQEIKS 1434
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAkkKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1435 KNQQLEDALvsrrKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAErlrkqvAEETQRKKNAED 1514
Cdd:COG2268 271 AEANAEREV----QRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEAE------AEAIRAKGLAEA 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1515 ELKRksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAeeEKIRQIRVVEEVAQKSAATQLQTKAMsfseqtTKLEES 1594
Cdd:COG2268 341 EGKR---ALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPL--EKIDKITIIDGGNGGNGAGSAVAEAL------APLLES 409
|
250 260 270
....*....|....*....|....*....|..
gi 1389908286 1595 LKKEQGnvLKLQEEADKLKKQQKEANTAREEA 1626
Cdd:COG2268 410 LLEETG--LDLPGLLKGLTGAGAAAPAGEPAE 439
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1359-1706 |
5.23e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 58.73 E-value: 5.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1359 RKMAEIQAELdkqKQMAEAHAKSVAKaeqealelKMKMKEEASKRQDVAadaEKQKQNIQQELQ----HLKSLSDQEIKS 1434
Cdd:COG2268 116 RDPEEIEELA---EEKLEGALRAVAA--------QMTVEELNEDREKFA---EKVQEVAGTDLAknglELESVAITDLED 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1435 KNQQLeDALvSRRKIEEEihiiriqleKTTAHKAKSEAElQELRDRAAEAEKLRKAAQDEAERlrkqvaeetqrkknaed 1514
Cdd:COG2268 182 ENNYL-DAL-GRRKIAEI---------IRDARIAEAEAE-RETEIAIAQANREAEEAELEQER----------------- 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1515 ELKRKSDAEKEAAKQKQRAlddlqkykmqaeEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAmsfseqttklees 1594
Cdd:COG2268 233 EIETARIAEAEAELAKKKA------------EERREAETARAEAEAAYEIAEANAEREVQRQLEIAE------------- 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1595 lkkeqgnvlklQEEADKLKKQQKEantaREEAEQELEIwrQKANEALRLRLQAEEEAqkkshaqeEAEKQKLEAERDAKK 1674
Cdd:COG2268 288 -----------REREIELQEKEAE----REEAELEADV--RKPAEAEKQAAEAEAEA--------EAEAIRAKGLAEAEG 342
|
330 340 350
....*....|....*....|....*....|....
gi 1389908286 1675 RGKAEEAALKQKENAEKE--LDKQRKFAEQIAQQ 1706
Cdd:COG2268 343 KRALAEAWNKLGDAAILLmlIEKLPEIAEAAAKP 376
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1358-1768 |
5.61e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 59.43 E-value: 5.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1358 RRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMkeeASKRQDVaadaeKQKQniqQELQHLKSLSDQEIKSKNQ 1437
Cdd:PRK10246 425 RQRLVALHGQIVPQQKRLAQLQVAIQNVTQEQTQRNAAL---NEMRQRY-----KEKT---QQLADVKTICEQEARIKDL 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1438 QLEDALVSRRKIEEeihiiriqLEKTTAHKAKSEAELQELRD---RAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAED 1514
Cdd:PRK10246 494 EAQRAQLQAGQPCP--------LCGSTSHPAVEAYQALEPGVnqsRLDALEKEVKKLGEEGAALRGQLDALTKQLQRDES 565
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1515 ELKRKSDAEKEAAKQKQRAL----------DDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAT-QLQTKAMS 1583
Cdd:PRK10246 566 EAQSLRQEEQALTQQWQAVCaslnitlqpqDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqQIEQRQQQ 645
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1584 FSEQTTKLEESLKKEQGNVLKL---QEEADKLKKQQKEANTAREEAEQ---------------------ELEIWRQKANE 1639
Cdd:PRK10246 646 LLTALAGYALTLPQEDEEASWLatrQQEAQSWQQRQNELTALQNRIQQltplletlpqsddlphseetvALDNWRQVHEQ 725
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1640 ALRL-------RLQAEEEAQKKSHAQ---EEAEKQKLEAERDAKKRGKAEEAAL----KQKENAEKELDKQRKFAEQiAQ 1705
Cdd:PRK10246 726 CLSLhsqlqtlQQQDVLEAQRLQKAQaqfDTALQASVFDDQQAFLAALLDEETLtqleQLKQNLENQRQQAQTLVTQ-TA 804
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1706 QKLSAEQ----ECIRLKADFEHAEQQRGLLDnelQRLKNEVNSTEKQRKQL-EDELNkvRSEMDSLLQ 1768
Cdd:PRK10246 805 QALAQHQqhrpDGLDLTVTVEQIQQELAQLA---QQLRENTTRQGEIRQQLkQDADN--RQQQQALMQ 867
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1465-1899 |
5.93e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 59.54 E-value: 5.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1465 AHKAKSEAELQELRDRAA--EAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELK----RKSDAEKEAAKQKQRALDDLQ 1538
Cdd:COG4913 265 AAARERLAELEYLRAALRlwFAQRRLELLEAELEELRAELARLEAELERLEARLDalreELDELEAQIRGNGGDRLEQLE 344
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 KYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAA--TQLQTKAMSFSEQTTKLEEslkkeqgnvlKLQEEADKLKKQQ 1616
Cdd:COG4913 345 REIERLERELEERERRRARLEALLAALGLPLPASAEefAALRAEAAALLEALEEELE----------ALEEALAEAEAAL 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1617 KEANTAREEAEQELEIWRQKAN----EALRLRLQAEEEAQKKS------------HAQEE-----AEK------------ 1663
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSnipaRLLALRDALAEALGLDEaelpfvgelievRPEEErwrgaIERvlggfaltllvp 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1664 ----------------------QKLEAERDAKKRGKAEEAALKQK----EN-----AEKELDKQRKFA-----EQIAQQK 1707
Cdd:COG4913 495 pehyaaalrwvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKldfkPHpfrawLEAELGRRFDYVcvdspEELRRHP 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1708 LSAEQEC-IRLKAD-FEH---------------AEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMK 1770
Cdd:COG4913 575 RAITRAGqVKGNGTrHEKddrrrirsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLA 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1771 ------INAEKASMVNTEKSKQL--LESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEaekilkeklaaIN 1842
Cdd:COG4913 655 eyswdeIDVASAEREIAELEAELerLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKE-----------LE 723
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1843 EATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQT 1899
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA 780
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1589-1950 |
6.48e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 58.75 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1589 TKLEESLKkEQGNVLKLQEEADKLKKQQKEAntaREEAEQELEIWRQkaneALRLRLQ-AEEEAQKKSHAQEEAEKQKLE 1667
Cdd:pfam07888 34 NRLEECLQ-ERAELLQAQEAANRQREKEKER---YKRDREQWERQRR----ELESRVAeLKEELRQSREKHEELEEKYKE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1668 AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEK 1747
Cdd:pfam07888 106 LSASSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1748 QRKQLEDELNKVRSEMD----SLLQMKINAEKASMVNTEKSKQLLESEALKmkqladeaARMRSVAEEAKKQRQIAE--- 1820
Cdd:pfam07888 186 ELRSLSKEFQELRNSLAqrdtQVLQLQDTITTLTQKLTTAHRKEAENEALL--------EELRSLQERLNASERKVEglg 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1821 ---EEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEA----ENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEK 1893
Cdd:pfam07888 258 eelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRArwaqERETLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1894 ITQLQtSSDSELGRQKNIveeTLKQKKVVEEEIHIIKINFHKASKEKADLESELKKL 1950
Cdd:pfam07888 338 RMERE-KLEVELGREKDC---NRVQLSESRRELQELKASLRVAQKEKEQLQAEKQEL 390
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1526-1698 |
8.23e-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: 56.47 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1526 AAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvVEEVAQKSAAtqLQTKAMSFSEQTTKLEESLKKEQGNVLKL 1605
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHRLKELPAE-------LAELEDELAA--LEARLEAAKTELEDLEKEIKRLELEIEEV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1606 QEEADKLKKQQKEANTARE--EAEQELEIW--RQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKrgKAEEA 1681
Cdd:COG1579 72 EARIKKYEEQLGNVRNNKEyeALQKEIESLkrRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKK--AELDE 149
|
170
....*....|....*..
gi 1389908286 1682 ALKQKENAEKELDKQRK 1698
Cdd:COG1579 150 ELAELEAELEELEAERE 166
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1538-1748 |
8.26e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.89 E-value: 8.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1538 QKYKMQAEEAERRMKQAEEEKirqirvvEEVAQKSAATQLQTKAMsfsEQTTKLEESLKKEQGNVLKL----QEEADKLK 1613
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQA-------EELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQaalkQKQAEEAA 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1614 KQQKEANTAREEAEQE-LEIWRQKANEALRLRLQAEEEAQKKSHAQEEAE-KQKLEAERDAKKRGKAeEAALKQKENAEK 1691
Cdd:PRK09510 139 AKAAAAAKAKAEAEAKrAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEaEAAAKAAAEAKKKAEA-EAKKKAAAEAKK 217
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 1692 ELDKQRKFAEQ--IAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQ 1748
Cdd:PRK09510 218 KAAAEAKAAAAkaAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLFGGLDSGKNAPKTG 276
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1386-1722 |
8.45e-08 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 58.34 E-value: 8.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1386 EQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLS------DQEIKSKNQQLEDalvSRRKIEEEIHIIRIQ 1459
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGqggldeEEAFLDRTAKREE---RRQKRLQEALERQKE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1460 LEKTTAHKAKSEAElQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKnaEDELKRKSDAEKEAAKQKQralddlQK 1539
Cdd:pfam02029 89 FDPTIADEKESVAE-RKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREK--EYQENKWSTEVRQAEEEGE------EE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1540 YKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEA 1619
Cdd:pfam02029 160 EDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1620 NTAREEAEQELEIWRQKANEAlrlrlqAEEEAQKKSHAQEEAEkqkLEAERDAKKRgkaeeaalKQKENAEKELDKQRKF 1699
Cdd:pfam02029 240 AEVFLEAEQKLEELRRRRQEK------ESEEFEKLRQKQQEAE---LELEELKKKR--------EERRKLLEEEEQRRKQ 302
|
330 340
....*....|....*....|...
gi 1389908286 1700 AEqiAQQKLSAEQECIRLKADFE 1722
Cdd:pfam02029 303 EE--AERKLREEEEKRRMKEEIE 323
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1406-1665 |
9.80e-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: 57.85 E-value: 9.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1406 VAADAEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAE 1485
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQ----QEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1486 KLRKAAQDEAERLRKQVAEE--TQRKKNAEDELKRKSDAEkeAAKQKQRALDDLQKYkmqaeeAERRMKQAEEekirqir 1563
Cdd:COG4942 90 KEIAELRAELEAQKEELAELlrALYRLGRQPPLALLLSPE--DFLDAVRRLQYLKYL------APARREQAEE------- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1564 vveevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL 1643
Cdd:COG4942 155 ------LRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
250 260
....*....|....*....|....
gi 1389908286 1644 --RLQAEEEAQKKSHAQEEAEKQK 1665
Cdd:COG4942 229 iaRLEAEAAAAAERTPAAGFAALK 252
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1347-1557 |
1.15e-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: 57.16 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1347 EKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQdvAADAEKQKQNiqqelqhlks 1426
Cdd:TIGR02794 79 EAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKA--EAEAERKAKE---------- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1427 lsdqeiKSKNQQLEDALVSrrkieeeihiiriqlEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDE----AERLRKQV 1502
Cdd:TIGR02794 147 ------EAAKQAEEEAKAK---------------AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEakakAEAAKAKA 205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 1503 AEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEE 1557
Cdd:TIGR02794 206 AAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1704-1903 |
1.20e-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: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1704 AQQKLSAEQECIR-LKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLlQMKINAEKASMVNTE 1782
Cdd:COG4942 25 AEAELEQLQQEIAeLEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAEL-EKEIAELRAELEAQK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1783 KSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEN 1862
Cdd:COG4942 104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAEL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1389908286 1863 ERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDS 1903
Cdd:COG4942 184 EEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEE 224
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1592-1751 |
1.23e-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: 57.71 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1592 EESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEeeAQKKSHAQEEAEKQKLEAERD 1671
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPAD--TSSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1672 AKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKlsaeqecirlkadfeHAEQQRGLLD--NELQRLKNEVNSTEKQR 1749
Cdd:pfam05262 287 QIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDK---------------ELEAQKKREPvaEDLQKTKPQVEAQPTSL 351
|
..
gi 1389908286 1750 KQ 1751
Cdd:pfam05262 352 NE 353
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1678-1926 |
1.30e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.39 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1678 AEEAALKQKENAEKeLDKQRKFAEQIAQQKLSAE-QECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDEL 1756
Cdd:COG4913 240 AHEALEDAREQIEL-LEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1757 NKVRSEMDSLLQmkinaekasmvntekskQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKE 1836
Cdd:COG4913 319 DALREELDELEA-----------------QIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1837 KLAAINEATRLKTEAemalkakeaenERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQtssdselGRQKNIVEETL 1916
Cdd:COG4913 382 FAALRAEAAALLEAL-----------EEELEALEEALAEAEAALRDLRRELRELEAEIASLE-------RRKSNIPARLL 443
|
250
....*....|
gi 1389908286 1917 KQKKVVEEEI 1926
Cdd:COG4913 444 ALRDALAEAL 453
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1380-2040 |
1.54e-07 |
|
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: 57.81 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1380 KSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQ---ELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHII 1456
Cdd:pfam05483 85 KEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQElqfENEKVSLKLEEEIQENKDLIKENNATRHLCNLLKETC 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1457 RIQLEKTTAHKAKSEAELQELRDRAAEAEK-------LRKAAQDEAERLRKQVAEETQRKKNAEDELKRK-SDAEKEAA- 1527
Cdd:pfam05483 165 ARSAEKTKKYEYEREETRQVYMDLNNNIEKmilafeeLRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEiNDKEKQVSl 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1528 -----KQKQRALDDLQkykMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTT-----KLEESLKK 1597
Cdd:pfam05483 245 lliqiTEKENKMKDLT---FLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstqkALEEDLQI 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1598 EQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL---RLQAEEEAQKKSHAQEEAEKQKLEAERDAKK 1674
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKIITMELQKKSSELEEMTKFKN 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1675 RGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLkadFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLED 1754
Cdd:pfam05483 402 NKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFL---LQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1755 ELNK----------------------VRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMK--QLADEaarMRSVAE 1810
Cdd:pfam05483 479 ELEKeklknieltahcdklllenkelTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKemNLRDE---LESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1811 EAKKQRQ-------IAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKE---AENERLKRQAEEE-----AYQ 1875
Cdd:pfam05483 556 EFIQKGDevkckldKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEelhQENKALKKKGSAEnkqlnAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1876 RKL--LEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGI 1953
Cdd:pfam05483 636 IKVnkLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQ 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1954 ADETQKSKlkaEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLkkkaedankqkekaEKEAEK 2033
Cdd:pfam05483 716 YDKIIEER---DSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKL--------------KMEAKE 778
|
....*..
gi 1389908286 2034 QVVLAKE 2040
Cdd:pfam05483 779 NTAILKD 785
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1592-1952 |
1.66e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1592 EESLKKEQGNVLKLQEEADklkkQQKEANTAREEAEQELEIWRQKANEALRL-----RLQAE-EEAQKKSHAQEEA--EK 1663
Cdd:PRK04863 299 RRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAASDHLNLVQTALRQqekieRYQADlEELEERLEEQNEVveEA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1664 QKLEAERDAKKRgKAEEAAL---KQKENAEKELDKQRKFAEQI--AQQKLSAEQECIRLK-----------ADFEHAEQQ 1727
Cdd:PRK04863 375 DEQQEENEARAE-AAEEEVDelkSQLADYQQALDVQQTRAIQYqqAVQALERAKQLCGLPdltadnaedwlEEFQAKEQE 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1728 rglLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSllqmkINAEKASmvntEKSKQLLEsEALKMKQLADEAARMRS 1807
Cdd:PRK04863 454 ---ATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGE-----VSRSEAW----DVARELLR-RLREQRHLAEQLQQLRM 520
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1808 VAEEAKkQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALkakeaenERLKRQAEEEAYQRKLLEDQAAQHK 1887
Cdd:PRK04863 521 RLSELE-QRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARL-------ESLSESVSEARERRMALRQQLEQLQ 592
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1888 QDIEE---KITQLQTSSDSeLGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKG 1952
Cdd:PRK04863 593 ARIQRlaaRAPAWLAAQDA-LARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDE 659
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1701-2359 |
1.99e-07 |
|
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: 57.93 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1701 EQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQ----RLKNEVNSTEKQRKQLEDELN-----------KVRSEMDS 1765
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaELNQLLRTLDDQWKEKRDELNgelsaadaavaKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1766 LLQMKINAEKAsmvNTEKSKQLLESEALKMKQLADEAARM-------RSVAEEAKKQRQIAEEEAARQRSEaekiLKEKL 1838
Cdd:pfam12128 327 LEDQHGAFLDA---DIETAAADQEQLPSWQSELENLEERLkaltgkhQDVTAKYNRRRSKIKEQNNRDIAG----IKDKL 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1839 AAINEA-TRLKTEAEMALKAKEAE-NERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKItqlqtssdselgrqknIVEETL 1916
Cdd:pfam12128 400 AKIREArDRQLAVAEDDLQALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQAT----------------ATPELL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1917 KQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKklaaeeerrrkeaeekvkriTAAE 1996
Cdd:pfam12128 464 LQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQ--------------------SALD 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1997 EEAARQCKAAQEEVERLKKKAEDANKQKEKaekeaekqvVLAKEAAQKC------TAAEQKAQDVLSKNKEDVLA----- 2065
Cdd:pfam12128 524 ELELQLFPQAGTLLHFLRKEAPDWEQSIGK---------VISPELLHRTdldpevWDGSVGGELNLYGVKLDLKRidvpe 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2066 ----QEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKqkkaaENEAAKQAKAQND------TEKQRKEAEEE 2135
Cdd:pfam12128 595 waasEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR-----EETFARTALKNARldlrrlFDEKQSEKDKK 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2136 AARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQ-----LDETDKQKVLLDQELQRVKGEVNDAF 2210
Cdd:pfam12128 670 NKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAywqvvEGALDAQLALLKAAIAARRSGAKAEL 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2211 KQ-KSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDST-----------------QKLLAEEAEKMKSLAEEAGR 2272
Cdd:pfam12128 750 KAlETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQevlryfdwyqetwlqrrPRLATQLSNIERAISELQQQ 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2273 LSVEAEETARQRQIAESNLAEQRALAEKIlkekmqaIQEATKLKAEAEKLQKQK-----DQAQETAKRLQEDKQQIQQRL 2347
Cdd:pfam12128 830 LARLIADTKLRRAKLEMERKASEKQQVRL-------SENLRGLRCEMSKLATLKedansEQAQGSIGERLAQLEDLKLKR 902
|
730
....*....|..
gi 1389908286 2348 DKETEGFQKSLE 2359
Cdd:pfam12128 903 DYLSESVKKYVE 914
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1581-1804 |
2.08e-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: 2.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1581 AMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIwRQKANEALRLRLQAEEEAQKKSHAQEE 1660
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAA-LARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1661 AEKQKLEAERD--------AKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLD 1732
Cdd:COG4942 94 ELRAELEAQKEelaellraLYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEE---LRADLAELAALRAELE 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 1733 NELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSlLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAAR 1804
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLAR-LEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1460-1810 |
2.68e-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: 2.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1460 LEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQrkknAEDELKRKsdaekeaAKQKQRALDDLQK 1539
Cdd:COG3096 356 LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQ----ALDVQQTR-------AIQYQQAVQALEK 424
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1540 YKMQAEEAERRMKQAEeekirqirvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKlkkqQKEA 1619
Cdd:COG3096 425 ARALCGLPDLTPENAE----------DYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAG----EVER 490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1620 NTAREEAEQELEIWRQKANEALRLR-LQAE-EEAQKKSHAQEEAEKQkleAERDAKKRGKAEEAALkQKENAEKELDKQR 1697
Cdd:COG3096 491 SQAWQTARELLRRYRSQQALAQRLQqLRAQlAELEQRLRQQQNAERL---LEEFCQRIGQQLDAAE-ELEELLAELEAQL 566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1698 kfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLL----------DNELQRLKNEVNSTekqrkqLEDelnkvRSEMDSLL 1767
Cdd:COG3096 567 ---EELEEQAAEAVEQRSELRQQLEQLRARIKELaarapawlaaQDALERLREQSGEA------LAD-----SQEVTAAM 632
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1389908286 1768 QMKINAEKASMVNTEKS---KQLLESEALKMKQLA-DEAARMRSVAE 1810
Cdd:COG3096 633 QQLLEREREATVERDELaarKQALESQIERLSQPGgAEDPRLLALAE 679
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1351-1708 |
2.80e-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: 56.08 E-value: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1351 EKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEaskRQDVAADAEKQKQNIQQELQhlkslsdq 1430
Cdd:pfam13868 26 AQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRY---RQELEEQIEEREQKRQEEYE-------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1431 eiksknQQLEDALVSRRKIEEEIHIIRIQLEKttahKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKK 1510
Cdd:pfam13868 95 ------EKLQEREQMDEIVERIQEEDQAEAEE----KLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1511 NAEDELKRKSDAEKEAAKQKQRAlddlqkyKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKamsfsEQTTK 1590
Cdd:pfam13868 165 AEREEEREAEREEIEEEKEREIA-------RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEA-----EKKAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1591 LEESLKKEQgnvlkLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEAlrlRLQAEEEAQKKSHAQEEAEKQKLEAER 1670
Cdd:pfam13868 233 QRQELQQAR-----EEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIE---QEEAEKRRMKRLEHRRELEKQIEEREE 304
|
330 340 350
....*....|....*....|....*....|....*...
gi 1389908286 1671 dakKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKL 1708
Cdd:pfam13868 305 ---QRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2250-2442 |
3.07e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.23 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2250 DSTQKLLAEEAEKMKSLA---EEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQ-EATKLKAEAEKLQKQ 2325
Cdd:COG4913 238 ERAHEALEDAREQIELLEpirELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRaELARLEAELERLEAR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2326 KDQAQEtakRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAqtkAEDEAKKFKKQADEVKA 2405
Cdd:COG4913 318 LDALRE---ELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLP---LPASAEEFAALRAEAAA 391
|
170 180 190
....*....|....*....|....*....|....*....
gi 1389908286 2406 QLQRTEKHTTEIVVQ--KLETQRLQSTREADDLKSAIAD 2442
Cdd:COG4913 392 LLEALEEELEALEEAlaEAEAALRDLRRELRELEAEIAS 430
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1413-1708 |
3.33e-07 |
|
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: 55.81 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1413 QKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTtAHKAKSEAELQELRDR----AAEAEKLR 1488
Cdd:pfam15558 18 KEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKE-QRKARLGREERRRADRrekqVIEKESRW 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1489 KAAQDEAERLRKQ-----VAEETQRKKNAEDELKrksdaEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirQIR 1563
Cdd:pfam15558 97 REQAEDQENQRQEkleraRQEAEQRKQCQEQRLK-----EKEEELQALREQNSLQLQERLEEACHKRQLKEREE---QKK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1564 VVEEVAQKSAATQLQTKAMSFSEQTTK------LEESLKKEQGN--------VLKLQEEADKLKKQQKEANTAREEAEQE 1629
Cdd:pfam15558 169 VQENNLSELLNHQARKVLVDCQAKAEEllrrlsLEQSLQRSQENyeqlveerHRELREKAQKEEEQFQRAKWRAEEKEEE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1630 LEIWrqkanealrLRLQAEEEAQKKSHAQEEAEKQKLE-AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKL 1708
Cdd:pfam15558 249 RQEH---------KEALAELADRKIQQARQVAHKTVQDkAQRARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKE 319
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1468-1698 |
3.37e-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: 3.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1468 AKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELkrksdaekeaaKQKQRALDDLQKykmQAEEA 1547
Cdd:COG3883 12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-----------EALQAEIDKLQA---EIAEA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1548 ERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLE--ESLKKEQGNVLKLQEEA-DKLKKQQKEANTARE 1624
Cdd:COG3883 78 EAEIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSalSKIADADADLLEELKADkAELEAKKAELEAKLA 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 1625 EAEQeleiwRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRK 1698
Cdd:COG3883 158 ELEA-----LKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1492-1891 |
3.83e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.41 E-value: 3.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1492 QDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAER-----RMKQAEEEKIRqirvve 1566
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEeafldRTAKREERRQK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1567 evaqksaatqlqtkamsfseqttKLEESLKKEQGNVLKLQEEADKLkkqqkeANTAREEAEQELEIWRQKANEALRLRLQ 1646
Cdd:pfam02029 78 -----------------------RLQEALERQKEFDPTIADEKESV------AERKENNEEEENSSWEKEEKRDSRLGRY 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1647 AEEEAQKKShaQEEAEKQKLEAERDAKKRGKAEEaalkQKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQ 1726
Cdd:pfam02029 129 KEEETEIRE--KEYQENKWSTEVRQAEEEGEEEE----DKSEEAEEVPTENFAKEEVKDEKIKKEKK---VKYESKVFLD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1727 QRglldnelqRLKNEVNStekqrKQLEDELNKVRSEMDSLLQMKINAEKASmvntEKSKQLLESEALKmkqladeaarmr 1806
Cdd:pfam02029 200 QK--------RGHPEVKS-----QNGEEEVTKLKVTTKRRQGGLSQSQERE----EEAEVFLEAEQKL------------ 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1807 svaEEAKKQRQIAEEEaarqrsEAEKILKEKLAAINEATRLKTEAEMALKAKEAEnERLKRQAEEEAYQRKllEDQAAQH 1886
Cdd:pfam02029 251 ---EELRRRRQEKESE------EFEKLRQKQQEAELELEELKKKREERRKLLEEE-EQRRKQEEAERKLRE--EEEKRRM 318
|
....*
gi 1389908286 1887 KQDIE 1891
Cdd:pfam02029 319 KEEIE 323
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1381-1951 |
4.25e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.29 E-value: 4.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1381 SVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQeIKSKNQQLEDALVSRRKIEEEIHIIRIQL 1460
Cdd:pfam05557 7 SKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKR-IRLLEKREAEAEEALREQAELNRLKKKYL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1461 EktTAHKAKSEAELQElrdraAEAEKLRKAAQDEAERLRKQVAE---ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDL 1537
Cdd:pfam05557 86 E--ALNKKLNEKESQL-----ADAREVISCLKNELSELRRQIQRaelELQSTNSELEELQERLDLLKAKASEAEQLRQNL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1538 QKYKMQAEEAERRMKQAEEEkirqirvveevAQKSAATQLQTKAMsfseqttkleeslKKEQGNVLKLQEEADKLKKQQK 1617
Cdd:pfam05557 159 EKQQSSLAEAEQRIKELEFE-----------IQSQEQDSEIVKNS-------------KSELARIPELEKELERLREHNK 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1618 EANTAREEAeqelEIWRQKANEaLRLRLQAEEEAQKKShAQEEAEKQKLEAERDA-KKRGKAEEAALKQKENAekeldkq 1696
Cdd:pfam05557 215 HLNENIENK----LLLKEEVED-LKRKLEREEKYREEA-ATLELEKEKLEQELQSwVKLAQDTGLNLRSPEDL------- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1697 RKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNE-------LQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM 1769
Cdd:pfam05557 282 SRRIEQLQQREIVLKEENSSLTSSARQLEKARRELEQElaqylkkIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAI 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1770 KINAEKaSMVNTEKSKQLLEsealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRS-----EAEKILKEKLAAINEA 1844
Cdd:pfam05557 362 LESYDK-ELTMSNYSPQLLE----RIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGYKQqaqtlERELQALRQQESLADP 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1845 TRLKTEAEmALKAK----EAENERLKRQAEE---EAYQRKLLEDQ--------------AAQHKQDIEEKITQLQtssdS 1903
Cdd:pfam05557 437 SYSKEEVD-SLRRKletlELERQRLREQKNElemELERRCLQGDYdpkktkvlhlsmnpAAEAYQQRKNQLEKLQ----A 511
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1389908286 1904 ELGRQKNIVEE-TLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLK 1951
Cdd:pfam05557 512 EIERLKRLLKKlEDDLEQVLRLPETTSTMNFKEVLDLRKELESAELKNQ 560
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1412-1973 |
4.78e-07 |
|
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: 56.18 E-value: 4.78e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1412 KQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAA 1491
Cdd:TIGR04523 50 KNKEKELKNLDKNLNKDEEKINNSNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEVELNKL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1492 QDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIR---QIRVVEEV 1568
Cdd:TIGR04523 130 EKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKlelLLSNLKKK 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1569 AQKSaaTQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADK-------LKKQQKEANTAREEAEQELEIWRQK----- 1636
Cdd:TIGR04523 210 IQKN--KSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNtqtqlnqLKDEQNKIKKQLSEKQKELEQNNKKikele 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1637 ------ANEALRLRLQAEEEAQKKSHAQ-EEAEKQKLEAERDAKKRGKA------------EEAALKQKENAEK--ELDK 1695
Cdd:TIGR04523 288 kqlnqlKSEISDLNNQKEQDWNKELKSElKNQEKKLEEIQNQISQNNKIisqlneqisqlkKELTNSESENSEKqrELEE 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1696 QRKFAEQIAQQKLSAEQECIRLKAD-------FEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQ 1768
Cdd:TIGR04523 368 KQNEIEKLKKENQSYKQEIKNLESQindleskIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTN 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1769 mKINAEKASMVNTEKSKQLLESealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEaEKILKEKLAAINEATRLK 1848
Cdd:TIGR04523 448 -QDSVKELIIKNLDNTRESLET---QLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE-KKELEEKVKDLTKKISSL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1849 TEAEMALKAKEAENERLKRQAEEE------AYQRKLLEDQAAQHKQDIEEkITQLQTSSDSELGRQKNIVEETLKQKKVV 1922
Cdd:TIGR04523 523 KEKIEKLESEKKEKESKISDLEDElnkddfELKKENLEKEIDEKNKEIEE-LKQTQKSLKKKQEEKQELIDQKEKEKKDL 601
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 1923 EEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKK 1973
Cdd:TIGR04523 602 IKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKE 652
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1870-2590 |
4.93e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.34 E-value: 4.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1870 EEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKqkkvVEEEIhiikinFHKASKEKADLESELKK 1949
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ----AETEL------CAEAEEMRARLAARKQE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1950 LKGIADETQKsklKAEEEAEKLKKLAAEEERRRKEAEEKVKRItaAEEEAARQcKAAQEEVE---RLKKKAEDankqkek 2026
Cdd:pfam01576 73 LEEILHELES---RLEEEEERSQQLQNEKKKMQQHIQDLEEQL--DEEEAARQ-KLQLEKVTteaKIKKLEED------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2027 aekeaekqvVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKlrdefENAKKLAQEAEKAKEKAEKEAALLRQKA---EE 2103
Cdd:pfam01576 140 ---------ILLLEDQNSKLSKERKLLEERISEFTSNLAEEE-----EKAKSLSKLKNKHEAMISDLEERLKKEEkgrQE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2104 AEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKL 2183
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2184 QLDETDKQKVLLDQELQRVKGEVNDAFkQKSQVEVELARVRIQmeELVKLKLKIEEENRRLMQKDKDSTQK------LLA 2257
Cdd:pfam01576 286 ARNKAEKQRRDLGEELEALKTELEDTL-DTTAAQQELRSKREQ--EVTELKKALEEETRSHEAQLQEMRQKhtqaleELT 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2258 EEAEKMK-----------SLAEEAGRLSVE-------AEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEA 2319
Cdd:pfam01576 363 EQLEQAKrnkanlekakqALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSEL 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2320 EKLQKQKDQAQETAKRLQEDK-------QQIQQRLDKETEgfQKSLEAERKRQLeasaEAEKLKLRvkelslAQTKAEDE 2392
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVsslesqlQDTQELLQEETR--QKLNLSTRLRQL----EDERNSLQ------EQLEEEEE 510
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2393 AKK-FKKQADEVKAQLQRTEKHTTEI--VVQKLETQRLQSTREADDLKSaiadleeerkklkkeaeelQRKSKEMAnaqQ 2469
Cdd:pfam01576 511 AKRnVERQLSTLQAQLSDMKKKLEEDagTLEALEEGKKRLQRELEALTQ-------------------QLEEKAAA---Y 568
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2470 EQIEQQKAELQQSfLTEKGLLLKREKEV----EGEKKRFEKQLEDEmkKAKALKDEQERQRKLMEEERKKLQAI-----M 2540
Cdd:pfam01576 569 DKLEKTKNRLQQE-LDDLLVDLDHQRQLvsnlEKKQKKFDQMLAEE--KAISARYAEERDRAEAEAREKETRALslaraL 645
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2541 DEAVRKQKEAEEEMKNKQREMDVLDKKR---------LEQEKQLAEEN-KKLREQLQTFE 2590
Cdd:pfam01576 646 EEALEAKEELERTNKQLRAEMEDLVSSKddvgknvheLERSKRALEQQvEEMKTQLEELE 705
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1471-1835 |
4.95e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 56.03 E-value: 4.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1471 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKrksDAEKEAAKQKQRALDDLQKykmQAEEAERR 1550
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELK---PSGQGGLDEEEAFLDRTAK---REERRQKR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1551 MKQAEEEkirqirvveevaQKSAATQLQTKAMSFSEQTTKLEESlkkEQGNVLKLQEEADKLKKQQKEANTAREEAEQEl 1630
Cdd:pfam02029 79 LQEALER------------QKEFDPTIADEKESVAERKENNEEE---ENSSWEKEEKRDSRLGRYKEEETEIREKEYQE- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1631 EIWRQKANealrlrlQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQklsA 1710
Cdd:pfam02029 143 NKWSTEVR-------QAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN---G 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1711 EQECIRLKadFEHAEQQRGLLDNELQRLKNEV-----NSTEKQRKQLEDelnKVRSEMDSLLQMKINAE------KASMv 1779
Cdd:pfam02029 213 EEEVTKLK--VTTKRRQGGLSQSQEREEEAEVfleaeQKLEELRRRRQE---KESEEFEKLRQKQQEAEleleelKKKR- 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1780 ntEKSKQLLESEALKMKQLADEaarmRSVAEEAKKQRQiaEEEAARQRSEA-EKILK 1835
Cdd:pfam02029 287 --EERRKLLEEEEQRRKQEEAE----RKLREEEEKRRM--KEEIERRRAEAaEKRQK 335
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1459-1675 |
5.04e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 55.54 E-value: 5.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1459 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQ 1538
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 K-----YKMQAEEAERRMKQAEE--EKIRQIRVVEEVAQksaatQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADK 1611
Cdd:COG4942 108 EllralYRLGRQPPLALLLSPEDflDAVRRLQYLKYLAP-----ARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 1612 LKKQQKEANTAREEAEQELEIWRQKANEalrlrLQAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1675
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAE-----LAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2148-2635 |
5.14e-07 |
|
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: 56.28 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2148 KQKQQADAEMSKHKKEAEQALQQ-KSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEvNDAFKQKS-----QVEVELA 2221
Cdd:pfam15921 306 EQARNQNSMYMRQLSDLESTVSQlRSELREAKRMYEDKIEELEKQLVLANSELTEARTE-RDQFSQESgnlddQLQKLLA 384
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2222 RVRIQMEELVKLKlkieEENRRLMQKDKDSTQKLlaeeaekmkslaeeaGRLSVEAEETARQRQIAESNLAEQRALAEKI 2301
Cdd:pfam15921 385 DLHKREKELSLEK----EQNKRLWDRDTGNSITI---------------DHLRRELDDRNMEVQRLEALLKAMKSECQGQ 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2302 LKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQED---KQQIQQRLDKETEGFQKSLEaERKRQLEAS-AEAEKLKL 2377
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQ-EKERAIEATnAEITKLRS 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2378 RV----KELSLAQTKaEDEAKKFKKQADEVKAQLQRTEKhTTEIVVQKLE--TQRL-QSTREADDLKSaiadleeerkkl 2450
Cdd:pfam15921 525 RVdlklQELQHLKNE-GDHLRNVQTECEALKLQMAEKDK-VIEILRQQIEnmTQLVgQHGRTAGAMQV------------ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2451 kkeaeelqrkskEMANAQQEqIEQQKAELQQSfltekgLLLKREKEveGEKKRFEKQLED-EMKKAKALKDEQERQRKLM 2529
Cdd:pfam15921 591 ------------EKAQLEKE-INDRRLELQEF------KILKDKKD--AKIRELEARVSDlELEKVKLVNAGSERLRAVK 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2530 EEERKKlqaimDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEK 2609
Cdd:pfam15921 650 DIKQER-----DQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGH 724
|
490 500
....*....|....*....|....*.
gi 1389908286 2610 LVAVtTVGTSKGVLNGSTEVDGVKKE 2635
Cdd:pfam15921 725 AMKV-AMGMQKQITAKRGQIDALQSK 749
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2299-2584 |
5.22e-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: 55.73 E-value: 5.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2299 EKILKEKMQAIQEATKLKAEAEKLQKQKDqAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLR 2378
Cdd:pfam15709 214 ESKAEKKSELISKGKKTGAKRKRTQKERN-LEVAAELSGPDVINSKETEDASERGAFSSDSVVEDPWLSSKYDAEESQVS 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2379 VKELSLAQtkaedeakkfkkQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQ 2458
Cdd:pfam15709 293 IDGRSSPT------------QTFVVTGNMESEEERSEEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQ 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2459 RKSKEmanAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRfekQLEDEMKKAKALKDEQERQRKLMEEERKKLQA 2538
Cdd:pfam15709 361 RRLQQ---EQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQR---QEEEERKQRLQLQAAQERARQQQEEFRRKLQE 434
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1389908286 2539 IMDEavRKQKEAEEEMKNKQRemdvldkkRLEQEKQLAEENKKLRE 2584
Cdd:pfam15709 435 LQRK--KQQEEAERAEAEKQR--------QKELEMQLAEEQKRLME 470
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4134-4162 |
5.39e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.48 E-value: 5.39e-07
10 20
....*....|....*....|....*....
gi 1389908286 4134 IVDPESGKEMSVYEAYQKGLIDHQTYLEL 4162
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
611-703 |
5.62e-07 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 50.79 E-value: 5.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 611 HAFVVAATKELMWLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAVQTTGDKLLRDGHPARKTIEAFTA 690
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1389908286 691 ALQTQWSWLLQLC 703
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2236-2585 |
5.87e-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: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2236 KIEEENRRLMQKDKDSTQKLLAEEAEKMKSlaeEAGRLSVEAEETARQRQIAESNlAEQRALAEKILKEKMQ---AIQEA 2312
Cdd:NF033838 69 KILSEIQKSLDKRKHTQNVALNKKLSDIKT---EYLYELNVLKEKSEAELTSKTK-KELDAAFEQFKKDTLEpgkKVAEA 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2313 TKLKAEAEKlqKQKDQAQEtakrlqedkqqiqQRLDKETEGFqKSLEAERkrqleasAEAEkLKLRVKELSLAQTKAEDE 2392
Cdd:NF033838 145 TKKVEEAEK--KAKDQKEE-------------DRRNYPTNTY-KTLELEI-------AESD-VEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2393 AKKFKKQADEVKAQLQRTEKHTTEivvqKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQ--E 2470
Cdd:NF033838 201 RDEEKIKQAKAKVESKKAEATRLE----KIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPatP 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2471 QIEQQKAELQQSFLTEKGL---LLKREKEV-EGEKKRFEKQledemKKAKALKDEQERQ-----RKLMEEE--------- 2532
Cdd:NF033838 277 DKKENDAKSSDSSVGEETLpspSLKPEKKVaEAEKKVEEAK-----KKAKDQKEEDRRNyptntYKTLELEiaesdvkvk 351
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 2533 RKKLQAIMDEAVR-----KQKEAEEEMKNKQREMDVLD------KKRLEQEKQLAEENKKLREQ 2585
Cdd:NF033838 352 EAELELVKEEAKEprneeKIKQAKAKVESKKAEATRLEkiktdrKKAEEEAKRKAAEEDKVKEK 415
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1323-1606 |
6.29e-07 |
|
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: 56.38 E-value: 6.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1323 SELMTLTNQYIKFIID---AQRRLEDDEKA---SEKLKEEERRKMAEI---QAEL---DKQKQMAEAHAKSVA-KAEQEA 1389
Cdd:NF012221 1538 SESSQQADAVSKHAKQddaAQNALADKERAeadRQRLEQEKQQQLAAIsgsQSQLestDQNALETNGQAQRDAiLEESRA 1617
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1390 L--ELKMKMKE-EASKRQDVAAD----------AEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIeeeihii 1456
Cdd:NF012221 1618 VtkELTTLAQGlDALDSQATYAGesgdqwrnpfAGGLLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDA------- 1690
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1457 riqLEKTTAHKAKSEAELQELRDRAAEAEKlrKAAQDEAERLRKQvaeetQRKKNAEdelkrkSDAEKEAAKQKQRALDD 1536
Cdd:NF012221 1691 ---VAKSEAGVAQGEQNQANAEQDIDDAKA--DAEKRKDDALAKQ-----NEAQQAE------SDANAAANDAQSRGEQD 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1537 LQKYKMQAEEAE---RRMKQAEEEKIRQIRV-----------VEEVAQKSAA--TQLQTKAMS-FSEQTTKLE-ESLKKE 1598
Cdd:NF012221 1755 ASAAENKANQAQadaKGAKQDESDKPNRQGAagsglsgkaysVEGVAEPGSHinPDSPAAADGrFSEGLTEQEqEALEGA 1834
|
....*...
gi 1389908286 1599 QGNVLKLQ 1606
Cdd:NF012221 1835 TNAVNRLQ 1842
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1330-2536 |
6.93e-07 |
|
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: 56.21 E-value: 6.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1330 NQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEAL--ELKMKMKEEA------- 1400
Cdd:TIGR01612 616 NEYIKKAIDLKKIIENNNAYIDELAKISPYQVPEHLKNKDKIYSTIKSELSKIYEDDIDALynELSSIVKENAidntedk 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1401 SKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIriQLEKTTAHKAKSEAEL-QELRD 1479
Cdd:TIGR01612 696 AKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGEINK--DLNKILEDFKNKEKELsNKIND 773
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1480 RAAEAEKLRKAAQDEAErLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKykmqaeeAERRMKQAEEEKI 1559
Cdd:TIGR01612 774 YAKEKDELNKYKSKISE-IKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFK-------IINEMKFMKDDFL 845
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1560 RQIRVVEEVaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLklQEEADKLKKQQKEANTAREEAEQELEIWRqKANE 1639
Cdd:TIGR01612 846 NKVDKFINF-ENNCKEKIDSEHEQFAELTNKIKAEISDDKLNDY--EKKFNDSKSLINEINKSIEEEYQNINTLK-KVDE 921
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1640 ALRLrLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQK-----ENAEKELDKqrKFAEQIAQQKLSAEQEC 1714
Cdd:TIGR01612 922 YIKI-CENTKESIEKFHNKQNILKEILNKNIDTIKESNLIEKSYKDKfdntlIDKINELDK--AFKDASLNDYEAKNNEL 998
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1715 IRLKADFehaeqQRGLLDNELQRLKNEVNSTEKQRKQLE---DELNKVRSEMDSLLQMKI-NAEKASMVNTEKSKQLLES 1790
Cdd:TIGR01612 999 IKYFNDL-----KANLGKNKENMLYHQFDEKEKATNDIEqkiEDANKNIPNIEIAIHTSIyNIIDEIEKEIGKNIELLNK 1073
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1791 EALKMKQLAdeAARMRSVAEEAKKQR--QIAEEEAARQRSEAEKI------LKEKL-AAINEATRLKTEAEMALKAKEAE 1861
Cdd:TIGR01612 1074 EILEEAEIN--ITNFNEIKEKLKHYNfdDFGKEENIKYADEINKIkddiknLDQKIdHHIKALEEIKKKSENYIDEIKAQ 1151
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1862 NERLKRQAEEEAYQrklledqaaQHKQDIEEKITQLQTSSDselgRQKNIVEETlkqKKVVEEeihIIKInfhkaSKEKA 1941
Cdd:TIGR01612 1152 INDLEDVADKAISN---------DDPEEIEKKIENIVTKID----KKKNIYDEI---KKLLNE---IAEI-----EKDKT 1207
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1942 DLEselkKLKGIADETQKS--KLKAEEEAEKLKKlaaeeerrrkeaeekvkritaaEEEAARQCKAAQEEVERLKKKAED 2019
Cdd:TIGR01612 1208 SLE----EVKGINLSYGKNlgKLFLEKIDEEKKK----------------------SEHMIKAMEAYIEDLDEIKEKSPE 1261
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2020 ANKQKEKAEKEAEKQVVLakeaaqKCTAAEQKAQDVLSKNKEdvlaqEKLRDEFENAKKLAQEAEKAKEKaekeaallrq 2099
Cdd:TIGR01612 1262 IENEMGIEMDIKAEMETF------NISHDDDKDHHIISKKHD-----ENISDIREKSLKIIEDFSEESDI---------- 1320
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2100 kaeeaekqkkaaeneaakqakaqNDTEKQRkeaeeeaarraaaeaaalkQKQQADAEmsKHKKEAEQALQQKSQVEKELT 2179
Cdd:TIGR01612 1321 -----------------------NDIKKEL-------------------QKNLLDAQ--KHNSDINLYLNEIANIYNILK 1356
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2180 VVKLQ--LDETDKQKVLLDQELQRVKGEVNdafkqKSQVEVELARVRIQMEELvklKLKIEEEnrrLMQKDKDSTQKLLA 2257
Cdd:TIGR01612 1357 LNKIKkiIDEVKEYTKEIEENNKNIKDELD-----KSEKLIKKIKDDINLEEC---KSKIEST---LDDKDIDECIKKIK 1425
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2258 EEaeKMKSLAEEAGRLSV--EAEETARQRQIAESNLAEQRALAEKILK-EKMQAIQEA----TKLKAEAEKLQKQKDQAQ 2330
Cdd:TIGR01612 1426 EL--KNHILSEESNIDTYfkNADENNENVLLLFKNIEMADNKSQHILKiKKDNATNDHdfniNELKEHIDKSKGCKDEAD 1503
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2331 ETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASA-EAEKLKLRVKEL----SLAQTKAEDEAKKFKKQADEVKA 2405
Cdd:TIGR01612 1504 KNAKAIEKNKELFEQYKKDVTELLNKYSALAIKNKFAKTKkDSEIIIKEIKDAhkkfILEAEKSEQKIKEIKKEKFRIED 1583
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2406 QLQRTEKHTTEIV-----VQKLETQRLQST----------READDLKSAIA----DLEEERKKLKKEAEELQRKSKEMAN 2466
Cdd:TIGR01612 1584 DAAKNDKSNKAAIdiqlsLENFENKFLKISdikkkindclKETESIEKKISsfsiDSQDTELKENGDNLNSLQEFLESLK 1663
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 2467 AQQEQIEQQKAELQQsfLTEKglLLKREKEVEGEKKRFEKQLEDEMKK-AKALKDEQERQRKLMEEERKKL 2536
Cdd:TIGR01612 1664 DQKKNIEDKKKELDE--LDSE--IEKIEIDVDQHKKNYEIGIIEKIKEiAIANKEEIESIKELIEPTIENL 1730
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1606-1741 |
7.63e-07 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 55.26 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1606 QEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKShAQEEAEKQ-KLEAERDAKKRGKAEEAALK 1684
Cdd:COG2268 210 RETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET-ARAEAEAAyEIAEANAEREVQRQLEIAER 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 1685 QKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADfEHAEQQ----RGLLDNELQRLKNE 1741
Cdd:COG2268 289 EREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE-AEAEAEairaKGLAEAEGKRALAE 348
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1724-1894 |
8.29e-07 |
|
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: 53.39 E-value: 8.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1724 AEQQRGLLDneLQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEalkMKQLADEAA 1803
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEA-RLEAAKTELEDLEKEIKRLELE---IEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1804 RMRSVAEEAKKQRQIA-----EEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKL 1878
Cdd:COG1579 77 KYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1389908286 1879 LEDQAAQHKQDIEEKI 1894
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2197-2554 |
8.50e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.26 E-value: 8.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2197 QELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRL---MQKDKDSTQKLLAEEAEKMKSLAEEAGRL 2273
Cdd:pfam02029 17 EERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFldrTAKREERRQKRLQEALERQKEFDPTIADE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2274 SVEAEETARQRQIAESNLAEQRalaEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQqiqqrldketeg 2353
Cdd:pfam02029 97 KESVAERKENNEEEENSSWEKE---EKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEED------------ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2354 fqKSLEAERKRQLEASAEAEKLKLRVKELslaqtKAEDEAKKF---KKQADEVKAQlqRTEKHTTEIVVQKLETQRLQST 2430
Cdd:pfam02029 162 --KSEEAEEVPTENFAKEEVKDEKIKKEK-----KVKYESKVFldqKRGHPEVKSQ--NGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2431 READDLKSAiadlEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELqqsfltEKGLLLKREKEVEGEKKRFEKQLED 2510
Cdd:pfam02029 233 SQEREEEAE----VFLEAEQKLEELRRRRQEKESEEFEKLRQKQQEAEL------ELEELKKKREERRKLLEEEEQRRKQ 302
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1389908286 2511 EMKKAKALKDEQERQRKlMEEERKKLQAimdeAVRKQKEAEEEM 2554
Cdd:pfam02029 303 EEAERKLREEEEKRRMK-EEIERRRAEA----AEKRQKLPEDSS 341
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2148-2339 |
9.18e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 9.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2148 KQKQQADAEMSKHKKEAEQA--LQQKSQVE----KELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAfkQKSQVEVELA 2221
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAeeLQQKQAAEqerlKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEA--AAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2222 RVRIQMEELVKLKLKIEEENRRLMQKDKDSTQ----KLLAEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRAL 2297
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAaaeaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA-------EAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1389908286 2298 AEKilkeKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQED 2339
Cdd:PRK09510 221 AEA----KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1689-1885 |
9.45e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.45 E-value: 9.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1689 AEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQ 1768
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1769 -MKINAEKASMVNtekskQLLESEAL---------------KMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEK 1832
Cdd:COG3883 94 aLYRSGGSVSYLD-----VLLGSESFsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEA 168
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 1833 ILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQ 1885
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAA 221
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1462-1759 |
1.13e-06 |
|
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: 54.76 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1462 KTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSD----AEKEAAKQKQRALDDL 1537
Cdd:pfam09731 94 QSGVSSEVAEEEKEATKDAAEAKAQLPKSEQEKEKALEEVLKEAISKAESATAVAKEAKDdaiqAVKAHTDSLKEASDTA 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1538 QKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTkleESLKKEQGNVLKLQEEADKLKKQQK 1617
Cdd:pfam09731 174 EISREKATDSALQKAEALAEKLKEVINLAKQSEEEAAPPLLDAAPETPPKLP---EHLDNVEEKVEKAQSLAKLVDQYKE 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1618 EANTAREEAEQELE---------------IWRQKAN----------EALRLRLQaEEEAQKKSHAQEEAEKQKLE----- 1667
Cdd:pfam09731 251 LVASERIVFQQELVsifpdiipvlkednlLSNDDLNsliahahreiDQLSKKLA-ELKKREEKHIERALEKQKEEldkla 329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1668 -----------AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLS---AEQEcIRLKADF-----EHAEQQR 1728
Cdd:pfam09731 330 eelsarleevrAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKdvlVEQE-IELQREFlqdikEKVEEER 408
|
330 340 350
....*....|....*....|....*....|....
gi 1389908286 1729 GLLDNELQRLKNEVNSTEKQ---RKQLEDELNKV 1759
Cdd:pfam09731 409 AGRLLKLNELLANLKGLEKAtssHSEVEDENRKA 442
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1965-2352 |
1.19e-06 |
|
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: 54.52 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1965 EEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQK 2044
Cdd:pfam07888 37 EECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2045 ctaaeqkaQDVLSKNKEDvlAQEKLRDEFENAKKLAQEAEKAKEKAEKeaalLRQKAEEAEKQKKAAENE-AAKQAKAQN 2123
Cdd:pfam07888 117 --------KDALLAQRAA--HEARIRELEEDIKTLTQRVLERETELER----MKERAKKAGAQRKEEEAErKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2124 dTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKkeaeQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVK 2203
Cdd:pfam07888 183 -TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLT----QKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2204 GEVNDAFKQKSQVEVELARVRIQMEE----LVKLKLKIEEENRRlMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEE 2279
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQARLQAAQltlqLADASLALREGRAR-WAQERETLQQSAEADKDRIEKLSAELQRLEERLQE 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 2280 TARQRQIAESNLAEQRALAEKILKEKMQAIQEatkLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETE 2352
Cdd:pfam07888 337 ERMEREKLEVELGREKDCNRVQLSESRRELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2097-2601 |
1.25e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2097 LRQKAEEAEKQKKAAENEAAKQAKAQndtEKQRKEaeeeaarraaaeaaalkqkqqadaeMSKHKKEAEQALQQKSQVEK 2176
Cdd:COG4717 51 LEKEADELFKPQGRKPELNLKELKEL---EEELKE-------------------------AEEKEEEYAELQEELEELEE 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2177 ELTVVKLQLDETDKQKVLLDQELQRVkgevnDAFKQKSQVEVELARVRIQMEElvkLKLKIEEENRRLMQKdkdstQKLL 2256
Cdd:COG4717 103 ELEELEAELEELREELEKLEKLLQLL-----PLYQELEALEAELAELPERLEE---LEERLEELRELEEEL-----EELE 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2257 AEEAEKMKSLAEEAGRLSVEAEETARQrqiaesnLAEQRalaEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRL 2336
Cdd:COG4717 170 AELAELQEELEELLEQLSLATEEELQD-------LAEEL---EELQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2337 QEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAE-AEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRtekhtt 2415
Cdd:COG4717 240 ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPAL------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2416 eivvQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQ--QEQIEQQKAELQQSF-------LTE 2486
Cdd:COG4717 314 ----EELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEElqLEELEQEIAALLAEAgvedeeeLRA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2487 KGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDK 2566
Cdd:COG4717 390 ALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQLEE 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1389908286 2567 -----KRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKE 2601
Cdd:COG4717 468 dgelaELLQELEELKAELRELAEEWAALKLALELLEEARE 507
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2235-2590 |
1.29e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.96 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2235 LKIEEENRRL------MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLA---EQRALAEKI---- 2301
Cdd:PRK04863 275 MRHANERRVHleealeLRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDHLNlvqTALRQQEKIeryq 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2302 ---------LKEKMQAIQEATKLKAEAEKlqkQKDQAQETAKRLQEDKQQIQQRLD---KETEGFQKSLEA-ERKRQL-- 2366
Cdd:PRK04863 355 adleeleerLEEQNEVVEEADEQQEENEA---RAEAAEEEVDELKSQLADYQQALDvqqTRAIQYQQAVQAlERAKQLcg 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2367 EASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKhtTEIVVQKL--ETQRLQSTREAddlKSAIADLE 2444
Cdd:PRK04863 432 LPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQ--AYQLVRKIagEVSRSEAWDVA---RELLRRLR 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2445 EERKKLKKEAEELQRkskeMANAQQEQIEQQKAE-LQQSFLTEKGLLLKREKEVEGEKKRFEKQLED---EMKKAKALKD 2520
Cdd:PRK04863 507 EQRHLAEQLQQLRMR----LSELEQRLRQQQRAErLLAEFCKRLGKNLDDEDELEQLQEELEARLESlseSVSEARERRM 582
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 2521 EQERQRKLMEEERKKLQAI------MDEAV-RKQKEAEEEMKNKQREMDVLdKKRLEQEKQLAEENKKLREQLQTFE 2590
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAARapawlaAQDALaRLREQSGEEFEDSQDVTEYM-QQLLERERELTVERDELAARKQALD 658
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2205-2393 |
1.30e-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: 54.62 E-value: 1.30e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2205 EVNDAFKQKSQVEVELARVRIQMEELvklklKIEEENRRLMQKDKDSTQKllAEEAEKMKSLAEEAGRLSVEAEETARQR 2284
Cdd:pfam05262 181 KVVEALREDNEKGVNFRRDMTDLKER-----ESQEDAKRAQQLKEELDKK--QIDADKAQQKADFAQDNADKQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2285 QIAESNLAEQRALAEKILKEKMQAIQeatklKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGF--QKSLEAER 2362
Cdd:pfam05262 254 QQEAKNLPKPADTSSPKEDKQVAENQ-----KREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEaeDKELEAQK 328
|
170 180 190
....*....|....*....|....*....|.
gi 1389908286 2363 KRqLEASAEAEKLKLRVKelslAQTKAEDEA 2393
Cdd:pfam05262 329 KR-EPVAEDLQKTKPQVE----AQPTSLNED 354
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1313-1692 |
1.31e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1313 QEYVNLRTRYSELMTLTNQyIKFIIDAQRRLEDDEKASEKLKEEERR------KMAEIQAELDKQKQMAEAHAKSVAKAE 1386
Cdd:COG4717 102 EELEELEAELEELREELEK-LEKLLQLLPLYQELEALEAELAELPERleeleeRLEELRELEEELEELEAELAELQEELE 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1387 QEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQ------- 1459
Cdd:COG4717 181 ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQ----EELEELEEELEQLENELEAAALEERLKEARlllliaa 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1460 ----LEKTTAHKAKSEAELQEL-----------RDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEK 1524
Cdd:COG4717 257 allaLLGLGGSLLSLILTIAGVlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1525 EAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQ-----IRVVEEVAQKSAATQLQtKAMSFSEQTTKLEESLKKEQ 1599
Cdd:COG4717 337 EELLELLDRIEELQELLREAEELEEELQLEELEQEIAallaeAGVEDEEELRAALEQAE-EYQELKEELEELEEQLEELL 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1600 GNVLKLQEEADK--LKKQQKEANTAREEAEQELEIWRQK--ANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1675
Cdd:COG4717 416 GELEELLEALDEeeLEEELEELEEELEELEEELEELREElaELEAELEQLEEDGELAELLQELEELKAELRELAEEWAAL 495
|
410
....*....|....*..
gi 1389908286 1676 GKAEEAALKQKENAEKE 1692
Cdd:COG4717 496 KLALELLEEAREEYREE 512
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
8-125 |
1.48e-06 |
|
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: 50.11 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 8 DFMETLIQRGQDERDRVqKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQN 83
Cdd:cd21306 1 DAFDTLFDHAPDKLNVV-KKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHN 79
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908286 84 VQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 125
Cdd:cd21306 80 VQFAFELMQDAGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1421-1755 |
1.49e-06 |
|
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: 54.13 E-value: 1.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1421 LQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRK 1500
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1501 QVAEEtqrkknaedelKRKSDAEKEAAKQKQRALDDLQK---YKMQAEEAE-RRMKQAEEEKIRQIRVVEEVAQKSAATQ 1576
Cdd:pfam07888 112 ELSEE-----------KDALLAQRAAHEARIRELEEDIKtltQRVLERETElERMKERAKKAGAQRKEEEAERKQLQAKL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1577 LQTKA--MSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWR---------QKANEALRLRL 1645
Cdd:pfam07888 181 QQTEEelRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRslqerlnasERKVEGLGEEL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1646 qaEEEAQKKSHAQEEAEKQKLEAE-------------RDAKKRGKAEEAALKQkeNAEKELDKQRKFAEQIAQ-QKLSAE 1711
Cdd:pfam07888 261 --SSMAAQRDRTQAELHQARLQAAqltlqladaslalREGRARWAQERETLQQ--SAEADKDRIEKLSAELQRlEERLQE 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1712 QECIRLKADFEHAEQ------QRGLLDNELQRLKNEVNSTEKQRKQLEDE 1755
Cdd:pfam07888 337 ERMEREKLEVELGREkdcnrvQLSESRRELQELKASLRVAQKEKEQLQAE 386
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1068-1958 |
1.58e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 54.67 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1068 LTLKKMEQVYGLSSVYLDKLKTVDVVIRNTADAEEtlkNYEARLRDVSK--------VPSEQKEVEKHRSQMKSMRSEAE 1139
Cdd:TIGR00606 196 QTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKE---AQLESSREIVKsyeneldpLKNRLKEIEHNLSKIMKLDNEIK 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1140 ADQVMFDRLQDDLRKATTVHDKMTRIHSERDADLEHYRQLVNGLLERwqaVFAQIELRLRELDLLGRHMNSYRDSYEWLI 1219
Cdd:TIGR00606 273 ALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKER---ELVDCQRELEKLNKERRLLNQEKTELLVEQ 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1220 RWLT-EARQRQEKIQAvpiSDSRALREQLTDEKKLLGEIEKNKDKIDDCHK--------NAKAYIDSVKDYEFQILTYKA 1290
Cdd:TIGR00606 350 GRLQlQADRHQEHIRA---RDSLIQSLATRLELDGFERGPFSERQIKNFHTlvierqedEAKTAAQLCADLQSKERLKQE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1291 LQDPIasplkKPKMECASDDIIQEYVNLRTRYSELmtltnqyiKFIIDAQRRLEDDEKASEKLKEEERRKMAEIqaELDK 1370
Cdd:TIGR00606 427 QADEI-----RDEKKGLGRTIELKKEILEKKQEEL--------KFVIKELQQLEGSSDRILELDQELRKAEREL--SKAE 491
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1371 QKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQniQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIE 1450
Cdd:TIGR00606 492 KNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQ--MEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYF 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1451 EEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQR------KKNAEDELKRKSDAEK 1524
Cdd:TIGR00606 570 PNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcgSQDEESDLERLKEEIE 649
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1525 EAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSaaTQLQTKAMSFSEQTTKLEESLKKE------ 1598
Cdd:TIGR00606 650 KSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFI--SDLQSKLRLAPDKLKSTESELKKKekrrde 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1599 -------QGNVL--------KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL--------RLQAEEEAQKKS 1655
Cdd:TIGR00606 728 mlglapgRQSIIdlkekeipELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCltdvtimeRFQMELKDVERK 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1656 HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKAD---FEHAEQQRGLLD 1732
Cdd:TIGR00606 808 IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSEklqIGTNLQRRQQFE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1733 NELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMkiNAEKASMVNTEKSKQLLESEALKmKQLADEAARMRSVAEEa 1812
Cdd:TIGR00606 888 EQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQE--KEELISSKETSNKKAQDKVNDIK-EKVKNIHGYMKDIENK- 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1813 kkqrqiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEmalkakeaENERLKRQAEEEAYQR-KLLEDQAAQHKqdIE 1891
Cdd:TIGR00606 964 ------IQDGKDDYLKQKETELNTVNAQLEECEKHQEKIN--------EDMRLMRQDIDTQKIQeRWLQDNLTLRK--RE 1027
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 1892 EKITQLQTSSDSELGR--QKNIVEETLKQKKvVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQ 1958
Cdd:TIGR00606 1028 NELKEVEEELKQHLKEmgQMQVLQMKQEHQK-LEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1475-1777 |
1.59e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.84 E-value: 1.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1475 QELRDRAAEAEKLRKAAQDEAERLRKQVA------EETQRK--------KNAEDELKRKSDAEKEAAKQKQRALddlqky 1540
Cdd:pfam12128 600 EELRERLDKAEEALQSAREKQAAAEEQLVqangelEKASREetfartalKNARLDLRRLFDEKQSEKDKKNKAL------ 673
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1541 kmqaeeaERRMKQAEeekirqirvveevaqksaatqlqtkamsfsEQTTKLEESLKKeqgNVLKLQEEADKLKKQQKEAN 1620
Cdd:pfam12128 674 -------AERKDSAN------------------------------ERLNSLEAQLKQ---LDKKHQAWLEEQKEQKREAR 713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1621 TAREEAEQELEIWRQKANEALRLRLQAEEEAQKkshAQEEAEKQklEAERDAKKRGKAEEAALKQK---ENAEKELDKQR 1697
Cdd:pfam12128 714 TEKQAYWQVVEGALDAQLALLKAAIAARRSGAK---AELKALET--WYKRDLASLGVDPDVIAKLKreiRTLERKIERIA 788
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1698 KFAEQIAQ----QKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEV-----------NSTEKQRKQLEDELNKVRSE 1762
Cdd:pfam12128 789 VRRQEVLRyfdwYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTklrraklemerKASEKQQVRLSENLRGLRCE 868
|
330
....*....|....*
gi 1389908286 1763 MDSLLQMKINAEKAS 1777
Cdd:pfam12128 869 MSKLATLKEDANSEQ 883
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2097-2587 |
1.80e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 54.54 E-value: 1.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2097 LRQKAEEAEKQKKA---AENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQA-DAEMSKHKKEAEQALQQKS 2172
Cdd:COG4913 240 AHEALEDAREQIELlepIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEElRAELARLEAELERLEARLD 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2173 QVEKELTVVKLQLDETDkqkvllDQELQRVKGEVNDAFKQKSQVEVELARvriQMEELVKLKLKIEEEnRRLMQKDKDST 2252
Cdd:COG4913 320 ALREELDELEAQIRGNG------GDRLEQLEREIERLERELEERERRRAR---LEALLAALGLPLPAS-AEEFAALRAEA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2253 QKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKI---LKEKMQAIQEATKLKAE-----AEKLQ- 2323
Cdd:COG4913 390 AALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDALAEALGLDEAelpfvGELIEv 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2324 KQKDQAQETA----------------KRLQE-----DKQQIQQRLDkeTEGFQKSLEAERKRQLEASAEAEKLKLRVKEL 2382
Cdd:COG4913 470 RPEEERWRGAiervlggfaltllvppEHYAAalrwvNRLHLRGRLV--YERVRTGLPDPERPRLDPDSLAGKLDFKPHPF 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2383 S------LAQTKA------EDEAKKFKK---QADEVKAQLQRTEKHTTEIV-------------VQKLETQRLQSTREAD 2434
Cdd:COG4913 548 RawleaeLGRRFDyvcvdsPEELRRHPRaitRAGQVKGNGTRHEKDDRRRIrsryvlgfdnrakLAALEAELAELEEELA 627
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2435 DLKSAIADLEEERKKLKKEAEELQRKSK--------EMANAQQEQIEQQKAELQQSF--LTEkglLLKREKEVEGEKKRF 2504
Cdd:COG4913 628 EAEERLEALEAELDALQERREALQRLAEyswdeidvASAEREIAELEAELERLDASSddLAA---LEEQLEELEAELEEL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2505 EKQLEDEMKKAKALKDEQERqrklMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLRE 2584
Cdd:COG4913 705 EEELDELKGEIGRLEKELEQ----AEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRA 780
|
...
gi 1389908286 2585 QLQ 2587
Cdd:COG4913 781 RLN 783
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2270-2612 |
1.81e-06 |
|
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: 54.37 E-value: 1.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2270 AGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKL----------KAEAEKLQKQKDQAQETAKRLQED 2339
Cdd:pfam07111 58 SQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAMELdalavaekagQAEAEGLRAALAGAEMVRKNLEEG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2340 KQQI--------QQRLDKETEGFQKSLE--AERKRQLEASAEAEKLKL--RVKELSLAQTKAEDEAKKFKKQADEVKAQL 2407
Cdd:pfam07111 138 SQREleeiqrlhQEQLSSLTQAHEEALSslTSKAEGLEKSLNSLETKRagEAKQLAEAQKEAELLRKQLSKTQEELEAQV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2408 QRTE---KHTTEIVVQKLETQRLQSTREA--DDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIE--QQKAELQ 2480
Cdd:pfam07111 218 TLVEslrKYVGEQVPPEVHSQTWELERQEllDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRkiQPSDSLE 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2481 QSFLTEKGLLLKREKE-VEGEKKRFEKQLEDEMKKAKALKDE-QERQRKLMEEERKklQAIMDEAVR-KQKEAEEE---M 2554
Cdd:pfam07111 298 PEFPKKCRSLLNRWREkVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQVTSQSQE--QAILQRALQdKAAEVEVErmsA 375
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2555 KNKQREMDVLDKKRLEQEKQLAEENKKLReqlqtFEISSKTVSQTK-ESQTVSVEKLVA 2612
Cdd:pfam07111 376 KGLQMELSRAQEARRRQQQQTASAEEQLK-----FVVNAMSSTQIWlETTMTRVEQAVA 429
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1237-1670 |
1.85e-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: 54.26 E-value: 1.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1237 ISDSRALREQLTDEKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDyefQILTYKALQDPIASPL--KKPKMECASDDIIQE 1314
Cdd:TIGR04523 210 IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT---QLNQLKDEQNKIKKQLseKQKELEQNNKKIKEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1315 YVNLRTRYSELMTLTNQYIKfiiDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKM 1394
Cdd:TIGR04523 287 EKQLNQLKSEISDLNNQKEQ---DWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQR 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1395 KMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSD--QEIKSKNQQLEDALvsrRKIEEEIHIIRIQLEKTTAHKAKSEA 1472
Cdd:TIGR04523 364 ELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESkiQNQEKLNQQKDEQI---KKLQQEKELLEKEIERLKETIIKNNS 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1473 ELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKsdaeKEAAKQKQRALDDLQKYKMQAEEAERRMK 1552
Cdd:TIGR04523 441 EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQK----QKELKSKEKELKKLNEEKKELEEKVKDLT 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1553 QAEEEKIRQIRVVEevaqkSAATQLQTKAMSFSEQTTKLEESLKKEQ--GNVLKLQEEADKLKKQQKEANTAREEAEQEL 1630
Cdd:TIGR04523 517 KKISSLKEKIEKLE-----SEKKEKESKISDLEDELNKDDFELKKENleKEIDEKNKEIEELKQTQKSLKKKQEEKQELI 591
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1389908286 1631 EiwrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAER 1670
Cdd:TIGR04523 592 D---QKEKEKKDLIKEIEEKEKKISSLEKELEKAKKENEK 628
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1337-1645 |
2.11e-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: 53.38 E-value: 2.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1337 IDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQN 1416
Cdd:pfam13868 45 LDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1417 IQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAE 1496
Cdd:pfam13868 125 QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERD 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1497 RLRKQVAEETQRKKNAEdelkrksdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQ 1576
Cdd:pfam13868 205 ELRAKLYQEEQERKERQ--------KEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEI 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 1577 LQtkamsfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL 1645
Cdd:pfam13868 277 EQ-------EEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1825-2433 |
2.28e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 54.28 E-value: 2.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1825 RQRSEAEKILKEKLAAINEatrlKTEAEMALKAKEAENERLKRQAEEEAYQRKllEDQAAQHKQDIEEKITQLqtssdse 1904
Cdd:PRK02224 180 RVLSDQRGSLDQLKAQIEE----KEEKDLHERLNGLESELAELDEEIERYEEQ--REQARETRDEADEVLEEH------- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1905 lgrqknivEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEklkklaaeeerrrke 1984
Cdd:PRK02224 247 --------EERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAG--------------- 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1985 aeekvkrITAAEEEAArqcKAAQEEVERLKKKAEDAnkqkekaekeAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVL 2064
Cdd:PRK02224 304 -------LDDADAEAV---EARREELEDRDEELRDR----------LEECRVAAQAHNEEAESLREDADDLEERAEELRE 363
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2065 AQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEa 2144
Cdd:PRK02224 364 EAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERV- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2145 aalkQKQQADAEMSKHkKEAEQALQQKSQVEKeltvvklqLDETDKQKVLLDQELQRVKGEVNDafkqksqVEVELARVr 2224
Cdd:PRK02224 443 ----EEAEALLEAGKC-PECGQPVEGSPHVET--------IEEDRERVEELEAELEDLEEEVEE-------VEERLERA- 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2225 iqmEELVKLKLKIE--EENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNlAEQRALAEKIL 2302
Cdd:PRK02224 502 ---EDLVEAEDRIErlEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE-AEEAREEVAEL 577
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2303 KEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKslEAERKRQLEASAEA---EKLKLRV 2379
Cdd:PRK02224 578 NSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAE--KRERKRELEAEFDEariEEAREDK 655
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 2380 KELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREA 2433
Cdd:PRK02224 656 ERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEA 709
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1471-1727 |
2.58e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 53.45 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1471 EAELQELRDRAAEAEKLRkAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERR 1550
Cdd:PRK07735 4 EKDLEDLKKEAARRAKEE-ARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1551 MKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQEL 1630
Cdd:PRK07735 83 EEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1631 EIWRQKANEALRLR---LQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAAL-KQKEN-----AEKELDKQRKFAE 1701
Cdd:PRK07735 163 EKAKAKAAAAAKAKaaaLAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALaKQKASqgngdSGDEDAKAKAIAA 242
|
250 260
....*....|....*....|....*.
gi 1389908286 1702 QIAQQKLSAEQECIRLKADFEHAEQQ 1727
Cdd:PRK07735 243 AKAKAAAAARAKTKGAEGKKEEEPKQ 268
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
1476-1862 |
2.64e-06 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 53.57 E-value: 2.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1476 ELRDRAAEAEKLRKaaqdEAERLRKQVAEETQRKK--------NAEDELKRKSDAEKEAakqkQRALDDLQKYKMQAeea 1547
Cdd:pfam03528 5 DLQQRVAELEKENA----EFYRLKQQLEAEFNQKRakfkelylAKEEDLKRQNAVLQEA----QVELDALQNQLALA--- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1548 errmkQAEEEKIRQIRVVEEVAQKSAATQLQTKamsFSEQTTKLEeSLKKEQGNVLKLQEEAdKLKKQQKEANTAREEAE 1627
Cdd:pfam03528 74 -----RAEMENIKAVATVSENTKQEAIDEVKSQ---WQEEVASLQ-AIMKETVREYEVQFHR-RLEQERAQWNQYRESAE 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1628 QELEIWRQKANEAlrlrlQAEEEAQKK-SHAQEEAEKQkleaeRDAKKRGKAEEAALKQK-ENAEKELDKQRKFAEQIAQ 1705
Cdd:pfam03528 144 REIADLRRRLSEG-----QEEENLEDEmKKAQEDAEKL-----RSVVMPMEKEIAALKAKlTEAEDKIKELEASKMKELN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1706 QKLSAEQECirlKADFEhaeQQRGLLDNELQRLKNEvnsTEKQRKQLEDELNKVRSEMDSLLQMKINAEKAsmvntekSK 1785
Cdd:pfam03528 214 HYLEAEKSC---RTDLE---MYVAVLNTQKSVLQED---AEKLRKELHEVCHLLEQERQQHNQLKHTWQKA-------ND 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1786 QLLESEALKMKQLadeaARMRSV--------AEEAKKQRQIAEEEA-ARQRSEAEKILKEKLAAINEATRLKTEAEMALK 1856
Cdd:pfam03528 278 QFLESQRLLMRDM----QRMESVltseqlrqVEEIKKKDQEEHKRArTHKEKETLKSDREHTVSIHAVFSPAGVETSAPL 353
|
....*.
gi 1389908286 1857 AKEAEN 1862
Cdd:pfam03528 354 SNVEEQ 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1473-1947 |
2.91e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 53.77 E-value: 2.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1473 ELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAE-DELKRKSDAEKEAAKQKQRALDDLQKYKMQA-----EE 1546
Cdd:COG4913 263 RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAElARLEAELERLEARLDALREELDELEAQIRGNggdrlEQ 342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1547 AERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAM--SFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTARE 1624
Cdd:COG4913 343 LEREIERLERELEERERRRARLEALLAALGLPLPASaeEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1625 EAEQELEIWRQKAN----EALRLRLQAEEEAQKKS------------HAQEE-----AEK-------------------- 1663
Cdd:COG4913 423 ELEAEIASLERRKSnipaRLLALRDALAEALGLDEaelpfvgelievRPEEErwrgaIERvlggfaltllvppehyaaal 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1664 --------------QKLEAERDAKKRGKAEEAALKQK----EN-----AEKELDKQRKFA-----EQIAQQKLSAEQEC- 1714
Cdd:COG4913 503 rwvnrlhlrgrlvyERVRTGLPDPERPRLDPDSLAGKldfkPHpfrawLEAELGRRFDYVcvdspEELRRHPRAITRAGq 582
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1715 IRLKAD-FEHAEQQRGLLDNELQRlknevnSTEKQRKQLEDELNKVRSEMDSLlqmkinaekasmvntEKSKQLLESEAL 1793
Cdd:COG4913 583 VKGNGTrHEKDDRRRIRSRYVLGF------DNRAKLAALEAELAELEEELAEA---------------EERLEALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1794 KMKQLADEAARMRSVAEEAKKQRQIAEEEAArqrseaekiLKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEA 1873
Cdd:COG4913 642 ALQERREALQRLAEYSWDEIDVASAEREIAE---------LEAELERLDASSDDLAALEEQLEELEAELEELEEELDELK 712
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1874 YQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQ---KKVVEEEIHIIKINFHKASKEKADLESEL 1947
Cdd:COG4913 713 GEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAalgDAVERELRENLEERIDALRARLNRAEEEL 789
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
22-121 |
2.97e-06 |
|
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: 49.19 E-value: 2.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 22 DRVQKKTFTKWVNKHLVKA--QRHVTDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLKHRQVK 97
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1389908286 98 LVNIRNDDIADGNPKLTLGLIWTI 121
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2061-2545 |
3.24e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2061 EDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRA 2140
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2141 AAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKV-LLDQELQRVKGEVNDAFKQKSQVEVE 2219
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEeLLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2220 LARVRiqmEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAE 2299
Cdd:COG4717 208 LAELE---EELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2300 KILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLE-AERKRQLEASAEAEKLKLR 2378
Cdd:COG4717 285 LLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDrIEELQELLREAEELEEELQ 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2379 VKE--------LSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLeeerkkl 2450
Cdd:COG4717 365 LEEleqeiaalLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEEL------- 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2451 kkeaeelqRKSKEMANAQQEQIEQQKAELQQ--SFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKL 2528
Cdd:COG4717 438 --------EEELEELEEELEELREELAELEAelEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEY 509
|
490
....*....|....*..
gi 1389908286 2529 MEEerkKLQAIMDEAVR 2545
Cdd:COG4717 510 REE---RLPPVLERASE 523
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2051-2335 |
3.47e-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: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2051 KAQDVLSKNKEDvLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEK--- 2127
Cdd:pfam05667 204 VVPSLLERNAAE-LAAAQEWEEEWNSQGLASRLTPEEYRKRKRTKLLKRIAEQLRSAALAGTEATSGASRSAQDLAElls 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2128 ------QRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSqvEKELTVVKLQLDETDKQKVLLDQELQR 2201
Cdd:pfam05667 283 sfsgssTTDTGLTKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQQQR--EEELEELQEQLEDLESSIQELEKEIKK 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2202 VKGEVndafkqkSQVEVELARVRIQMEEL---VKLK------LKIEEENRRLMQKD-KDSTQKL--LAEEAEKMKS-LAE 2268
Cdd:pfam05667 361 LESSI-------KQVEEELEELKEQNEELekqYKVKkktldlLPDAEENIAKLQALvDASAQRLveLAGQWEKHRVpLIE 433
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2269 EAGRLSVeaeetarqrQIAESNLAEQRALAE-KILKEKMQAIQEATKLKAEAEK-LQKQKDQAQETAKR 2335
Cdd:pfam05667 434 EYRALKE---------AKSNKEDESQRKLEEiKELREKIKEVAEEAKQKEELYKqLVAEYERLPKDVSR 493
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1341-1626 |
3.92e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.41 E-value: 3.92e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1341 RRLEDDEKASEKLKE--EERrkmaeiQAELDKQKQMAEAHAKsvAKAEQEAlelkmkmkeeASKRQDVAADAEKQKQNIQ 1418
Cdd:PRK05035 439 RAIEQEKKKAEEAKArfEAR------QARLEREKAAREARHK--KAAEARA----------AKDKDAVAAALARVKAKKA 500
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1419 QELQhlKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERL 1498
Cdd:PRK05035 501 AATQ--PIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1499 RKQVAEETQRKKNaedelKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAerRMKQAEEEKIRQIRVVEEVAQKSAATQlq 1578
Cdd:PRK05035 579 KAAVAAAIARAKA-----KKAAQQAASAEPEEQVAEVDPKKAAVAAAIA--RAKAKKAEQQANAEPEEPVDPRKAAVA-- 649
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1389908286 1579 tKAMSFSeqttkleESLKKEQGNVLKLQEEADKLKKQQKEANTAREEA 1626
Cdd:PRK05035 650 -AAIARA-------KARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1459-1741 |
4.02e-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: 52.23 E-value: 4.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1459 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVaEETQRKKNAEDELKRKSDAEKeaakqKQRALDDLQ 1538
Cdd:pfam13868 60 EEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQM-DEIVERIQEEDQAEAEEKLEK-----QRQLREEID 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 KYKMQAEEAERRMKQAEEEKIRQIRvveevaqkSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1618
Cdd:pfam13868 134 EFNEEQAEWKELEKEEEREEDERIL--------EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1619 ANTAREEAEQElEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRG------KAEEAALKQKENAEKE 1692
Cdd:pfam13868 206 LRAKLYQEEQE-RKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEfermlrKQAEDEEIEQEEAEKR 284
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1693 LDKQRKFAEQIAQQKLSAEQECIRLKAD-FEHAEQQRGLLDNELQRLKNE 1741
Cdd:pfam13868 285 RMKRLEHRRELEKQIEEREEQRAAEREEeLEEGERLREEEAERRERIEEE 334
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1311-1968 |
4.21e-06 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 53.54 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1311 IIQEYVNLRTRYSEL--MTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKqkqmAEAHAKSVAKAEQE 1388
Cdd:COG5022 792 KWRLFIKLQPLLSLLgsRKEYRSYLACIIKLQKTIKREKKLRETEEVEFSLKAEVLIQKFGR----SLKAKKRFSLLKKE 867
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1389 ALELKMKMKEEASKRQDVaadaEKQKQNiqQELQHLKSLS---DQEIKSKNQQLEDalvSRRKIEEEIHIIRIQLEKtta 1465
Cdd:COG5022 868 TIYLQSAQRVELAERQLQ----ELKIDV--KSISSLKLVNlelESEIIELKKSLSS---DLIENLEFKTELIARLKK--- 935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1466 HKAKSEAELQELRdraaEAEKLRKAAQD-EAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQA 1544
Cdd:COG5022 936 LLNNIDLEEGPSI----EYVKLPELNKLhEVESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAELSKQYGAL 1011
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1545 EEAERRMKQaeeekiRQIRVVEevaqksaatqlQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTARE 1624
Cdd:COG5022 1012 QESTKQLKE------LPVEVAE-----------LQSASKIISSESTELSILKPLQKLKGLLLLENNQLQARYKALKLRRE 1074
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1625 -EAEQELEIWRQKANEALRLRLQA-EEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQ 1702
Cdd:COG5022 1075 nSLLDDKQLYQLESTENLLKTINVkDLEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVNTLEPVFQKLSVLQL 1154
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1703 IA-----QQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNStekqrkqLEDELNKVRSEMDSLLQMKI---NAE 1774
Cdd:COG5022 1155 ELdglfwEANLEALPSPPPFAALSEKRLYQSALYDEKSKLSSSEVND-------LKNELIALFSKIFSGWPRGDklkKLI 1227
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1775 KASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKqrqiaeeeaARQRSEAEKILKEKLAAI--NEATRLKTEAE 1852
Cdd:COG5022 1228 SEGWVPTEYSTSLKGFNNLNKKFDTPASMSNEKLLSLLNS---------IDNLLSSYKLEEEVLPATinSLLQYINVGLF 1298
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1853 MALKAKEAENERlkRQAEEEAYQRKLLEDQAAQHK-QDIEEKITQLQTSSDSELGRQKNIveETLKQKKVVEEEIHIIKI 1931
Cdd:COG5022 1299 NALRTKASSLRW--KSATEVNYNSEELDDWCREFEiSDVDEELEELIQAVKVLQLLKDDL--NKLDELLDACYSLNPAEI 1374
|
650 660 670
....*....|....*....|....*....|....*....
gi 1389908286 1932 NFHKASKEKADLESELKK--LKGIADETQKSKLKAEEEA 1968
Cdd:COG5022 1375 QNLKSRYDPADKENNLPKeiLKKIEALLIKQELQLSLEG 1413
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1471-1631 |
4.67e-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: 4.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1471 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQ-----KQRALDDLQKykmQAE 1545
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQlgnvrNNKEYEALQK---EIE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1546 EAERRMKQAEEEkirQIRVVEEVAQKSAATQLQTKAMSfseqttKLEESLKKEQGnvlKLQEEADKLKKQQKEANTAREE 1625
Cdd:COG1579 100 SLKRRISDLEDE---ILELMERIEELEEELAELEAELA------ELEAELEEKKA---ELDEELAELEAELEELEAEREE 167
|
....*.
gi 1389908286 1626 AEQELE 1631
Cdd:COG1579 168 LAAKIP 173
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1683-1884 |
4.88e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1683 LKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlkadfehAEQQRglldneLQRLKNEVNSTEKQRKQLEDELNKVRSE 1762
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQA----------AEQER------LKQLEKERLAAQEQKKQAEEAAKQAALK 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1763 MDsllqmkiNAEKASMVNTEKSKQLLESEAlkmKQLADEAARmrsVAEEAKKQrqiAEEEAARQRSEAEKILKEKLAAIN 1842
Cdd:PRK09510 131 QK-------QAEEAAAKAAAAAKAKAEAEA---KRAAAAAKK---AAAEAKKK---AEAEAAKKAAAEAKKKAEAEAAAK 194
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1389908286 1843 EATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAA 1884
Cdd:PRK09510 195 AAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA 236
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1819-2587 |
5.04e-06 |
|
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: 53.20 E-value: 5.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1819 AEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAEnerLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQ 1898
Cdd:pfam15921 72 GKEHIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVID---LQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQ 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1899 TSSdSELGRQKNIVEETLKQKKV--------------VEEEIHIIKINFHKASKEKA----------------------- 1941
Cdd:pfam15921 149 NTV-HELEAAKCLKEDMLEDSNTqieqlrkmmlshegVLQEIRSILVDFEEASGKKIyehdsmstmhfrslgsaiskilr 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1942 DLESELKKLKG--IADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAAR---QCKAAQEEVERLKKK 2016
Cdd:pfam15921 228 ELDTEISYLKGriFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSarsQANSIQSQLEIIQEQ 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2017 AEDANKQKEKAEKEAEKQVvlakeaaqkctaaeqkaqdvlsknkedvlaqEKLRDEFENAKKLAQeaekakekaekeaal 2096
Cdd:pfam15921 308 ARNQNSMYMRQLSDLESTV-------------------------------SQLRSELREAKRMYE--------------- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2097 lrQKAEEAEKQKKAAENEAAkQAKAQNDTEKQRKEAEEeaarraaaeaaalKQKQQADAEMSKHKKEAEQALQQKSQVEK 2176
Cdd:pfam15921 342 --DKIEELEKQLVLANSELT-EARTERDQFSQESGNLD-------------DQLQKLLADLHKREKELSLEKEQNKRLWD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2177 ELTVVKLQLDETDKQKVLLDQELQRVKGEVNdAFKQKSQVEVELARVRIQ-----MEELVKLKLKIEEENRRLMQKDKDS 2251
Cdd:pfam15921 406 RDTGNSITIDHLRRELDDRNMEVQRLEALLK-AMKSECQGQMERQMAAIQgknesLEKVSSLTAQLESTKEMLRKVVEEL 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2252 T-QKLLAEEAEKMKSlaeeagRLSVEAEETARQRQIAESNLAEQRALAEkiLKekmqaIQEATKLKAEAEKLQKQkdQAQ 2330
Cdd:pfam15921 485 TaKKMTLESSERTVS------DLTASLQEKERAIEATNAEITKLRSRVD--LK-----LQELQHLKNEGDHLRNV--QTE 549
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2331 ETAKRLQ-EDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLaqtkaedEAKKFKKQADEVKAQLQR 2409
Cdd:pfam15921 550 CEALKLQmAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRL-------ELQEFKILKDKKDAKIRE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2410 TEKHTTEIVVQKLE-----TQRLQSTREA--------DDLKSAIADLEEERKKLKKEAEELQRKSKEM---ANAQQEQIE 2473
Cdd:pfam15921 623 LEARVSDLELEKVKlvnagSERLRAVKDIkqerdqllNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMettTNKLKMQLK 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2474 QQKAELQQSFLTEKGL----------LLKREKEVEGEKKRFEKqLEDEMKKAKALKDEQERQRKLMEEERKKL-QAIMDE 2542
Cdd:pfam15921 703 SAQSELEQTRNTLKSMegsdghamkvAMGMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLsQELSTV 781
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2543 AVRKQKEA---------EEEMKNKQREMDV-LDKKRLE----QEKQLAEENKKLREQLQ 2587
Cdd:pfam15921 782 ATEKNKMAgelevlrsqERRLKEKVANMEVaLDKASLQfaecQDIIQRQEQESVRLKLQ 840
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1546-1925 |
5.22e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 53.30 E-value: 5.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1546 EAERRMKQAEEEKIRQI---RVVEEVAQKSAATQLQTKAMSFSEQTTKLE-------ESLKKEQGNVL---KLQEEADKL 1612
Cdd:NF012221 1468 DFARRAGLSTNNGIEVLwngEVVFASSGDASAWQQKTLKLTAKAGSNRLEfkgtghnDGLGYILDNVVatsESSQQADAV 1547
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1613 KKQQKEaNTAREEAEQEleiwrQKANEALRLRLQAEEEAQ----KKSHAQEEA-EKQKLEaerdakKRGKAEEAALKQKE 1687
Cdd:NF012221 1548 SKHAKQ-DDAAQNALAD-----KERAEADRQRLEQEKQQQlaaiSGSQSQLEStDQNALE------TNGQAQRDAILEES 1615
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1688 NA-EKELDKQRKFAEQIAQQKLSAEQECIRLKADFehAEqqrGLLDNelqrlknevnstekqrkqledelnkVRSEMDsl 1766
Cdd:NF012221 1616 RAvTKELTTLAQGLDALDSQATYAGESGDQWRNPF--AG---GLLDR-------------------------VQEQLD-- 1663
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1767 lqmkiNAEKASMVNTEKSKQLLESEALKMKqlaDEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATR 1846
Cdd:NF012221 1664 -----DAKKISGKQLADAKQRHVDNQQKVK---DAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQ 1735
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 1847 LKTEAEMALKAKEAENERLKRQAEEEAYQrklLEDQAAQHKQDIEEKITQlQTSSDSELGRQKNIVEETLKQKKVVEEE 1925
Cdd:NF012221 1736 AESDANAAANDAQSRGEQDASAAENKANQ---AQADAKGAKQDESDKPNR-QGAAGSGLSGKAYSVEGVAEPGSHINPD 1810
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1484-1838 |
5.33e-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: 51.84 E-value: 5.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1484 AEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRksdaEKEAAKQKQRALDDLQKykmQAEEAERRMKQAEEEKIRQIR 1563
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEK----EEERKEERKRYRQELEE---QIEEREQKRQEEYEEKLQERE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1564 VVEEVAQKsaatqlqtkamsfseqttkleeslkkeqgnvLKLQEEADKLKKQQKEANTARE--EAEQELEIWRQKANEAL 1641
Cdd:pfam13868 102 QMDEIVER-------------------------------IQEEDQAEAEEKLEKQRQLREEidEFNEEQAEWKELEKEEE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1642 RLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELdkqrkfAEQIAQQKLSAEQECIRLKADF 1721
Cdd:pfam13868 151 REEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAE------RDELRAKLYQEEQERKERQKER 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1722 EHAEQQRGLLDNELQRLKNEVnstEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADE 1801
Cdd:pfam13868 225 EEAEKKARQRQELQQAREEQI---ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
330 340 350
....*....|....*....|....*....|....*..
gi 1389908286 1802 AARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKL 1838
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
20-128 |
5.80e-06 |
|
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: 48.44 E-value: 5.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 20 ERDRVQKKTFTKWVNKhlVKAQRHVTDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 90
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908286 91 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 128
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2100-2432 |
6.51e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 52.20 E-value: 6.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2100 KAEEAEKQKKAAENEAAKQAKAQND---TEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEK 2176
Cdd:pfam07888 48 QAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAH 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2177 ELTVVKLQLD-ETDKQKVLL-DQELQRVKGEVNDAFKQKSQVEVElarvriqmEELVKLKLKIEEENRRLMQKDKDSTQK 2254
Cdd:pfam07888 128 EARIRELEEDiKTLTQRVLErETELERMKERAKKAGAQRKEEEAE--------RKQLQAKLQQTEEELRSLSKEFQELRN 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2255 LLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKmqaiQEATKLKAEAEKLQKQKDQAQ---- 2330
Cdd:pfam07888 200 SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRSLQERLNASE----RKVEGLGEELSSMAAQRDRTQaelh 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2331 --------------ETAKRLQEDKQQIQQrldkETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKF 2396
Cdd:pfam07888 276 qarlqaaqltlqlaDASLALREGRARWAQ----ERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGRE 351
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1389908286 2397 KkqaDEVKAQLQRTEKHTTEI-----VVQKLETQRLQSTRE 2432
Cdd:pfam07888 352 K---DCNRVQLSESRRELQELkaslrVAQKEKEQLQAEKQE 389
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1763-2304 |
6.56e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 6.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1763 MDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKILKEKLAAI 1841
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1842 NEATRLKTEAEMALKAKEAENERLKRQAEEeayqRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKV 1921
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEE----LRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEE 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1922 VEEEIHIIKINFHKASKEKADLESELKKLkgiadetqKSKLKAEEEAEKLKKLAAEEERrrkeaeekvkritaaeeeAAR 2001
Cdd:COG4717 204 LQQRLAELEEELEEAQEELEELEEELEQL--------ENELEAAALEERLKEARLLLLI------------------AAA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2002 QCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQkctaAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQ 2081
Cdd:COG4717 258 LLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS----LGKEAEELQALPALEELEEEELEELLAALGLPPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2082 EAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQrkeaeeeaarraAAEAAALKQKQQADAEMSKHK 2161
Cdd:COG4717 334 LSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAG------------VEDEEELRAALEQAEEYQELK 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2162 KEAEQAlqqKSQVEKELTVVKLQLDETDKQKvlLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELvklklkieEEN 2241
Cdd:COG4717 402 EELEEL---EEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELEELREELAELEAELEQL--------EED 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 2242 RRLMQKdkdstQKLLAEEAEKMKSLAEEAGRLSVEAE--ETARQRQIaESNLAEQRALAEKILKE 2304
Cdd:COG4717 469 GELAEL-----LQELEELKAELRELAEEWAALKLALEllEEAREEYR-EERLPPVLERASEYFSR 527
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1785-1946 |
7.27e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1785 KQLLESEALKMKQLAD---EAARMRsvAEEAKKQRQI-AEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEA 1860
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKE--AEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1861 ENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQT--SSDSELGRQ--KNIVEETLKqKKVVEEEIHIIKiNFHKA 1936
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQelERISGLTAEeaKEILLEKVE-EEARHEAAVLIK-EIEEE 181
|
170
....*....|
gi 1389908286 1937 SKEKADLESE 1946
Cdd:PRK12704 182 AKEEADKKAK 191
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1471-1766 |
7.49e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 52.65 E-value: 7.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1471 EAELQELRDRAAEAEKLRKAAQDEAERLRKQVaeetqrkknaedelkrksdaekEAAKQKQRALDDLQKYKM-------- 1542
Cdd:COG3096 835 EAELAALRQRRSELERELAQHRAQEQQLRQQL----------------------DQLKEQLQLLNKLLPQANlladetla 892
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1543 -QAEEAERRMKQAEEEK--IRQirvveevaQKSAATQLQTKAMSFsEQTTKLEESLKKEqgnVLKLQEEADKLKKQ---- 1615
Cdd:COG3096 893 dRLEELREELDAAQEAQafIQQ--------HGKALAQLEPLVAVL-QSDPEQFEQLQAD---YLQAKEQQRRLKQQifal 960
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1616 ----QKEANTAREEAEQELEIwRQKANEALRLRL-QAEEEAQKKSHAQEEAEKQKLEAerdakkrgKAEEAALKQKENAe 1690
Cdd:COG3096 961 sevvQRRPHFSYEDAVGLLGE-NSDLNEKLRARLeQAEEARREAREQLRQAQAQYSQY--------NQVLASLKSSRDA- 1030
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908286 1691 keldKQRKFAEqiAQQKLSAeqecIRLKADFEHAEQQRGlldnELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSL 1766
Cdd:COG3096 1031 ----KQQTLQE--LEQELEE----LGVQADAEAEERARI----RRDELHEELSQNRSRRSQLEKQLTRCEAEMDSL 1092
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2181-2387 |
7.54e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 7.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2181 VKLQLDETDKQKVLLDQELQRVKGEVNDA------FKQKS-------QVEVELARVRIQMEELVKLKLKIEEENRRLmqk 2247
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELEEAeaaleeFRQKNglvdlseEAKLLLQQLSELESQLAEARAELAEAEARL--- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2248 dkDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAES------------NLAEQRALAEKILKEKMQAIQEATK- 2314
Cdd:COG3206 243 --AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsarytpnhpdviALRAQIAALRAQLQQEAQRILASLEa 320
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 2315 ----LKAEAEKLQKQKDQAQETAKRLQEdKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQT 2387
Cdd:COG3206 321 eleaLQAREASLQAQLAQLEARLAELPE-LEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDPAVV 396
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1645-1850 |
7.79e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 52.09 E-value: 7.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1645 LQAEEEAQK-KSHAQEEAEKQKLEAERDAKkrgkaeEAALKQKENAEKEL-DKQRKFAEQiaqqklsaEQeciRLKADFE 1722
Cdd:PRK12704 34 KEAEEEAKRiLEEAKKEAEAIKKEALLEAK------EEIHKLRNEFEKELrERRNELQKL--------EK---RLLQKEE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1723 HAEQQRGLLDNELQRLKNEVNSTEKQRKQLEdelnKVRSEMDSLLQMKINA-EKASMVNTEKSKQLLesealkMKQLADE 1801
Cdd:PRK12704 97 NLDRKLELLEKREEELEKKEKELEQKQQELE----KKEEELEELIEEQLQElERISGLTAEEAKEIL------LEKVEEE 166
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1802 AarmrsVAEEAKKQRQIaEEEAarqRSEAEKILKEKLA-AIneaTRLKTE 1850
Cdd:PRK12704 167 A-----RHEAAVLIKEI-EEEA---KEEADKKAKEILAqAI---QRCAAD 204
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2265-2479 |
7.94e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 7.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2265 SLAEEAGRLSvEAEETARQRQIAESNLAEQRA--LAEKILKEKmqaiQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQ 2342
Cdd:PRK09510 59 AVVEQYNRQQ-QQQKSAKRAEEQRKKKEQQQAeeLQQKQAAEQ----ERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2343 IQQRLDKETEGFQKSLEAERKRQLEASAEAEklklrvkelSLAQTKAEDEAKKfkKQADEVKAQLQRTEKHTTEIVVQKL 2422
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---------AEAKKKAEAEAAK--KAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 2423 ETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAEL 2479
Cdd:PRK09510 203 AEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1571-1768 |
8.14e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 8.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1571 KSAATQLQTKAMSFSEQTTKLEESLK--KEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANealRLRLQAE 1648
Cdd:COG3206 174 RKALEFLEEQLPELRKELEEAEAALEefRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLA---ALRAQLG 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1649 EEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAE-KELDKQRkfAEQIAQQKLSAEQECIRLKADFEHAEQQ 1727
Cdd:COG3206 251 SGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDvIALRAQI--AALRAQLQQEAQRILASLEAELEALQAR 328
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1389908286 1728 RGLLDNELQRLKNEV---NSTEKQRKQLEDELNKVRSEMDSLLQ 1768
Cdd:COG3206 329 EASLQAQLAQLEARLaelPELEAELRRLEREVEVARELYESLLQ 372
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
25-132 |
8.28e-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: 48.50 E-value: 8.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 25 QKKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 91
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1389908286 92 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 132
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2170-2554 |
8.32e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 8.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2170 QKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDK 2249
Cdd:PRK02224 322 RDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2250 DSTQKLlAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEK-----------------ILKEKMQAIQEA 2312
Cdd:PRK02224 402 DAPVDL-GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAgkcpecgqpvegsphveTIEEDRERVEEL 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2313 TKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQqRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDE 2392
Cdd:PRK02224 481 EAELEDLEEEVEEVEERLERAEDLVEAEDRIE-RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREA 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2393 AKKFKKQADEVKAQLQRTEKHTTEIvvqKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQI 2472
Cdd:PRK02224 560 AAEAEEEAEEAREEVAELNSKLAEL---KERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2473 EQQKAELQQSFLTEKGLLLKREKE----VEGEKKRFEKQLEDEMKKAKALKDEQERQRKLmEEERKKLQAIMD--EAVRK 2546
Cdd:PRK02224 637 RELEAEFDEARIEEAREDKERAEEyleqVEEKLDELREERDDLQAEIGAVENELEELEEL-RERREALENRVEalEALYD 715
|
....*...
gi 1389908286 2547 QKEAEEEM 2554
Cdd:PRK02224 716 EAEELESM 723
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2246-2416 |
8.51e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 51.73 E-value: 8.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2246 QKDKDSTQKLLAE--EAEKMKSLAEEAGRL-SVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQ-EATKLKAEAEK 2321
Cdd:PRK09510 74 AKRAEEQRKKKEQqqAEELQQKQAAEQERLkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAaAAAKAKAEAEA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2322 lqkqkDQAQETAKRLQEDKQQiqqrldKETEGFQKSLEAERKRQLEASAEAeklklrvkelslaqtKAEDEAKKFKKQAD 2401
Cdd:PRK09510 154 -----KRAAAAAKKAAAEAKK------KAEAEAAKKAAAEAKKKAEAEAAA---------------KAAAEAKKKAEAEA 207
|
170
....*....|....*
gi 1389908286 2402 EVKAQLQRTEKHTTE 2416
Cdd:PRK09510 208 KKKAAAEAKKKAAAE 222
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1522-1777 |
1.07e-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: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1522 AEKEAAKQKQRALDDLQKykmQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQlqtkamsfsEQTTKLEESLKKEQGN 1601
Cdd:COG4942 17 AQADAAAEAEAELEQLQQ---EIAELEKELAALKKEEKALLKQLAALERRIAALA---------RRIRALEQELAALEAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1602 VLKLQEEADKLKKQQKEanTAREEAEQELEIWRQKANEALRLRLQAEEEAQkkshaqeeaekqkleAERDA---KKRGKA 1678
Cdd:COG4942 85 LAELEKEIAELRAELEA--QKEELAELLRALYRLGRQPPLALLLSPEDFLD---------------AVRRLqylKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1679 EEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLdneLQRLKNEVNSTEKQRKQLEDELNK 1758
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKL---LARLEKELAELAAELAELQQEAEE 224
|
250
....*....|....*....
gi 1389908286 1759 VRSEMDSLLQMKINAEKAS 1777
Cdd:COG4942 225 LEALIARLEAEAAAAAERT 243
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1860-1972 |
1.10e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.75 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1860 AENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQ-KKVVEEEIHIIKI---NFHK 1935
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAIKEaKKEADEIIKELRQlqkGGYA 602
|
90 100 110
....*....|....*....|....*....|....*..
gi 1389908286 1936 ASKEKaDLESELKKLKGIADETQKSKLKAEEEAEKLK 1972
Cdd:PRK00409 603 SVKAH-ELIEARKRLNKANEKKEKKKKKQKEKQEELK 638
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2761-2797 |
1.10e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.10e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908286 2761 RLLSAERAATGFKDPYTGAKISLFEAMNKGLIEKEQA 2797
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3087-3123 |
1.14e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.14e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908286 3087 RLLSAEKAVSGYHDPYTGKKVSLFEALKLGLIKKDHG 3123
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1094-1654 |
1.14e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 51.99 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1094 IRNTADAEETLKNYEARL----RDVSKVPSEQKEVEKHRSQMKSMRSEAEADQVMFDRLQDDLRKATTVHDKMTRIHSER 1169
Cdd:PRK03918 185 IKRTENIEELIKEKEKELeevlREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIREL 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1170 DADLEHYRQLVNGLLERWQAVfAQIELRLRELDLLGRHMNSYRDSYEWLIRWLTEARQRQEKIQAVpISDSRALREQLTD 1249
Cdd:PRK03918 265 EERIEELKKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER-IKELEEKEERLEE 342
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1250 EKKLLGEIEKNKDKIDDchknakayidSVKDYEfqilTYKALQDPIASpLKKPKMECASDDIIQEYVNLRTRYSELMTLT 1329
Cdd:PRK03918 343 LKKKLKELEKRLEELEE----------RHELYE----EAKAKKEELER-LKKRLTGLTPEKLEKELEELEKAKEEIEEEI 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1330 NQYIKFIIDAQRRLEDDEKASEKLK---------------EEERRKMAEIQAELDK-QKQMAEAHAK-SVAKAEQEALEL 1392
Cdd:PRK03918 408 SKITARIGELKKEIKELKKAIEELKkakgkcpvcgrelteEHRKELLEEYTAELKRiEKELKEIEEKeRKLRKELRELEK 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1393 KMKMKEEASKRQDVAadaeKQKQNIQQELqhlKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEA 1472
Cdd:PRK03918 488 VLKKESELIKLKELA----EQLKELEEKL---KKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1473 ---ELQELRDRAAEAEK-LRKAAQDEAERLRKQVAE------ETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKM 1542
Cdd:PRK03918 561 lekKLDELEEELAELLKeLEELGFESVEELEERLKElepfynEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1543 QAEEAERRMKQAE----EEKIRQIRvveevaqkSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1618
Cdd:PRK03918 641 RLEELRKELEELEkkysEEEYEELR--------EEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKE 712
|
570 580 590
....*....|....*....|....*....|....*.
gi 1389908286 1619 ANTArEEAEQELEIWRQKaneALRLRLQAEEEAQKK 1654
Cdd:PRK03918 713 LEKL-EKALERVEELREK---VKKYKALLKERALSK 744
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
129-239 |
1.17e-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: 47.49 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 129 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGKLFSAIIHKHRPALI-DMNQVYRQSNQENLEQAFSVA 207
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|..
gi 1389908286 208 ERELGVTKLLDPEDVDVPHPDEKSIITYVSSL 239
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLSQF 109
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1426-1598 |
1.20e-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: 51.54 E-value: 1.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1426 SLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAelQELRDRAAEAEKLRKAAQDEAERLRKQVAEE 1505
Cdd:pfam05262 176 SISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEEL--DKKQIDADKAQQKADFAQDNADKQRDEVRQK 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1506 TQRKKNAEDELKRKSDAEKE--AAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAAtQLQTKAMS 1583
Cdd:pfam05262 254 QQEAKNLPKPADTSSPKEDKqvAENQKREIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKEL-EAQKKREP 332
|
170
....*....|....*
gi 1389908286 1584 FSEQTTKLEESLKKE 1598
Cdd:pfam05262 333 VAEDLQKTKPQVEAQ 347
|
|
| MscS_porin |
pfam12795 |
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ... |
1509-1768 |
1.25e-05 |
|
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: 49.99 E-value: 1.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1509 KKNAEDELKRKsdAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkIRQIRvvEEVAQKSAATQLQTKAMSFSEQT 1588
Cdd:pfam12795 6 EKAKLDEAAKK--KLLQDLQQALSLLDKIDASKQRAAAYQKALDDAPAE-LRELR--QELAALQAKAEAAPKEILASLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1589 TKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEaLRLRLQAEEEAQKkshAQEEAEKQKLEA 1668
Cdd:pfam12795 81 EELEQRLLQTSAQLQELQNQLAQLNSQLIELQTRPERAQQQLSEARQRLQQ-IRNRLNGPAPPGE---PLSEAQRWALQA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1669 ERdakkrgkaeeAALKQkenaekELDKQRKfaeqiAQQKLSAEQECIRLKADFEHAEQQRglLDNELQRLKNEVNS---- 1744
Cdd:pfam12795 157 EL----------AALKA------QIDMLEQ-----ELLSNNNRQDLLKARRDLLTLRIQR--LEQQLQALQELLNEkrlq 213
|
250 260
....*....|....*....|....*
gi 1389908286 1745 -TEKQRKQLEDELNKVRSEMDSLLQ 1768
Cdd:pfam12795 214 eAEQAVAQTEQLAEEAAGDHPLVQQ 238
|
|
| Granin |
pfam01271 |
Granin (chromogranin or secretogranin); |
1345-1842 |
1.28e-05 |
|
Granin (chromogranin or secretogranin);
Pssm-ID: 279595 [Multi-domain] Cd Length: 584 Bit Score: 51.57 E-value: 1.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1345 DDEKASEKLKEEERRKMAEIQAELDKQKQmAEAHAKSVAKAE---QEALELKMKMKEEASKRQDVAADAEKQKQNIQQEL 1421
Cdd:pfam01271 69 EASHLSSRSRDGLSDEDMQIITEALRQAE-NEPGGHSRENQPyalQVEKEFKTDHSDDYETQQWEEEKLKHMRFPLRYEE 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1422 QHLKSLSDQEIKSKNQQLedalvsrrkieeeIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLrkaAQDEAERLRKQ 1501
Cdd:pfam01271 148 NSEEKHSEREGELSEVFE-------------NPRSQATLKKVFEEVSRLDTPSKQKREKSDEREKS---SQESGEDTYRQ 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1502 --VAEETQRKKNAEDElkrksDAEKEaakqkqralddlqkyKMQAEEAERRMKQaEEEKIRQIrvvEEVAQKSAATQLQT 1579
Cdd:pfam01271 212 enIPQEDQVGPEDQEP-----SEEGE---------------EDATQEEVKRSRP-RTHHGRSL---PDESSRGGQLGLEE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1580 KAMSFSEQTTKLEESLKKEQGNVLKLqEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL--RLQAEEEAQKK--- 1654
Cdd:pfam01271 268 EASEEEEEYGEESRGLSAVQTYLLRL-VNARGRGRSEKRAERERSEESEEEELKRASPYEELEItaNLQIPPSEEERmlk 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1655 ----SHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDK--QRKFAEQIAQQ-------KLSAEQECIRLKADF 1721
Cdd:pfam01271 347 kagrSPRGRVDEAGALEALEALEEKRKLDLDHSRVFESSEDGAPRapQGAWVEALRNYlsygeegMEGKWNQQGPYFPNE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1722 EHAEQQRGLLDNELQRLKNE-------VNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSkqlLESEALK 1794
Cdd:pfam01271 427 ENREEARFRLPQYLGELSNPwedpkqwKPSDFERKELTADKFLEGEEENEYTLSMKNSFPEYNYDGYEKR---VPSPGLD 503
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 1795 MKQLADEAAR---------------MRSVAEEAKKQRQIA--EEEAARQRSEAEKILKEKLAAIN 1842
Cdd:pfam01271 504 LKRQYDPVARedqllhyrkkssefpDFYDSEEKKEPPVGAekEEDSANRQTRDEDKELENLAAMD 568
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3919-3957 |
1.33e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.33e-05
10 20 30
....*....|....*....|....*....|....*....
gi 1389908286 3919 YLEGSSCIAGVYVESSKDRLSIYQAMKKNMIRPGTAFEL 3957
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2280-2586 |
1.56e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.69 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2280 TARQRQIAEsnlAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLE 2359
Cdd:pfam13868 22 KERDAQIAE---KKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQ 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2360 AERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVvqkLETQRLQSTREADdlksa 2439
Cdd:pfam13868 99 EREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI---LEYLKEKAEREEE----- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2440 iadleeeRKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQsfltekgLLLKREKEvEGEKKRFEKQLEDEMKKAKALK 2519
Cdd:pfam13868 171 -------REAEREEIEEEKEREIARLRAQQEKAQDEKAERDE-------LRAKLYQE-EQERKERQKEREEAEKKARQRQ 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 2520 DEQERQRKLMEEERKKLQaimdEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQL 2586
Cdd:pfam13868 236 ELQQAREEQIELKERRLA----EEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1468-1558 |
1.66e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 51.37 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1468 AKSEAELQELRDRAAEAEKLRKaaqdEAERLRKQVAEETQRKKNAEDELKRKSDAE--------KEAAKQKQRALDDLQK 1539
Cdd:PRK00409 523 ASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLLEEAEKEaqqaikeaKKEADEIIKELRQLQK 598
|
90 100
....*....|....*....|....*
gi 1389908286 1540 YKM------QAEEAERRMKQAEEEK 1558
Cdd:PRK00409 599 GGYasvkahELIEARKRLNKANEKK 623
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1936-2596 |
1.71e-05 |
|
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: 51.38 E-value: 1.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1936 ASKEKADLESELKKLKG--IADETQKSKLKaEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERL 2013
Cdd:pfam12128 249 EFNTLESAELRLSHLHFgyKSDETLIASRQ-EERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEAL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2014 ---KKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAA-EQKAQDVLSKNKedvlAQEKLRDEfENAKKLAQEAEKAKEK 2089
Cdd:pfam12128 328 edqHGAFLDADIETAAADQEQLPSWQSELENLEERLKAlTGKHQDVTAKYN----RRRSKIKE-QNNRDIAGIKDKLAKI 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2090 AekeaallrqkaEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALK--------------QKQQADA 2155
Cdd:pfam12128 403 R-----------EARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKlrlnqatatpelllQLENFDE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2156 EMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAfkqksqvevelarvriqMEELVKLKL 2235
Cdd:pfam12128 472 RIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDEL-----------------ELQLFPQAG 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2236 KIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETA-----RQRQI-------AESNLAEQRALAEKIL- 2302
Cdd:pfam12128 535 TLLHFLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvklDLKRIdvpewaaSEEELRERLDKAEEALq 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2303 --KEKMQAIQEA-TKLKAEAEKLQKQK-------DQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEaERKRQLEasAEA 2372
Cdd:pfam12128 615 saREKQAAAEEQlVQANGELEKASREEtfartalKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ERLNSLE--AQL 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2373 EKLKLRVKELSLAQTKAEDEAKKFKKQADEVkaqLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKK 2452
Cdd:pfam12128 692 KQLDKKHQAWLEEQKEQKREARTEKQAYWQV---VEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLASLGVDPD 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2453 EAEELQRKSKEMaNAQQEQIEQQKAE-------LQQSFLTEKGLLLKREKEVEGEKKRFEKQLedemkkaKALKDEQERQ 2525
Cdd:pfam12128 769 VIAKLKREIRTL-ERKIERIAVRRQEvlryfdwYQETWLQRRPRLATQLSNIERAISELQQQL-------ARLIADTKLR 840
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2526 RKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQR--------EMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTV 2596
Cdd:pfam12128 841 RAKLEMERKASEKQQVRLSENLRGLRCEMSKLATlkedanseQAQGSIGERLAQLEDLKLKRDYLSESVKKYVEHFKNV 919
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1401-1654 |
1.84e-05 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 50.46 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1401 SKRQDVaadAEKQKqNIQQELQHLKSLSDQeIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKseaelqeLRDR 1480
Cdd:PRK11637 51 SIQQDI---AAKEK-SVRQQQQQRASLLAQ-LKKQEEAISQASRKLRETQNTLNQLNKQIDELNASIAK-------LEQQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1481 AAEAEKLRKAAQDEAERLRKQVA-------EETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEaerrmKQ 1553
Cdd:PRK11637 119 QAAQERLLAAQLDAAFRQGEHTGlqlilsgEESQRGERILAYFGYLNQARQETIAELKQTREELAAQKAELEE-----KQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1554 AEEEKIrqirvveeVAQKSAATQLQTKAMSFSEQT-TKLEESLKKEQGNVLKL-QEEA---DKLKKQQKEantAREEAEQ 1628
Cdd:PRK11637 194 SQQKTL--------LYEQQAQQQKLEQARNERKKTlTGLESSLQKDQQQLSELrANESrlrDSIARAERE---AKARAER 262
|
250 260
....*....|....*....|....*.
gi 1389908286 1629 EleiwrqkANEALRLRlQAEEEAQKK 1654
Cdd:PRK11637 263 E-------AREAARVR-DKQKQAKRK 280
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2148-2603 |
1.99e-05 |
|
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: 51.33 E-value: 1.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2148 KQKQQADAEMSKHKKEaEQALQQKSQVEKELTVVKLQLDETDkqkvLLDQELQRVKGEvndafKQKSQVEVELARVRIQM 2227
Cdd:pfam01576 99 KKMQQHIQDLEEQLDE-EEAARQKLQLEKVTTEAKIKKLEED----ILLLEDQNSKLS-----KERKLLEERISEFTSNL 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2228 EElvklklkiEEENRRLMQKDKDSTQKLLAEEAEKMKSlaEEAGRLSVEAEETARQRQIAE--SNLAEQRALAEKILKEK 2305
Cdd:pfam01576 169 AE--------EEEKAKSLSKLKNKHEAMISDLEERLKK--EEKGRQELEKAKRKLEGESTDlqEQIAELQAQIAELRAQL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2306 MQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQrlDKETEGFQKSLEAERKRQLEASAEAEKLKL-------- 2377
Cdd:pfam01576 239 AKKEEELQAALARLEEETAQKNNALKKIRELEAQISELQE--DLESERAARNKAEKQRRDLGEELEALKTELedtldtta 316
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2378 --------RVKELSLAQTKAEDEAKKFKKQADEV-KAQLQRTEKHTTEIVVQKLETQRLQSTREAddLKSAIADLEEERK 2448
Cdd:pfam01576 317 aqqelrskREQEVTELKKALEEETRSHEAQLQEMrQKHTQALEELTEQLEQAKRNKANLEKAKQA--LESENAELQAELR 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2449 KLKKEAEELQRKSKEMANAQQE-QIEQQKAELQQSFLTEKGLLLKREKE-VEGEKKRFEKQLEDEMKKAKALKDE-QERQ 2525
Cdd:pfam01576 395 TLQQAKQDSEHKRKKLEGQLQElQARLSESERQRAELAEKLSKLQSELEsVSSLLNEAEGKNIKLSKDVSSLESQlQDTQ 474
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2526 RKLMEEERKKLQAimdeaVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQ 2603
Cdd:pfam01576 475 ELLQEETRQKLNL-----STRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEEGK 547
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1606-1797 |
2.09e-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: 50.23 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1606 QEEADKLKKQQKEANTAREEAEQELEiwRQKANEA----LRLRLQAEEEAQKKSHAQEEAEKQKLEAERdAKKRGKAEEA 1681
Cdd:TIGR02794 57 QQKKPAAKKEQERQKKLEQQAEEAEK--QRAAEQArqkeLEQRAAAEKAAKQAEQAAKQAEEKQKQAEE-AKAKQAAEAK 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1682 ALKQKENAEKELDKQRKFAEQIAQQKLSAE----QECIRLKADFEHAEQQrgllDNELQRLKNEVNSTEKQRKQLEDELN 1757
Cdd:TIGR02794 134 AKAEAEAERKAKEEAAKQAEEEAKAKAAAEakkkAEEAKKKAEAEAKAKA----EAEAKAKAEEAKAKAEAAKAKAAAEA 209
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1389908286 1758 KVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQ 1797
Cdd:TIGR02794 210 AAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1094-1918 |
2.14e-05 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 51.21 E-value: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1094 IRNTADaEETLKNYEARLRDVSKVPSEQKEVEKHRSQMKSMRSEAEADQVMFDRLQDDLR-KATTVHDKMT----RIHSE 1168
Cdd:TIGR01612 801 IDNIKD-EDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDDFLNKVDKFINFENNCKeKIDSEHEQFAeltnKIKAE 879
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1169 -RDADLEHYRQLVNGllerwqaVFAQIELRLRELDLLGRHMNSYR--DSYEWLIRWLTEARQRQEKIQAVpisdsraLRE 1245
Cdd:TIGR01612 880 iSDDKLNDYEKKFND-------SKSLINEINKSIEEEYQNINTLKkvDEYIKICENTKESIEKFHNKQNI-------LKE 945
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1246 QLTDEKKLLGE---IEKN-KDKIDDCHKNAKAYID------SVKDYEFQILTYKALQDPIASPLKKPK----------ME 1305
Cdd:TIGR01612 946 ILNKNIDTIKEsnlIEKSyKDKFDNTLIDKINELDkafkdaSLNDYEAKNNELIKYFNDLKANLGKNKenmlyhqfdeKE 1025
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1306 CASDDIIQEYVNLRTRYSELMTLTNQYIKFIID--------------------AQRRLEDDEKASEKLK--------EEE 1357
Cdd:TIGR01612 1026 KATNDIEQKIEDANKNIPNIEIAIHTSIYNIIDeiekeigkniellnkeileeAEINITNFNEIKEKLKhynfddfgKEE 1105
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1358 RRKMA----EIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADA---------EKQKQNIQQELQHL 1424
Cdd:TIGR01612 1106 NIKYAdeinKIKDDIKNLDQKIDHHIKALEEIKKKSENYIDEIKAQINDLEDVADKAisnddpeeiEKKIENIVTKIDKK 1185
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1425 KSLSDQ---------EIKSKNQQLEDalVSRRKIEEEIHIIRIQLEKTTAHKAKSE----------AELQELRDRAAEAE 1485
Cdd:TIGR01612 1186 KNIYDEikkllneiaEIEKDKTSLEE--VKGINLSYGKNLGKLFLEKIDEEKKKSEhmikameayiEDLDEIKEKSPEIE 1263
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1486 KLRKAAQDEAERLR-------KQVAEETQRKKNAED--ELKRKSDAEKEAAKQKQRALD---DLQKYKMQAEEAERRMKQ 1553
Cdd:TIGR01612 1264 NEMGIEMDIKAEMEtfnishdDDKDHHIISKKHDENisDIREKSLKIIEDFSEESDINDikkELQKNLLDAQKHNSDINL 1343
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1554 AEEE--------KIRQIR-VVEEVaqKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVlKLQEEADKLK----------- 1613
Cdd:TIGR01612 1344 YLNEianiynilKLNKIKkIIDEV--KEYTKEIEENNKNIKDELDKSEKLIKKIKDDI-NLEECKSKIEstlddkdidec 1420
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1614 -KQQKEANTAREEAEQELEIWRQKA---NEALRLRLQAEEEAQKKSHAQEEAEK-----------QKLEAERDAKKRGKA 1678
Cdd:TIGR01612 1421 iKKIKELKNHILSEESNIDTYFKNAdenNENVLLLFKNIEMADNKSQHILKIKKdnatndhdfniNELKEHIDKSKGCKD 1500
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1679 EEAALKQKENAEKELDKQRKFAEQIAQQKLSAeqecIRLKADFEHAEQQRGLLDNELQRLKN----EVNSTEKQRKQLED 1754
Cdd:TIGR01612 1501 EADKNAKAIEKNKELFEQYKKDVTELLNKYSA----LAIKNKFAKTKKDSEIIIKEIKDAHKkfilEAEKSEQKIKEIKK 1576
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1755 ElnKVRSEMDSllqMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKqrQIAEEEAARQRSEaekiL 1834
Cdd:TIGR01612 1577 E--KFRIEDDA---AKNDKSNKAAIDIQLSLENFENKFLKISDIKKKINDCLKETESIEK--KISSFSIDSQDTE----L 1645
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1835 KEKLAAINEatrLKTEAEmALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIE----EKITQLQTSSDSELGRQKN 1910
Cdd:TIGR01612 1646 KENGDNLNS---LQEFLE-SLKDQKKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEigiiEKIKEIAIANKEEIESIKE 1721
|
....*...
gi 1389908286 1911 IVEETLKQ 1918
Cdd:TIGR01612 1722 LIEPTIEN 1729
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
162-239 |
2.19e-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: 2.19e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 162 DNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQAFSvAERELGVTKLLDPEDVDVPHPDEKSIITYVSSL 239
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3917-3954 |
2.21e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.21e-05
10 20 30
....*....|....*....|....*....|....*...
gi 1389908286 3917 KKYLEGSSCIAGVYVESSKDRLSIYQAMKKNMIRPGTA 3954
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1652-1861 |
2.31e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1652 QKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlKADFEHAEQQRgll 1731
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQ----KQAEEAAAKAA--- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1732 dnELQRLKnevnsTEKQRKQLEDELNKVRSEMDsllqmKINAEKASMVNTEKSKQLLESEAlkmKQLADEAARMRSVAEE 1811
Cdd:PRK09510 143 --AAAKAK-----AEAEAKRAAAAAKKAAAEAK-----KKAEAEAAKKAAAEAKKKAEAEA---AAKAAAEAKKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 1812 AKKQRQIAEEEAARQ-RSEAEKILKEKLAAINEATRLKTEAEMALKAKEAE 1861
Cdd:PRK09510 208 KKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2264-2478 |
2.32e-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: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2264 KSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKilkekmQAIQEATKLKAEAEKLQKQKD--QAQETAKRLQEDKQ 2341
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK------QRAAEQARQKELEQRAAAEKAakQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2342 QIQQRLDKETEGFQKSLEAERKRQLEA----SAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTE-KHTTE 2416
Cdd:TIGR02794 120 QAEEAKAKQAAEAKAKAEAEAERKAKEeaakQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEaKAKAE 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 2417 IVVQKLETqrlQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAE 2478
Cdd:TIGR02794 200 AAKAKAAA---EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3457-3492 |
2.37e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.37e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1389908286 3457 LLEAQLATGGIIDPASSHRVPTDVAIQRGYFSKQMA 3492
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2195-2549 |
2.58e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.82 E-value: 2.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2195 LDQELQRVKGEVNDAfkQKSQVEVELARVRIQMEElvklklKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEagRLS 2274
Cdd:PRK10929 28 ITQELEQAKAAKTPA--QAEIVEALQSALNWLEER------KGSLERAKQYQQVIDNFPKLSAELRQQLNNERDE--PRS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2275 VEAEETARqrqiaesnlaeqrALAEKILKEKMQAIQEATKLKAEAEKLQKQKD------QAQETAKRLQEDkqqIQQRLd 2348
Cdd:PRK10929 98 VPPNMSTD-------------ALEQEILQVSSQLLEKSRQAQQEQDRAREISDslsqlpQQQTEARRQLNE---IERRL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2349 ketEGFQKSLEAERKRQLEA-SAEAEKLKLRVKELSLAQTKAED-------EAKKFKKQADEVKAQLQRTEKHTTEIVVQ 2420
Cdd:PRK10929 161 ---QTLGTPNTPLAQAQLTAlQAESAALKALVDELELAQLSANNrqelarlRSELAKKRSQQLDAYLQALRNQLNSQRQR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2421 KLEtQRLQSTR----EADDLKSAIADlEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQ--SFLTEKGLLLKrE 2494
Cdd:PRK10929 238 EAE-RALESTEllaeQSGDLPKSIVA-QFKINRELSQALNQQAQRMDLIASQQRQAASQTLQVRQalNTLREQSQWLG-V 314
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908286 2495 KEVEGEKKRFE----------KQLEDEMKK--AKALK--DEQERQRKLMEEERKKLQA-------IMDEAVRKQKE 2549
Cdd:PRK10929 315 SNALGEALRAQvarlpempkpQQLDTEMAQlrVQRLRyeDLLNKQPQLRQIRQADGQPltaeqnrILDAQLRTQRE 390
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3418-3454 |
2.69e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.69e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908286 3418 KLLSAEKAITGYRDPYTGNKISLFQAMKKELVLREHA 3454
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1459-1688 |
2.77e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 50.99 E-value: 2.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1459 QLEKTTAHKAKSEAELQELRDRA-AEAEKLRkaAQDEAERLRKQVAEeTQRKKNAEDE--LKRKSDAEKEAAKQKQRA-- 1533
Cdd:NF012221 1543 QADAVSKHAKQDDAAQNALADKErAEADRQR--LEQEKQQQLAAISG-SQSQLESTDQnaLETNGQAQRDAILEESRAvt 1619
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1534 ---------LDDLQKYKMQAEEAERRMKQAEEEKIRQiRVVEEV--AQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNV 1602
Cdd:NF012221 1620 kelttlaqgLDALDSQATYAGESGDQWRNPFAGGLLD-RVQEQLddAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGV 1698
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1603 LKLQEeadklKKQQKEANTAREEAEQEleiwrQKANEALRlrlqAEEEAQK-KSHAQEEAEKQKLEAERDAKKRG----- 1676
Cdd:NF012221 1699 AQGEQ-----NQANAEQDIDDAKADAE-----KRKDDALA----KQNEAQQaESDANAAANDAQSRGEQDASAAEnkanq 1764
|
250
....*....|...
gi 1389908286 1677 -KAEEAALKQKEN 1688
Cdd:NF012221 1765 aQADAKGAKQDES 1777
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4127-4155 |
2.97e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.62 E-value: 2.97e-05
10 20
....*....|....*....|....*....
gi 1389908286 4127 VRKRRVVIVDPESGKEMSVYEAYQKGLID 4155
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2311-2568 |
3.13e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 50.68 E-value: 3.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2311 EATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQ--QRLDKETEGFQKSL-EAERKRQLEASAEAEKLKLRVKELSLAQT 2387
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEALEDAREQIEllEPIRELAERYAAAReRLAELEYLRAALRLWFAQRRLELLEAELE 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2388 KAEDEAKKFKKQADEVKAQLQRTEKHtteivVQKLETQRLQS-TREADDLKSAIADleeerkklkkeaeelqrkskemAN 2466
Cdd:COG4913 299 ELRAELARLEAELERLEARLDALREE-----LDELEAQIRGNgGDRLEQLEREIER----------------------LE 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2467 AQQEQIEQQKAELQQsFLTEKGLllkrekEVEGEKKRFEKQLEdemkKAKALKDEQERQRKLMEEERkklqaimDEAVRK 2546
Cdd:COG4913 352 RELEERERRRARLEA-LLAALGL------PLPASAEEFAALRA----EAAALLEALEEELEALEEAL-------AEAEAA 413
|
250 260
....*....|....*....|..
gi 1389908286 2547 QKEAEEEMKNKQREMDVLDKKR 2568
Cdd:COG4913 414 LRDLRRELRELEAEIASLERRK 435
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1610-1974 |
3.23e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 50.12 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1610 DKLKKQQKEANTAREEAEqeleiwrqkaNEALRLRLQAEEEAQKKSHAQEEAEK-QKLEAERDAKKRGKAEEAALKQK-- 1686
Cdd:pfam05557 16 NEKKQMELEHKRARIELE----------KKASALKRQLDRESDRNQELQKRIRLlEKREAEAEEALREQAELNRLKKKyl 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1687 ENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLkNEVNSTEKQRKQledELNKVRSEMDSL 1766
Cdd:pfam05557 86 EALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEEL-QERLDLLKAKAS---EAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1767 LQMKINAEkASMVNTEKSKQLLESEALKMKQLADEAARMRSVaeEAKKQRQIAEEEAARQRSEAEKILKEKLAAINeaTR 1846
Cdd:pfam05557 162 QSSLAEAE-QRIKELEFEIQSQEQDSEIVKNSKSELARIPEL--EKELERLREHNKHLNENIENKLLLKEEVEDLK--RK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1847 LKTEAEMALKAKEAENERLKRQAEEEAYQrKLLEDQAAQHK--QDIEEKITQLQtSSDSELGRQKNIVEETLKQKKVVEE 1924
Cdd:pfam05557 237 LEREEKYREEAATLELEKEKLEQELQSWV-KLAQDTGLNLRspEDLSRRIEQLQ-QREIVLKEENSSLTSSARQLEKARR 314
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1925 EIHIIKINfhkASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKL 1974
Cdd:pfam05557 315 ELEQELAQ---YLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERDGYRAI 361
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1362-1774 |
3.37e-05 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 50.30 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1362 AEIQAELD---KQKQmAEAHAKSVAKAEQEALEL---KMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSK 1435
Cdd:PRK11281 39 ADVQAQLDalnKQKL-LEAEDKLVQQDLEQTLALldkIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRET 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1436 -----NQQLEDALVSRRkieeeihiiriqlekttahkakseAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKK 1510
Cdd:PRK11281 118 lstlsLRQLESRLAQTL------------------------DQLQNAQNDLAEYNSQLVSLQTQPERAQAALYANSQRLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1511 NAEDELKrKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRM-------------KQAEEEKIRQIRVVEEVAqksaatQL 1577
Cdd:PRK11281 174 QIRNLLK-GGKVGGKALRPSQRVLLQAEQALLNAQNDLQRKslegntqlqdllqKQRDYLTARIQRLEHQLQ------LL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1578 QT----KAMSFSEQTTKLEESLKKEQgnvlklQEEADKLKKQQKEANTareEAEQELEIWRQKANEALRLRLQAeeeaqk 1653
Cdd:PRK11281 247 QEainsKRLTLSEKTVQEAQSQDEAA------RIQANPLVAQELEINL---QLSQRLLKATEKLNTLTQQNLRV------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1654 kshaqeeaeKQKLE----AERDAKKRGKAEEAAL-------KQKENAEKeLDKQRKFAEQIAQqklsaeqecIRLKAdFE 1722
Cdd:PRK11281 312 ---------KNWLDrltqSERNIKEQISVLKGSLllsrilyQQQQALPS-ADLIEGLADRIAD---------LRLEQ-FE 371
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1723 hAEQQRGLL-------DNELQRLKNEVNSTEKQ--------RKQLEDELNKvrsEMDSLLQMKINAE 1774
Cdd:PRK11281 372 -INQQRDALfqpdayiDKLEAGHKSEVTDEVRDallqlldeRRELLDQLNK---QLNNQLNLAINLQ 434
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
25-133 |
3.80e-05 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 46.97 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 25 QKKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 91
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908286 92 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 133
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
31-121 |
3.82e-05 |
|
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: 45.75 E-value: 3.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 31 KWVNKHLVKAQR---HVTDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLkhRQVKLVN-IRN 103
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1389908286 104 DDIADGNPKLTLGLIWTI 121
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2368-2587 |
3.99e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 49.38 E-value: 3.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2368 ASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKH--TTEIVVQKLETQRLQSTREADDLKSAIADlee 2445
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaALARRIRALEQELAALEAELAELEKEIAE--- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2446 erkklkkeaeelQRKSKEmanAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgekkrfekQLEDEMKKAKALKDEQERQ 2525
Cdd:COG4942 95 ------------LRAELE---AQKEELAELLRALYRLGRQPPLALLLSPEDFL--------DAVRRLQYLKYLAPARREQ 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 2526 RKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQ 2587
Cdd:COG4942 152 AEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAA 213
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2177-2576 |
4.29e-05 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 49.90 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2177 ELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIeeenrrlmqKDKDSTQKLL 2256
Cdd:PRK01156 198 ELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI---------KTAESDLSME 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2257 AEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRL 2336
Cdd:PRK01156 269 LEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKKKSRY 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2337 QEDKQQIQQRLDKETE--GFQKSLEAERKRQLEASAEAEKLKlrvKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHT 2414
Cdd:PRK01156 349 DDLNNQILELEGYEMDynSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEINVKLQDISSKV 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2415 TEIvvqkleTQRLQSTRE-ADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQsfltekgllLKR 2493
Cdd:PRK01156 426 SSL------NQRIRALREnLDELSRNMEMLNGQSVCPVCGTTLGEEKSNHIINHYNEKKSRLEEKIRE---------IEI 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2494 EKEVEGEKKRFEKQLEDEMKKAKAlkDEQERQRKLMEEERKKLQAIMD-EAVRKQKEAE-EEMKNKQREMDV--LDKKRL 2569
Cdd:PRK01156 491 EVKDIDEKIVDLKKRKEYLESEEI--NKSINEYNKIESARADLEDIKIkINELKDKHDKyEEIKNRYKSLKLedLDSKRT 568
|
....*..
gi 1389908286 2570 EQEKQLA 2576
Cdd:PRK01156 569 SWLNALA 575
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3048-3084 |
4.53e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.53e-05
10 20 30
....*....|....*....|....*....|....*..
gi 1389908286 3048 LNFLEAQAATGFVIDPIKNERVPVDEAVKSGLVGPEI 3084
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1424-1573 |
4.65e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 49.39 E-value: 4.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1424 LKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAElQELRDRAAEAEKLRKAAQDEAERLRKQVA 1503
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFE-KELRERRNELQKLEKRLLQKEENLDRKLE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1504 EETQRKKNAEDELKRKSDAEKEAAKQK-------QRALDDLQKY-KMQAEEA-ERRMKQAEE----EKIRQIRVVEEVAQ 1570
Cdd:PRK12704 104 LLEKREEELEKKEKELEQKQQELEKKEeeleeliEEQLQELERIsGLTAEEAkEILLEKVEEearhEAAVLIKEIEEEAK 183
|
...
gi 1389908286 1571 KSA 1573
Cdd:PRK12704 184 EEA 186
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1344-1588 |
4.77e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 4.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1344 EDDEKASEKLKEEERRKMAEIQAELDKQKQmaeahakSVAKAEQEALELKMKMKEeaskrqdvaadAEKQKQNIQQELQH 1423
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQA-------ELEELNEEYNELQAELEA-----------LQAEIDKLQAEIAE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1424 LKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAE-LQELRDRAAEAEKLRKAAQDEAERLRKQV 1502
Cdd:COG3883 77 AE----AEIEERREELGERARALYRSGGSVSYLDVLLGSESFSDFLDRLSaLSKIADADADLLEELKADKAELEAKKAEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1503 AEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAM 1582
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
....*.
gi 1389908286 1583 SFSEQT 1588
Cdd:COG3883 233 AAAAAA 238
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1498-1934 |
4.84e-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: 49.52 E-value: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1498 LRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQ---AEEEKIRQIRVVEEVAQKSAA 1574
Cdd:pfam15964 319 VRSSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKelaSQQEKRAQEKEALRKEMKKER 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1575 TQLQTKAMSFSEqttkleeslkkeqgNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEAL-RLRLQAEEEAQK 1653
Cdd:pfam15964 399 EELGATMLALSQ--------------NVAQLEAQVEKVTREKNSLVSQLEEAQKQLASQEMDVTKVCgEMRYQLNQTKMK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1654 KshaqEEAEKQKLEAErdaKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDN 1733
Cdd:pfam15964 465 K----DEAEKEHREYR---TKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRL 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1734 E----LQRLKNEVNSTEKQRKQLEDELNKvrsemdSLLQMKINAEKAsmVNTEKSkqLLESEALKMKQLADEAARMrsva 1809
Cdd:pfam15964 538 EkesiQQSFSNEAKAQALQAQQREQELTQ------KMQQMEAQHDKT--VNEQYS--LLTSQNTFIAKLKEECCTL---- 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1810 eeAKKQRQIAEeeaaRQRSEAEKILKEKLAAINEAtrlkteaemalkakeaenERLKRQAEEeayqrklLEDQAAQH--- 1886
Cdd:pfam15964 604 --AKKLEEITQ----KSRSEVEQLSQEKEYLQDRL------------------EKLQKRNEE-------LEEQCVQHgrm 652
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 1887 KQDIEEKITQL----QTSSdSELGRQKNIVEETLKQKKVVEEEIHIIKINFH 1934
Cdd:pfam15964 653 HERMKQRLRQLdkhcQATA-QQLVQLLSKQNQLFKERQNLTEEVQSLRSQVP 703
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
2053-2611 |
4.84e-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: 4.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2053 QDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAEneaAKQAKAQNDTEKQRKEA 2132
Cdd:TIGR00606 230 EAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELE---LKMEKVFQGTDEQLNDL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2133 EEEAARRAAAEAAALKQKQQadaEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVN-DAFK 2211
Cdd:TIGR00606 307 YHNHQRTVREKERELVDCQR---ELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLElDGFE 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2212 QKSQVEvelarvrIQMEELVKLKlkieeenRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNL 2291
Cdd:TIGR00606 384 RGPFSE-------RQIKNFHTLV-------IERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEIL 449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2292 AEQRALAEKILKEKMQAIQEATK-LKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASA 2370
Cdd:TIGR00606 450 EKKQEELKFVIKELQQLEGSSDRiLELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNH 529
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2371 EAEKLKlrvKELSLAQTKAEDEAKKFK---KQADEVKAQL---------------QRTEKHTTE-------IVVQKLETQ 2425
Cdd:TIGR00606 530 HTTTRT---QMEMLTKDKMDKDEQIRKiksRHSDELTSLLgyfpnkkqledwlhsKSKEINQTRdrlaklnKELASLEQN 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2426 RLQSTREADDLK---SAIADLEEERKKLKKEAEELQRKSKEMANA-QQEQIEQQKAELQQSFLTEKGL-------LLKRE 2494
Cdd:TIGR00606 607 KNHINNELESKEeqlSSYEDKLFDVCGSQDEESDLERLKEEIEKSsKQRAMLAGATAVYSQFITQLTDenqsccpVCQRV 686
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2495 KEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKL-------QAIMDEAVRKQKEAEEEMKNKQREMDVLDKK 2567
Cdd:TIGR00606 687 FQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMlglapgrQSIIDLKEKEIPELRNKLQKVNRDIQRLKND 766
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2568 RLEQEKQLAEENKKL--------------REQLQTFEISSKTVSQTKESQTVSVEKLV 2611
Cdd:TIGR00606 767 IEEQETLLGTIMPEEesakvcltdvtimeRFQMELKDVERKIAQQAAKLQGSDLDRTV 824
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2177-2372 |
4.90e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.10 E-value: 4.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2177 ELTVVKLQlDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVElARVRI----QMEELVKLKLKIEEENRRLMQKDKDsT 2252
Cdd:COG2268 170 ELESVAIT-DLEDENNYLDALGRRKIAEIIRDARIAEAEAERE-TEIAIaqanREAEEAELEQEREIETARIAEAEAE-L 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2253 QKLLAE---EAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQA 2329
Cdd:COG2268 247 AKKKAEerrEAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1389908286 2330 QEtakrlqedKQQIQQRLDKETEGFQKSLEAERKRQLEASAEA 2372
Cdd:COG2268 327 AE--------AEAIRAKGLAEAEGKRALAEAWNKLGDAAILLM 361
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2004-2482 |
5.19e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 49.91 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2004 KAAQEEVERLKKKAEdankqkekaekeaekqvVLA--KEAAQKCTAAEQKA---QDVLSKNK--EDVLAQEKLRDEFENA 2076
Cdd:COG4913 238 ERAHEALEDAREQIE-----------------LLEpiRELAERYAAARERLaelEYLRAALRlwFAQRRLELLEAELEEL 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2077 KKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAE 2156
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2157 -MSKHKKEAEQALQQKSQVEKELTVvklQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVR----------- 2224
Cdd:COG4913 381 eFAALRAEAAALLEALEEELEALEE---ALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRdalaealglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2225 ---------IQMEE------------------------------------------LVKLKLKIEEENRRLMQKDKDS-T 2252
Cdd:COG4913 458 aelpfvgelIEVRPeeerwrgaiervlggfaltllvppehyaaalrwvnrlhlrgrLVYERVRTGLPDPERPRLDPDSlA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2253 QKLLAEE----AEKMKSLAEEAGRLSVEAEET-----------------------------ARQRQIAESNlAEQRALAE 2299
Cdd:COG4913 538 GKLDFKPhpfrAWLEAELGRRFDYVCVDSPEElrrhpraitragqvkgngtrhekddrrriRSRYVLGFDN-RAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2300 KILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE------DKQQIQQRLDketegfqkSLEAERKRQLEASAEAE 2373
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALQERREALQRLAEyswdeiDVASAEREIA--------ELEAELERLDASSDDLA 688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2374 KLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRtekhtteivvqkLETQRLQSTREADDLKSAIADLEEERKKLKKE 2453
Cdd:COG4913 689 ALEEQLEELEAELEELEEELDELKGEIGRLEKELEQ------------AEEELDELQDRLEAAEDLARLELRALLEERFA 756
|
570 580
....*....|....*....|....*....
gi 1389908286 2454 AEELQRKSKEMANAQQEQIEQQKAELQQS 2482
Cdd:COG4913 757 AALGDAVERELRENLEERIDALRARLNRA 785
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1804-2604 |
5.31e-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: 49.66 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1804 RMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMAlKAKEAENERLKRQaeeeayQRKLLEDQA 1883
Cdd:TIGR00606 190 TLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIV-KSYENELDPLKNR------LKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1884 AQHKqdIEEKITQLQTSsdsELGRQKNIVEETLKQKKV---VEEEIHIIKINFHKASKEK----ADLESELKKLkgiade 1956
Cdd:TIGR00606 263 KIMK--LDNEIKALKSR---KKQMEKDNSELELKMEKVfqgTDEQLNDLYHNHQRTVREKerelVDCQRELEKL------ 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1957 TQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRitaaeeEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVV 2036
Cdd:TIGR00606 332 NKERRLLNQEKTELLVEQGRLQLQADRHQEHIRAR------DSLIQSLATRLELDGFERGPFSERQIKNFHTLVIERQED 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2037 LAKEAAQKCTAAeqkaqdvlsknkedvlaQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAA 2116
Cdd:TIGR00606 406 EAKTAAQLCADL-----------------QSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEG 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2117 KQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQK----QQADAEMSKHKKEAEQALQQKSQVEKELTvvklQLDETDKQK 2192
Cdd:TIGR00606 469 SSDRILELDQELRKAERELSKAEKNSLTETLKKEvkslQNEKADLDRKLRKLDQEMEQLNHHTTTRT----QMEMLTKDK 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2193 VLLDQELQRVKGEVNDAF---------------------KQKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDS 2251
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELtsllgyfpnkkqledwlhsksKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2252 TQKLLaeEAEKMKSLAEEAGRLSVEAEETARQRQI--AESNLAEQRAL------------------AEKILKEKMQAIQE 2311
Cdd:TIGR00606 625 EDKLF--DVCGSQDEESDLERLKEEIEKSSKQRAMlaGATAVYSQFITqltdenqsccpvcqrvfqTEAELQEFISDLQS 702
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2312 ATKL----KAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQksleaERKRQLEASAEAEKLKLRVKELSLAQT 2387
Cdd:TIGR00606 703 KLRLapdkLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR-----NKLQKVNRDIQRLKNDIEEQETLLGTI 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2388 KAEDEAKK-----------FKKQADEVK----AQLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKK 2452
Cdd:TIGR00606 778 MPEEESAKvcltdvtimerFQMELKDVErkiaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQE 857
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2453 EAEELQRKSKEM---------ANAQQEQIEQQKAELQ---QSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKD 2520
Cdd:TIGR00606 858 QIQHLKSKTNELkseklqigtNLQRRQQFEEQLVELStevQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNK 937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2521 EQERQRKLMEEERKKLQAIMDEAVRK-QKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQT 2599
Cdd:TIGR00606 938 KAQDKVNDIKEKVKNIHGYMKDIENKiQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWL 1017
|
....*
gi 1389908286 2600 KESQT 2604
Cdd:TIGR00606 1018 QDNLT 1022
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
26-91 |
5.33e-05 |
|
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: 45.34 E-value: 5.33e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 26 KKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 91
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1588-1776 |
5.37e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 49.23 E-value: 5.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1588 TTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEaeqeleiwrQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLE 1667
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQ---------QLKEELDKKQIDADKAQQKADFAQDNADKQRDE 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1668 AERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKlsAEQECIRLKADFEHAEQQrglldnelqrLKNEVNSTEK 1747
Cdd:pfam05262 250 VRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIE--IKKNDEEALKAKDHKAFD----------LKQESKASEK 317
|
170 180
....*....|....*....|....*....
gi 1389908286 1748 QRKQLEDELNKVRSEMDSLLQMKINAEKA 1776
Cdd:pfam05262 318 EAEDKELEAQKKREPVAEDLQKTKPQVEA 346
|
|
| 2A1904 |
TIGR00927 |
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ... |
1485-1755 |
5.45e-05 |
|
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273344 [Multi-domain] Cd Length: 1096 Bit Score: 49.61 E-value: 5.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1485 EKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQaeeAERRMKQAEEEKIRQIRv 1564
Cdd:TIGR00927 628 GDLSKGDVAEAEHTGERTGEEGERPTEAEGENGEESGGEAEQEGETETKGENESEGEIP---AERKGEQEGEGEIEAKE- 703
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1565 vEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLR 1644
Cdd:TIGR00927 704 -ADHKGETEAEEVEHEGETEAEGTEDEGEIETGEEGEEVEDEGEGEAEGKHEVETEGDRKETEHEGETEAEGKEDEDEGE 782
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1645 LQAEEEAQKKShaqEEAEKQKLEAERDAKKRGKAEEaalkqkENAEKELDKQRKFAEQIAQQKLSAEQECiRLKADFEHA 1724
Cdd:TIGR00927 783 IQAGEDGEMKG---DEGAEGKVEHEGETEAGEKDEH------EGQSETQADDTEVKDETGEQELNAENQG-EAKQDEKGV 852
|
250 260 270
....*....|....*....|....*....|...
gi 1389908286 1725 EQQRGLL--DNELQRLKNEVNSTEKQRKQLEDE 1755
Cdd:TIGR00927 853 DGGGGSDggDSEEEEEEEEEEEEEEEEEEEEEE 885
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2325-2632 |
5.58e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2325 QKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVK 2404
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDA----LQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2405 AQLQRTEKHTTEIVVqkletqrLQSTREADDLKSAIADLeeerkklkkeaeelqrksKEMANAQQEQIEQQKAELQqsfl 2484
Cdd:COG3883 93 RALYRSGGSVSYLDV-------LLGSESFSDFLDRLSAL------------------SKIADADADLLEELKADKA---- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2485 tekglllkrekevegEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVL 2564
Cdd:COG3883 144 ---------------ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAA 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2565 DKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVAVTTVGTSKGVLNGSTEVDGV 2632
Cdd:COG3883 209 EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGA 276
|
|
| Selenoprotein_S |
pfam06936 |
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) ... |
1615-1692 |
5.76e-05 |
|
Selenoprotein S (SelS); This family consists of several mammalian selenoprotein S (SelS) sequences. SelS is a plasma membrane protein and is present in a variety of tissues and cell types. Selenoprotein S (SelS) is an intrinsically disordered protein. It formsa selenosulfide bond between cys 174 and Sec 188, that has a redox potential -234 mV. In vitro, SelS is an efficient reductase that depends on the presence of selenocysteine. Due to the high reactivity, SelS also has peroxidase activity that can catalyze the reduction of hydrogen peroxide. It is also resistant to inactivation by hydrogen peroxide which might provide evolutionary advantage compared to cysteine containing peroxidases.
Pssm-ID: 462043 [Multi-domain] Cd Length: 192 Bit Score: 47.14 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1615 QQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQ------KKSHAQEEAEKQKLEaERDAKKRGKAEEAALKQKEN 1688
Cdd:pfam06936 62 RQRSSDHSAATVDPDLVVKRQEALEASRLRMQEELDAQaekfkeKQKQLEEEKRRQKIE-MWESMQEGKSYKGNAKLAQE 140
|
....
gi 1389908286 1689 AEKE 1692
Cdd:pfam06936 141 ETEE 144
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1418-1715 |
6.27e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1418 QQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAER 1497
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1498 LRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQL 1577
Cdd:COG4372 92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQ 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1578 QTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHA 1657
Cdd:COG4372 172 ELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEEL 251
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1658 QEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECI 1715
Cdd:COG4372 252 LEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSL 309
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1690-1844 |
6.47e-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: 47.61 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1690 EKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRS--EMDSLL 1767
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQ 95
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1768 QmkinaEKASMvntEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEA 1844
Cdd:COG1579 96 K-----EIESL---KRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2506-2588 |
6.72e-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: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2506 KQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQ 2585
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
...
gi 1389908286 2586 LQT 2588
Cdd:COG4942 110 LRA 112
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1489-1834 |
6.89e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1489 KAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEV 1568
Cdd:COG4372 41 DKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEEL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1569 AQksaatqlqtkamsfseQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAE 1648
Cdd:COG4372 121 QK----------------ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1649 EEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQR 1728
Cdd:COG4372 185 LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1729 GLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSV 1808
Cdd:COG4372 265 LAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQ 344
|
330 340
....*....|....*....|....*.
gi 1389908286 1809 AEEAKKQRQIAEEEAARQRSEAEKIL 1834
Cdd:COG4372 345 LLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
7-126 |
7.28e-05 |
|
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: 45.37 E-value: 7.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 7 RDFMETLIQRGQDERDrVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQ 82
Cdd:cd21337 4 RDAFDTLFDHAPDKLN-VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVL 82
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1389908286 83 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 126
Cdd:cd21337 83 NVSFAFELMQDGGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1875-2073 |
7.63e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 7.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1875 QRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLK---QKKVVEEEIHIIKINfHKASKEKADLESELKKLK 1951
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAaqeQKKQAEEAAKQAALK-QKQAEEAAAKAAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1952 GIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEkvkritaAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEA 2031
Cdd:PRK09510 149 AEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAK-------KKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA 221
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 1389908286 2032 EKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEF 2073
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2505-2654 |
8.08e-05 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 49.05 E-value: 8.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2505 EKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQ--------KEAEEEMKNKQREMDVLDKKRLEQ--EKQ 2574
Cdd:PRK00409 529 ERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAHE 608
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2575 LAEENKKLREQLQTFEisSKTVSQTKESQTVSVEKLVAVTTVGtSKGvlngstEVDGVKKEGDSPLSFEGIREKVPAERL 2654
Cdd:PRK00409 609 LIEARKRLNKANEKKE--KKKKKQKEKQEELKVGDEVKYLSLG-QKG------EVLSIPDDKEAIVQAGIMKMKVPLSDL 679
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
2273-2411 |
9.16e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 48.12 E-value: 9.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2273 LSVEAEETARQRQIAESNLAEQRALAEKiLKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE-DKQQI--QQRLDk 2349
Cdd:COG1566 74 ARLDPTDLQAALAQAEAQLAAAEAQLAR-LEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQAlYKKGAvsQQELD- 151
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 2350 etegfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTK-AEDEAKKFKKQADEVKAQLQRTE 2411
Cdd:COG1566 152 -----EARAALDAAQAQLEAAQAQLAQAQAGLREEEELAaAQAQVAQAEAALAQAELNLARTT 209
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1568-1712 |
9.28e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.62 E-value: 9.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1568 VAQKSAATQL---QTKAMSFSEQTTKLEESLKKEQgnVLKLQEEADKLkkqqkeantaREEAEQELEIWRQKANEALRlR 1644
Cdd:PRK12704 24 VRKKIAEAKIkeaEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKL----------RNEFEKELRERRNELQKLEK-R 90
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1645 LQAEEEAQKKShaQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqkLSAEQ 1712
Cdd:PRK12704 91 LLQKEENLDRK--LELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISG--LTAEE 154
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1644-1919 |
9.39e-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: 47.92 E-value: 9.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1644 RLQAEEEAQKKshAQEEAEKQKLEAERDAKKRGKAEEAALKQKEnAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEh 1723
Cdd:TIGR02794 54 RIQQQKKPAAK--KEQERQKKLEQQAEEAEKQRAAEQARQKELE-QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQA- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1724 AEQQRGLLDNELQRLKnevnstEKQRKQLEDElnkvrsemdsllqmkinaekasmvntekskqllesealkmkQLADEAA 1803
Cdd:TIGR02794 130 AEAKAKAEAEAERKAK------EEAAKQAEEE-----------------------------------------AKAKAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1804 RMRSVAEEAKKQrqiAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQA 1883
Cdd:TIGR02794 163 EAKKKAEEAKKK---AEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFG 239
|
250 260 270
....*....|....*....|....*....|....*.
gi 1389908286 1884 AQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQK 1919
Cdd:TIGR02794 240 LASGSNAEKQGGARGAAAGSEVDKYAAIIQQAIQQN 275
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2292-2566 |
9.44e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.86 E-value: 9.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2292 AEQRALAEKILKEKMQAIQEATklkaeaekLQKQKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASAE 2371
Cdd:COG3206 144 SPDPELAAAVANALAEAYLEQN--------LELRREEARKALEFLEEQLPELRKELEE----AEAALEEFRQKNGLVDLS 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2372 AEKLKL--RVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEI----VVQKLETQRLQSTREADDLKSaiadlee 2445
Cdd:COG3206 212 EEAKLLlqQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELlqspVIQQLRAQLAELEAELAELSA------- 284
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2446 erkklkkeaeELQRKSKEMANAQQE------QIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEmkkakalk 2519
Cdd:COG3206 285 ----------RYTPNHPDVIALRAQiaalraQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAEL-------- 346
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1389908286 2520 DEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDK 2566
Cdd:COG3206 347 PELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVIDP 393
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1338-1711 |
9.65e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 9.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1338 DAQRRLEDDEKASEKLKEEERRKMAEIQAeLDKQKQMAEAHAKSVAKAEQ----------EALELKMKMKEEASKRQDVA 1407
Cdd:PRK10246 527 VNQSRLDALEKEVKKLGEEGAALRGQLDA-LTKQLQRDESEAQSLRQEEQaltqqwqavcASLNITLQPQDDIQPWLDAQ 605
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1408 ADAEKQKQNIQQELQHLKSLSDQEikSKNQQLEDALVSRRkieeeiHIIRIQLEKTTAHKAKSEAELQELRDRAAEAeKL 1487
Cdd:PRK10246 606 EEHERQLRLLSQRHELQGQIAAHN--QQIIQYQQQIEQRQ------QQLLTALAGYALTLPQEDEEASWLATRQQEA-QS 676
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1488 RKAAQDEAERLRKQVAeetqRKKNAEDELKRKSDAEKEAAKQkqrALDDLQKYKMQ--AEEAERRMKQAEEEKIRQiRVV 1565
Cdd:PRK10246 677 WQQRQNELTALQNRIQ----QLTPLLETLPQSDDLPHSEETV---ALDNWRQVHEQclSLHSQLQTLQQQDVLEAQ-RLQ 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1566 EEVAQKSAATQlqtkAMSFSEQTTKLEESLKKEqgNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL 1645
Cdd:PRK10246 749 KAQAQFDTALQ----ASVFDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTV 822
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908286 1646 QAEEeaqkkSHAQEEAEKQKLeaeRDAKKRGKAEEAALKQKENAEKEldkQRKFAEQIAQQKLSAE 1711
Cdd:PRK10246 823 TVEQ-----IQQELAQLAQQL---RENTTRQGEIRQQLKQDADNRQQ---QQALMQQIAQATQQVE 877
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2198-2637 |
9.90e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 48.58 E-value: 9.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2198 ELQRVKGEVNDAFKQKSQVEVELARVRIQMEELV---KLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLS 2274
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKAsalKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2275 VEAEETARQRQIAESNLAEQRALAEKILKEkmqaiqeatkLKAEAEKLQKQKDQAQETAKRLQEdkqqIQQRLDKETEGF 2354
Cdd:pfam05557 83 KYLEALNKKLNEKESQLADAREVISCLKNE----------LSELRRQIQRAELELQSTNSELEE----LQERLDLLKAKA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2355 Q-----------------------KSLEAERKRQLEASAEAEKLK---LRVKELSLAQTKAEDEAKKF----------KK 2398
Cdd:pfam05557 149 SeaeqlrqnlekqqsslaeaeqriKELEFEIQSQEQDSEIVKNSKselARIPELEKELERLREHNKHLnenienklllKE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2399 QADEVKAQLQRTEKHTTEIVVQKLETQRLQstREADDLKSAIADLEEERkklkkeaeelqrKSKEMANAQQEQIEQQKAE 2478
Cdd:pfam05557 229 EVEDLKRKLEREEKYREEAATLELEKEKLE--QELQSWVKLAQDTGLNL------------RSPEDLSRRIEQLQQREIV 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2479 LQQ---SFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQER-QRK--LMEEERKKLQAIMDEAVRKQKEAEE 2552
Cdd:pfam05557 295 LKEensSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRvlLLTKERDGYRAILESYDKELTMSNY 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2553 EMKNKQREMDVLDkkrLEQEKQLAEENKKLR-EQLQTFEISSKTVSQTKESQTVSVEKLVAVTTVGTSKgvlngsTEVDG 2631
Cdd:pfam05557 375 SPQLLERIEEAED---MTQKMQAHNEEMEAQlSVAEEELGGYKQQAQTLERELQALRQQESLADPSYSK------EEVDS 445
|
....*.
gi 1389908286 2632 VKKEGD 2637
Cdd:pfam05557 446 LRRKLE 451
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
25-132 |
1.11e-04 |
|
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: 45.39 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 25 QKKTFTKWVNK---------HLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 91
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1389908286 92 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 132
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4267-4300 |
1.12e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.12e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908286 4267 EETGPIAGILDTDTLEKVSVTEAIHRNLVDNITG 4300
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1444-1661 |
1.12e-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: 48.41 E-value: 1.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1444 VSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQE--------LRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKnaEDE 1515
Cdd:pfam15709 350 VERKRREQEEQRRLQQEQLERAEKMREELELEQqrrfeeirLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQ--QEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1516 LKRKsdaekeaakqkqraLDDLQKyKMQAEEAERrmkqAEEEKIRQirvveevaqksaatqlqtkamsfseqtTKLEESL 1595
Cdd:pfam15709 428 FRRK--------------LQELQR-KKQQEEAER----AEAEKQRQ---------------------------KELEMQL 461
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908286 1596 KKEQGNVLKLQEEADKLKKQQKEanTAREEAEQELEIWRQKANEALRLrlqAEEEAQKKshAQEEA 1661
Cdd:pfam15709 462 AEEQKRLMEMAEEERLEYQRQKQ--EAEEKARLEAEERRQKEEEAARL---ALEEAMKQ--AQEQA 520
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2276-2587 |
1.20e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 48.33 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2276 EAEETARQRqiaesnlaEQRALAEKI-LKEKMQAIQEATKLKAEAEKLQKQKDQ-AQETAKRLQEDKQQIQQRLDKETEG 2353
Cdd:pfam02029 3 DEEEAARER--------RRRAREERRrQKEEEEPSGQVTESVEPNEHNSYEEDSeLKPSGQGGLDEEEAFLDRTAKREER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2354 FQKSLE--AERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTR 2431
Cdd:pfam02029 75 RQKRLQeaLERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2432 EADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQ--IEQQK-----AELQQSFLTEKGLLLKREKEVEGEKKRF 2504
Cdd:pfam02029 155 EGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESkvFLDQKrghpeVKSQNGEEEVTKLKVTTKRRQGGLSQSQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2505 EKQLEDEMKKAKALKDEQERQR--KLMEEERKKLQaimdeavRKQKEAEEEM---------KNKQREMDVLDKKRLEQEK 2573
Cdd:pfam02029 235 EREEEAEVFLEAEQKLEELRRRrqEKESEEFEKLR-------QKQQEAELELeelkkkreeRRKLLEEEEQRRKQEEAER 307
|
330
....*....|....*.
gi 1389908286 2574 QLA--EENKKLREQLQ 2587
Cdd:pfam02029 308 KLReeEEKRRMKEEIE 323
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1489-1974 |
1.26e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 48.36 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1489 KAAQDEAERLRKQVAEETQRKKNAEDELKRKS----------DAEKEAAKQKQRALDDLQKYKMQAEEAERRmKQAEEEK 1558
Cdd:PRK01156 193 KSSNLELENIKKQIADDEKSHSITLKEIERLSieynnamddyNNLKSALNELSSLEDMKNRYESEIKTAESD-LSMELEK 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1559 IRQIRVVEE---------------------------VAQKSAATQLQTKAMSFSEQTTKLEEsLKKEQGNVLKLQEEADK 1611
Cdd:PRK01156 272 NNYYKELEErhmkiindpvyknrnyindyfkykndiENKKQILSNIDAEINKYHAIIKKLSV-LQKDYNDYIKKKSRYDD 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1612 LKKQQKEA-------NTAREEAEQeLEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALK 1684
Cdd:PRK01156 351 LNNQILELegyemdyNSYLKSIES-LKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLN 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1685 QKENAEKE-LDKQRKFAEQiaqqkLSAEQECIRLKADF--EHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRS 1761
Cdd:PRK01156 430 QRIRALREnLDELSRNMEM-----LNGQSVCPVCGTTLgeEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKK 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1762 EMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE------------------AKKQRQIAEEEA 1823
Cdd:PRK01156 505 RKEYLESEEINKSINEYNKIESARADLEDIKIKINELKDKHDKYEEIKNRykslkledldskrtswlnALAVISLIDIET 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1824 ARQRSEaekilkEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAY----QRKLLEDQAAQhKQDIEEKITQLQT 1899
Cdd:PRK01156 585 NRSRSN------EIKKQLNDLESRLQEIEIGFPDDKSYIDKSIREIENEANnlnnKYNEIQENKIL-IEKLRGKIDNYKK 657
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 1900 SSDSELGRQKNIVEETLKQKKvVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKL 1974
Cdd:PRK01156 658 QIAEIDSIIPDLKEITSRIND-IEDNLKKSRKALDDAKANRARLESTIEILRTRINELSDRINDINETLESMKKI 731
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1951-2171 |
1.31e-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: 47.53 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1951 KGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAA--EEEAARQCKAAQEEVERLKKKAEdankqkekae 2028
Cdd:TIGR02794 60 KPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAkqAEQAAKQAEEKQKQAEEAKAKQA---------- 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2029 keaekqvvlaKEAAQKCTA-AEQKAQDVLSKNKEdvlaQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQ 2107
Cdd:TIGR02794 130 ----------AEAKAKAEAeAERKAKEEAAKQAE----EEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAK 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2108 KKA------AENEAAKQA----KAQNDTEKQRKEAEEEAARRAAAEAAALKQKQ------QADAEMSKHKKEAEQALQQK 2171
Cdd:TIGR02794 196 AKAeaakakAAAEAAAKAeaeaAAAAAAEAERKADEAELGDIFGLASGSNAEKQggargaAAGSEVDKYAAIIQQAIQQN 275
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1716-1970 |
1.31e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.21 E-value: 1.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1716 RLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLESEALKM 1795
Cdd:COG1340 19 ELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNE-KVKELKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1796 KQLADEAARMRsvAEEAKKQRQIAEEEAARQRS----EAEKILKEKLAAINE-ATRLKTEAEMALKAKEAENE--RLKRQ 1868
Cdd:COG1340 98 RKELAELNKAG--GSIDKLRKEIERLEWRQQTEvlspEEEKELVEKIKELEKeLEKAKKALEKNEKLKELRAElkELRKE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1869 AEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEetlKQKKVVEEEIHIIKInfhkaSKEKADLESELK 1948
Cdd:COG1340 176 AEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVE---AQEKADELHEEIIEL-----QKELRELRKELK 247
|
250 260
....*....|....*....|..
gi 1389908286 1949 KLKGIADETQKSKLKAEEEAEK 1970
Cdd:COG1340 248 KLRKKQRALKREKEKEELEEKA 269
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2368-2641 |
1.32e-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: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2368 ASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHtteivVQKLETQRLQSTREADDLKSAIADLeeer 2447
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-----LEALQAEIDKLQAEIAEAEAEIEER---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2448 kklkkeaeelQRKSKEMANAQQEQIEQQK-------AELQQSFLTEKGLLlkrekevegekKRFEKQLEDEMKKAKALKD 2520
Cdd:COG3883 85 ----------REELGERARALYRSGGSVSyldvllgSESFSDFLDRLSAL-----------SKIADADADLLEELKADKA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2521 EQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTK 2600
Cdd:COG3883 144 ELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1389908286 2601 ESQTVSVEKLVAVTTVGTSKGVLNGSTEVDGVKKEGDSPLS 2641
Cdd:COG3883 224 AAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGA 264
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1525-1885 |
1.34e-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: 48.10 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1525 EAAKQKQRALDDLQK----YKMQAEEAERRMKQAEEEKIRQIRVVEEvaqksaatqlqtkamsfseqttkLEESLKKEQG 1600
Cdd:pfam05701 35 ERRKLVELELEKVQEeipeYKKQSEAAEAAKAQVLEELESTKRLIEE-----------------------LKLNLERAQT 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1601 NVLKLQEEAD--KLKKQQKEANTAREE---AEQELEIWRQKANEALrlrlqAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1675
Cdd:pfam05701 92 EEAQAKQDSElaKLRVEEMEQGIADEAsvaAKAQLEVAKARHAAAV-----AELKSVKEELESLRKEYASLVSERDIAIK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1676 gKAEEAALKQKE------------NAEKELDKQRKFAEQIAQQK-----LSAEQECIRLKADFEHAEQqrglldnELQRL 1738
Cdd:pfam05701 167 -RAEEAVSASKEiektveeltielIATKESLESAHAAHLEAEEHrigaaLAREQDKLNWEKELKQAEE-------ELQRL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1739 KNEVNSTEKQRKQLE---DELNKVRSEMDSLLQMKINAEKASMVNTEKS-----------KQLLESEALKMKQLADEAAR 1804
Cdd:pfam05701 239 NQQLLSAKDLKSKLEtasALLLDLKAELAAYMESKLKEEADGEGNEKKTstsiqaalasaKKELEEVKANIEKAKDEVNC 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1805 MRSVAE--EAKKQRQIAEEEAARQRSEAEKILKEKLAAinEATRLKTEAEMA-LKAKEAENERLK-----RQAEEEAYQR 1876
Cdd:pfam05701 319 LRVAAAslRSELEKEKAELASLRQREGMASIAVSSLEA--ELNRTKSEIALVqAKEKEAREKMVElpkqlQQAAQEAEEA 396
|
....*....
gi 1389908286 1877 KLLEdQAAQ 1885
Cdd:pfam05701 397 KSLA-QAAR 404
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1340-2021 |
1.59e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.41 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1340 QRRLEDDEKASEKLKEEErrkmaEIQAELDKQKQMAEAHAKSvakAEQEALELKMKMKEeASKRQDVAADAEKQKQNIQQ 1419
Cdd:PRK04863 351 ERYQADLEELEERLEEQN-----EVVEEADEQQEENEARAEA---AEEEVDELKSQLAD-YQQALDVQQTRAIQYQQAVQ 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1420 ELQHLKSLSD-------------QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEK------------------------ 1462
Cdd:PRK04863 422 ALERAKQLCGlpdltadnaedwlEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQayqlvrkiagevsrseawdvarel 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1463 -TTAHKAKSEAE-LQELRDRAAEAEKlRKAAQDEAERLRKQVAEETQRKKNAEDELkrksdaEKEAAKQKQRaLDDLQKY 1540
Cdd:PRK04863 502 lRRLREQRHLAEqLQQLRMRLSELEQ-RLRQQQRAERLLAEFCKRLGKNLDDEDEL------EQLQEELEAR-LESLSES 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1541 KmqAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTtklEESLKKEQGNVLKLQEEADKLKKQQKEAN 1620
Cdd:PRK04863 574 V--SEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREQS---GEEFEDSQDVTEYMQQLLERERELTVERD 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1621 TAREEAEQ-ELEIWR---QKANEALRLRLQAE----------------EEAQKKS-------HA----QEEAEKQKLEAE 1669
Cdd:PRK04863 649 ELAARKQAlDEEIERlsqPGGSEDPRLNALAErfggvllseiyddvslEDAPYFSalygparHAivvpDLSDAAEQLAGL 728
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1670 RD---------------AKKRGKAEE--AALKQKENA-------------------EKELDKQRKFAEQIAQQ--KLSAE 1711
Cdd:PRK04863 729 EDcpedlyliegdpdsfDDSVFSVEEleKAVVVKIADrqwrysrfpevplfgraarEKRIEQLRAEREELAERyaTLSFD 808
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1712 -QECIRLKADFEH--------------------AEQQRGLLDNELQRLKNEVNSTEKQRKQLE---DELNKVRSEMDSL- 1766
Cdd:PRK04863 809 vQKLQRLHQAFSRfigshlavafeadpeaelrqLNRRRVELERALADHESQEQQQRSQLEQAKeglSALNRLLPRLNLLa 888
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1767 ---LQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE-AKKQRQIAEEEAARQRSEAEKILkekLAAIN 1842
Cdd:PRK04863 889 detLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVLQSDPEQfEQLKQDYQQAQQTQRDAKQQAFA---LTEVV 965
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1843 E-ATRLKTEAEMALKAKEAE-NERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKiTQLQTSSDSELGRQKNIVEEtlkqkk 1920
Cdd:PRK04863 966 QrRAHFSYEDAAEMLAKNSDlNEKLRQRLEQAEQERTRAREQLRQAQAQLAQY-NQVLASLKSSYDAKRQMLQE------ 1038
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1921 vveeeihiikinfhkaskekadLESELKKLKGIADETQKSKLKAEEEaeKLKKLAAEEERRRKEAEEKVKRITAAEEEAA 2000
Cdd:PRK04863 1039 ----------------------LKQELQDLGVPADSGAEERARARRD--ELHARLSANRSRRNQLEKQLTFCEAEMDNLT 1094
|
810 820
....*....|....*....|.
gi 1389908286 2001 RQCKAAQEEVERLKKKAEDAN 2021
Cdd:PRK04863 1095 KKLRKLERDYHEMREQVVNAK 1115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1788-2015 |
1.62e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1788 LESEALKMKQLADEAARMRSVAEEAKKQRQIAEE-EAARQRSEAEKILKEKLAAINEATRLKTeAEMALKAKEAENERLK 1866
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1867 RQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSdselGRQKNIVEETLKQKKvveeeihiikinfhkasKEKADLESE 1946
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNG----GDRLEQLEREIERLE-----------------RELEERERR 360
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 1947 LKKLkgiADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKK 2015
Cdd:COG4913 361 RARL---EALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEA 426
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1624-1974 |
1.63e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.55 E-value: 1.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1624 EEAEQELeiwRQKANEAlRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKK----RGKAEEAALKQKEnAEKELDKQRKF 1699
Cdd:pfam02029 5 EEAARER---RRRAREE-RRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKpsgqGGLDEEEAFLDRT-AKREERRQKRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1700 AEQIAQQKlsaeqecirlkadfehaeqqrgLLDNELQRLKNEVNStEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMV 1779
Cdd:pfam02029 80 QEALERQK----------------------EFDPTIADEKESVAE-RKENNEEEENSSWEKEEKRDSRLGRYKEEETEIR 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1780 NTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRqIAEEEAARQRSEAEKILKEKLAAINEATRLKTEA------EM 1853
Cdd:pfam02029 137 EKEYQENKWSTEVRQAEEEGEEEEDKSEEAEEVPTEN-FAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVksqngeEE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1854 ALKAKEAENERLK-----RQAEEEAYQR----KLLEDQAAQHkQDIE----EKITQLQTSSDSELGRQKNIVEEtlkQKK 1920
Cdd:pfam02029 216 VTKLKVTTKRRQGglsqsQEREEEAEVFleaeQKLEELRRRR-QEKEseefEKLRQKQQEAELELEELKKKREE---RRK 291
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1921 VVEEEihiikinfhkasKEKADLESELKKLKGiadETQKSKLKAE------EEAEKLKKL 1974
Cdd:pfam02029 292 LLEEE------------EQRRKQEEAERKLRE---EEEKRRMKEEierrraEAAEKRQKL 336
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2147-2428 |
1.68e-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: 47.11 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2147 LKQKQQADAEMSKHKKEaeqalqqksqVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQ 2226
Cdd:pfam15905 61 LKKKSQKNLKESKDQKE----------LEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQ 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2227 MEELVK----LKLKIEEE-NRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKI 2301
Cdd:pfam15905 131 LLELTRvnelLKAKFSEDgTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLEHSKGKVAQLEEKLVST 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2302 LKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRlDKETEGFQKSLEAerkRQLEASAEAEKLKLRVKE 2381
Cdd:pfam15905 211 EKEKIEEKSETEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEK-NDEIESLKQSLEE---KEQELSKQIKDLNEKCKL 286
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1389908286 2382 LslaQTKAEDEAKKFKKQADEVKAQLQRTEKhttEIVVQKLETQRLQ 2428
Cdd:pfam15905 287 L---ESEKEELLREYEEKEQTLNAELEELKE---KLTLEEQEHQKLQ 327
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1346-1527 |
1.75e-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: 1.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1346 DEKASEKLKEEErrkmaeiQAELDKQKQMAEAHAKSvakaEQEALELKMKMKEEASKRQDVAAD-----------AEKQK 1414
Cdd:pfam05262 179 DKKVVEALREDN-------EKGVNFRRDMTDLKERE----SQEDAKRAQQLKEELDKKQIDADKaqqkadfaqdnADKQR 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1415 QNIQQELQHLKSLSD----QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAkseaelQELRDRAAEAEKLRKA 1490
Cdd:pfam05262 248 DEVRQKQQEAKNLPKpadtSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHKA------FDLKQESKASEKEAED 321
|
170 180 190
....*....|....*....|....*....|....*..
gi 1389908286 1491 AQDEAERLRKQVAEETQRKKNaedELKRKSDAEKEAA 1527
Cdd:pfam05262 322 KELEAQKKREPVAEDLQKTKP---QVEAQPTSLNEDA 355
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1592-1762 |
1.76e-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: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1592 EESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQA-------EEEAQKKSHAQEEAEKQ 1664
Cdd:pfam15709 340 AERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRleeerqrQEEEERKQRLQLQAAQE 419
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1665 KLEAERDAKKRGKAEEAALKQKENAEK-ELDKQRKFAEQIaqqKLSAEQecirlKADFEHAEQQRglldNELQRLKNEvn 1743
Cdd:pfam15709 420 RARQQQEEFRRKLQELQRKKQQEEAERaEAEKQRQKELEM---QLAEEQ-----KRLMEMAEEER----LEYQRQKQE-- 485
|
170
....*....|....*....
gi 1389908286 1744 stEKQRKQLEDELNKVRSE 1762
Cdd:pfam15709 486 --AEEKARLEAEERRQKEE 502
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1684-2068 |
1.82e-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: 47.64 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1684 KQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSem 1763
Cdd:COG5185 142 KLDEIADIEASYGEVETGIIKDIFGKLTQELNQNLKKLEIFGLTLGLLKGISELKKAEPSGTVNSIKESETGNLGSES-- 219
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1764 dslLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEaarmrsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINE 1843
Cdd:COG5185 220 ---TLLEKAKEIINIEEALKGFQDPESELEDLAQTSDK-------LEKLVEQNTDLRLEKLGENAESSKRLNENANNLIK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1844 ATRlKTEAEMALKAKEAENERLKRQAEEEAyQRKLLEDQAAQHKQDIEEKITQLQtssdSELGRQKNIVEEtlKQKKVVE 1923
Cdd:COG5185 290 QFE-NTKEKIAEYTKSIDIKKATESLEEQL-AAAEAEQELEESKRETETGIQNLT----AEIEQGQESLTE--NLEAIKE 361
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1924 EEIHIIKINFHKASKEKAD-LESELKKLKGIADETQKSKLKAEEE-AEKLKKLAAEEERRRKEAEEKVKRITAAEEEAAR 2001
Cdd:COG5185 362 EIENIVGEVELSKSSEELDsFKDTIESTKESLDEIPQNQRGYAQEiLATLEDTLKAADRQIEELQRQIEQATSSNEEVSK 441
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2002 QCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAK--EAAQKCTAAEQKAQDVLSKNKEDVLAQEK 2068
Cdd:COG5185 442 LLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKkeDLNEELTQIESRVSTLKATLEKLRAKLER 510
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2111-2345 |
1.89e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.13 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2111 AENEAAKQAKAQNDTEKQRKeaeeeaarraaaeaAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDK 2190
Cdd:COG3883 14 ADPQIQAKQKELSELQAELE--------------AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2191 QkvlLDQELQRVKGEVNDAFKQKSQVEVE------------LARVriqmeELVKlklKIEEENRRLMQKDKDSTQKLlae 2258
Cdd:COG3883 80 E---IEERREELGERARALYRSGGSVSYLdvllgsesfsdfLDRL-----SALS---KIADADADLLEELKADKAEL--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2259 eAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQE 2338
Cdd:COG3883 146 -EAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAA 224
|
....*..
gi 1389908286 2339 DKQQIQQ 2345
Cdd:COG3883 225 AAAAAAA 231
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1483-1850 |
1.91e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 47.59 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1483 EAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMKQAEEEKIRQI 1562
Cdd:pfam15964 357 QCEQLKSELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQ------NVAQLEAQVEKVTREKNSLV 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1563 RVVEEvaqksAATQLQTKAMSFSEQTTKLEESLKKEQgnvLKLQEEADKLKKQQKEANTAREEAEQELEiwrqkanealR 1642
Cdd:pfam15964 431 SQLEE-----AQKQLASQEMDVTKVCGEMRYQLNQTK---MKKDEAEKEHREYRTKTGRQLEIKDQEIE----------K 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1643 LRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKEnaEKElDKQRKFAEQIAQQKLSAEQECIRLKADFE 1722
Cdd:pfam15964 493 LGLELSESKQRLEQAQQDAARAREECLKLTELLGESEHQLHLTRL--EKE-SIQQSFSNEAKAQALQAQQREQELTQKMQ 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1723 HAEQQRGLLDNELQRLKNEVNSTEKQRKQ--------LEDELNKVRSEMDSLLQ----MKINAEKASMVNTEKSKQLLES 1790
Cdd:pfam15964 570 QMEAQHDKTVNEQYSLLTSQNTFIAKLKEecctlakkLEEITQKSRSEVEQLSQekeyLQDRLEKLQKRNEELEEQCVQH 649
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1791 EalKMKQladeaaRMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTE 1850
Cdd:pfam15964 650 G--RMHE------RMKQRLRQLDKHCQATAQQLVQLLSKQNQLFKERQNLTEEVQSLRSQ 701
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1476-2302 |
1.92e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1476 ELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSD------AEKEAAKQKQRALDDLQKYKMQAEEAER 1549
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAASDhlnlvqTALRQQEKIERYQADLEELEERLEEQNE 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1550 RMKQAEEEKIRQIRVVEEVAQ--KSAATQL----------QTKAMSFSEQTTKLEESLKKEQGNVL---KLQEEADKLKK 1614
Cdd:PRK04863 370 VVEEADEQQEENEARAEAAEEevDELKSQLadyqqaldvqQTRAIQYQQAVQALERAKQLCGLPDLtadNAEDWLEEFQA 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1615 QQKEANTAREEAEQEL----EIWRQ--KANEALRlRLQAE-EEAQKKSHAQE---EAEKQKLEAERDAKKRGKAEEaaLK 1684
Cdd:PRK04863 450 KEQEATEELLSLEQKLsvaqAAHSQfeQAYQLVR-KIAGEvSRSEAWDVAREllrRLREQRHLAEQLQQLRMRLSE--LE 526
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1685 QKENAEKELDKQRKFAEQIAQQKLSAEQEcirLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMD 1764
Cdd:PRK04863 527 QRLRQQQRAERLLAEFCKRLGKNLDDEDE---LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAP 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1765 SLLQMKinaEKASMVNTEKSKQLLESEALkmkqlaDEAarMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEA 1844
Cdd:PRK04863 604 AWLAAQ---DALARLREQSGEEFEDSQDV------TEY--MQQLLERERELTVERDELAARKQALDEEIERLSQPGGSED 672
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1845 TRLKTEAEmalkakeaeneRLKRQAEEEAYQRKLLEDQA--------AQHK---QDIEEKITQLQT-------------- 1899
Cdd:PRK04863 673 PRLNALAE-----------RFGGVLLSEIYDDVSLEDAPyfsalygpARHAivvPDLSDAAEQLAGledcpedlyliegd 741
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1900 -------SSDSELGRQKNIVEETLKQ---KKVVEEEIhiikinFHKASKEK--ADLESElkklkgiADETQKSKLKAEEE 1967
Cdd:PRK04863 742 pdsfddsVFSVEELEKAVVVKIADRQwrySRFPEVPL------FGRAAREKriEQLRAE-------REELAERYATLSFD 808
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1968 AEKLKKLAAEEERRRKEAEEKVkrITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAekeaekqvvlAKEAAQKCTA 2047
Cdd:PRK04863 809 VQKLQRLHQAFSRFIGSHLAVA--FEADPEAELRQLNRRRVELERALADHESQEQQQRSQ----------LEQAKEGLSA 876
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2048 AEQKAQDVlsknkeDVLAQEKLRDEF----------ENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAEneaak 2117
Cdd:PRK04863 877 LNRLLPRL------NLLADETLADRVeeireqldeaEEAKRFVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQ----- 945
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2118 QAKAQNDTEKQRK---------------EAEEEAARRAAAEAAALKQKQ-QADAEMSKHKKEAEQALQQKSQVEKELTvv 2181
Cdd:PRK04863 946 QAQQTQRDAKQQAfaltevvqrrahfsyEDAAEMLAKNSDLNEKLRQRLeQAEQERTRAREQLRQAQAQLAQYNQVLA-- 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2182 KLQLDETDKQKVL--LDQELQRV-----KGEVNDAFKQKSQVEVELARVRIQMEELVKLKLKIEEE----NRRLMQKDKD 2250
Cdd:PRK04863 1024 SLKSSYDAKRQMLqeLKQELQDLgvpadSGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEmdnlTKKLRKLERD 1103
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 2251 STQ-KLLAEEAEKMKSLAEEAGRLSvEAEETARQRQIAESNLAEQRALAEKIL 2302
Cdd:PRK04863 1104 YHEmREQVVNAKAGWCAVLRLVKDN-GVERRLHRRELAYLSADELRSMSDKAL 1155
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2285-2426 |
1.95e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 1.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2285 QIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD------------KETE 2352
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKkyeeqlgnvrnnKEYE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 2353 GFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQrTEKHTTEIVVQKLETQR 2426
Cdd:COG1579 93 ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD-EELAELEAELEELEAER 165
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1222-1448 |
1.99e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 47.07 E-value: 1.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1222 LTEARQRQEKIQAVPISDSRALREQLTDEKKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYKALQDPIASPLKK 1301
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1302 PKMECAsDDIIQEYVNlrTRYSELMTLTNQyiKFIIDAQRRLEDDEKASEKLKEEeRRKMAEIQAELDKQKQMAEAHAKS 1381
Cdd:COG4942 102 QKEELA-ELLRALYRL--GRQPPLALLLSP--EDFLDAVRRLQYLKYLAPARREQ-AEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1382 VAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSlSDQEIKSKNQQLEDALVSRRK 1448
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ-EAEELEALIARLEAEAAAAAE 241
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2505-2587 |
2.09e-04 |
|
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: 46.80 E-value: 2.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2505 EKQLEDEMKKAKALkdeqERQRKLMEEERKKLQAIMDEAVRKQKEA--------EEEMKNKQREMD-VLDKKRLEQEKQL 2575
Cdd:cd16269 197 EKEIEAERAKAEAA----EQERKLLEEQQRELEQKLEDQERSYEEHlrqlkekmEEERENLLKEQErALESKLKEQEALL 272
|
90
....*....|..
gi 1389908286 2576 AEENKKLREQLQ 2587
Cdd:cd16269 273 EEGFKEQAELLQ 284
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1792-2021 |
2.23e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.64 E-value: 2.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1792 ALKMKQLADEAARMRSvaeEAKKQRQIAEEEA--ARQRSEAEKILKEKLAAINEA-TRLK-----------TEAEMALKA 1857
Cdd:PRK05035 440 AIEQEKKKAEEAKARF---EARQARLEREKAAreARHKKAAEARAAKDKDAVAAAlARVKakkaaatqpivIKAGARPDN 516
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1858 KEAENERLKRQAEEEAYQRKLLEDQAAQHKQD-IEEKITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINfhKA 1936
Cdd:PRK05035 517 SAVIAAREARKAQARARQAEKQAAAAADPKKAaVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAK--KA 594
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1937 SKEKADLESELKKLkgiADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKK 2016
Cdd:PRK05035 595 AQQAASAEPEEQVA---EVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEE 671
|
....*
gi 1389908286 2017 AEDAN 2021
Cdd:PRK05035 672 AEDPK 676
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3714-3747 |
2.24e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.24e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908286 3714 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPE 3747
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3013-3048 |
2.36e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 41.16 E-value: 2.36e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1389908286 3013 LQGTPSIAGILDEPTKEKMPFYQAMKKEFLSPETAL 3048
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1951-2175 |
2.43e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1951 KGIADETQKSKLKAEEEAEKLKklaaeeerrrkeaeekvkritaaEEEAARQCKAAQEEVERL-----KKKAEDANKQKE 2025
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQ-----------------------QKQAAEQERLKQLEKERLaaqeqKKQAEEAAKQAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2026 KAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEdvlAQEKLRDEFENAKKLAQEAEKAKEKAEKEaallRQKAEEAE 2105
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---AEAKKKAEAEAAKKAAAEAKKKAEAEAAA----KAAAEAKK 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2106 KQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAaeaaalkqkqqADAEMSKHKKEAEQALQQKSQVE 2175
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAA-----------AEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1489-1907 |
2.48e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 2.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1489 KAAQDEAERLRKQVA-----EETQRKKnAEDELKRKSDAEKEAAKQKQRA---------LDDLQKYKMQAEEAERRMKQA 1554
Cdd:PRK10246 194 KSARTELEKLQAQASgvallTPEQVQS-LTASLQVLTDEEKQLLTAQQQQqqslnwltrLDELQQEASRRQQALQQALAA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1555 EEEKIRQIRVVEeVAQksAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWR 1634
Cdd:PRK10246 273 EEKAQPQLAALS-LAQ--PARQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSAELQAQQQSLN 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1635 QKANEALRLRLQAEEEA--------QKKSHAQEE-------AEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR-- 1697
Cdd:PRK10246 350 TWLAEHDRFRQWNNELAgwraqfsqQTSDREQLRqwqqqltHAEQKLNALPAITLTLTADEVAAALAQHAEQRPLRQRlv 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1698 ----------KFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNeVNSTEKQRKQLEDELNKVRSEMDSLL 1767
Cdd:PRK10246 430 alhgqivpqqKRLAQLQVAIQNVTQEQTQRNAALNEMRQRYKEKTQQLADVKT-ICEQEARIKDLEAQRAQLQAGQPCPL 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1768 -----QMKINAEKASMVNTEKSKQL-LESEalkMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEaEKILKEKLAAI 1841
Cdd:PRK10246 509 cgstsHPAVEAYQALEPGVNQSRLDaLEKE---VKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE-EQALTQQWQAV 584
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 1842 NEATRLKTEAEMALKAKEAENERLKRQAEEEAyQRKLLEDQAAQHKQDI---EEKITQLQTSSDSELGR 1907
Cdd:PRK10246 585 CASLNITLQPQDDIQPWLDAQEEHERQLRLLS-QRHELQGQIAAHNQQIiqyQQQIEQRQQQLLTALAG 652
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2163-2481 |
2.49e-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: 2.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2163 EAEQALQQKSQVEKELTvvkLQLDETDKQKVLLDQELQRVKGEVNDAfkqkSQVEVELARVRIQMEELVKLKlkieEENR 2242
Cdd:COG3096 358 ELTERLEEQEEVVEEAA---EQLAEAEARLEAAEEEVDSLKSQLADY----QQALDVQQTRAIQYQQAVQAL----EKAR 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2243 RLMQKDkDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKE--KMQAIQEATKLKAEAE 2320
Cdd:COG3096 427 ALCGLP-DLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEveRSQAWQTARELLRRYR 505
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2321 KLQKQKDQAQETAKRLQEDKQQI--QQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKK 2398
Cdd:COG3096 506 SQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQ 585
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2399 QADEVKAQLQRTEK-----HTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKeaeelqrkSKEMANAQQEQIE 2473
Cdd:COG3096 586 QLEQLRARIKELAArapawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATV--------ERDELAARKQALE 657
|
....*...
gi 1389908286 2474 QQKAELQQ 2481
Cdd:COG3096 658 SQIERLSQ 665
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1397-1628 |
2.50e-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: 46.76 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1397 KEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDAlvSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQE 1476
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKEL--EQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1477 lrdrAAEAEKLRKAaqdEAERLRKQvAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKykmqAEEAERRmKQAEE 1556
Cdd:TIGR02794 127 ----KQAAEAKAKA---EAEAERKA-KEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKA----KAEAEAK-AKAEE 193
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 1557 EKIRQirvveEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQE-EADKLKKQQKEANTAREEAEQ 1628
Cdd:TIGR02794 194 AKAKA-----EAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGlASGSNAEKQGGARGAAAGSEV 261
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1496-1681 |
2.53e-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: 46.92 E-value: 2.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1496 ERLRKQVAEETQRKKNAEDELKRKSdaeKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEvAQKSAAT 1575
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDLKERES---QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQ-KQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1576 QLQTKAMSFSEQTTKLEESLKKEqgnVLKLQEEAdklkkqQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKS 1655
Cdd:pfam05262 260 LPKPADTSSPKEDKQVAENQKRE---IEKAQIEI------KKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKR 330
|
170 180
....*....|....*....|....*.
gi 1389908286 1656 HAQEEaEKQKLEAERDAKKRGKAEEA 1681
Cdd:pfam05262 331 EPVAE-DLQKTKPQVEAQPTSLNEDA 355
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1213-1656 |
2.61e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.07 E-value: 2.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1213 DSYEWLIRWLTEARQRQEKIQAVpISDSRALREQLTDEKKLLG------EIEKNKDKIDDCHKNAKAYIDSVKDYEFQIL 1286
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAE-LEELREELEKLEKLLQLLPlyqeleALEAELAELPERLEELEERLEELRELEEELE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1287 TYKALQDPIASPLKKpKMECASDDIIQEYVNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRkmAEIQA 1366
Cdd:COG4717 167 ELEAELAELQEELEE-LLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEA--AALEE 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1367 ELDKQKQMAEAHAksvakaeqEALELKMKMKEEASKRQDVAADAekqkQNIQQELQHLKSLSDQEIKSKNQQLEDALVSR 1446
Cdd:COG4717 244 RLKEARLLLLIAA--------ALLALLGLGGSLLSLILTIAGVL----FLVLGLLALLFLLLAREKASLGKEAEELQALP 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1447 RKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKnaedeLKRKSDAEKEA 1526
Cdd:COG4717 312 ALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL-----LAEAGVEDEEE 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1527 AKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQgNVLKLQ 1606
Cdd:COG4717 387 LRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELE-AELEQL 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1607 EEADKLKKQQKEANTAREEAEQELEIWRqkaneALRLRLQAEEEAQKKSH 1656
Cdd:COG4717 466 EEDGELAELLQELEELKAELRELAEEWA-----ALKLALELLEEAREEYR 510
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2724-2757 |
2.63e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.63e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908286 2724 LLEAQAASGFIVDPVKNKFLSVDEAVKDKVIGPE 2757
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1611-1973 |
2.65e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.82 E-value: 2.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1611 KLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAE 1690
Cdd:COG4372 7 KVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1691 KELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLK-------NEVNSTEKQRKQLEDELNKVRSEM 1763
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEaqiaelqSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1764 DSLLQMKINAEKASMVNtekskqllesealKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINE 1843
Cdd:COG4372 167 AALEQELQALSEAEAEQ-------------ALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1844 ATRLKTEAEMALKAKEAENERLK-RQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQKKVV 1922
Cdd:COG4372 234 ALSALLDALELEEDKEELLEEVIlKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGAL 313
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 1923 EEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKK 1973
Cdd:COG4372 314 EDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAE 364
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1604-1711 |
2.67e-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: 44.39 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1604 KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALrlrlqaeEEAQKKSHAQEEAEKQKLEAERDAKKRgKAEEAAL 1683
Cdd:COG0711 35 KIADGLAEAERAKEEAEAALAEYEEKLAEARAEAAEII-------AEARKEAEAIAEEAKAEAEAEAERIIA-QAEAEIE 106
|
90 100 110
....*....|....*....|....*....|...
gi 1389908286 1684 KQKENAEKELDKQ-----RKFAEQIAQQKLSAE 1711
Cdd:COG0711 107 QERAKALAELRAEvadlaVAIAEKILGKELDAA 139
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1384-1888 |
2.86e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 47.49 E-value: 2.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1384 KAEQEALElkmKMKEEASkrqDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKT 1463
Cdd:PRK10246 194 KSARTELE---KLQAQAS---GVALLTPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQALQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1464 TAHKAKSEAELQELRDRAAE-AEKLRKAaqdeAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDdlQKYKM 1542
Cdd:PRK10246 268 QALAAEEKAQPQLAALSLAQpARQLRPH----WERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAK--QSAEL 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1543 QAEEAERRMKQAEEEKIRQIRvvEEVA--------QKSAATQLQTKAMSFSEQTTKL-------------EESLKKEQGN 1601
Cdd:PRK10246 342 QAQQQSLNTWLAEHDRFRQWN--NELAgwraqfsqQTSDREQLRQWQQQLTHAEQKLnalpaitltltadEVAAALAQHA 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1602 --------VLKLQEEADKLKKQQKEANTAREEAEQELeiwrQKANEALRLRLQ-----AEEEAQKKSHAQEEAEKQKLEA 1668
Cdd:PRK10246 420 eqrplrqrLVALHGQIVPQQKRLAQLQVAIQNVTQEQ----TQRNAALNEMRQrykekTQQLADVKTICEQEARIKDLEA 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1669 ERDAKKRGK-------AEEAALKQKENAEKELDKQRKfaEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNE 1741
Cdd:PRK10246 496 QRAQLQAGQpcplcgsTSHPAVEAYQALEPGVNQSRL--DALEKEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQE 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1742 VNSTEKQRKQLEDELNKVRSEMDSL----------------------LQMKINAEKASMVN----TEKSKQLLESE---- 1791
Cdd:PRK10246 574 EQALTQQWQAVCASLNITLQPQDDIqpwldaqeeherqlrllsqrheLQGQIAAHNQQIIQyqqqIEQRQQQLLTAlagy 653
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1792 ALKMKQLADEAARMRSVAEEAKK-QRQIAEEEAARQRSEAEKILKEKLAAINEATrlkTEAEMAL--KAKEAENERLKRQ 1868
Cdd:PRK10246 654 ALTLPQEDEEASWLATRQQEAQSwQQRQNELTALQNRIQQLTPLLETLPQSDDLP---HSEETVAldNWRQVHEQCLSLH 730
|
570 580
....*....|....*....|.
gi 1389908286 1869 AEEEAYQRKL-LEDQAAQHKQ 1888
Cdd:PRK10246 731 SQLQTLQQQDvLEAQRLQKAQ 751
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2163-2436 |
2.87e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 2.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2163 EAEQALQQKSQVEKEltvVKLQLDETDKQKVLLDQELQRVKGEVND-------------AFKQKSQVeVELARVRIQMEE 2229
Cdd:PRK04863 359 ELEERLEEQNEVVEE---ADEQQEENEARAEAAEEEVDELKSQLADyqqaldvqqtraiQYQQAVQA-LERAKQLCGLPD 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2230 LV--KLKLKIEEenrrLMQKDKDSTQKLLAEE-----AEKMKSLAEEAGRL------SVEAEETARQRQIAESNLAEQRA 2296
Cdd:PRK04863 435 LTadNAEDWLEE----FQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRH 510
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2297 LAEKI--LKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEK 2374
Cdd:PRK04863 511 LAEQLqqLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQ 590
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 2375 LKLRVKEL------------SLAQTKAEDEAKKFKKQA-DEVKAQLQRTEKHTTEiVVQKLETQRLQSTREADDL 2436
Cdd:PRK04863 591 LQARIQRLaarapawlaaqdALARLREQSGEEFEDSQDvTEYMQQLLERERELTV-ERDELAARKQALDEEIERL 664
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1613-1766 |
2.88e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 47.32 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1613 KKQQKEANTAREEAEQE----LEiwRQKanealrLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKEN 1688
Cdd:PTZ00491 662 KSQEAAARHQAELLEQEargrLE--RQK------MHDKAKAEEQRTKLLELQAESAAVESSGQSRAEALAEAEARLIEAE 733
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1689 AEKELDKQRKFAEQIAQQklsAEQECIRLKADFEHAEQQRgllDNELQRlknevnstEKQRKQLEDELNKVRSEMDSL 1766
Cdd:PTZ00491 734 AEVEQAELRAKALRIEAE---AELEKLRKRQELELEYEQA---QNELEI--------AKAKELADIEATKFERIVEAL 797
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1340-1573 |
2.93e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 2.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1340 QRRLEDdekasEKLKEEERRKMAEiqAELDKQKQMAEAHAKSVAKAEQEALELKMKMK-EEASKRQDVAADAEKQKQNIQ 1418
Cdd:PRK05035 459 QARLER-----EKAAREARHKKAA--EARAAKDKDAVAAALARVKAKKAAATQPIVIKaGARPDNSAVIAAREARKAQAR 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1419 QELQhlKSLSDQEIKSKNQQLEDALV-SRRKIEEEIHIIRIQLEKTTAHKAKSEAELqelrdraAEAeKLRKAAQDEAER 1497
Cdd:PRK05035 532 ARQA--EKQAAAAADPKKAAVAAAIArAKAKKAAQQAANAEAEEEVDPKKAAVAAAI-------ARA-KAKKAAQQAASA 601
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1498 LRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALD--DLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSA 1573
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEpvDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAA 679
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3788-3824 |
3.07e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.07e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1389908286 3788 LRLLEAQNATGGYMDPEYYFRLPIDVAMQRGYINKET 3824
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3381-3414 |
3.07e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.07e-04
10 20 30
....*....|....*....|....*....|....
gi 1389908286 3381 LLEAQAATGFITDPVKDKKCSVDDAVKEGIVGPE 3414
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2148-2398 |
3.33e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 46.06 E-value: 3.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2148 KQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQK---SQVEVELARVR 2224
Cdd:COG1340 43 EKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREELDELRKELAELNKAGgsiDKLRKEIERLE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2225 IQMEELVklkLKIEEEnRRLMQKDKDSTQKLlaEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKE 2304
Cdd:COG1340 123 WRQQTEV---LSPEEE-KELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEE 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2305 KMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKetegFQKSLEAERKRQLEASaeaeklklRVKELSL 2384
Cdd:COG1340 197 MIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELKKLRKKQRALK--------REKEKEE 264
|
250
....*....|....
gi 1389908286 2385 AQTKAEDEAKKFKK 2398
Cdd:COG1340 265 LEEKAEEIFEKLKK 278
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1787-2021 |
3.43e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1787 LLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLK 1866
Cdd:COG4942 10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1867 RQAEEeayqrklLEDQAAQHKQDIEEKITQLQTSSDSE----LGRQKNIVE-----ETLKQ-KKVVEEEIHIIKINFHKA 1936
Cdd:COG4942 90 KEIAE-------LRAELEAQKEELAELLRALYRLGRQPplalLLSPEDFLDavrrlQYLKYlAPARREQAEELRADLAEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1937 SKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKK 2016
Cdd:COG4942 163 AALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
....*
gi 1389908286 2017 AEDAN 2021
Cdd:COG4942 243 TPAAG 247
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
7-129 |
3.55e-04 |
|
second calponin homology (CH) domain found in beta-parvin; 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. It is involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia and also plays a role in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Beta-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: 409187 Cd Length: 130 Bit Score: 43.42 E-value: 3.55e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 7 RDFMETLIQRGQDERDrVQKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQ 82
Cdd:cd21338 5 RDAFDTLFDHAPDKLS-VVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVH 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1389908286 83 NVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 129
Cdd:cd21338 84 NVSFAFELMQDGGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2106-2372 |
3.71e-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: 47.14 E-value: 3.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2106 KQKKAAENEAAKQAKAQNDteKQRkeaeeeaarraaaeaaaLKQ-KQQADAEMSKHKKEAE----QALQQKSQVEKEltV 2180
Cdd:NF012221 1552 KQDDAAQNALADKERAEAD--RQR-----------------LEQeKQQQLAAISGSQSQLEstdqNALETNGQAQRD--A 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2181 VKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELA---RVRIQmEELVKLKLKIEEENRRLMQKDKDSTQKLla 2257
Cdd:NF012221 1611 ILEESRAVTKELTTLAQGLDALDSQATYAGESGDQWRNPFAgglLDRVQ-EQLDDAKKISGKQLADAKQRHVDNQQKV-- 1687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2258 eeaekMKSLAE-EAGrlsveAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLK----AEAEKLQKQKDQAQET 2332
Cdd:NF012221 1688 -----KDAVAKsEAG-----VAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAEsdanAAANDAQSRGEQDASA 1757
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1389908286 2333 AK----RLQEDKQQIQQRLDK--ETEGFQKSLEAERKRQLEASAEA 2372
Cdd:NF012221 1758 AEnkanQAQADAKGAKQDESDkpNRQGAAGSGLSGKAYSVEGVAEP 1803
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1339-1597 |
3.80e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 45.90 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1339 AQRRLEDDEKASEKLKE----EERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMkeeaskrQDVAADAEKQK 1414
Cdd:pfam09787 16 AARILQSKEKLIASLKEgsgvEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTEL-------QELEAQQQEEA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1415 QNIQQELQHLKSlsDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTahkakseaeLQE-LRDRAAEAEKlrkaaqd 1493
Cdd:pfam09787 89 ESSREQLQELEE--QLATERSARREAEAELERLQEELRYLEEELRRSKAT---------LQSrIKDREAEIEK------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1494 eaerLRKQVAEETQrKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYK----MQAEEAERRMKQAEEEKIRQIRVVEEVA 1569
Cdd:pfam09787 151 ----LRNQLTSKSQ-SSSSQSELENRLHQLTETLIQKQTMLEALSTEKnslvLQLERMEQQIKELQGEGSNGTSINMEGI 225
|
250 260
....*....|....*....|....*...
gi 1389908286 1570 QKSAATQLQTKAMSFSEQTTKLEESLKK 1597
Cdd:pfam09787 226 SDGEGTRLRNVPGLFSESDSDRAGMYGK 253
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2284-2433 |
3.83e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 46.69 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2284 RQIAESNLAEQRALAEKILKE---KMQAIQEATKLKAEaEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEA 2360
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEakkEAEAIKKEALLEAK-EEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2361 ERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ--------ADEVKAQ-LQRTE---KHTTEIVVQKLETQ-RL 2427
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQElerisgltAEEAKEIlLEKVEeeaRHEAAVLIKEIEEEaKE 184
|
....*.
gi 1389908286 2428 QSTREA 2433
Cdd:PRK12704 185 EADKKA 190
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1815-2498 |
3.94e-04 |
|
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: 46.76 E-value: 3.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1815 QRQIAEEEAARQrsEAEKILKEKLAA--------INEATRLKTEAEMALKAKEAENERLKRQA----EEEAYQRKLLEDQ 1882
Cdd:pfam12128 271 ETLIASRQEERQ--ETSAELNQLLRTlddqwkekRDELNGELSAADAAVAKDRSELEALEDQHgaflDADIETAAADQEQ 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1883 AAQHKQDIE--EKITQLQTSSDSEL-----GRQKNIVEETLKQKKVVEEEIHIIKinfHKASKEKADLESELKKLKG-IA 1954
Cdd:pfam12128 349 LPSWQSELEnlEERLKALTGKHQDVtakynRRRSKIKEQNNRDIAGIKDKLAKIR---EARDRQLAVAEDDLQALESeLR 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1955 DETQKSKLKAEEEAEKLKklaaeeeRRRKEAEEKVKRITAAEEEAARQcKAAQEEVERLKKKAEDANKQKEkaekeaekq 2034
Cdd:pfam12128 426 EQLEAGKLEFNEEEYRLK-------SRLGELKLRLNQATATPELLLQL-ENFDERIERAREEQEAANAEVE--------- 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2035 vvlakeAAQKctaaEQKAQDVLSKNKEDVLAQEKLRDEfENAKKLAQEAEKAKEKAEKEAALLRQkaeEAEKQKKAAENE 2114
Cdd:pfam12128 489 ------RLQS----ELRQARKRRDQASEALRQASRRLE-ERQSALDELELQLFPQAGTLLHFLRK---EAPDWEQSIGKV 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2115 AAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSkhkkeaEQALQQK-SQVEKELTVVKLQLDETDKQKV 2193
Cdd:pfam12128 555 ISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAAS------EEELRERlDKAEEALQSAREKQAAAEEQLV 628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2194 LLDQELQRVKGEVNDAFKQKSQVEVELARVRIQMEElvkLKLKIEEENRRLMQKDKDSTQKLLAE----EAEKMKSLAEE 2269
Cdd:pfam12128 629 QANGELEKASREETFARTALKNARLDLRRLFDEKQS---EKDKKNKALAERKDSANERLNSLEAQlkqlDKKHQAWLEEQ 705
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2270 AGRLSVEAEETARQRQIAESNLAEQRA-LAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLD 2348
Cdd:pfam12128 706 KEQKREARTEKQAYWQVVEGALDAQLAlLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIE 785
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2349 KETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRtEKHTTEivvqKLETQRLQ 2428
Cdd:pfam12128 786 RIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEM-ERKASE----KQQVRLSE 860
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 2429 STREADDLKSAIADLeeerkklkkeaeelqrksKEMANAQQEQ--IEQQKAELQQSFLTEKGLLLKREKEVE 2498
Cdd:pfam12128 861 NLRGLRCEMSKLATL------------------KEDANSEQAQgsIGERLAQLEDLKLKRDYLSESVKKYVE 914
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1782-2012 |
4.25e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 4.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1782 EKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAe 1861
Cdd:TIGR02794 69 RQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEE- 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1862 nerLKRQAEEEAyqrKLLEDQAAQHKQDIEEKITqlqtssdselgrqknivEETLKQKKVVEEeihiikinfhKASKEKA 1941
Cdd:TIGR02794 148 ---AAKQAEEEA---KAKAAAEAKKKAEEAKKKA-----------------EAEAKAKAEAEA----------KAKAEEA 194
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 1942 DLESELKKLKGIADetqksklkAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEE--AARQCKAAQEEVER 2012
Cdd:TIGR02794 195 KAKAEAAKAKAAAE--------AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGsnAEKQGGARGAAAGS 259
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1340-1973 |
4.48e-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: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1340 QRRLEDDEKASEKLKEEErrkmaEIQAELDKQKQMAEAHAKSvakAEQEALELKMKMK--EEASKRQDVAADAEKQKQNI 1417
Cdd:COG3096 350 ERYQEDLEELTERLEEQE-----EVVEEAAEQLAEAEARLEA---AEEEVDSLKSQLAdyQQALDVQQTRAIQYQQAVQA 421
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1418 QQELQHLKSLSD----------QEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEK--------------TTAHKAKSE-- 1471
Cdd:COG3096 422 LEKARALCGLPDltpenaedylAAFRAKEQQATEEVLELEQKLSVADAARRQFEKayelvckiageverSQAWQTAREll 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1472 ----------AELQELRDRAAEAEKlRKAAQDEAERLRKQVAEETQRKKNAEDELkrksDAEKEAAKQKQRALDDLQkyk 1541
Cdd:COG3096 502 rryrsqqalaQRLQQLRAQLAELEQ-RLRQQQNAERLLEEFCQRIGQQLDAAEEL----EELLAELEAQLEELEEQA--- 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1542 mqAEEAERRMK-QAEEEKIRQiRVVEEVAQKSAATQLQTKAMSFSEQTtklEESLKKEQGNVLKLQEEADKLKKQQKEAN 1620
Cdd:COG3096 574 --AEAVEQRSElRQQLEQLRA-RIKELAARAPAWLAAQDALERLREQS---GEALADSQEVTAAMQQLLEREREATVERD 647
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1621 TAREEAEQ-ELEIWRQKA---NEALRLRLQAE----------------EEAQKKS------------------------- 1655
Cdd:COG3096 648 ELAARKQAlESQIERLSQpggAEDPRLLALAErlggvllseiyddvtlEDAPYFSalygparhaivvpdlsavkeqlagl 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1656 ----------------------HAQEEA----------------------------EKQ--KLEAERDAKKRGKAEEAAL 1683
Cdd:COG3096 728 edcpedlyliegdpdsfddsvfDAEELEdavvvklsdrqwrysrfpevplfgraarEKRleELRAERDELAEQYAKASFD 807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1684 KQkenaekeldKQRKFAEQIAQqkLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQ-RKQLE------DEL 1756
Cdd:COG3096 808 VQ---------KLQRLHQAFSQ--FVGGHLAVAFAPDPEAELAALRQRRSELERELAQHRAQEQQlRQQLDqlkeqlQLL 876
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1757 NKVRSEM----DSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEE-----AKKQRQIAEEEAARQR 1827
Cdd:COG3096 877 NKLLPQAnllaDETLADRLEELREELDAAQEAQAFIQQHGKALAQLEPLVAVLQSDPEQfeqlqADYLQAKEQQRRLKQQ 956
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1828 SEAEKILKEKLAAINEAtrlktEAEMALKAKEAENERLK---RQAEEEAYQ-RKLLEDQAAQHKQdieekITQLQTSSDS 1903
Cdd:COG3096 957 IFALSEVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREaREQLRQAQAQYSQ-----YNQVLASLKS 1026
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 1904 ELgRQKNiveETLKQkkvVEEEIHIIKINF-----HKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKK 1973
Cdd:COG3096 1027 SR-DAKQ---QTLQE---LEQELEELGVQAdaeaeERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQK 1094
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2254-2579 |
4.48e-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: 4.48e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2254 KLLAEEAEkmkSLAEEAGRLSVEAEETARQRQIAESNLAEQRALA-----EKILKEKMQAIQEATK-LKAEAEKLQKQKD 2327
Cdd:COG3096 788 EELRAERD---ELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAfapdpEAELAALRQRRSELEReLAQHRAQEQQLRQ 864
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2328 QAQETAKRLQE-----------DKQQIQQRLDKETEGFQKSLEAER--KRQLEASAEAEKL--KLRVKELSLAQTKAEDE 2392
Cdd:COG3096 865 QLDQLKEQLQLlnkllpqanllADETLADRLEELREELDAAQEAQAfiQQHGKALAQLEPLvaVLQSDPEQFEQLQADYL 944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2393 akkfkkQADEVKAQLQRTEKHTTEIVvqkletQRLQ--STREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQE 2470
Cdd:COG3096 945 ------QAKEQQRRLKQQIFALSEVV------QRRPhfSYEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQA 1012
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2471 QIEQQKAELQQ---SFLTEKGLLlkreKEVEGEKKRFEKQLEDEMK-KAKALKDE------QERQRK-LMEEERKKLQAI 2539
Cdd:COG3096 1013 QYSQYNQVLASlksSRDAKQQTL----QELEQELEELGVQADAEAEeRARIRRDElheelsQNRSRRsQLEKQLTRCEAE 1088
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1389908286 2540 MDEAVRKQKEAEEEMKNkQREMDVLDKKRLEQEKQLAEEN 2579
Cdd:COG3096 1089 MDSLQKRLRKAERDYKQ-EREQVVQAKAGWCAVLRLARDN 1127
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3013-3047 |
4.69e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.69e-04
10 20 30
....*....|....*....|....*....|....*
gi 1389908286 3013 LQGTPSIAGILDEPTKEKMPFYQAMKKEFLSPETA 3047
Cdd:smart00250 4 LEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2272-2586 |
4.77e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.05 E-value: 4.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2272 RLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKEt 2351
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAA- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2352 egfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVVQKLETQRLQSTR 2431
Cdd:COG4372 93 ---QAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2432 EADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDE 2511
Cdd:COG4372 170 EQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKE 249
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 2512 MKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQL 2586
Cdd:COG4372 250 ELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2147-2313 |
4.89e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 4.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2147 LKQKQQADAEMSKHKKEA-EQALQQKSQVEKELTVVKLQLDETDKQKVLLD-QELQRvkgEVNDAFKQKSQVEVELARVR 2224
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARRErEELQR---EEERLVQKEEQLDARAEKLD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2225 IQMEELVKLKLKIEEENRRLMQKDKDSTQKLlaEEAEKMKS---LAEEAGRLSVEAEETARQR--QIAESNLAEQRALAE 2299
Cdd:PRK12705 102 NLENQLEEREKALSARELELEELEKQLDNEL--YRVAGLTPeqaRKLLLKLLDAELEEEKAQRvkKIEEEADLEAERKAQ 179
|
170
....*....|....
gi 1389908286 2300 KILKEKMQAIQEAT 2313
Cdd:PRK12705 180 NILAQAMQRIASET 193
|
|
| Nup88 |
pfam10168 |
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal ... |
1380-1626 |
5.00e-04 |
|
Nuclear pore component; Nup88 can be divided into two structural domains; the N-terminal two-thirds of the protein has no obvious structural motifs but is the region for binding to Nup98, one of the components of the nuclear pore. the C-terminal end is a predicted coiled-coil domain. Nup88 is overexpressed in tumour cells.
Pssm-ID: 462975 [Multi-domain] Cd Length: 713 Bit Score: 46.19 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1380 KSVAKAEQEALELKMK----MKEEASKRQDVAadaekqkqniQQELQ-HLKSLSDQeiksKNQQLEDalvsrrkieeeih 1454
Cdd:pfam10168 524 KLSSPSPQECLQLLSRatqvFREEYLKKHDLA----------REEIQkRVKLLKLQ----KEQQLQE------------- 576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1455 iiriqlekttahkakseaeLQELRDraaEAEKLRKAAQDEAERLR----KQvaEETQRK-----KNAEDELKRKSDAEKE 1525
Cdd:pfam10168 577 -------------------LQSLEE---ERKSLSERAEKLAEKYEeikdKQ--EKLMRRckkvlQRLNSQLPVLSDAERE 632
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1526 AAKQkqralddLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQksaatQLQTKAMSFSEqttkleeslkkEQGNVLK- 1604
Cdd:pfam10168 633 MKKE-------LETINEQLKHLANAIKQAKKKMNYQRYQIAKSQS-----IRKKSSLSLSE-----------KQRKTIKe 689
|
250 260
....*....|....*....|...
gi 1389908286 1605 -LQEEADKLKKQQKEANTAREEA 1626
Cdd:pfam10168 690 iLKQLGSEIDELIKQVKDINKHV 712
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2798-2834 |
5.03e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.03e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1389908286 2798 TKFLDVQLATGGIIDPVNSHRVPLQTAYSQGQFDADM 2834
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1597-2177 |
5.30e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1597 KEQGNVLK-LQEEADKLKKQQKEANTARE--------EAEQELEIWRQK--ANEALRLRLQAEEEAQKKSHAQEEAEKQK 1665
Cdd:COG4913 248 REQIELLEpIRELAERYAAARERLAELEYlraalrlwFAQRRLELLEAEleELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1666 LEAERDAKKrGKAEEAALKQKENAEKELDKQR----KFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNE 1741
Cdd:COG4913 328 LEAQIRGNG-GDRLEQLEREIERLERELEERErrraRLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1742 VNSTEKQRKQLEDELNKVRSEMDSLlqmkinaekasmvntEKSKQLLESEALKM-KQLADE----AARMRSVAEEAkkqr 1816
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASL---------------ERRKSNIPARLLALrDALAEAlgldEAELPFVGELI---- 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1817 QIAEEEAARQRSeAEKILKeklaaiNEATRLKTEAEMALKAKEA-ENERLKRQ-------AEEEAYQRKLLEDQAAQHKQ 1888
Cdd:COG4913 468 EVRPEEERWRGA-IERVLG------GFALTLLVPPEHYAAALRWvNRLHLRGRlvyervrTGLPDPERPRLDPDSLAGKL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1889 DIEEkiTQLQTSSDSELGRQKNIV----EETLKQ-KKVVEEEIHIikinfhKASKEKADleselkklKGIADETQKSKLK 1963
Cdd:COG4913 541 DFKP--HPFRAWLEAELGRRFDYVcvdsPEELRRhPRAITRAGQV------KGNGTRHE--------KDDRRRIRSRYVL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1964 AEEEAEKLKKLAAEeerrrkeaeekVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEaekqvVLAKEAAQ 2043
Cdd:COG4913 605 GFDNRAKLAALEAE-----------LAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDE-----IDVASAER 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2044 KCTAAEQKAQDvLSKNKEDVLAQEKLRDEfenakklaqeaekakekaekeaalLRQKAEEAEKQKKAAENEAAKQAKAQN 2123
Cdd:COG4913 669 EIAELEAELER-LDASSDDLAALEEQLEE------------------------LEAELEELEEELDELKGEIGRLEKELE 723
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 2124 DTEKQRKEAEEEAARRAAAEAAALKQ---KQQADAEMSKHKKEAEQALQQKSQVEKE 2177
Cdd:COG4913 724 QAEEELDELQDRLEAAEDLARLELRAlleERFAAALGDAVERELRENLEERIDALRA 780
|
|
| Nop53 |
pfam07767 |
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ... |
1475-1597 |
5.65e-04 |
|
Nop53 (60S ribosomal biogenesis); This nucleolar family of proteins are involved in 60S ribosomal biogenesis. They are specifically involved in the processing beyond the 27S stage of 25S rRNA maturation. This family contains sequences that bear similarity to the glioma tumour suppressor candidate region gene 2 protein (p60). This protein has been found to interact with herpes simplex type 1 regulatory proteins.
Pssm-ID: 462259 [Multi-domain] Cd Length: 353 Bit Score: 45.75 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1475 QELRDRAAEAEKLRKAAQDEAERLRKQVAEEtqRKKNAEDELKRKSDAEKEAAKQKQRALddlqkyKMQAEEAERRMKQA 1554
Cdd:pfam07767 198 QELLQKAVEAEKKRLKEEEKLERVLEKIAES--AATAEAREEKRKTKAQRNKEKRRKEEE------REAKEEKALKKKLA 269
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1389908286 1555 EEEKIRQIRvvEEVAQKSAATQLQTKAMSFSEQTTKLEESLKK 1597
Cdd:pfam07767 270 QLERLKEIA--KEIAEKEKEREEKAEARKREKRKKKKEEKKLR 310
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1327-1603 |
5.69e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 46.16 E-value: 5.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1327 TLTNQYIKFIIDAQRrlEDDEKASEKLKEEerrkMAEIQAELDKqkqmaeahaksvakAEQEALELKMKMKEEASKRQdv 1406
Cdd:COG3206 156 ALAEAYLEQNLELRR--EEARKALEFLEEQ----LPELRKELEE--------------AEAALEEFRQKNGLVDLSEE-- 213
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1407 AADAEKQKQNIQQELQHLKSLSdQEIKSKNQQLEDALvSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEK 1486
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAEL-AEAEARLAALRAQL-GSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHP 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1487 LRKAAQDEAERLRKQVAEETQRkknaedeLKRKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMKQAEEEKIRQIRVVE 1566
Cdd:COG3206 292 DVIALRAQIAALRAQLQQEAQR-------ILASLEAELEALQAREASLQA------QLAQLEARLAELPELEAELRRLER 358
|
250 260 270
....*....|....*....|....*....|....*...
gi 1389908286 1567 EV-AQKSAATQLQTKAmsfseQTTKLEESLKKEQGNVL 1603
Cdd:COG3206 359 EVeVARELYESLLQRL-----EEARLAEALTVGNVRVI 391
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
25-122 |
5.74e-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: 43.42 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 25 QKKTFTKWVNKHLVKAQ--RHV-------TDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 91
Cdd:cd21292 25 EKVAFVNWINKNLGDDPdcKHLlpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1389908286 92 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 122
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1319-1713 |
5.75e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.05 E-value: 5.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1319 RTRYSELMTLTNQYIKF---IIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMK 1395
Cdd:COG5278 106 QARLDELEALIDQWLAEleqVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1396 MKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQ 1475
Cdd:COG5278 186 LALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAA 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1476 ELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAE 1555
Cdd:COG5278 266 ALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1556 EEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESlkkEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQ 1635
Cdd:COG5278 346 LLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGA---AEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1636 KANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQE 1713
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALS 500
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2285-2479 |
6.02e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.61 E-value: 6.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2285 QIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQIQQRLDKETEgfQKSLEAERKR 2364
Cdd:TIGR02794 36 EIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKA--AKQAEQAAKQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2365 QLEASAEAEKLKLrvKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIvvqKLETQRLQSTREADDLKSAIADLE 2444
Cdd:TIGR02794 114 AEEKQKQAEEAKA--KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEA---KKKAEEAKKKAEAEAKAKAEAEAK 188
|
170 180 190
....*....|....*....|....*....|....*
gi 1389908286 2445 EERKKLKKEAEELQRKSKEMANAQQEQIEQQKAEL 2479
Cdd:TIGR02794 189 AKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAA 223
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
160-241 |
6.11e-04 |
|
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: 42.29 E-value: 6.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 160 RCDNFTTSWRDGKLFSAIIHKHRPALIDMNQVYRQSNQENLEQ-AFSVAE--RELGVTKLLDPEDVDVPHPDEksIITYV 236
Cdd:cd21218 32 RVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEVLSEEDLEKrAEKVLQaaEKLGCKYFLTPEDIVSGNPRL--NLAFV 109
|
....*
gi 1389908286 237 SSLYD 241
Cdd:cd21218 110 ATLFN 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2465-2612 |
6.36e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.08 E-value: 6.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2465 ANAQQEQIEQQKAELQQsfltEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALkdeQERQRKLmEEERKKLQAIMDEAV 2544
Cdd:COG1196 237 LEAELEELEAELEELEA----ELEELEAELAELEAELEELRLELEELELELEEA---QAEEYEL-LAELARLEQDIARLE 308
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2545 RKQKEAEEEMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVA 2612
Cdd:COG1196 309 ERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE 376
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1722-1858 |
6.37e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 6.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1722 EHAEQQ-RGLLdnELQRLKNEVnSTEKQRKQLedelnkvrsemdslLQMKinAEKASMVNTEKSKQ--LLESEALKMKQL 1798
Cdd:PTZ00491 673 ELLEQEaRGRL--ERQKMHDKA-KAEEQRTKL--------------LELQ--AESAAVESSGQSRAeaLAEAEARLIEAE 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1799 AD-EAARMRSVAE------EAKKQRQIAEEEAARQRSEAE-KILKEKLAAINEATRLK---------TEAEMA-----LK 1856
Cdd:PTZ00491 734 AEvEQAELRAKALrieaeaELEKLRKRQELELEYEQAQNElEIAKAKELADIEATKFErivealgreTLIAIAragpeLQ 813
|
..
gi 1389908286 1857 AK 1858
Cdd:PTZ00491 814 AK 815
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1566-1749 |
6.47e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.59 E-value: 6.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1566 EEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALR--- 1642
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARaly 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1643 -------------------------LRLQAEEEAQKK-----SHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKE 1692
Cdd:COG3883 97 rsggsvsyldvllgsesfsdfldrlSALSKIADADADlleelKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQ 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1693 LDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1749
Cdd:COG3883 177 QAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAA 233
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1461-1696 |
6.65e-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: 45.79 E-value: 6.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1461 EKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKK---------NAEDELKRKSDAEKEAAKQKQ 1531
Cdd:pfam05667 255 QLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEklqftneapAATSSPPTKVETEEELQQQRE 334
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1532 RALDDLQKykmQAEEAERRMKQAEEE------KIRQirVVEEVAQKSAATQLQTKAMSFSEQTTKLeesLKKEQGNVLKL 1605
Cdd:pfam05667 335 EELEELQE---QLEDLESSIQELEKEikklesSIKQ--VEEELEELKEQNEELEKQYKVKKKTLDL---LPDAEENIAKL 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1606 QEEADKLKkqQKEANTAREeaeqeleiWrqkanEALRLRLQAEEEAQKKSHAQEEAE-KQKLEAERDAKKRGKAEEAALK 1684
Cdd:pfam05667 407 QALVDASA--QRLVELAGQ--------W-----EKHRVPLIEEYRALKEAKSNKEDEsQRKLEEIKELREKIKEVAEEAK 471
|
250
....*....|..
gi 1389908286 1685 QKENAEKELDKQ 1696
Cdd:pfam05667 472 QKEELYKQLVAE 483
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2279-2480 |
6.66e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 44.81 E-value: 6.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2279 ETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQ-KQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKS 2357
Cdd:pfam17045 57 EIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQrKQLKEAREEAKSREEDRSELSRLNGKLEEFRQKS 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2358 LEAERKR----QLEASAEAEKlKLRVKELSLAQTKAEDEAKKFKKQADE-VKAQLQR----TEKHTTEIVVQKLETQRLQ 2428
Cdd:pfam17045 137 LEWEQQRlqyqQQVASLEAQR-KALAEQSSLIQSAAYQVQLEGRKQCLEaSQSEIQRlrskLERAQDSLCAQELELERLR 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 2429 StreaddLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQ 2480
Cdd:pfam17045 216 M------RVSELGDSNRKLLEEQQRLLEELRMSQRQLQVLQNELMELKATLQ 261
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1801-2018 |
7.27e-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: 45.66 E-value: 7.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1801 EAARMRSVAEEAKKQRQIAEEEAARQRSEAE---KILKEKLAAINEATRLKTEAEMALKAKEAEnerLKRQAEEEAYQRK 1877
Cdd:pfam07888 42 ERAELLQAQEAANRQREKEKERYKRDREQWErqrRELESRVAELKEELRQSREKHEELEEKYKE---LSASSEELSEEKD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1878 LLEDQAAQHKQDIEE------KITQLQTSSDSELGRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLK 1951
Cdd:pfam07888 119 ALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELR 198
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1952 GIADETQKSKLKAEEEAEKLKKLAAEEerrrkeaeekvKRITAAEEEAARQCKAAQEEVERLKKKAE 2018
Cdd:pfam07888 199 NSLAQRDTQVLQLQDTITTLTQKLTTA-----------HRKEAENEALLEELRSLQERLNASERKVE 254
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1501-1668 |
7.31e-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: 44.31 E-value: 7.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1501 QVAEETQRKKNAEDELKRKSDAEKE---AAKQKQRalddlqKYKMQAEEAERRMKQAEEEKiRQirvveEVAQKSAATQL 1577
Cdd:pfam13904 34 QSSSLTYARKLEGLKLERQPLEAYEnwlAAKQRQR------QKELQAQKEEREKEEQEAEL-RK-----RLAKEKYQEWL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1578 QTKAmsfsEQTTKLEESLKKEQGNvLKLQEEADKLKKQQKEantarEEAEQELEIWRQKANEALRLRLQAEEEAQKKSHA 1657
Cdd:pfam13904 102 QRKA----RQQTKKREESHKQKAA-ESASKSLAKPERKVSQ-----EEAKEVLQEWERKKLEQQQRKREEEQREQLKKEE 171
|
170
....*....|.
gi 1389908286 1658 QEEAEKQKLEA 1668
Cdd:pfam13904 172 EEQERKQLAEK 182
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1362-1760 |
7.35e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.10 E-value: 7.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1362 AEIQAELDKQKQMA---EAHAKSVAKAEQEALELKMKMKEEASKRQDVAAdAEKQKQNIQQELQHLKSLsdqeiksknqq 1438
Cdd:PRK04863 897 EEIREQLDEAEEAKrfvQQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQ-AQQTQRDAKQQAFALTEV----------- 964
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1439 ledalVSRRkieeeihiiriqlekttAHKAKSEA--------ELQE-LRDRAAEAEKLRKAAQDEAERLRKQVAEETQRK 1509
Cdd:PRK04863 965 -----VQRR-----------------AHFSYEDAaemlaknsDLNEkLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVL 1022
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1510 KNAEDELKRKSDAEKEAAKqkqraldDLQKYKMQA-EEAERRMKQAEEEKIRQIRvveevAQKSAATQLQTkamsfseQT 1588
Cdd:PRK04863 1023 ASLKSSYDAKRQMLQELKQ-------ELQDLGVPAdSGAEERARARRDELHARLS-----ANRSRRNQLEK-------QL 1083
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1589 TKLEESLKKEQGnvlklqeeadKLKKQQKEANTAREEAEQeleiwrQKANEALRLRLQAEEEAQKKSHAQEEAEkQKLEA 1668
Cdd:PRK04863 1084 TFCEAEMDNLTK----------KLRKLERDYHEMREQVVN------AKAGWCAVLRLVKDNGVERRLHRRELAY-LSADE 1146
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1669 ERDAkkRGKAEEAALKQKENAEKELDKQR-----KFAEQIAQ------QKLS--AEQECIRLKADFEHAEQqrglLDNEL 1735
Cdd:PRK04863 1147 LRSM--SDKALGALRLAVADNEHLRDVLRlsedpKRPERKVQfyiavyQHLRerIRQDIIRTDDPVEAIEQ----MEIEL 1220
|
410 420 430
....*....|....*....|....*....|....*..
gi 1389908286 1736 QRLKNEVNSTEKQ------------RKQLEDELNKVR 1760
Cdd:PRK04863 1221 SRLTEELTSREQKlaissesvaniiRKTIQREQNRIR 1257
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2060-2377 |
7.67e-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: 45.72 E-value: 7.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2060 KEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARR 2139
Cdd:COG5185 261 QNTDLRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETGIQN 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2140 AAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDETDKQKVLLDQELQRVKGEVNDAF--------K 2211
Cdd:COG5185 341 LTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLedtlkaadR 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2212 QKSQVEVELARVRIQMEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSlaeeagRLSVEAEETARQRQIAESNL 2291
Cdd:COG5185 421 QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINR------SVRSKKEDLNEELTQIESRV 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2292 AEqralaekiLKEKMQaiQEATKLKAEAEKLQKQKDQAQETAKRLqEDKQQIQQRLDKETE----GFQKSLEAERKRQLE 2367
Cdd:COG5185 495 ST--------LKATLE--KLRAKLERQLEGVRSKLDQVAESLKDF-MRARGYAHILALENLipasELIQASNAKTDGQAA 563
|
330
....*....|
gi 1389908286 2368 ASAEAEKLKL 2377
Cdd:COG5185 564 NLRTAVIDEL 573
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
20-128 |
8.14e-04 |
|
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: 42.28 E-value: 8.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 20 ERDRVQKKTFTKWVNKHLVKAQrhVTDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 90
Cdd:cd21330 9 EGETREERTFRNWMNSLGVNPR--VNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1389908286 91 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 128
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1742-2076 |
8.35e-04 |
|
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: 45.50 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1742 VNSTEKQRKQLEDELNKVRSEMDSLLQmkinaekasmvNTEKSKQLLESEALKMKQLADEAA----RMRSVAEEAKKQRQ 1817
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEEKAR-----------EVERRRKLEEAEKARQAEMDRQAAiyaeQERMAMERERELER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1818 IAEEEAARqrsEAEKILKEKLAAinEATRLKtEAEMALKAKEAENERLkRQAEEEAYQRKLLEDQaaQHKQDIEEKITQL 1897
Cdd:pfam17380 353 IRQEERKR---ELERIRQEEIAM--EISRMR-ELERLQMERQQKNERV-RQELEAARKVKILEEE--RQRKIQQQKVEME 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1898 QTSSDSELGRQKNIveETLKQKKVVEEEihiikinfhKASKEKADLESELKKLKgiADETQKSKLKAEEEAEKLKKLAAE 1977
Cdd:pfam17380 424 QIRAEQEEARQREV--RRLEEERAREME---------RVRLEEQERQQQVERLR--QQEEERKRKKLELEKEKRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1978 EERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAA--EQKAQDV 2055
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKAteERSRLEA 570
|
330 340
....*....|....*....|....
gi 1389908286 2056 LSKNKE---DVLAQEKLRDEFENA 2076
Cdd:pfam17380 571 MEREREmmrQIVESEKARAEYEAT 594
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2251-2549 |
8.42e-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: 45.71 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2251 STQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAE-QRAL--AEKI-------------LKEKMQAIQEATK 2314
Cdd:COG3096 296 GARRQLAEEQYRLVEMARELEELSARESDLEQDYQAASDHLNLvQTALrqQEKIeryqedleelterLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2315 LKAEAEKlqkQKDQAQETAKRLQEDKQQIQQRLD-KETEGFQKsleaerkRQ-LEASAEAEKLkLRVKELSLAQtkAEDE 2392
Cdd:COG3096 376 QLAEAEA---RLEAAEEEVDSLKSQLADYQQALDvQQTRAIQY-------QQaVQALEKARAL-CGLPDLTPEN--AEDY 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2393 AKKFKKQADEVKAQLQRTEkhtteivvQKL---ETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQ 2469
Cdd:COG3096 443 LAAFRAKEQQATEEVLELE--------QKLsvaDAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRYRSQQALAQRL 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2470 EQIEQQKAELQQsfltekglLLKREKEVEGEKKRFEKQ----------LEDEMKKAKALKDEQERQRKLMEEERKKLQAI 2539
Cdd:COG3096 515 QQLRAQLAELEQ--------RLRQQQNAERLLEEFCQRigqqldaaeeLEELLAELEAQLEELEEQAAEAVEQRSELRQQ 586
|
330
....*....|
gi 1389908286 2540 MDEAVRKQKE 2549
Cdd:COG3096 587 LEQLRARIKE 596
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1575-1897 |
8.45e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.28 E-value: 8.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1575 TQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKK 1654
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1655 SHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNE 1734
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1735 LQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKK 1814
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1815 QRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKI 1894
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
...
gi 1389908286 1895 TQL 1897
Cdd:COG4372 368 ADG 370
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2475-2590 |
8.54e-04 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.59 E-value: 8.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2475 QKAELQQSFLTEKglllkreKEVEGEKKRFEKQL---EDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKE-- 2549
Cdd:pfam02841 173 KAEEVLQEFLQSK-------EAVEEAILQTDQALtakEKAIEAERAKAEAAEAEQELLREKQKEEEQMMEAQERSYQEhv 245
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 2550 ------AEEEMKNKQREMD-VLDKKRLEQEKQLAE----ENKKLREQLQTFE 2590
Cdd:pfam02841 246 kqliekMEAEREQLLAEQErMLEHKLQEQEELLKEgfktEAESLQKEIQDLK 297
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1724-2006 |
8.58e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 45.14 E-value: 8.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1724 AEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKvrsemdslLQMKINAEKASMVNTEKSKQLLESEalkMKQLADEAA 1803
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAA--------LERRIAALARRIRALEQELAALEAE---LAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1804 RMRsvAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEAtrlktEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQA 1883
Cdd:COG4942 94 ELR--AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFL-----DAVRRLQYLKYLAPARREQAEELRADLAELAALR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1884 AQHKQDIEEKITQLQtssdselgrqkniveetlkqkkvveeeihiikinfhKASKEKADLESELKKLKGIADETQKSKLK 1963
Cdd:COG4942 167 AELEAERAELEALLA------------------------------------ELEEERAALEALKAERQKLLARLEKELAE 210
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1389908286 1964 AEEEAEKLKKlaaeeerRRKEAEEKVKRITAAEEEAARQCKAA 2006
Cdd:COG4942 211 LAAELAELQQ-------EAEELEALIARLEAEAAAAAERTPAA 246
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1856-2116 |
8.98e-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: 44.84 E-value: 8.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1856 KAKEAENERLKRQAEEEAyqrklleDQAAQHKQDIEEKITQLQTSSDSELGRQKNiveetLKQKKVVEEEihiikinfhK 1935
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAA-------KKEQERQKKLEQQAEEAEKQRAAEQARQKE-----LEQRAAAEKA---------A 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1936 ASKEKADLESELKKlkgiadeTQKSKLKAEEEAEKLKKLAaeeerrrkeaeekvkritAAEEEAARQCKAAQEEVERLKK 2015
Cdd:TIGR02794 105 KQAEQAAKQAEEKQ-------KQAEEAKAKQAAEAKAKAE------------------AEAERKAKEEAAKQAEEEAKAK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2016 KAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAA 2095
Cdd:TIGR02794 160 AAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFG 239
|
250 260
....*....|....*....|.
gi 1389908286 2096 LlrQKAEEAEKQKKAAENEAA 2116
Cdd:TIGR02794 240 L--ASGSNAEKQGGARGAAAG 258
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2458-2581 |
9.78e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 9.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2458 QRKSKEMANAQQE---QIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERK 2534
Cdd:PRK09510 68 QQQQKSAKRAEEQrkkKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1389908286 2535 KLQAIMDEAVRKQKEAEEEMKnKQREMDVLDKKRLEQEKQLAEENKK 2581
Cdd:PRK09510 148 KAEAEAKRAAAAAKKAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAA 193
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2239-2347 |
9.97e-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: 41.83 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2239 EENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAE 2318
Cdd:pfam20492 12 EERLKQYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEE 91
|
90 100
....*....|....*....|....*....
gi 1389908286 2319 AEKLQKQKDQAQETAKRLQEDKQQIQQRL 2347
Cdd:pfam20492 92 IARLEEEVERKEEEARRLQEELEEAREEE 120
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2458-2578 |
1.01e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.86 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2458 QRKSKEMANAQQEQiEQQKAELQQSflTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKAlkdeqERQRKLMEEERKKLQ 2537
Cdd:COG2268 208 AERETEIAIAQANR-EAEEAELEQE--REIETARIAEAEAELAKKKAEERREAETARAEA-----EAAYEIAEANAEREV 279
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1389908286 2538 AIMDEAVRKQKEAEEEMKNKQREMDVLD---KKRLEQEKQLAEE 2578
Cdd:COG2268 280 QRQLEIAEREREIELQEKEAEREEAELEadvRKPAEAEKQAAEA 323
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1338-1937 |
1.01e-03 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 45.71 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1338 DAQRRLEDDEKASEKLKEEERRKMAEIQA------ELDKQKQMAEAHAKSVAKAeqeaLELKMKMKEEASkrqdvAADAE 1411
Cdd:COG3096 424 KARALCGLPDLTPENAEDYLAAFRAKEQQateevlELEQKLSVADAARRQFEKA----YELVCKIAGEVE-----RSQAW 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1412 KQKQNIQQELQHLKSLSDQE--IKSKNQQLEDALVSRRKIEEEIHIIRIQL-------EKTTAHKAKSEAELQELRDRAA 1482
Cdd:COG3096 495 QTARELLRRYRSQQALAQRLqqLRAQLAELEQRLRQQQNAERLLEEFCQRIgqqldaaEELEELLAELEAQLEELEEQAA 574
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1483 EAEKLRKAAQDEAERLRKQVAEETQRKKN---AEDELKR---KSDAEKEAAKQ----KQRALDDLQKYKMQAEEAERRmK 1552
Cdd:COG3096 575 EAVEQRSELRQQLEQLRARIKELAARAPAwlaAQDALERlreQSGEALADSQEvtaaMQQLLEREREATVERDELAAR-K 653
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1553 QAEEEKIRQIrvveEVAQKSAATQLQTKAMSF-----SE--QTTKLEE--------------------SLKKEQgnVLKL 1605
Cdd:COG3096 654 QALESQIERL----SQPGGAEDPRLLALAERLggvllSEiyDDVTLEDapyfsalygparhaivvpdlSAVKEQ--LAGL 727
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1606 QEEADKLKKQQKEANT----AREEAEQELEIWRQKANEALR---------------------LRLQAEEEAQKksHAQEE 1660
Cdd:COG3096 728 EDCPEDLYLIEGDPDSfddsVFDAEELEDAVVVKLSDRQWRysrfpevplfgraarekrleeLRAERDELAEQ--YAKAS 805
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1661 AEKQKLEAERDAKKRGKAE----------EAALKQKENAEKELDKQR-KFAEQIAQQKLSAEQECIRLKA---------- 1719
Cdd:COG3096 806 FDVQKLQRLHQAFSQFVGGhlavafapdpEAELAALRQRRSELERELaQHRAQEQQLRQQLDQLKEQLQLlnkllpqanl 885
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1720 -DFEHAEQQRGLLDNELQRL---KNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKAsmvntEKSKQLLESEALKM 1795
Cdd:COG3096 886 lADETLADRLEELREELDAAqeaQAFIQQHGKALAQLEPLVAVLQSDPEQFEQLQADYLQA-----KEQQRRLKQQIFAL 960
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1796 KQLA--------DEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAK-----EAEN 1862
Cdd:COG3096 961 SEVVqrrphfsyEDAVGLLGENSDLNEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDAKqqtlqELEQ 1040
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1863 E--RLKRQAEEEAyqrkllEDQAAQHKQDIEEKITQLQ---TSSDSELGRQKNIVEETLKQKKVVEEEIHIIK--INFHK 1935
Cdd:COG3096 1041 EleELGVQADAEA------EERARIRRDELHEELSQNRsrrSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEReqVVQAK 1114
|
..
gi 1389908286 1936 AS 1937
Cdd:COG3096 1115 AG 1116
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2246-2605 |
1.01e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2246 QKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQ 2325
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2326 KDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKA 2405
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2406 QLQRTEKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAELQQSFLT 2485
Cdd:COG4372 169 LEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2486 EKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEAVRKQKEAEEEMKNKQREMDVLD 2565
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1389908286 2566 KKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTV 2605
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVA 368
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2098-2442 |
1.02e-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: 45.13 E-value: 1.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2098 RQKAEEAEKQKKAAENEAAK----QAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHK-----------K 2162
Cdd:pfam09731 100 EVAEEEKEATKDAAEAKAQLpkseQEKEKALEEVLKEAISKAESATAVAKEAKDDAIQAVKAHTDSLKeasdtaeisreK 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2163 EAEQALQQKSQVEKEL--TVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVElarvriQMEELVKLKLKI-EE 2239
Cdd:pfam09731 180 ATDSALQKAEALAEKLkeVINLAKQSEEEAAPPLLDAAPETPPKLPEHLDNVEEKVEKA------QSLAKLVDQYKElVA 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2240 ENRRLMQKDKDST-QKLLAEEAEKMKSLAEEAGRL--SVEAEETARQRQIAESNLAEQRALAEKILKekmqaiQEATKLK 2316
Cdd:pfam09731 254 SERIVFQQELVSIfPDIIPVLKEDNLLSNDDLNSLiaHAHREIDQLSKKLAELKKREEKHIERALEK------QKEELDK 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2317 AEAEKLQKQKDQaqetakrLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQ---------- 2386
Cdd:pfam09731 328 LAEELSARLEEV-------RAADEAQLRLEFEREREEIRESYEEKLRTELERQAEAHEEHLKDVLVEQEIelqreflqdi 400
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 2387 -TKAEDEAKKFKKQADEVKAQLQRTEKHTTEIVV---QKLETQRLQSTREA--DDLKSAIAD 2442
Cdd:pfam09731 401 kEKVEEERAGRLLKLNELLANLKGLEKATSSHSEvedENRKAQQLWLAVEAlrSTLEDGSAD 462
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1474-1706 |
1.03e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 44.59 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1474 LQELRDRAAEAEK------LRKAAQDEAERLRKQVAEETQRKKnaeDELKRKSdaEKEAAKQKQRALDDLqkykmqAEEA 1547
Cdd:pfam02841 67 LQELLDLHRDCEKeaiavfMKRSFKDENQEFQKELVELLEAKK---DDFLKQN--EEASSKYCSALLQDL------SEPL 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1548 ERRMKQAEEEK-------IRQIRVVEEVAQKSAATQLQTKAM--SFSEQTTKLEESLkkeqgnvLKLQEEADKLKKQQKE 1618
Cdd:pfam02841 136 EEKISQGTFSKpggyklfLEERDKLEAKYNQVPRKGVKAEEVlqEFLQSKEAVEEAI-------LQTDQALTAKEKAIEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1619 ANTAREEAEQELEIWRQKANEalrlrLQAEEEAQKKSHAQEEAE-KQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR 1697
Cdd:pfam02841 209 ERAKAEAAEAEQELLREKQKE-----EEQMMEAQERSYQEHVKQlIEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFK 283
|
....*....
gi 1389908286 1698 KFAEQIAQQ 1706
Cdd:pfam02841 284 TEAESLQKE 292
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1467-1539 |
1.04e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 42.04 E-value: 1.04e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 1467 KAKSEAELQELRdraAEAEKLRKAAQDEAERLRKQVAEETQRKKNaedelKRKSDAEKEAAKQKQRALDDLQK 1539
Cdd:cd06503 53 LAEYEEKLAEAR---AEAQEIIEEARKEAEKIKEEILAEAKEEAE-----RILEQAKAEIEQEKEKALAELRK 117
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2239-2498 |
1.10e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.39 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2239 EENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAgrlsvEAEETARQRQIAESNLAEQRALAEKILKEkmqaiqeatklkae 2318
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSE-------------- 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2319 aekLQKQKDQAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEAsaEAEKLKLRVKELSLAQTKAEDEAKKFKK 2398
Cdd:COG3206 224 ---LESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRA--QLAELEAELAELSARYTPNHPDVIALRA 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2399 QADEVKAQLQRTekhtTEIVVQKLETQRLQSTREADDLKSAIADleeerkklkkeaeeLQRKSKEMANAQQEQIE-QQKA 2477
Cdd:COG3206 299 QIAALRAQLQQE----AQRILASLEAELEALQAREASLQAQLAQ--------------LEARLAELPELEAELRRlEREV 360
|
250 260
....*....|....*....|.
gi 1389908286 2478 ELQQSFLTEkglLLKREKEVE 2498
Cdd:COG3206 361 EVARELYES---LLQRLEEAR 378
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
2097-2612 |
1.17e-03 |
|
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: 45.12 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2097 LRQKAEEAEKQKKAAEN-----EAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQK 2171
Cdd:pfam05557 23 LEHKRARIELEKKASALkrqldRESDRNQELQKRIRLLEKREAEAEEALREQAELNRLKKKYLEALNKKLNEKESQLADA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2172 SQV----EKELTVVKLQLDETDKQKVLLDQELQRVKgEVNDAFKQK-SQVEVELARVRIQMEELVKLKLKIEEENRRLMQ 2246
Cdd:pfam05557 103 REVisclKNELSELRRQIQRAELELQSTNSELEELQ-ERLDLLKAKaSEAEQLRQNLEKQQSSLAEAEQRIKELEFEIQS 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2247 KDKDSTQ-KLLAEEAEKMKSLAEEAGRLSVEAE---ETARQRQIAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKL 2322
Cdd:pfam05557 182 QEQDSEIvKNSKSELARIPELEKELERLREHNKhlnENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQEL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2323 QKQKDQAQETA------KRLQEDKQQIQQRldKETEGFQKSLEAERKRQLEASaeaekLKLRVKELSLAQTKAEDEAKKF 2396
Cdd:pfam05557 262 QSWVKLAQDTGlnlrspEDLSRRIEQLQQR--EIVLKEENSSLTSSARQLEKA-----RRELEQELAQYLKKIEDLNKKL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2397 KKQaDEVKAQLQRT---------------EKHTTEIVVQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKS 2461
Cdd:pfam05557 335 KRH-KALVRRLQRRvllltkerdgyrailESYDKELTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2462 KEMANAQQEQIE---QQKAELQQSFLTEKGLLLKRE-KEVEGEKKRFEKQledemkkakalKDEQErqrklMEEERKKLQ 2537
Cdd:pfam05557 414 KQQAQTLERELQalrQQESLADPSYSKEEVDSLRRKlETLELERQRLREQ-----------KNELE-----MELERRCLQ 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 2538 AIMDEAVRKQKEAEEEMKNKQREmdvldkKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKLVA 2612
Cdd:pfam05557 478 GDYDPKKTKVLHLSMNPAAEAYQ------QRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVL 546
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2251-2442 |
1.17e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 45.29 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2251 STQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQiaesNLAEQRALAEKILKEKMQAIqEATKLKAEAEKLQKQKDQAQ 2330
Cdd:COG4913 607 DNRAKLAALEAELAELEEELAEAEERLEALEAELD----ALQERREALQRLAEYSWDEI-DVASAEREIAELEAELERLD 681
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2331 ETAKRLQEDKQQIQQrLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ-ADEVKAQLQR 2409
Cdd:COG4913 682 ASSDDLAALEEQLEE-LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAlLEERFAAALG 760
|
170 180 190
....*....|....*....|....*....|...
gi 1389908286 2410 TEKHTTeiVVQKLETQRLQSTREADDLKSAIAD 2442
Cdd:COG4913 761 DAVERE--LRENLEERIDALRARLNRAEEELER 791
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
78-122 |
1.23e-03 |
|
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: 41.66 E-value: 1.23e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1389908286 78 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 122
Cdd:cd21294 78 FQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2338-2578 |
1.28e-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: 44.94 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2338 EDKQQIQQRLdKETEGFQKSLEAERKRQleasAEAEKLKLRVKELslaqtkaedeakkfkKQADEVKAQLQRTEKHTTEI 2417
Cdd:pfam15709 329 EQEKASRDRL-RAERAEMRRLEVERKRR----EQEEQRRLQQEQL---------------ERAEKMREELELEQQRRFEE 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2418 VvqKLETQRLQSTREaddlksaiadleeerkklkkeaeelQRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEV 2497
Cdd:pfam15709 389 I--RLRKQRLEEERQ-------------------------RQEEEERKQRLQLQAAQERARQQQEEFRRKLQELQRKKQQ 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2498 E-GEKKRFEKQLEDEMKKAkaLKDEQERQRKLMEEERKKLQaimdeavRKQKEAEE----EMKNKQREMDVLDKKRLEQE 2572
Cdd:pfam15709 442 EeAERAEAEKQRQKELEMQ--LAEEQKRLMEMAEEERLEYQ-------RQKQEAEEkarlEAEERRQKEEEAARLALEEA 512
|
....*.
gi 1389908286 2573 KQLAEE 2578
Cdd:pfam15709 513 MKQAQE 518
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1465-1539 |
1.32e-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: 42.47 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1465 AHKAKSEAELQElrdraAEAEKLRKAAQDEAERLRKQVAEETQR-----KKNAEDELKR-KSDAEKEAAKQKQRALDDLQ 1538
Cdd:COG0711 43 AERAKEEAEAAL-----AEYEEKLAEARAEAAEIIAEARKEAEAiaeeaKAEAEAEAERiIAQAEAEIEQERAKALAELR 117
|
.
gi 1389908286 1539 K 1539
Cdd:COG0711 118 A 118
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1459-1885 |
1.35e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.90 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1459 QLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRkknaedelKRKSDAEKEAAKQKQRALDDLQ 1538
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLL--------LALALAALLLAAAALLLLLLAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 KYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKE 1618
Cdd:COG5278 183 AALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAAL 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1619 ANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRK 1698
Cdd:COG5278 263 LAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAA 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1699 FAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASM 1778
Cdd:COG5278 343 ALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEAL 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1779 VNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAK 1858
Cdd:COG5278 423 ELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLA 502
|
410 420
....*....|....*....|....*..
gi 1389908286 1859 EAENERLKRQAEEEAYQRKLLEDQAAQ 1885
Cdd:COG5278 503 LALAALLLAAAEAALAAALAAALASAE 529
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1586-2013 |
1.37e-03 |
|
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: 44.81 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1586 EQTTKLEESLKKeQGNVLKLQEEADKLKKQQKEANTAREEAEQELEiwrQKANEALRLRlqaeEEAQKKSHAQEEAEK-- 1663
Cdd:pfam10174 158 ESIKKLLEMLQS-KGLPKKSGEEDWERTRRIAEAEMQLGHLEVLLD---QKEKENIHLR----EELHRRNQLQPDPAKtk 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1664 --QKLEAERDAK----KRG--KAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAE---QECIRLKADFEHAEQQRGLLD 1732
Cdd:pfam10174 230 alQTVIEMKDTKisslERNirDLEDEVQMLKTNGLLHTEDREEEIKQMEVYKSHSKfmkNKIDQLKQELSKKESELLALQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1733 NELQRLKNEvNSTEKQRKQLEDELNKVRSEMDSLLQMKINA------EKASMVNtEKSKQLLE---------SEALKMKQ 1797
Cdd:pfam10174 310 TKLETLTNQ-NSDCKQHIEVLKESLTAKEQRAAILQTEVDAlrlrleEKESFLN-KKTKQLQDlteekstlaGEIRDLKD 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1798 LADEAARMRSVAEeaKKQRQIAEEEAARQRSEAEkiLKEKLAAI-----NEATRLKTeAEMALKAKEAENERLKRQAEEE 1872
Cdd:pfam10174 388 MLDVKERKINVLQ--KKIENLQEQLRDKDKQLAG--LKERVKSLqtdssNTDTALTT-LEEALSEKERIIERLKEQRERE 462
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1873 AYQRKLLEDQAAQHKQDIEEKITQLQT------SSDSELGRQKNIVEETLKQKkvvEEEIHIIKINFHKASKEKADLESE 1946
Cdd:pfam10174 463 DRERLEELESLKKENKDLKEKVSALQPeltekeSSLIDLKEHASSLASSGLKK---DSKLKSLEIAVEQKKEECSKLENQ 539
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1389908286 1947 LKKLKGIADETQKSklkaEEEAEKLKKLAaeeerrrkeaeekvKRITAAEEEAARqckaAQEEVERL 2013
Cdd:pfam10174 540 LKKAHNAEEAVRTN----PEINDRIRLLE--------------QEVARYKEESGK----AQAEVERL 584
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
25-122 |
1.43e-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: 41.36 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 25 QKKTFTKWVNKHLVK---------AQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 90
Cdd:cd21293 2 EKGSYVDHINRYLGDdpflkqflpIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1389908286 91 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 122
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1339-1442 |
1.50e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1339 AQRRLEDDEKAseklkEEERRKMAEIQAELDKQKQ--MAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAE--KQK 1414
Cdd:PTZ00491 684 ERQKMHDKAKA-----EEQRTKLLELQAESAAVESsgQSRAEALAEAEARLIEAEAEVEQAELRAKALRIEAEAEleKLR 758
|
90 100
....*....|....*....|....*...
gi 1389908286 1415 QNIQQELQHLKSLSDQEIKsKNQQLEDA 1442
Cdd:PTZ00491 759 KRQELELEYEQAQNELEIA-KAKELADI 785
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2245-2400 |
1.52e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.70 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2245 MQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNL--AEQRALAEKILKEKMQAIQEATKLKAEAEKL 2322
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARRerEELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 2323 QKQKDQAQETAKRLQEDKQQIQQRLdKETEGF-QKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQA 2400
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNEL-YRVAGLtPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1530-1895 |
1.59e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.65 E-value: 1.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1530 KQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEA 1609
Cdd:COG3064 6 EEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1610 DKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENA 1689
Cdd:COG3064 86 AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1690 EKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQM 1769
Cdd:COG3064 166 AAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1770 KINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKT 1849
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG 325
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1389908286 1850 EAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKIT 1895
Cdd:COG3064 326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1347-1581 |
1.66e-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: 44.56 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1347 EKASEKLKEEERRKMAEIQAELDKQKQMAEahaksvAKAEQEALELKMKMKEEASKRQDVAADAEK-QKQNIQQELQHlk 1425
Cdd:pfam15709 331 EKASRDRLRAERAEMRRLEVERKRREQEEQ------RRLQQEQLERAEKMREELELEQQRRFEEIRlRKQRLEEERQR-- 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1426 slsdQEIKSKNQQLEdalvsrrkieeeihiirIQLEKTTAHKAKSE--AELQELRdraaeaeklRKAAQDEAERlrkqVA 1503
Cdd:pfam15709 403 ----QEEEERKQRLQ-----------------LQAAQERARQQQEEfrRKLQELQ---------RKKQQEEAER----AE 448
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1504 EETQRKKNAEDELKRKSDAEKEAAKQKQralddlQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKA 1581
Cdd:pfam15709 449 AEKQRQKELEMQLAEEQKRLMEMAEEER------LEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2038-2210 |
1.69e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2038 AKEAAQKCTAAEQKAQDVlskNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAENEAAK 2117
Cdd:PRK09510 89 AEELQQKQAAEQERLKQL---EKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAA 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2118 QAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQ-----KSQVEKELTVVKLQLDETDKQK 2192
Cdd:PRK09510 166 EAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKaaaeaKAAAAKAAAEAKAAAEKAAAAK 245
|
170
....*....|....*...
gi 1389908286 2193 VLLDQELQRVKGEVNDAF 2210
Cdd:PRK09510 246 AAEKAAAAKAAAEVDDLF 263
|
|
| CH_PARVG_rpt2 |
cd21307 |
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role ... |
8-115 |
1.73e-03 |
|
second calponin homology (CH) domain found in gamma-parvin; Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. 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: 409156 [Multi-domain] Cd Length: 122 Bit Score: 41.18 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 8 DFMETLIQRGQDERDRVqKKTFTKWVNKHLVKAQRHVTDLYEDLRDGHNLISLLEVLSGETLPREKgrmrFH-------- 79
Cdd:cd21307 1 DAIDELFKLGPDKVNTV-KKAILHFVNKHLGNLGLNVKDLDSQFADGVILLLLIGQLEGFFIHLSE----FFltpsstse 75
|
90 100 110
....*....|....*....|....*....|....*.
gi 1389908286 80 KLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTL 115
Cdd:cd21307 76 MLHNVTLALELLKEGGLLNFPVNPEDIVNGDSKATI 111
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2316-2567 |
1.74e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2316 KAEAeKLQKQKDQAQETAKRLQEDKqqiQQRLDKEtegfqkslEAERKRQLEASAEAeklklRVKELSLAQTKAEDEAKK 2395
Cdd:PRK05035 435 KAEI-RAIEQEKKKAEEAKARFEAR---QARLERE--------KAAREARHKKAAEA-----RAAKDKDAVAAALARVKA 497
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2396 FKKQADEVKAQLQRTEKHTTEIVVQ--------KLETQRLQSTREADDLKSAIA---------DLEEERKKLKKEAEELQ 2458
Cdd:PRK05035 498 KKAAATQPIVIKAGARPDNSAVIAArearkaqaRARQAEKQAAAAADPKKAAVAaaiarakakKAAQQAANAEAEEEVDP 577
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2459 RKSK---EMANAQQEQIEQQKAELQQSfltekglllkrekEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKK 2535
Cdd:PRK05035 578 KKAAvaaAIARAKAKKAAQQAASAEPE-------------EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPR 644
|
250 260 270
....*....|....*....|....*....|...
gi 1389908286 2536 LQAIMDEAVR-KQKEAEEEMKNKQREMDVLDKK 2567
Cdd:PRK05035 645 KAAVAAAIARaKARKAAQQQANAEPEEAEDPKK 677
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1666-2112 |
1.74e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 44.51 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1666 LEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNST 1745
Cdd:COG5278 78 LEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRAR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1746 EKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEAAR 1825
Cdd:COG5278 158 LLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1826 QRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRKLLEDQAAQHKQDIEEKITQLQTSSDSEL 1905
Cdd:COG5278 238 LALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAA 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1906 GRQKNIVEETLKQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEA 1985
Cdd:COG5278 318 AAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAA 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1986 EEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLA 2065
Cdd:COG5278 398 AAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAAL 477
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1389908286 2066 QEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAAE 2112
Cdd:COG5278 478 AAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAA 524
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1516-1739 |
1.86e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1516 LKRKSDAEKEAAKQKQRALDDlqkykmQAEEAERRMKQAEEEkirqirvVEEVAQKSAATQLQTKAMSFSEQTTKLEESL 1595
Cdd:COG3206 162 LEQNLELRREEARKALEFLEE------QLPELRKELEEAEAA-------LEEFRQKNGLVDLSEEAKLLLQQLSELESQL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1596 KKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEA-LRLRLQAEEEAQKKSH-------AQEEAEKQKLE 1667
Cdd:COG3206 229 AEARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAeLEAELAELSARYTPNHpdvialrAQIAALRAQLQ 308
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 1668 AERDAKKRG-KAEEAALKQKENA-EKELDKQRKFAEQIAQQklsaEQECIRLKADFEHAEQqrgLLDNELQRLK 1739
Cdd:COG3206 309 QEAQRILASlEAELEALQAREASlQAQLAQLEARLAELPEL----EAELRRLEREVEVARE---LYESLLQRLE 375
|
|
| CAMSAP_CH |
pfam11971 |
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins. |
162-222 |
1.90e-03 |
|
CAMSAP CH domain; This domain is the N-terminal CH domain from the CAMSAP proteins.
Pssm-ID: 432229 Cd Length: 85 Bit Score: 39.98 E-value: 1.90e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 162 DNFTTSWRDGKLFSAIIHKHRPALIDMNQV--YRQSNQE----NLEQAFSVAERELGVTKL-LDPEDV 222
Cdd:pfam11971 14 EDLLRDLSDGCALAALIHFYCPQLIDLEDIclKESMSLAdslyNIQLLQEFCQRHLGNRCChLTLEDL 81
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1539-1863 |
1.92e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.55 E-value: 1.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 KYKMQAEEAERrmKQAEEEKIR----QIRVVEEVAQKSAAtqLQTKAmsfseqttkleESLKKEQGNVLKLQEEADKLKK 1614
Cdd:PRK05035 435 KAEIRAIEQEK--KKAEEAKARfearQARLEREKAAREAR--HKKAA-----------EARAAKDKDAVAAALARVKAKK 499
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1615 QQKEANTArEEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAerdAKKRGKAEEAALKQK--ENAEKE 1692
Cdd:PRK05035 500 AAATQPIV-IKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAA---AIARAKAKKAAQQAAnaEAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1693 LDKQRKFAEQIAqqklsaeqeciRLKAdfEHAEQQrglldnelqrlkNEVNSTEKQRKQLEDELNKVRSEMdsllqmkin 1772
Cdd:PRK05035 576 DPKKAAVAAAIA-----------RAKA--KKAAQQ------------AASAEPEEQVAEVDPKKAAVAAAI--------- 621
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1773 aEKASMVNTEKSKQLLESEALKMKQLADEAARMRSVAEEAKKQRQIAEEEaarqrsEAEKILKEKLAAineatrlkteAE 1852
Cdd:PRK05035 622 -ARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE------EAEDPKKAAVAA----------AI 684
|
330
....*....|.
gi 1389908286 1853 MALKAKEAENE 1863
Cdd:PRK05035 685 ARAKAKKAAQQ 695
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1378-1698 |
1.94e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1378 HAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKslsdQEIKSKNQQLEDALVSRRKIEEEIHIIR 1457
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLR----EELEQAREELEQLEEELEQARSELEQLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1458 IQLEKTtahkaksEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDL 1537
Cdd:COG4372 80 EELEEL-------NEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1538 QKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQK 1617
Cdd:COG4372 153 KELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1618 EANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQR 1697
Cdd:COG4372 233 LALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGA 312
|
.
gi 1389908286 1698 K 1698
Cdd:COG4372 313 L 313
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
1397-1711 |
1.96e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 44.28 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1397 KEEASKRQDVAADAEKQKQNIQQEL-----------QHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTA 1465
Cdd:pfam04747 14 QQLTNRRKNLGRVAKSQRNQFRQWLltavlpnsindQRKEAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1466 HKAKSEAELqelrdRAAEAEKLRKAAQdeaerlrkqvaEETQRKKNAEDELKRKSDAEKEAAKQKQRAlddlQKYKMQAE 1545
Cdd:pfam04747 94 AKKAAEKEA-----RRAEAEAKKRAAQ-----------EEEHKQWKAEQERIQKEQEKKEADLKKLQA----EKKKEKAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1546 EAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREE 1625
Cdd:pfam04747 154 KAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSAAPAPEPKTPTNTPAEPAEQVQEITGKKNKKNKKKSESEATAAPAS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1626 AEQELEIWRQKANEALRlrlQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQ 1705
Cdd:pfam04747 234 VEQVVEQPKVVTEEPHQ---QAAPQEKKNKKNKRKSESENVPAASETPVEPVVETTPPASENQKKNKKDKKKSESEKVVE 310
|
....*.
gi 1389908286 1706 QKLSAE 1711
Cdd:pfam04747 311 EPVQAE 316
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1387-1650 |
2.04e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1387 QEALElKMKMKEEASKRQDVAADAEKQKQNIQQELQHLKSLSDQ--EIKSKNQQLEDALVSRRKIEEEihiiriqLEKTt 1464
Cdd:COG2433 379 EEALE-ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQveRLEAEVEELEAELEEKDERIER-------LERE- 449
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1465 AHKAKSEAELQELRDRaaEAEKLRKaaqdEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQA 1544
Cdd:COG2433 450 LSEARSEERREIRKDR--EISRLDR----EIERLERELEEERERIEELKRKLERLKELWKLEHSGELVPVKVVEKFTKEA 523
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1545 -EEAERRMKQAEeekiRQIRVVEEV--AQKSAATQL---QTKAMSFSEQT-TKLEESLKKEQGNVLKLQE----EADKLk 1613
Cdd:COG2433 524 iRRLEEEYGLKE----GDVVYLRDAsgAGRSTAELLaeaGPRAVIVPGELsEAADEVLFEEGIPVLPAEDvtiqEVDDL- 598
|
250 260 270
....*....|....*....|....*....|....*..
gi 1389908286 1614 kqqkeANTAREEAEQELEIWRQKANEalRLRLQAEEE 1650
Cdd:COG2433 599 -----AVVDEEELEAAIEDWEERAEE--RRREKKAEM 628
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
623-703 |
2.19e-03 |
|
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in cytoskeletal structure. These include spectrin, alpha-actinin and dystrophin. The sequence repeat used in this family is taken from the structural repeat in reference. The spectrin domain- repeat forms a three helix bundle. The second helix is interrupted by proline in some sequences. The repeats are defined by a characteriztic tryptophan (W) residue at position 17 in helix A and a leucine (L) at 2 residues from the carboxyl end of helix C. Although the domain occurs in multiple repeats along sequences, the domains are actually stable on their own - ie they act, biophysically, like domains rather than repeats that along function when aggregated.
Pssm-ID: 395348 [Multi-domain] Cd Length: 105 Bit Score: 40.38 E-value: 2.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 623 WLNEKEEEEVNYDWSDKNTNMTAKKDNYSGLMRELELREKKVNAVQTTGDKLLRDGHPARKTIEAFTAALQTQWSWLLQL 702
Cdd:pfam00435 16 WIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLEL 95
|
.
gi 1389908286 703 C 703
Cdd:pfam00435 96 A 96
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1604-1686 |
2.22e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 41.69 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1604 KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEalrLRLQAEEEAQK-----KSHAQEEAEKQKLEAERDAKKRGKA 1678
Cdd:PRK05759 39 KIADGLAAAERAKKELELAQAKYEAQLAEARAEAAE---IIEQAKKRAAQiieeaKAEAEAEAARIKAQAQAEIEQERKR 115
|
....*...
gi 1389908286 1679 EEAALKQK 1686
Cdd:PRK05759 116 AREELRKQ 123
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1428-1655 |
2.27e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.67 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1428 SDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQVAE--- 1504
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1505 ETQRKKNAEDEL-------------------KRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEkirqirvv 1565
Cdd:COG3883 94 ALYRSGGSVSYLdvllgsesfsdfldrlsalSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAE-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1566 eevaQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRL 1645
Cdd:COG3883 166 ----LEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 241
|
250
....*....|
gi 1389908286 1646 QAEEEAQKKS 1655
Cdd:COG3883 242 AAASAAGAGA 251
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1472-1675 |
2.28e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.36 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1472 AELQELRDRAAEAEKLRKAAQDEAERL---RKQVAEETQRKKNAEDELKRKSD---AEKEAAKQKQRALDDLQkYKMQAE 1545
Cdd:COG1340 50 AQVKELREEAQELREKRDELNEKVKELkeeRDELNEKLNELREELDELRKELAelnKAGGSIDKLRKEIERLE-WRQQTE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1546 ----EAERR-MKQAE--EEKIRQIRVVEEVAQK-----SAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEEADKLK 1613
Cdd:COG1340 129 vlspEEEKElVEKIKelEKELEKAKKALEKNEKlkelrAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEADELR 208
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 1614 KQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKKR 1675
Cdd:COG1340 209 KEADELHKEIVEAQEKADELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAE 270
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1340-1657 |
2.29e-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: 2.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1340 QRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmKMKEEASKRQdvaadaekQKQNIQQ 1419
Cdd:pfam15558 61 EQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERA-RQEAEQRKQC--------QEQRLKE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1420 ELQHLKSLSDQEIKSKNQQLEDALVSRRKIEEEIHIIRIQLEKTTahKAKSEAELQELRDRAAEAEKLRKA--------A 1491
Cdd:pfam15558 132 KEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSE--LLNHQARKVLVDCQAKAEELLRRLsleqslqrS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1492 QDEAERLRKQVAEETQRKKNAEDELKRKSdaeKEAAKQKQRALDdlQKYKMQAEEAERRMKQAEEekirqirVVEEVAQK 1571
Cdd:pfam15558 210 QENYEQLVEERHRELREKAQKEEEQFQRA---KWRAEEKEEERQ--EHKEALAELADRKIQQARQ-------VAHKTVQD 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1572 SAAtqlqtkamsfseqttkleeslKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRLRLQAEEEA 1651
Cdd:pfam15558 278 KAQ---------------------RARELNLEREKNHHILKLKVEKEEKCHREGIKEAIKKKEQRSEQISREKEATLEEA 336
|
....*.
gi 1389908286 1652 QKKSHA 1657
Cdd:pfam15558 337 RKTARA 342
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
27-119 |
2.35e-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: 2.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 27 KTFTKWVNKHLVKAQrhVTDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLKHRQV 96
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100
....*....|....*....|...
gi 1389908286 97 KLVNIRNDDIADGNpKLTLGLIW 119
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVW 481
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1938-2399 |
2.43e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1938 KEKADLESELKKLKGIADETQKSKLKAEEEAEKLKKLAAEEERRRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKA 2017
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2018 EDANKQKEKAEKEAEKQVVLAKEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKAEKEAAlL 2097
Cdd:COG4717 133 ELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAE-L 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2098 RQKAEEAEKQKKAAENEAAKQAKAQNDTEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKE 2177
Cdd:COG4717 212 EEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2178 LTVVKLQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRI-----QMEELVKLKLKIEEENRRLMQKD-KDS 2251
Cdd:COG4717 292 LLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELlelldRIEELQELLREAEELEEELQLEElEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2252 TQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEKILkekmqAIQEATKLKAEAEKLQKQKDQAQE 2331
Cdd:COG4717 372 IAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEEELEELEEELEELEE 446
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2332 TAKRLQEDKQQIQQRLdKETEGFQKSLEAERKRQlEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQ 2399
Cdd:COG4717 447 ELEELREELAELEAEL-EQLEEDGELAELLQELE-ELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1556-1807 |
2.45e-03 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 43.27 E-value: 2.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1556 EEKIRQIRVVeeVAQKSAATQLQTKAMSFSEQTTklEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQ 1635
Cdd:pfam17045 9 QELMKQIDIM--VAHKKSEWEGQTRALETRLDIR--EEELLSARNTLERKHKEIGLLRQQLEELEKGKQELVAKYEQQLQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1636 KANEALRLRLQAEEEAQKKS--HAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQQKLSAEQE 1713
Cdd:pfam17045 85 KLQEELSKLKRSYEKLQRKQlkEAREEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1714 CIRLKADF----EHAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLL--QMKINAEKasmvntEKSKQL 1787
Cdd:pfam17045 165 SLIQSAAYqvqlEGRKQCLEASQSEIQRLRSKLERAQDSLCAQELELERLRMRVSELGdsNRKLLEEQ------QRLLEE 238
|
250 260
....*....|....*....|
gi 1389908286 1788 LESEALKMKQLADEAARMRS 1807
Cdd:pfam17045 239 LRMSQRQLQVLQNELMELKA 258
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2328-2478 |
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: 43.84 E-value: 2.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2328 QAQETAKRLQEDKQQIQQRldketegfQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQL 2407
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKK--------QIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAEN 278
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 2408 QRTEKHTTEIVVQKLETQRLQST-READDLKSaiaDLEEERKKLKKEAEELQRKSKEMANAQQEQIEQQKAE 2478
Cdd:pfam05262 279 QKREIEKAQIEIKKNDEEALKAKdHKAFDLKQ---ESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQ 347
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4377-4414 |
2.60e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.60e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1389908286 4377 QRFLEVQYLTGGLIEPDATNRVAIDEAVKKGTLDARTA 4414
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2489-2603 |
2.79e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2489 LLLKR--EKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKlmeEERKKLQAIMDEAVRKQKE--AEEEMKNKQREmDVL 2564
Cdd:PRK12704 23 FVRKKiaEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAK---EEIHKLRNEFEKELRERRNelQKLEKRLLQKE-ENL 98
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908286 2565 DKKRLE---QEKQLAEENKKLREQLQTFEISSKTVSQTKESQ 2603
Cdd:PRK12704 99 DRKLELlekREEELEKKEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1407-1748 |
2.82e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 44.18 E-value: 2.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1407 AADAEKQKQNIQQELQHL-KSLSDQEikSKNQQLEDALvsrrkieeeihiiriqlekttahkAKSEAELQELRDRAAEAE 1485
Cdd:PRK04863 832 EADPEAELRQLNRRRVELeRALADHE--SQEQQQRSQL------------------------EQAKEGLSALNRLLPRLN 885
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1486 KL-RKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAK--QKQRALDDLQKYKMQAEEAERRMKQaeeekirQI 1562
Cdd:PRK04863 886 LLaDETLADRVEEIREQLDEAEEAKRFVQQHGNALAQLEPIVSVlqSDPEQFEQLKQDYQQAQQTQRDAKQ-------QA 958
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1563 RVVEEVAQKSAAtqlqtkaMSFSEQttklEESLKKEQGNVlklqeeaDKLKKQQKEANTAREEAEQELEIWRQKANEALR 1642
Cdd:PRK04863 959 FALTEVVQRRAH-------FSYEDA----AEMLAKNSDLN-------EKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQ 1020
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1643 LR--LQAEEEAQKKSHAQEEAEKQKL------EAERDAKKRGKAEEAALKQKENAEKELDKQRKFAE---QIAQQKLSAE 1711
Cdd:PRK04863 1021 VLasLKSSYDAKRQMLQELKQELQDLgvpadsGAEERARARRDELHARLSANRSRRNQLEKQLTFCEaemDNLTKKLRKL 1100
|
330 340 350
....*....|....*....|....*....|....*..
gi 1389908286 1712 QEciRLKADFEHAEQQRGLLDNELQRLKNevNSTEKQ 1748
Cdd:PRK04863 1101 ER--DYHEMREQVVNAKAGWCAVLRLVKD--NGVERR 1133
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1604-1696 |
2.84e-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: 40.88 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1604 KLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALrlrlqaeEEAQKKshAQEEAEKQKLEAERDAKK-RGKAEEAA 1682
Cdd:cd06503 34 KIAESLEEAEKAKEEAEELLAEYEEKLAEARAEAQEII-------EEARKE--AEKIKEEILAEAKEEAERiLEQAKAEI 104
|
90
....*....|....
gi 1389908286 1683 LKQKENAEKELDKQ 1696
Cdd:cd06503 105 EQEKEKALAELRKE 118
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2164-2415 |
2.89e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.53 E-value: 2.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2164 AEQALQQKSQVEKeltvvkLQLDETDKQKVLLDQELQRvkGEVNDAFKQKSQVEVELAR-VRIQMEELVKLKLKIEEENR 2242
Cdd:PRK11637 39 SAHASDNRDQLKS------IQQDIAAKEKSVRQQQQQR--ASLLAQLKKQEEAISQASRkLRETQNTLNQLNKQIDELNA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2243 RL--MQKDKDSTQKLLAEEAEKMKSLAEEAG-RLSVEAEETARQRQIaesnLAEQRALAekilkekmQAIQEA-TKLKAE 2318
Cdd:PRK11637 111 SIakLEQQQAAQERLLAAQLDAAFRQGEHTGlQLILSGEESQRGERI----LAYFGYLN--------QARQETiAELKQT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2319 AEKLQKQKD---QAQETAKRLQEDKQQIQQRLDKETEGFQKSLEAerkrqLEASAEAEK---LKLRVKELSLAQT--KAE 2390
Cdd:PRK11637 179 REELAAQKAeleEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTG-----LESSLQKDQqqlSELRANESRLRDSiaRAE 253
|
250 260 270
....*....|....*....|....*....|
gi 1389908286 2391 DEAK----KFKKQADEVKA-QLQRTEKHTT 2415
Cdd:PRK11637 254 REAKaraeREAREAARVRDkQKQAKRKGST 283
|
|
| HOOK |
pfam05622 |
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from ... |
2263-2600 |
2.98e-03 |
|
HOOK protein coiled-coil region; This family consists of several HOOK1, 2 and 3 proteins from different eukaryotic organizms. The different members of the human gene family are HOOK1, HOOK2 and HOOK3. Different domains have been identified in the three human HOOK proteins, and it was demonstrated that the highly conserved NH2-domain mediates attachment to microtubules, whereas this central coiled-coil motif mediates homodimerization and the more divergent C-terminal domains are involved in binding to specific organelles (organelle-binding domains). It has been demonstrated that endogenous HOOK3 binds to Golgi membranes, whereas both HOOK1 and HOOK2 are localized to discrete but unidentified cellular structures. In mice the Hook1 gene is predominantly expressed in the testis. Hook1 function is necessary for the correct positioning of microtubular structures within the haploid germ cell. Disruption of Hook1 function in mice causes abnormal sperm head shape and fragile attachment of the flagellum to the sperm head. This entry includes the central coiled-coiled domain and the divergent C-terminal domain.
Pssm-ID: 461694 [Multi-domain] Cd Length: 528 Bit Score: 43.52 E-value: 2.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2263 MKSLAEEAGRLSVEAEETARQRQIAESNLAEQRALAEkilkEKMQAIQEATKLKAEAEKLQKQKDQAQ------ETAKRL 2336
Cdd:pfam05622 68 LEQLQEENFRLETARDDYRIKCEELEKEVLELQHRNE----ELTSLAEEAQALKDEMDILRESSDKVKkleatvETYKKK 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2337 QED----KQQIQQRLDKETEGFQK--SLEAERKRQLEASAEAEKLKLRVKELslaQTKAEDEAKKFKKQADEVKaqlQRT 2410
Cdd:pfam05622 144 LEDlgdlRRQVKLLEERNAEYMQRtlQLEEELKKANALRGQLETYKRQVQEL---HGKLSEESKKADKLEFEYK---KLE 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2411 EKHTTeivVQKlETQRLQSTREA-----DDLKSAIADLEEERKKLKkeaeelqrkskeMANAQQEQIEQQKAELQQSFLT 2485
Cdd:pfam05622 218 EKLEA---LQK-EKERLIIERDTlretnEELRCAQLQQAELSQADA------------LLSPSSDPGDNLAAEIMPAEIR 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2486 EKGLLLKREKEVEGEKKrfEKQLEDEMKKAKALKDE-QERQRKLMEEERKKLQAIMD--EAVRKQKEAEEEMKNKQREMD 2562
Cdd:pfam05622 282 EKLIRLQHENKMLRLGQ--EGSYRERLTELQQLLEDaNRRKNELETQNRLANQRILElqQQVEELQKALQEQGSKAEDSS 359
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 1389908286 2563 VLDKKRLEQEKQLAE---ENKKLREQLQTFEISSKTVSQTK 2600
Cdd:pfam05622 360 LLKQKLEEHLEKLHEaqsELQKKKEQIEELEPKQDSNLAQK 400
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
1461-1666 |
3.01e-03 |
|
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: 43.26 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1461 EKT--TAHKAKSEAELQELRdRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQ 1538
Cdd:pfam15905 116 EKTslSASVASLEKQLLELT-RVNELLKAKFSEDGTQKKMSSLSMELMKLRNKLEAKMKEVMAKQEGMEGKLQVTQKNLE 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1539 KYKMQAEEAERRMKQAEEEKIRQ----IRVVEEVAQKSAATQlqtKAMSFSEQTTKLEESLKKEQGNVL----KLQEEAD 1610
Cdd:pfam15905 195 HSKGKVAQLEEKLVSTEKEKIEEksetEKLLEYITELSCVSE---QVEKYKLDIAQLEELLKEKNDEIEslkqSLEEKEQ 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908286 1611 KLKKQQKEANTAREEAEQELEIWRQKaNEALRLRLQAEEEAQKKSHAQEEAEKQKL 1666
Cdd:pfam15905 272 ELSKQIKDLNEKCKLLESEKEELLRE-YEEKEQTLNAELEELKEKLTLEEQEHQKL 326
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
1489-1679 |
3.15e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 43.46 E-value: 3.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1489 KAAQDEAERLRKQVAEETQRKKNAEDELKRKsdaEKEAAKQKQRALDDLQKYKMQAEEAERRMKqaeeeKIRQirvveEV 1568
Cdd:PHA02562 198 KTYNKNIEEQRKKNGENIARKQNKYDELVEE---AKTIKAEIEELTDELLNLVMDIEDPSAALN-----KLNT-----AA 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1569 AQKSAATQLQTKAMSFSEQTT---KLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEIWRQKANEALRL-- 1643
Cdd:PHA02562 265 AKIKSKIEQFQKVIKMYEKGGvcpTCTQQISEGPDRITKIKDKLKELQHSLEKLDTAIDELEEIMDEFNEQSKKLLELkn 344
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1389908286 1644 -----------------RLQAEEEAQKKSHAQEEAEKQKLEAERDAKKRGKAE 1679
Cdd:PHA02562 345 kistnkqslitlvdkakKVKAAIEELQAEFVDNAEELAKLQDELDKIVKTKSE 397
|
|
| PRK11519 |
PRK11519 |
tyrosine-protein kinase Wzc; |
1586-1745 |
3.21e-03 |
|
tyrosine-protein kinase Wzc;
Pssm-ID: 183173 [Multi-domain] Cd Length: 719 Bit Score: 43.60 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1586 EQTTKLEESLKKE--QGNVLKLQEEADK----LKKQQKEANTAREEAEQELEIWRQKaNEALRLRLQAEE--------EA 1651
Cdd:PRK11519 240 EQIRDILNSITRNylEQNIERKSEEASKslafLAQQLPEVRSRLDVAENKLNAFRQD-KDSVDLPLEAKAvldsmvniDA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1652 QKKSHAQEEAEKQKLEAerdakKRGKAEEAALKQKENAEKELDKQRKFAEQIAQqklsAEQECIRLKADFEHAEQQRGLL 1731
Cdd:PRK11519 319 QLNELTFKEAEISKLYT-----KEHPAYRTLLEKRKALEDEKAKLNGRVTAMPK----TQQEIVRLTRDVESGQQVYMQL 389
|
170
....*....|....
gi 1389908286 1732 DNELQRLKNEVNST 1745
Cdd:PRK11519 390 LNKQQELKITEAST 403
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
1509-1621 |
3.23e-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: 40.70 E-value: 3.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1509 KKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERR-----MKQAEE-EKIRQIRvvEEVAQ-KSAATQLQTKA 1581
Cdd:pfam07926 3 LSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREAQQNyerelVLHAEDiKALQALR--EELNElKAEIAELKAEA 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1389908286 1582 MSFSEQTTKLEESLKKEQGnvlKLQEEADKLKKQQKEANT 1621
Cdd:pfam07926 81 ESAKAELEESEESWEEQKK---ELEKELSELEKRIEDLNE 117
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2218-2404 |
3.25e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.66 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2218 VELARVRIQMEELvKLKLKIE--EENRRLMQKDKDSTQKLLaEEAEKMK-SLAEEAGRLSvEAEETARQRQiaesnlaEQ 2294
Cdd:PRK00409 504 IEEAKKLIGEDKE-KLNELIAslEELERELEQKAEEAEALL-KEAEKLKeELEEKKEKLQ-EEEDKLLEEA-------EK 573
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2295 RAlaEKILKEkmqAIQEATKLKAEAEKLQKQKDQAQeTAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQL-------- 2366
Cdd:PRK00409 574 EA--QQAIKE---AKKEADEIIKELRQLQKGGYASV-KAHELIEARKRLNKANEKKEKKKKKQKEKQEELKVgdevkyls 647
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 2367 --------------EASAEAEKLKLRVK--ELSLAQTKAEDEAKKFKKQADEVK 2404
Cdd:PRK00409 648 lgqkgevlsipddkEAIVQAGIMKMKVPlsDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4272-4303 |
3.26e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.08 E-value: 3.26e-03
10 20 30
....*....|....*....|....*....|..
gi 1389908286 4272 IAGILDTDTLEKVSVTEAIHRNLVDNITGQRL 4303
Cdd:pfam00681 8 TGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2147-2610 |
3.34e-03 |
|
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: 43.67 E-value: 3.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2147 LKQKQQADAEmsKHKKEAEQALQQKSQVEKELTVVKLQLD-------ETDKQKVLLDQELQRVKGEVNDAF-KQKSQVEV 2218
Cdd:pfam12128 331 HGAFLDADIE--TAAADQEQLPSWQSELENLEERLKALTGkhqdvtaKYNRRRSKIKEQNNRDIAGIKDKLaKIREARDR 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2219 ELARVRIQMEELvklklkiEEENRRLMQKDKDStqklLAEEAEKMKS-LAEEAGRLS--VEAEETARQRQIAESNLAEQR 2295
Cdd:pfam12128 409 QLAVAEDDLQAL-------ESELREQLEAGKLE----FNEEEYRLKSrLGELKLRLNqaTATPELLLQLENFDERIERAR 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2296 ALAEKILKEKMQAIQEATKLKA----EAEKLQKQKDQAQETAKRLQEDKQQIQQR-------LDKETEGFQKSLEAERKR 2364
Cdd:pfam12128 478 EEQEAANAEVERLQSELRQARKrrdqASEALRQASRRLEERQSALDELELQLFPQagtllhfLRKEAPDWEQSIGKVISP 557
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2365 QL-----------EASAEAEK----LKLRVKEL----SLAQTKA-EDEAKKFKKQADEVKAQLQRTEKHTTEIVVQkLET 2424
Cdd:pfam12128 558 ELlhrtdldpevwDGSVGGELnlygVKLDLKRIdvpeWAASEEElRERLDKAEEALQSAREKQAAAEEQLVQANGE-LEK 636
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2425 QRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKE---MANAQQEQIEQQK-----------AELQQSFLTEKGLL 2490
Cdd:pfam12128 637 ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAErkdSANERLNSLEAQLkqldkkhqawlEEQKEQKREARTEK 716
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2491 LKREKEVEGEKKRFEKQLEDEMKKAKALKD------EQERQRKL------------MEEERKKLQAIMDEAVRKQKEAEE 2552
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKAAIAARRSGAKaelkalETWYKRDLaslgvdpdviakLKREIRTLERKIERIAVRRQEVLR 796
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 2553 EMKNKQREMDVLDKKRLEQEKQLAEENKKLREQLQTFEISSKTVSQTKESQTVSVEKL 2610
Cdd:pfam12128 797 YFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQ 854
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2460-2627 |
3.42e-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: 43.45 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2460 KSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEgEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAi 2539
Cdd:pfam05262 213 KRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVR-QKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQIEI- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2540 mdeavrkQKEAEEEMKNKQREMDVLDKKRLEQEKQlaEENKKLREQLQTFEISS---KTVSQTKESQTVSVEKLVAVTTV 2616
Cdd:pfam05262 291 -------KKNDEEALKAKDHKAFDLKQESKASEKE--AEDKELEAQKKREPVAEdlqKTKPQVEAQPTSLNEDAIDSSNP 361
|
170
....*....|.
gi 1389908286 2617 GTSKGVLNGST 2627
Cdd:pfam05262 362 VYGLKVVDPIT 372
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1516-1820 |
3.54e-03 |
|
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: 43.41 E-value: 3.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1516 LKRKSDAEKEAAKQ----KQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQLQTKAMSFSEQTTKL 1591
Cdd:COG5185 248 LAQTSDKLEKLVEQntdlRLEKLGENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQEL 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1592 EESLKKEQGNVLKLQEEADKLKKQQKEA-NTAREEAEQELEIWRQKANEALRLRLQAEEEAQKKS-----HAQEEAEKQK 1665
Cdd:COG5185 328 EESKRETETGIQNLTAEIEQGQESLTENlEAIKEEIENIVGEVELSKSSEELDSFKDTIESTKESldeipQNQRGYAQEI 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1666 LEAERDAKKRGKAE---------------EAALKQKENAEKELDKQRKFAEQIAQQKLSAEQecirlKADFEHAEQQRGL 1730
Cdd:COG5185 408 LATLEDTLKAADRQieelqrqieqatssnEEVSKLLNELISELNKVMREADEESQSRLEEAY-----DEINRSVRSKKED 482
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1731 LDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEA--LKMKQLADEAARMRSV 1808
Cdd:COG5185 483 LNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHILALENLipASELIQASNAKTDGQA 562
|
330
....*....|..
gi 1389908286 1809 AEEAKKQRQIAE 1820
Cdd:COG5185 563 ANLRTAVIDELT 574
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1572-1831 |
3.64e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 43.28 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1572 SAATQLQTKAmsfsEQTTKLEESLKKEQGNVLKLQEEADKLKKQQKEANTAREEAEQELEiwrqkanealrlrlQAEEEA 1651
Cdd:COG3883 13 FADPQIQAKQ----KELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEID--------------KLQAEI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1652 QKKSHAQEEAEKQKLEAERDAKKRGKAE------------EAALKQKENAEKELDKQRKFAEQIAQQKLSAEQEcirlKA 1719
Cdd:COG3883 75 AEAEAEIEERREELGERARALYRSGGSVsyldvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAK----KA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1720 DfehAEQQRGLLDNELQRLKNEVNSTEKQRKQLEDELNKVRSEMDSLLQMKINAEKASMVNTEKSKQLLESEALKMKQLA 1799
Cdd:COG3883 151 E---LEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
|
250 260 270
....*....|....*....|....*....|..
gi 1389908286 1800 DEAARMRSVAEEAKKQRQIAEEEAARQRSEAE 1831
Cdd:COG3883 228 AAAAAAAAAAAAAAAAASAAGAGAAGAAGAAA 259
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1339-1599 |
3.71e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.05 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1339 AQRRLEDDEKASE-KLKEEERRKMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKMKMKEEASKRQDVAADAEKQKqni 1417
Cdd:PRK07735 28 AKHGAEISKLEEEnREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAK--- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1418 QQELQHLKSLSDQEIKSknqqlEDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAER 1497
Cdd:PRK07735 105 AAALAKQKREGTEEVTE-----EEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1498 LRKQVAEEtqrkknAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRVVEEVAQKSAATQL 1577
Cdd:PRK07735 180 LAKQKAAE------AGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSGDEDAKAKAIAAAKAKAAAAARA 253
|
250 260
....*....|....*....|..
gi 1389908286 1578 QTKAMSFSEQTTKLEESLKKEQ 1599
Cdd:PRK07735 254 KTKGAEGKKEEEPKQEEPSVNQ 275
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1461-1560 |
3.83e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.67 E-value: 3.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1461 EKTtahKAKSEAELQELRDRAAEAEklRKAAQDEAERLRkQVAEETQRKKNAEDE-LKRKSDAEKEAAKQKQRALDDLQK 1539
Cdd:cd03406 174 EKT---KLLIAEQHQKVVEKEAETE--RKRAVIEAEKDA-EVAKIQMQQKIMEKEaEKKISEIEDEMHLAREKARADAEY 247
|
90 100
....*....|....*....|.
gi 1389908286 1540 YKMqaeeaerrMKQAEEEKIR 1560
Cdd:cd03406 248 YRA--------LREAEANKLK 260
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1474-1674 |
4.13e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1474 LQELRDRAAEAEKLRKAAQDEAERLRKQVaeetqrkknaedELKRKSDAEKEAAKQKQRALDDLQKYKmqaeEAERRMKQ 1553
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAA------------LLEAKELLLRERNQQRQEARREREELQ----REEERLVQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1554 AEEekirqirvveevaqksaatQLQTKAmsfsEQTTKLEEslkkeqgnvlKLQEEADKLKKQQKEANTAREEAEQELE-- 1631
Cdd:PRK12705 89 KEE-------------------QLDARA----EKLDNLEN----------QLEEREKALSARELELEELEKQLDNELYrv 135
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1389908286 1632 --IWRQKANEALRLRLQAEEEAQKKSHAQEEAEKQKLEAERDAKK 1674
Cdd:PRK12705 136 agLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
2458-2578 |
4.17e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.00 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2458 QRKSKEMANAQQEQIEQQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQERQrKLMEEERKKLQ 2537
Cdd:pfam13904 67 QRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAESASKSLAKPERK-VSQEEAKEVLQ 145
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1389908286 2538 AIMDEAVRKQKEAEEEMKNKQREmdvldKKRLEQE-KQLAEE 2578
Cdd:pfam13904 146 EWERKKLEQQQRKREEEQREQLK-----KEEEEQErKQLAEK 182
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2248-2435 |
4.20e-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: 43.07 E-value: 4.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2248 DKDSTQKLLaEEAEKMKSLAEEAGRL-SVEAEETARQRQIAESNLAEQRALAEKilkekmqAIQEATKLKAEAEKLQKQK 2326
Cdd:pfam05262 179 DKKVVEALR-EDNEKGVNFRRDMTDLkERESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEV 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2327 DQAQETAKRLqEDKQQIQQRLDKETEGFQKSLEAErKRQLEASAEAEKLKlrvKELSLAQTKAEDEAKKFKKQADEVKAQ 2406
Cdd:pfam05262 251 RQKQQEAKNL-PKPADTSSPKEDKQVAENQKREIE-KAQIEIKKNDEEAL---KAKDHKAFDLKQESKASEKEAEDKELE 325
|
170 180
....*....|....*....|....*....
gi 1389908286 2407 LQRTEKHTTEIVVQKLETQRLQSTREADD 2435
Cdd:pfam05262 326 AQKKREPVAEDLQKTKPQVEAQPTSLNED 354
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2257-2523 |
4.22e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.40 E-value: 4.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2257 AEEAEKMKslAEEAgRLSVEAEEtARQRQIAESNLAEQRALAEKILKEKMQAIQEA-----TKLKAEAEKLQKQKDQAQE 2331
Cdd:PRK05035 440 AIEQEKKK--AEEA-KARFEARQ-ARLEREKAAREARHKKAAEARAAKDKDAVAAAlarvkAKKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2332 TAKRLQEDKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTE 2411
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2412 KHTTEIVVQKLETqrlqstrEADDLKSAIAdleeerkkLKKEAEELQRKSKEMANAQQEQIEQQKAELQ------QSFLT 2485
Cdd:PRK05035 596 QQAASAEPEEQVA-------EVDPKKAAVA--------AAIARAKAKKAEQQANAEPEEPVDPRKAAVAaaiaraKARKA 660
|
250 260 270
....*....|....*....|....*....|....*...
gi 1389908286 2486 EKGLLLKREKEVEGEKKrfeKQLEDEMKKAKALKDEQE 2523
Cdd:PRK05035 661 AQQQANAEPEEAEDPKK---AAVAAAIARAKAKKAAQQ 695
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1814-1960 |
4.43e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.16 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1814 KQRQIAEEEAARQRSEAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAYQRK------------LLED 1881
Cdd:PRK12705 26 KKRQRLAKEAERILQEAQKEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKeeqldaraekldNLEN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1882 Q---AAQHKQDIEEKITQLQTSSDSELGRQKNIVEETLKQK--KVVEEEIHIIKINFHKASKEKADLESELKKLKGIADE 1956
Cdd:PRK12705 106 QleeREKALSARELELEELEKQLDNELYRVAGLTPEQARKLllKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
....
gi 1389908286 1957 TQKS 1960
Cdd:PRK12705 186 MQRI 189
|
|
| DUF612 |
pfam04747 |
Protein of unknown function, DUF612; This family includes several uncharacterized proteins ... |
2039-2421 |
4.95e-03 |
|
Protein of unknown function, DUF612; This family includes several uncharacterized proteins from Caenorhabditis elegans.
Pssm-ID: 282585 [Multi-domain] Cd Length: 511 Bit Score: 43.13 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2039 KEAAQKCTAAEQKAQDVLSKNKEDVLAQEKLRDEFENAKKLAQEAEKAKEKaekeaallrqKAEEAEKQKKAAENEAAKQ 2118
Cdd:pfam04747 52 KEAFASLELTEQPQQVEKVKKSEKKKAQKQIAKDHEAEQKVNAKKAAEKEA----------RRAEAEAKKRAAQEEEHKQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2119 AKAqndtEKQRKEAEEEAARRAAAEAAALKQKQQADAEMSKHKKEAEQALQQKSQVEKELTVVKLQLDET---------- 2188
Cdd:pfam04747 122 WKA----EQERIQKEQEKKEADLKKLQAEKKKEKAVKAEKAEKAEKTKKASTPAPVEEEIVVKKVANDRSaapapepktp 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2189 DKQKVLLDQELQRVKGEVNDAFKQKSQVEVELARVRIQmEELVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAE 2268
Cdd:pfam04747 198 TNTPAEPAEQVQEITGKKNKKNKKKSESEATAAPASVE-QVVEQPKVVTEEPHQQAAPQEKKNKKNKRKSESENVPAASE 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2269 EAGRLSVEAEETARQRQiAESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKL---------QKQKDQAQET-AKRLQE 2338
Cdd:pfam04747 277 TPVEPVVETTPPASENQ-KKNKKDKKKSESEKVVEEPVQAEAPKSKKPTADDNMdfldfvtakEEPKDEPAETpAAPVEE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2339 DKQQIQQRLDKETEGFQKSLEAERKRQLEASAEAEKLKLRVKELSLAQTKAEDEAKKFKKQADEVKAQLQRTEKHTTEIV 2418
Cdd:pfam04747 356 VVENVVENVVEKSTTPPATENKKKNKKDKKKSESEKVTEQPVESAPAPPQVEQVVETTPPASENKKKNKKDKKKSESEKA 435
|
...
gi 1389908286 2419 VQK 2421
Cdd:pfam04747 436 VEE 438
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1485-1662 |
5.16e-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: 42.68 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1485 EKLRKAAQDEAERLRkqvaEETQRKKNAEDELKRKSDAEKEAAKQKQRALDDLQKYKMQAEEAERRMKQAEEEKIRQIRV 1564
Cdd:pfam05262 184 EALREDNEKGVNFRR----DMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKN 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1565 VEEVAQKSAATQLQTKAMSFSEQTTKLEESLKKEQGNVLKLQEE-ADKLKKQQKEANTAREEAEQELEIWRQKANEALRl 1643
Cdd:pfam05262 260 LPKPADTSSPKEDKQVAENQKREIEKAQIEIKKNDEEALKAKDHkAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQ- 338
|
170
....*....|....*....
gi 1389908286 1644 RLQAEEEAQKKSHAQEEAE 1662
Cdd:pfam05262 339 KTKPQVEAQPTSLNEDAID 357
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2419-2586 |
5.22e-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: 5.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2419 VQKLETQRLQSTREADDLKSAIADLEEERKKLKKEAEELQRKSKEmANAQQEQIEQQKAELQQSFLTEKGLLLK----RE 2494
Cdd:COG1579 12 LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELED-LEKEIKRLELEIEEVEARIKKYEEQLGNvrnnKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2495 -----KEVEGEKKRfEKQLEDEMKKAKALKDEQERQRKLMEEERKKLQAIMDEavrKQKEAEEEMKNKQREMDVLDKKRL 2569
Cdd:COG1579 91 yealqKEIESLKRR-ISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAERE 166
|
170
....*....|....*..
gi 1389908286 2570 EQEKQLAEENKKLREQL 2586
Cdd:COG1579 167 ELAAKIPPELLALYERI 183
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2276-2412 |
5.47e-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: 5.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2276 EAEETARQrQIAESN--LAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQK------DQA---QETAKRLQEDKQQIQ 2344
Cdd:COG2268 207 EAERETEI-AIAQANreAEEAELEQEREIETARIAEAEAELAKKKAEERREAEtaraeaEAAyeiAEANAEREVQRQLEI 285
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1389908286 2345 QRLDKETEGFQKSLEAERKRQ---LEASAEAEKLKLRVKEL-----SLAQTKAEDEAKKFKKQADEVKAQLQRTEK 2412
Cdd:COG2268 286 AEREREIELQEKEAEREEAELeadVRKPAEAEKQAAEAEAEaeaeaIRAKGLAEAEGKRALAEAWNKLGDAAILLM 361
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3994-4025 |
5.65e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.65e-03
10 20 30
....*....|....*....|....*....|..
gi 1389908286 3994 KLVSAERAVTGYKDPYSGKVISLFQAMKKGLI 4025
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2147-2586 |
5.88e-03 |
|
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: 42.89 E-value: 5.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2147 LKQKQQADAEMSKHKKEAEQALQQKSQVEKELTvvklQLDETDKQKVLLDQELQRVKGEVNDAFKQKSQVEV-----ELA 2221
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEHerqakELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2222 RVRIQMEELvklKLKIEEENRRLMQKDkDSTQKLLaeEAEKMKSLAEEAGrlsVEAEETARQRQIAESNLAEQRALAEKI 2301
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLL--EMLQSKGLPKKSG---EEDWERTRRIAEAEMQLGHLEVLLDQK 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2302 LKEKMQAiqeatklkaeAEKLQKQKDQAQETAKrlqedKQQIQQRLD-KETegfqKSLEAERK-RQLEASAEAEK----L 2375
Cdd:pfam10174 205 EKENIHL----------REELHRRNQLQPDPAK-----TKALQTVIEmKDT----KISSLERNiRDLEDEVQMLKtnglL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2376 KLRVKELSLAQTKAEDEAKKF-KKQADEVKAQLQRTEkhtTEIVV--QKLET---QRLQSTREADDLKSAIA--DLEEER 2447
Cdd:pfam10174 266 HTEDREEEIKQMEVYKSHSKFmKNKIDQLKQELSKKE---SELLAlqTKLETltnQNSDCKQHIEVLKESLTakEQRAAI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2448 KKLKKEAEELQRKSKE-MANAQQEQIE---QQKAELQQSFLTEKGLLLKREKEVEGEKKRFEKQLEDEMKKAKALKDEQE 2523
Cdd:pfam10174 343 LQTEVDALRLRLEEKEsFLNKKTKQLQdltEEKSTLAGEIRDLKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKE 422
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1389908286 2524 RQRKLMEEERKKLQAI--MDEAVRKQKEAEEEMKnKQREMDvlDKKRLEQEKQLAEENKKLREQL 2586
Cdd:pfam10174 423 RVKSLQTDSSNTDTALttLEEALSEKERIIERLK-EQRERE--DRERLEELESLKKENKDLKEKV 484
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1799-2129 |
6.37e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1799 ADEAARMRSVAEEAKKQRQIAEEEAARQRSE----AEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKRQAEEEAY 1874
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVTEsvepNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1875 QR-KLLEDQAAQHKQDIEEKITQLQTSSDSELGRQKNIVEEtlkQKKVVEEEIHIIKINFHKASKEKADLESElkklkgi 1953
Cdd:pfam02029 84 ERqKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSR---LGRYKEEETEIREKEYQENKWSTEVRQAE------- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1954 aDETQKSKLKAEEEAEKLKklaaeeerrRKEAEEKVKRITAAEEEAARQCKAAQEEVERLKKKAEDANKQKEKAEKEAEK 2033
Cdd:pfam02029 154 -EEGEEEEDKSEEAEEVPT---------ENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2034 QVVLAKEAAQKCTAAEQKAQDVLSKNKEDVL--AQEKLRDEFENAKKLAQEAEKAKEKAEKEAALLRQKAEEAEKQKKAA 2111
Cdd:pfam02029 224 KRRQGGLSQSQEREEEAEVFLEAEQKLEELRrrRQEKESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQE 303
|
330
....*....|....*...
gi 1389908286 2112 EneaaKQAKAQNDTEKQR 2129
Cdd:pfam02029 304 E----AERKLREEEEKRR 317
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
2226-2329 |
6.55e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 41.90 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2226 QMEElVKLKLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEEAGRLSVEAEETARQRQI--AESNLAEQRALAE---- 2299
Cdd:cd03406 170 AMEA-EKTKLLIAEQHQKVVEKEAETERKRAVIEAEKDAEVAKIQMQQKIMEKEAEKKISEieDEMHLAREKARADaeyy 248
|
90 100 110
....*....|....*....|....*....|
gi 1389908286 2300 KILKEKmqaiqEATKLKAEAEKLQKQKDQA 2329
Cdd:cd03406 249 RALREA-----EANKLKLTPEYLELKKYQA 273
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1573-1705 |
6.94e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1573 AATQLQTKAMSFSEQTTKLEESLKKeqgnvlkLQEEADKLKKQQKEANTAR-EEAEQELEIWRQKANEalrlrLQAEEEA 1651
Cdd:COG0542 398 AAARVRMEIDSKPEELDELERRLEQ-------LEIEKEALKKEQDEASFERlAELRDELAELEEELEA-----LKARWEA 465
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1389908286 1652 QKKSHAQEEAEKQKLEAERDAKKRGKAEEAALKQKENAEKELDKQRKFAEQIAQ 1705
Cdd:COG0542 466 EKELIEEIQELKEELEQRYGKIPELEKELAELEEELAELAPLLREEVTEEDIAE 519
|
|
| OmpH |
pfam03938 |
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ... |
2494-2561 |
7.13e-03 |
|
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.
Pssm-ID: 461098 [Multi-domain] Cd Length: 140 Bit Score: 39.87 E-value: 7.13e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1389908286 2494 EKEVEGEKKRFEKQLEDEMKKAKALKDEQERQRKLMEEERKK----LQAIMDEAVRKQKEAEEEMKNKQREM 2561
Cdd:pfam03938 21 QAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEEREEkeqeLQKKEQELQQLQQKAQQELQKKQQEL 92
|
|
| PRK07352 |
PRK07352 |
F0F1 ATP synthase subunit B; Validated |
1612-1741 |
7.46e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180941 [Multi-domain] Cd Length: 174 Bit Score: 40.71 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1612 LKKQQKEANTAREEAEQELeiwrQKANEALrlrlqaEEEAQKKSHAQEEAEKQKLEAERDAK-------KRGKAEEAALK 1684
Cdd:PRK07352 48 LEERREAILQALKEAEERL----RQAAQAL------AEAQQKLAQAQQEAERIRADAKARAEairaeieKQAIEDMARLK 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1389908286 1685 QKENAEKELDKQRKFAE---QIAQQKLS-AEQEcirLKADFEHAEQQRgLLDNELQRLKNE 1741
Cdd:PRK07352 118 QTAAADLSAEQERVIAQlrrEAAELAIAkAESQ---LPGRLDEDAQQR-LIDRSIANLGGN 174
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1746-1898 |
7.64e-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: 42.30 E-value: 7.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1746 EKQRKQLEDELNKVRSEMD-SLLQMKINAEKASMVNTEKSKQLLESEALKMK-QLADEAA-RMRSVAEEAKKQRQIAEEE 1822
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTDlKERESQEDAKRAQQLKEELDKKQIDADKAQQKaDFAQDNAdKQRDEVRQKQQEAKNLPKP 263
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1389908286 1823 AARQRSEAEKILKEKLAAINEATRLKTE--AEMALKAKEAENERLKRQAEEeayQRKLLEDQAAQHKQDIEEKITQLQ 1898
Cdd:pfam05262 264 ADTSSPKEDKQVAENQKREIEKAQIEIKknDEEALKAKDHKAFDLKQESKA---SEKEAEDKELEAQKKREPVAEDLQ 338
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
1062-1539 |
7.97e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 42.58 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1062 LRSELDLTLKKMEQVYGLSSVYLDKLKTVDVVIRNTADAEETLKNYEARLRDV-SKVPSEQKEVEKHRS-QMKSMRSEAE 1139
Cdd:PRK01156 209 DEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEIKTAeSDLSMELEKNNYYKElEERHMKIIND 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1140 ADQVMFDRLQDDLRKATTVHDKmTRIHSERDADLEHYRQLVNGL---------LERWQAVFAQIELRLRELDLLGRHMNS 1210
Cdd:PRK01156 289 PVYKNRNYINDYFKYKNDIENK-KQILSNIDAEINKYHAIIKKLsvlqkdyndYIKKKSRYDDLNNQILELEGYEMDYNS 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1211 YRDSYEWLIRWLTEARQRQEKIQAvPISDSRALREQLTDE-KKLLGEIEKNKDKIDDCHKNAKAYIDSVKDYEFQILTYK 1289
Cdd:PRK01156 368 YLKSIESLKKKIEEYSKNIERMSA-FISEILKIQEIDPDAiKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNM 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1290 A-LQDPIASPLKKPKM-ECASDDIIQEYVNLRTRYSELMTLTNQYIKFIIDAQRRLEDDEK--ASEKLKE--EERRKMAE 1363
Cdd:PRK01156 447 EmLNGQSVCPVCGTTLgEEKSNHIINHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKKRKEylESEEINKsiNEYNKIES 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1364 IQAEL----DKQKQMAEAHAKSVAKAEQ------EALELK-------------------MKMKEEASKRQDvaaDAEKQK 1414
Cdd:PRK01156 527 ARADLedikIKINELKDKHDKYEEIKNRykslklEDLDSKrtswlnalavislidietnRSRSNEIKKQLN---DLESRL 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1415 QNIQQELQHLKSLSDQEIKSKNQQLeDALVSRRKIEEEIHIIRIQLEKTTAHKAKSEAELQELRDRAAEA---------- 1484
Cdd:PRK01156 604 QEIEIGFPDDKSYIDKSIREIENEA-NNLNNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSIIPDLKEItsrindiedn 682
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1389908286 1485 -EKLRKAAQD-EAERLRKQVAEETQRKKNAEDElKRKSDAEK--EAAKQKQRALDDLQK 1539
Cdd:PRK01156 683 lKKSRKALDDaKANRARLESTIEILRTRINELS-DRINDINEtlESMKKIKKAIGDLKR 740
|
|
| valS |
TIGR00422 |
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase ... |
1829-1968 |
8.09e-03 |
|
valyl-tRNA synthetase; The valyl-tRNA synthetase (ValS) is a class I amino acyl-tRNA ligase and is particularly closely related to the isoleucyl tRNA synthetase. [Protein synthesis, tRNA aminoacylation]
Pssm-ID: 273070 [Multi-domain] Cd Length: 861 Bit Score: 42.35 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1829 EAEKILKEKLAAINEATRLKTEAEMALKAKEAENERLKrqaeeeayqrkllEDQAAQHKQDIEEKITQLQTSSDSELGRQ 1908
Cdd:TIGR00422 721 EAEKAFELLKEIIVSIRNLKAESNIPPNAPLKVLLIYT-------------EAETAERLKLNAVDIKGAINFSEVEVVIE 787
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1909 KNIVEETLkQKKVVEEEIHIIKINFHKASKEKADLESELKKLKGiadETQKSKLKAEEEA 1968
Cdd:TIGR00422 788 KPEVTEAV-VELVPGFEIIIPVKGLINKAKELARLQKQLDKEKK---EVIRIEGKLENEG 843
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1002-1501 |
8.40e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 8.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1002 TVTRLRQPVDKEPLKACALKtSEQKKVQSELEG-LKRDLTCVSEKTEEV----LMSPQQSSSAPLLRSELD-LTLKKMeq 1075
Cdd:pfam15921 413 TIDHLRRELDDRNMEVQRLE-ALLKAMKSECQGqMERQMAAIQGKNESLekvsSLTAQLESTKEMLRKVVEeLTAKKM-- 489
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1076 vyglssvyldklktvdvvirntadaeeTLKNYEARLRDVSKVPSE-QKEVEKHRSQMKSMRSEAEADQVMFDRLQ---DD 1151
Cdd:pfam15921 490 ---------------------------TLESSERTVSDLTASLQEkERAIEATNAEITKLRSRVDLKLQELQHLKnegDH 542
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1152 LRKATTVHDKMTRIHSERDADLEHYRQlvngllerwqavfaQIELRLRELDLLGRhmnsyrdsyewlirwlTEARQRQEK 1231
Cdd:pfam15921 543 LRNVQTECEALKLQMAEKDKVIEILRQ--------------QIENMTQLVGQHGR----------------TAGAMQVEK 592
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1232 IQavpisdsraLREQLTDEKKLLGEIEKNKDKIDDCHKNAKAyidSVKDYEFQILTYKALQDPIASPLKKPKMEcaSDDI 1311
Cdd:pfam15921 593 AQ---------LEKEINDRRLELQEFKILKDKKDAKIRELEA---RVSDLELEKVKLVNAGSERLRAVKDIKQE--RDQL 658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1312 IQEYVNLRtrySELMTLTNQYIKFIIDAQRRLEDDEKASEKLKEEERRKMAEIQAELDKQKQM--AEAHAKSVAKAEQ-- 1387
Cdd:pfam15921 659 LNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMegSDGHAMKVAMGMQkq 735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1388 --------EALELKMKMKEEAskrqdvAADAEKQKQNIQQELQHLkslsdqeikskNQQLEDALVSRRKIEEEIHIIRIQ 1459
Cdd:pfam15921 736 itakrgqiDALQSKIQFLEEA------MTNANKEKHFLKEEKNKL-----------SQELSTVATEKNKMAGELEVLRSQ 798
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1389908286 1460 LEKTTAHKAKSEAELQELRDRAAEAEKLRKAAQDEAERLRKQ 1501
Cdd:pfam15921 799 ERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1360-1539 |
8.57e-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: 41.06 E-value: 8.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1360 KMAEIQAELDKQKQMAEAHAKSVAKAEQEALELKmkmkEEASKRQDVAADAEKQKQNIQQELQHLKSLsdqeIKSKNQQL 1439
Cdd:COG1579 11 DLQELDSELDRLEHRLKELPAELAELEDELAALE----ARLEAAKTELEDLEKEIKRLELEIEEVEAR----IKKYEEQL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1440 EDALVSRrkieeeihiIRIQLEKttahkakseaELQELRDRAAEAEKLRKAAQDEAERLRKQVAEETQRKKNAEDELKRK 1519
Cdd:COG1579 83 GNVRNNK---------EYEALQK----------EIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEK 143
|
170 180
....*....|....*....|
gi 1389908286 1520 SDAEKEAAKQKQRALDDLQK 1539
Cdd:COG1579 144 KAELDEELAELEAELEELEA 163
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1611-1875 |
9.24e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 9.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1611 KLKKQQKEANTAREEAEQEL----EIWRQKANEALRLRLQAE--EEAQKKSHA-----QEEAEKQKLEAERDAKKRGKAE 1679
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLrknlTVEPVKGSNVIEISYTSPdpELAAAVANAlaeayLEQNLELRREEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1680 EAALKQK-ENAEKELDKQRK---------FAEQIAQQKLSAEQECIRLKADFEHAEQQRGLLDNELQRLKNEVNSTEKQR 1749
Cdd:COG3206 184 LPELRKElEEAEAALEEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSP 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1750 --KQLEDELNKVRSEMDSLLQmKINAEKASMVNTEKSKQLLEsealkmKQLADEAARmrsVAEEAKKQRQIAEEEAARQR 1827
Cdd:COG3206 264 viQQLRAQLAELEAELAELSA-RYTPNHPDVIALRAQIAALR------AQLQQEAQR---ILASLEAELEALQAREASLQ 333
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1389908286 1828 SEAEKiLKEKLAAINEatrlkteaemalkaKEAENERLKRQAE--EEAYQ 1875
Cdd:COG3206 334 AQLAQ-LEARLAELPE--------------LEAELRRLEREVEvaRELYE 368
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4415-4452 |
9.71e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 36.69 E-value: 9.71e-03
10 20 30
....*....|....*....|....*....|....*...
gi 1389908286 4415 QKLRDVSAYSKYLTCPKTKLKISYKDAMERSMTEEGTG 4452
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
2195-2427 |
9.85e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 9.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2195 LDQELQRVKGEVNDAFKQKSQVEVELARVRIQ-----MEELVKLkLKIEEENRRLMQKDKDSTQKLLAEEAEKMKSLAEE 2269
Cdd:PRK04778 254 IEKEIQDLKEQIDENLALLEELDLDEAEEKNEeiqerIDQLYDI-LEREVKARKYVEKNSDTLPDFLEHAKEQNKELKEE 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2270 AGRLS----VEAEETARQRQIaESNLAEQRALAEKILKEKMQAIQEATKLKAEAEKLQKQKDQAQETAKRLQEDKQQI-- 2343
Cdd:PRK04778 333 IDRVKqsytLNESELESVRQL-EKQLESLEKQYDEITERIAEQEIAYSELQEELEEILKQLEEIEKEQEKLSEMLQGLrk 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1389908286 2344 -QQRLDKETEGFQKSLEaERKRQLEASA-----EAEKLKLRVKELSLAQTKAEDEAKKF-----KKQADEVKAQLQRTEK 2412
Cdd:PRK04778 412 dELEAREKLERYRNKLH-EIKRYLEKSNlpglpEDYLEMFFEVSDEIEALAEELEEKPInmeavNRLLEEATEDVETLEE 490
|
250
....*....|....*
gi 1389908286 2413 HTTEIVVQKLETQRL 2427
Cdd:PRK04778 491 ETEELVENATLTEQL 505
|
|
| |
