|
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 ... |
227-331 |
1.30e-74 |
|
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409037 Cd Length: 105 Bit Score: 243.85 E-value: 1.30e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 227 DRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNI 306
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 1207141724 307 RNDDIADGNPKLTLGLIWTIILHFQ 331
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
224-342 |
4.77e-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: 4.77e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 224 DERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 303
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141724 304 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQSD 342
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
344-449 |
2.70e-71 |
|
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: 234.53 E-value: 2.70e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 1207141724 424 PEDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
216-340 |
1.18e-69 |
|
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: 230.64 E-value: 1.18e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 216 ERAVIRIADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDF 295
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDY 83
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1207141724 296 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQ 340
Cdd:cd21236 84 LKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
345-449 |
1.03e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.41 E-value: 1.03e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 1207141724 425 EDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
224-341 |
1.46e-61 |
|
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409086 Cd Length: 118 Bit Score: 207.19 E-value: 1.46e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 224 DERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKL 303
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141724 304 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQS 341
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
345-449 |
9.71e-59 |
|
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: 198.67 E-value: 9.71e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 424
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 1207141724 425 EDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
343-449 |
6.24e-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: 6.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 343 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLL 422
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 1207141724 423 DPEDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
229-332 |
2.90e-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: 174.49 E-value: 2.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 229 VQKKTFTKWVNKHLVKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 307
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 1207141724 308 NDDIADGNPKLTLGLIWTIILHFQI 332
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 ... |
216-328 |
4.46e-50 |
|
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: 174.48 E-value: 4.46e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 216 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 293
Cdd:cd21246 2 ERSRIKaLADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 294 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21246 82 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
345-445 |
7.74e-48 |
|
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: 167.59 E-value: 7.74e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 1207141724 425 EDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
345-445 |
6.91e-46 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 161.79 E-value: 6.91e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141724 425 EDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
216-328 |
6.05e-45 |
|
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: 159.77 E-value: 6.05e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 216 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 293
Cdd:cd21193 2 EKGRIRaLQEERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKAL 81
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 294 DFLkHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21193 82 AFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
225-332 |
3.13e-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: 157.54 E-value: 3.13e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 225 ERDRVQKKTFTKWVNKHLVKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 300
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 1207141724 301 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
223-445 |
1.68e-43 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 170.89 E-value: 1.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 223 ADERDRVQKKTFTKWVNKHLVKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHR 299
Cdd:COG5069 3 AKKWQKVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 300 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVNGQsddMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSWRDGRL 378
Cdd:COG5069 83 GVKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATINEEGE---LTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLA 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 379 FNAIIHKHRPNLIDINKVYRQTNLE--NLEQAFSIAERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSMY 445
Cdd:COG5069 160 FSALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSWYI 229
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
222-328 |
4.10e-43 |
|
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: 155.18 E-value: 4.10e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 222 IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQ 300
Cdd:cd21318 31 LADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLKEQR 110
|
90 100
....*....|....*....|....*...
gi 1207141724 301 VKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21318 111 VHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
216-328 |
3.87e-42 |
|
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: 152.13 E-value: 3.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 216 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 293
Cdd:cd21317 17 ERSRIKaLADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKAL 96
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 294 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21317 97 QFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
225-332 |
5.93e-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: 148.10 E-value: 5.93e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 225 ERDRVQKKTFTKWVNKHLVKAQRH--ITDLYEDLRDGHNLISLLEVLSGETLPREKGRM--RFHKLQNVQIALDFLKHRQ 300
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLTKRC 80
|
90 100 110
....*....|....*....|....*....|..
gi 1207141724 301 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21190 81 IKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
332-445 |
6.17e-40 |
|
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: 145.20 E-value: 6.17e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 332 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 412 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYY 111
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
344-449 |
8.70e-40 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and similar proteins; SYNE-1, also called nesprin-1, enaptin, KASH domain-containing protein 1 (KASH1), myocyte nuclear envelope protein 1 (MYNE-1), or nuclear envelope spectrin repeat protein 1, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-1 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409092 Cd Length: 109 Bit Score: 144.77 E-value: 8.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 1207141724 424 PEDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
345-445 |
2.25e-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: 143.61 E-value: 2.25e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21319 5 SAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITKLLDP 84
|
90 100
....*....|....*....|.
gi 1207141724 425 EDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21319 85 EDVFTENPDEKSIITYVVAFY 105
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
1091-1168 |
1.64e-38 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 139.66 E-value: 1.64e-38
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 1091 LSWQYLMRDITLINSWNFIMFKTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKATQHYDNLLRS 1168
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
229-330 |
3.05e-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: 3.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 229 VQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 306
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 1207141724 307 RNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
227-328 |
3.75e-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: 139.83 E-value: 3.75e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 227 DRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLKHRQVKLVN 305
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 1207141724 306 IRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
344-445 |
4.06e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 140.00 E-value: 4.06e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 1207141724 424 PEDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
225-332 |
5.12e-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: 139.58 E-value: 5.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 225 ERDRVQKKTFTKWVNKHLVKAQ--RHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 302
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 1207141724 303 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
341-445 |
8.00e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.42 E-value: 8.00e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 341 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 420
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 1207141724 421 LLDPEDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
348-449 |
8.95e-37 |
|
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: 8.95e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 348 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141724 427 VDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
329-445 |
4.85e-36 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 134.80 E-value: 4.85e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 329 HFQISDIQVNGQSDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQA 408
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141724 409 FSIAERDLGVTRLLDPEDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
224-332 |
8.06e-36 |
|
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: 133.51 E-value: 8.06e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 224 DERDRVQKKTFTKWVNKHLVKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVK 302
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 1207141724 303 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1974-2819 |
1.27e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 151.06 E-value: 1.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1974 QQKSKAEKETmsnTEKSKQLLESEAAKMRELAEEATKLRSV---AEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 2050
Cdd:PTZ00121 1083 AKEDNRADEA---TEEAFGKAEEAKKTETGKAEEARKAEEAkkkAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARK 1159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2051 TRLKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--------KIGQLKKSSDTELDRQKKIVEETL 2122
Cdd:PTZ00121 1160 AEDARKAEEARKAEDAKKAEAARKAEE---VRKAEELRKAEDARKAEAarkaeeerKAEEARKAEDAKKAEAVKKAEEAK 1236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2123 KQ----RKVVEEEIHILKLNFEKASSGKQELELELKKlkgiADETQKSKAkaeeeaekFRKLALEEEKKRKEAEAKVKQI 2198
Cdd:PTZ00121 1237 KDaeeaKKAEEERNNEEIRKFEEARMAHFARRQAAIK----AEEARKADE--------LKKAEEKKKADEAKKAEEKKKA 1304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2199 QAAEEEAARQHKAAQeevgrLMKLAEEAKKQKEIAEKEAEkqvilvqEAAQKCSAAEQKAQnvlvqqnkdsmaqdKLKEE 2278
Cdd:PTZ00121 1305 DEAKKKAEEAKKADE-----AKKKAEEAKKKADAAKKKAE-------EAKKAAEAAKAEAE--------------AAADE 1358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2279 FEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEasrraeaeaaalKLKQE 2358
Cdd:PTZ00121 1359 AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKK------------------ADEAKKKAEED------------KKKAD 1408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2359 ADSEMAKYKKLAEKtLKQKSSVEEELVKVKVQLDETDKQKsvldvELKRLKQEVSDA--IKQKAQVEDELSKVKIQMEDL 2436
Cdd:PTZ00121 1409 ELKKAAAAKKKADE-AKKKAEEKKKADEAKKKAEEAKKAD-----EAKKKAEEAKKAeeAKKKAEEAKKADEAKKKAEEA 1482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2437 LKLklkiekenQELMKKDKDNTKKlleeeAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2516
Cdd:PTZ00121 1483 KKA--------DEAKKKAEEAKKK-----ADEAKKAAEAKKK----ADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEK 1545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2517 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQE--------TEGFQKSLEAERKRQLEITAEAEKLKVKVTQL 2588
Cdd:PTZ00121 1546 KKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeearIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEEL 1625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2589 SdaqsKAEEEAKK---FKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEkeklkkeAADL 2665
Cdd:PTZ00121 1626 K----KAEEEKKKveqLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKA-------AEAL 1694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2666 QKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2745
Cdd:PTZ00121 1695 KKEAEEAKKAEELKKKEAEEK------KKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 2746 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEE 2819
Cdd:PTZ00121 1769 KAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIFDNFAniiEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEE 1845
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
345-445 |
3.76e-35 |
|
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: 131.37 E-value: 3.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 1207141724 425 EDVDVPHPDEKSIITYVSSMY 445
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
216-328 |
5.84e-35 |
|
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: 132.47 E-value: 5.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 216 ERAVIR-IADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIAL 293
Cdd:cd21316 39 ERSRIKaLADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKAL 118
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 294 DFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 328
Cdd:cd21316 119 QFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1813-2605 |
6.24e-35 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 148.75 E-value: 6.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1813 EEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQ- 1891
Cdd:PTZ00121 1077 KDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEi 1156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1892 -KEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEEELIKVRKEME 1970
Cdd:PTZ00121 1157 aRKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKA--EAARKAEEERKAEEARKAEDAKKAEAVKKAEE 1234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1971 ILLQQKSKAEKETMSNTEKSKQLLESEAAKM--RELAEEATKLRSvAEEAKKQRQIAEEEAARQRAEAEKI--LKEKLTA 2046
Cdd:PTZ00121 1235 AKKDAEEAKKAEEERNNEEIRKFEEARMAHFarRQAAIKAEEARK-ADELKKAEEKKKADEAKKAEEKKKAdeAKKKAEE 1313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2047 INEATRLKTEAEIALKEKEAendrLKRKAEEEGYQ---RKVLEDQAAQHKQAIEEKigqlKKSSDTELDRQKKIVEETLK 2123
Cdd:PTZ00121 1314 AKKADEAKKKAEEAKKKADA----AKKKAEEAKKAaeaAKAEAEAAADEAEAAEEK----AEAAEKKKEEAKKKADAAKK 1385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2124 QRKVVEEEIHILKlnfeKASSGKQElelelkklkgiADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEE 2203
Cdd:PTZ00121 1386 KAEEKKKADEAKK----KAEEDKKK-----------ADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAK 1450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2204 EAARQHKAAQEevgrLMKLAEEAKKQKEIAEKEAEKQVilVQEAAQKCSAAEQKAQNVlvqqnKDSMAQDKLKEEFEKAK 2283
Cdd:PTZ00121 1451 KKAEEAKKAEE----AKKKAEEAKKADEAKKKAEEAKK--ADEAKKKAEEAKKKADEA-----KKAAEAKKKADEAKKAE 1519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2284 KlAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEM 2363
Cdd:PTZ00121 1520 E-AKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVM 1598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2364 AKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVldvelKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKI 2443
Cdd:PTZ00121 1599 KLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV-----EQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEED 1673
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2444 EKENQELMKKDKDNTKK--LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKL 2521
Cdd:PTZ00121 1674 KKKAEEAKKAEEDEKKAaeALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKA-EEAKKD 1752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2522 KAEAEKLQKQKDQAQVEAQKLLEAKKE-MQQRLDQETE---------------GFQKSLEAERKRQLEITAEAEKLKVKV 2585
Cdd:PTZ00121 1753 EEEKKKIAHLKKEEEKKAEEIRKEKEAvIEEELDEEDEkrrmevdkkikdifdNFANIIEGGKEGNLVINDSKEMEDSAI 1832
|
810 820
....*....|....*....|
gi 1207141724 2586 TQLSDAQSKAEEEAKKFKKQ 2605
Cdd:PTZ00121 1833 KEVADSKNMQLEEADAFEKH 1852
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
228-333 |
1.11e-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: 124.87 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQ-VKLV 304
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
332-445 |
1.72e-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: 1.72e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 332 ISDIQVNGqsddMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21291 1 IADINEEG----LTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 412 AERDLGVTRLLDPEDV-DVPHPDEKSIITYVSSMY 445
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYF 111
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
344-442 |
2.15e-32 |
|
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) family; The SYNE family includes SYNE-1, -2 and calmin. SYNE-1 (also called nesprin-1, enaptin, KASH domain-containing protein 1, KASH1, myocyte nuclear envelope protein 1, MYNE-1, or nuclear envelope spectrin repeat protein 1) and SYNE-2 (also called nesprin-2, KASH domain-containing protein 2, KASH2, nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE) may act redundantly. They are multi-isomeric modular proteins which form a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. They also act as components of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409041 Cd Length: 107 Bit Score: 123.30 E-value: 2.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 1207141724 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
348-450 |
5.34e-32 |
|
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: 122.34 E-value: 5.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 348 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLDPE 425
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 1207141724 426 DVDVPHPDEKSIITYVSSMYDVMPR 450
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1553-2429 |
8.28e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 138.35 E-value: 8.28e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1553 QDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQE 1632
Cdd:PTZ00121 1083 AKEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAED 1162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1633 LKTLSEQEIKAKSQQVEEAllsrtRIEEEIHiirlqlettmkqkntaetELLQLRaKAVDADKLRNAaqEEAEKLRKqvA 1712
Cdd:PTZ00121 1163 ARKAEEARKAEDAKKAEAA-----RKAEEVR------------------KAEELR-KAEDARKAEAA--RKAEEERK--A 1214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1713 EETqkkRKAEEELKRKSEAEkdaakekkkaledLEKFKLQAEEAERHLKQAELEKQRQIQ--VVEEVAKKTAATQLESKQ 1790
Cdd:PTZ00121 1215 EEA---RKAEDAKKAEAVKK-------------AEEAKKDAEEAKKAEEERNNEEIRKFEeaRMAHFARRQAAIKAEEAR 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1791 VALTAR-LEESLKNEQVMVIQLQEEAEHLKKQQAEADKArEQAEKELETWRQKANEALRlrlqAEEEANKKtaaqeeaek 1869
Cdd:PTZ00121 1279 KADELKkAEEKKKADEAKKAEEKKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADAAKK----KAEEAKKA--------- 1344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1870 qKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEEtAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVN 1949
Cdd:PTZ00121 1345 -AEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEEDKKKA----DELKKAAAAKK 1418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1950 SAVKQKKELEEelikVRKEMEIllqqKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlrsvAEEAKKQRQIAEE-E 2028
Cdd:PTZ00121 1419 KADEAKKKAEE----KKKADEA----KKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKK----ADEAKKKAEEAKKaD 1486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2029 AARQRAEAEKILKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEegyQRKVLEDQAAQHKQAIEE--KIGQLKKS 2106
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEA---KKKADEAKKAEEAKKADEAKKAEE---AKKADEAKKAEEKKKADElkKAEELKKA 1560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2107 SDTELDRQKKIVEETLKQ--------RKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKaeeeaekfR 2178
Cdd:PTZ00121 1561 EEKKKAEEAKKAEEDKNMalrkaeeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE--------K 1632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2179 KLALEEEKKRKEAEAKVKQIQAAEEE----AARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCS 2252
Cdd:PTZ00121 1633 KKVEQLKKKEAEEKKKAEELKKAEEEnkikAAEEAKKAEEDKKKAeeAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2253 AAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEkaKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAE 2332
Cdd:PTZ00121 1713 EEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAK--KDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDE 1790
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2333 KLRKEAEKEASRRAEAEAAAlklkQEADSEMAKYKKLAEKTlkQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLK 2409
Cdd:PTZ00121 1791 KRRMEVDKKIKDIFDNFANI----IEGGKEGNLVINDSKEM--EDSAIKEVADSKNMQLEEADafeKHKFNKNNENGEDG 1864
|
890 900
....*....|....*....|
gi 1207141724 2410 QEVSDAIKQKAQVEDELSKV 2429
Cdd:PTZ00121 1865 NKEADFNKEKDLKEDDEEEI 1884
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
344-442 |
1.95e-31 |
|
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: 120.71 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 344 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 1207141724 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
229-332 |
1.97e-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: 120.88 E-value: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 229 VQKKTFTKWVNKHLVKAQR-HITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLVNIR 307
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 1207141724 308 NDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1522-2098 |
2.46e-31 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 135.83 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1522 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANE 1600
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1601 LKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKsQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1680
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELE-EELEELEEELEEAEEELEEAEAELAEAEEALLEAE 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1681 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledLEKFKLQAEEAERHL 1760
Cdd:COG1196 372 AELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER------------------LEEELEELEEALAEL 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1761 KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1840
Cdd:COG1196 434 EEEEEEEEEALE--EAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVK 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1841 QKANEALR------LRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM----AEETA 1910
Cdd:COG1196 512 AALLLAGLrglagaVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIraraALAAA 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1911 KQKLAAEQELIRLRADFEHAEQQRTVLDDEL---QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnT 1987
Cdd:COG1196 592 LARGAIGAAVDLVASDLREADARYYVLGDTLlgrTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGS----R 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1988 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 2067
Cdd:COG1196 668 RELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEEL 747
|
570 580 590
....*....|....*....|....*....|.
gi 1207141724 2068 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 2098
Cdd:COG1196 748 LEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
229-332 |
5.73e-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: 119.31 E-value: 5.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 229 VQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR--EKGRMRFHKLQNVQIALDFLKHRQVKLVNI 306
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 1207141724 307 RNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
348-449 |
1.03e-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: 118.52 E-value: 1.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 348 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 1207141724 427 VDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
350-445 |
1.72e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 117.83 E-value: 1.72e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 350 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 428
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 1207141724 429 VPHPDEKSIITYVSSMY 445
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
225-334 |
2.44e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 117.68 E-value: 2.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 225 ERDRVQKKTFTKWVNKHLVKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQ 300
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 1207141724 301 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 334
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1571-2773 |
8.21e-30 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 131.49 E-value: 8.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1571 AEMQAELEkqkqlAETHAKAIAKAEQEANEL-------KTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKA 1643
Cdd:NF041483 111 AEHQARLQ-----AELHTEAVQRRQQLDQELaerrqtvESHVNENVAWAEQLRARTESQA---RRLLDESRAEAEQALAA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1644 KSQQVEeallsrtRIEEEIHIiRLQLETtmkQKNTAETELLQLRAKAvDADKLRNAAQEEA-------EKLRKQVAEETQ 1716
Cdd:NF041483 183 ARAEAE-------RLAEEARQ-RLGSEA---ESARAEAEAILRRARK-DAERLLNAASTQAqeatdhaEQLRSSTAAESD 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1717 KKRKAEEELKRKSEAekdaakekkkaledlekfklQAEEAERHLKQAELEKQRqiqVVEEvAKKTAATQLESKQVALTAR 1796
Cdd:NF041483 251 QARRQAAELSRAAEQ--------------------RMQEAEEALREARAEAEK---VVAE-AKEAAAKQLASAESANEQR 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1797 LEESLKNEQVMVIQLQEEAEHLKkqqAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKR 1876
Cdd:NF041483 307 TRTAKEEIARLVGEATKEAEALK---AEAEQALADARAEAEKLVAEAAEKAR-TVAAEDTAAQLAKAARTAEEVLTKASE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1877 EAKK--RAKAEEAALKQKEAaEMELGNQRKMAEETAKQ-KLAA--------------EQELIRLRADfehAEQQRTVLDD 1939
Cdd:NF041483 383 DAKAttRAAAEEAERIRREA-EAEADRLRGEAADQAEQlKGAAkddtkeyraktvelQEEARRLRGE---AEQLRAEAVA 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1940 ELQRLKNDV-NSAVKQKKE----LEEELIKVRKEMEILLQQ-KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRS 2013
Cdd:NF041483 459 EGERIRGEArREAVQQIEEaartAEELLTKAKADADELRSTaTAESERVRTEAIERATTLRRQAEETLERTRAEAERLRA 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2014 VAEE-AKKQRQIAEEEAARQRAEAEK-ILKEKLTAINEATRLKTEAE-------IALKEKEAENDRLKRKAEEEGYQrkv 2084
Cdd:NF041483 539 EAEEqAEEVRAAAERAARELREETERaIAARQAEAAEELTRLHTEAEerltaaeEALADARAEAERIRREAAEETER--- 615
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2085 LEDQAAqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHIlKLNFEKASSGKQelelelkklkgIADETQ 2164
Cdd:NF041483 616 LRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAARAEGENVAV-RLRSEAAAEAER-----------LKSEAQ 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2165 KSKAkaeeeaekfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE-----------EVGRLMKLAEE--AKKQKE 2231
Cdd:NF041483 677 ESAD---------RVRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEEtlgsaraeadqERERAREQSEEllASARKR 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2232 IAEKEAEKQViLVQEAAQKC----SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAAllhk 2305
Cdd:NF041483 748 VEEAQAEAQR-LVEEADRRAtelvSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEAQ---- 814
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2306 kaEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELv 2385
Cdd:NF041483 815 --EEADRVRS--------------DAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL- 867
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2386 kvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKL 2461
Cdd:NF041483 868 ----RSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDE 943
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2462 LEEEAENMK-KLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEA 2539
Cdd:NF041483 944 ARAEAERVRaDAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEA 1017
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2540 QKLL-EAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEK 2618
Cdd:NF041483 1018 DRTLdEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAE 1089
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2619 HTSEKHTVVEK----------------------LEVQRLQSKQEADGLH-KAIADLEKEKEKLKKEAADLQKQSKEManv 2675
Cdd:NF041483 1090 ATVEGNSLVEKartdadellvgarrdatairerAEELRDRITGEIEELHeRARRESAEQMKSAGERCDALVKAAEEQ--- 1166
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2676 QQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKlqsAMDAAIKKQ 2755
Cdd:NF041483 1167 LAEAEAKAKELVSDANSEASKVRIAAVKKAEGLLKEAEQKKAELVREAEKIKAEAEAEAKRTVEEGKR---ELDVLVRRR 1243
|
1290
....*....|....*...
gi 1207141724 2756 KEAEEEMNGKQKEMQDLE 2773
Cdd:NF041483 1244 EDINAEISRVQDVLEALE 1261
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
228-330 |
1.30e-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: 1.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1748-2340 |
7.38e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 124.66 E-value: 7.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1748 KFKLQAEEAERHLKQA------------ELEKQR---QIQVveEVAKK--TAATQLESKQVALTA----RLEESLKNEQV 1806
Cdd:COG1196 169 KYKERKEEAERKLEATeenlerledilgELERQLeplERQA--EKAERyrELKEELKELEAELLLlklrELEAELEELEA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1807 MVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE 1886
Cdd:COG1196 247 ELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1887 AALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR 1966
Cdd:COG1196 327 ELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1967 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 2046
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2047 INEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRK-----VLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEET 2121
Cdd:COG1196 487 AEAAARLLLLLE-AEADYEGFLEGVKAALLLAGLRGLagavaVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEY 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2122 LKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIADEtqkskakaeEEAEKFRKLALEEEKKRKEAEAKVKQIQAA 2201
Cdd:COG1196 566 LKAAK--AGRATFLPLDKIRARAALAAALARGAIGAAVDLV---------ASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2202 EEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKLKEEFEK 2281
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE--LAERLAEEELELEEALLAEEEEERELAEA 712
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2282 AKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2340
Cdd:COG1196 713 EEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELER 771
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
348-447 |
1.02e-27 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 110.07 E-value: 1.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 348 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED- 426
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 1207141724 427 VDVPHPDEKSIITYVSSMYDV 447
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1546-2165 |
2.87e-27 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 123.33 E-value: 2.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1546 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1625
Cdd:PTZ00121 1214 AEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD 1293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1626 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEeihiirlqlettmkQKNTAEtellQLRAKAVDADKLRNAAQEEAE 1705
Cdd:PTZ00121 1294 EAKKAEEKKKA--DEAKKKAEEAKKADEAKKKAEE--------------AKKKAD----AAKKKAEEAKKAAEAAKAEAE 1353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1706 KLRKQvAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER---HLKQAELEKQRQIQVVEEVAKKTA 1782
Cdd:PTZ00121 1354 AAADE-AEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKkadELKKAAAAKKKADEAKKKAEEKKK 1432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1783 ATQLESKqvALTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRlrlqAEEEANKKTA 1862
Cdd:PTZ00121 1433 ADEAKKK--AEEAKKADEAKKKA----EEAKKAEEAKKKAEEAKKADEAKKKAEE--AKKADEAKK----KAEEAKKKAD 1500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1863 aqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlddelq 1942
Cdd:PTZ00121 1501 --------------EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELK-------- 1558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1943 rlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 2022
Cdd:PTZ00121 1559 --KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVE 1636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2023 QIAEEEA--------ARQRAEAEKILKEKLTAINEATRLKTE-----------AEIALKEKEAEN---DRLKRKAEEEgy 2080
Cdd:PTZ00121 1637 QLKKKEAeekkkaeeLKKAEEENKIKAAEEAKKAEEDKKKAEeakkaeedekkAAEALKKEAEEAkkaEELKKKEAEE-- 1714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2081 QRKVLEDQAAQHKQAIeeKIGQLKKSSDTELDRQKKIVEETLKQRKV----VEEEIHILKLNFEKASSGKQELELELKKL 2156
Cdd:PTZ00121 1715 KKKAEELKKAEEENKI--KAEEAKKEAEEDKKKAEEAKKDEEEKKKIahlkKEEEKKAEEIRKEKEAVIEEELDEEDEKR 1792
|
....*....
gi 1207141724 2157 KGIADETQK 2165
Cdd:PTZ00121 1793 RMEVDKKIK 1801
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
330-445 |
3.23e-27 |
|
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: 109.40 E-value: 3.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 330 FQISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAF 409
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 1207141724 410 SIAERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFY 114
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
228-330 |
4.03e-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: 4.03e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
221-332 |
1.17e-26 |
|
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: 107.92 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 221 RIADERDRVQKKTFTKWVNKHLVKAQR--HITDLYEDLRDGHNLISLLEVLSGETLPR-EKGRMRFHKLQNVQIALDFLK 297
Cdd:cd21247 12 KLQEQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLK 91
|
90 100 110
....*....|....*....|....*....|....*.
gi 1207141724 298 HR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21247 92 TKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1546-2130 |
1.24e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.40 E-value: 1.24e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1546 IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHN 1625
Cdd:PTZ00121 1130 AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAE 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1626 IQRELQELKTLSEQEIKAKSQQVEEAllsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNA-----A 1700
Cdd:PTZ00121 1210 EERKAEEARKAEDAKKAEAVKKAEEA---KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKAdelkkA 1286
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1701 QE--EAEKLRK----QVAEETQKK----RKAEE------ELKRKSEAEKD----AAKEKKKALEDLEKFKLQAEEAERHL 1760
Cdd:PTZ00121 1287 EEkkKADEAKKaeekKKADEAKKKaeeaKKADEakkkaeEAKKKADAAKKkaeeAKKAAEAAKAEAEAAADEAEAAEEKA 1366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1761 KQAELEKQRQIQVVEEVAKKT----AATQLESKQVALTARLEESLKNEQVmviqlQEEAEHLKKQQAE---ADKAREQAE 1833
Cdd:PTZ00121 1367 EAAEKKKEEAKKKADAAKKKAeekkKADEAKKKAEEDKKKADELKKAAAA-----KKKADEAKKKAEEkkkADEAKKKAE 1441
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1834 --KELETWRQKANEALR---LRLQAEE-----EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR 1903
Cdd:PTZ00121 1442 eaKKADEAKKKAEEAKKaeeAKKKAEEakkadEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEA 1521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1904 KMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQrlKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKET 1983
Cdd:PTZ00121 1522 KKADEAKKAEEAKKADEAKKAEEKKKADELKKA--EELK--KAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEV 1597
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1984 MSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRaEAEKILKE----KLTAINEATRLKTEAEI 2059
Cdd:PTZ00121 1598 MKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKK-KAEELKKAeeenKIKAAEEAKKAEEDKKK 1676
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2060 ALKEKEAENDrlKRKAEEEGYQRKVLEDQAAQHKQAIEE---KIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 2130
Cdd:PTZ00121 1677 AEEAKKAEED--EKKAAEALKKEAEEAKKAEELKKKEAEekkKAEELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
228-333 |
1.42e-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: 107.42 E-value: 1.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1575-2140 |
1.90e-26 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 120.04 E-value: 1.90e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1575 AELEKQ-KQLAEthaKAiAKAEQeANELKTKMKDevsKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALL 1653
Cdd:COG1196 196 GELERQlEPLER---QA-EKAER-YRELKEELKE---LEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1654 SRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEK 1733
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1734 DAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQE 1813
Cdd:COG1196 348 EAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--ELLEALRAAAELAAQLEELEEAEEALLERLE----RLEE 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1814 EAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1893
Cdd:COG1196 422 ELEELEEALAELEEEEEEEEEALEE-AAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAE 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1894 AAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1973
Cdd:COG1196 501 ADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLD 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1974 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEakkqRQIAEEEAARQRAEAEKILKEKLTAINEATRL 2053
Cdd:COG1196 581 KIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLG----RTLVAARLEAALRRAVTLAGRLREVTLEGEGG 656
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2054 KTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIH 2133
Cdd:COG1196 657 SAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREE 736
|
....*..
gi 1207141724 2134 ILKLNFE 2140
Cdd:COG1196 737 LLEELLE 743
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
332-445 |
6.78e-26 |
|
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: 105.55 E-value: 6.78e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 332 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 412 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFY 111
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
350-445 |
1.10e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 104.16 E-value: 1.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 350 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED-VD 428
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 1207141724 429 VPHPDEKSIITYVSSMY 445
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
332-445 |
2.72e-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: 103.65 E-value: 2.72e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 332 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 412 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFY 111
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1706-2610 |
1.07e-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: 114.77 E-value: 1.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1706 KLRKqvaEETQKK-RKAEEELKRkseaekdAAKEKKKALEDLEKFKLQAEEAERH--LKQAELEKQRQIQVVEEVAKKTA 1782
Cdd:TIGR02168 171 KERR---KETERKlERTRENLDR-------LEDILNELERQLKSLERQAEKAERYkeLKAELRELELALLVLRLEELREE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1783 ATQLESKQvaltARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEA-LRLRLQAEEEANkkt 1861
Cdd:TIGR02168 241 LEELQEEL----KEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLeQQKQILRERLAN--- 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1862 aaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDEL 1941
Cdd:TIGR02168 314 ------------LERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1942 QRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEketmsnTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQ 2021
Cdd:TIGR02168 382 ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ------QEIEELLKKLEEAELKELQAELEELEEELEELQEE 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2022 RQIAEEEAARQRAEaekilkekltaINEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKVLedQAAQHKQAIEEKI 2100
Cdd:TIGR02168 456 LERLEEALEELREE-----------LEEAEQALDAAERELAQLQARLDSLERLQENlEGFSEGVK--ALLKNQSGLSGIL 522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2101 GQLKKSSDTELDRQKKIV---EETLKQRKVVEEEIHILKLNF-EKASSGKQELELELKKLkgiADETQKSKAKAEEEAEK 2176
Cdd:TIGR02168 523 GVLSELISVDEGYEAAIEaalGGRLQAVVVENLNAAKKAIAFlKQNELGRVTFLPLDSIK---GTEIQGNDREILKNIEG 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2177 FRKLALEEEKKRKEAEAK----------VKQIQAAEEEAARQH---------------------KAAQEEVGRLMKLAEE 2225
Cdd:TIGR02168 600 FLGVAKDLVKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRpgyrivtldgdlvrpggvitgGSAKTNSSILERRREI 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2226 AKKQKEIAekeaekqvilvqEAAQKCSAAEQKAQNVLVQqnkdsmaQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHK 2305
Cdd:TIGR02168 680 EELEEKIE------------ELEEKIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEA 740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2306 KAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2385
Cdd:TIGR02168 741 EVEQLEE--------------RIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALD 806
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2386 KVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkdkdntKKLLEEE 2465
Cdd:TIGR02168 807 ELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL----------------------AAEIEEL 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2466 AENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA 2545
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQER 944
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2546 KKEMQQRLDQETEGFQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2610
Cdd:TIGR02168 945 LSEEYSLTLEEAEALENKIEDDEE---EARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLT 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1876-2562 |
1.19e-24 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 114.26 E-value: 1.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1876 REAKK----RAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1951
Cdd:COG1196 207 RQAEKaeryRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1952 VKQKKELEEELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 2031
Cdd:COG1196 287 QAEEYELLAELARLEQD-IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2032 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLKKSSDTEL 2111
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEA-------LLERLERLEEELEELEEALAELEEEEE 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2112 DRQKKIVEETLKQRKVVEEEIHILKLnfekassgkqelelelkklkgIADETQKskakaeeeaekfRKLALEEEKKRKEA 2191
Cdd:COG1196 439 EEEEALEEAAEEEAELEEEEEALLEL---------------------LAELLEE------------AALLEAALAELLEE 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2192 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEkeaEKQVILVQEAAQKCSAAEQKAQNVLvqqnkdsma 2271
Cdd:COG1196 486 LAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAV---LIGVEAAYEAALEAALAAALQNIVV--------- 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2272 qdklkeefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAA 2351
Cdd:COG1196 554 --------EDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2352 ALklkQEADSEMAKYkkLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2431
Cdd:COG1196 626 TL---VAARLEAALR--RAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2432 QMEDLLKLKLKIEKENQELmKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEK 2511
Cdd:COG1196 701 AEEEEERELAEAEEERLEE-ELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAL 779
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2512 K----QAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEA----KKEMQQRLdQET-----EGFQK 2562
Cdd:COG1196 780 GpvnlLAIEEYEELEERYDFLSEQREDLEEARETLEEAieeiDRETRERF-LETfdavnENFQE 842
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
346-445 |
1.92e-24 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 100.71 E-value: 1.92e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 346 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 425
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 1207141724 426 D-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1334-2059 |
2.04e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 114.08 E-value: 2.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1334 EASQTQLQKLRSEAEGKQATFD----RLEEELQRATEVNKRMSQLHSERDVELEHYRQlVGNLRERWQAVFAQ----IEL 1405
Cdd:PTZ00121 1102 EAKKTETGKAEEARKAEEAKKKaedaRKAEEARKAEDARKAEEARKAEDAKRVEIARK-AEDARKAEEARKAEdakkAEA 1180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1406 RQRELDLlnRQMQAYRESYDwlIRWIADAKQRQDKLHAVPIggSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKfakgyid 1485
Cdd:PTZ00121 1181 ARKAEEV--RKAEELRKAED--ARKAEAARKAEEERKAEEA--RKAEDAKKAEAVKKAEEAKKDAEEAKKAEE------- 1247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1486 aIKDYELQLVTYKALVEPIASPLKKAKMESAsddiiqeyvtlrtRYSELMTLSsqyikfiiETQRRLQDEEKAAEKLKEE 1565
Cdd:PTZ00121 1248 -ERNNEEIRKFEEARMAHFARRQAAIKAEEA-------------RKADELKKA--------EEKKKADEAKKAEEKKKAD 1305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1566 ERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANElkTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQ----EI 1641
Cdd:PTZ00121 1306 EAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE--AKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKkkadAA 1383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1642 KAKSQQVEEALLSRTRIEEEihiirLQLETTMKQKNTAETELLQLRAKAVD---ADKLRNAAQE--EAEKLRKQvAEETQ 1716
Cdd:PTZ00121 1384 KKKAEEKKKADEAKKKAEED-----KKKADELKKAAAAKKKADEAKKKAEEkkkADEAKKKAEEakKADEAKKK-AEEAK 1457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1717 K----KRKAEE-----ELKRKSEAEKDAAKEKKKAledlEKFKLQAEEAERhlKQAELEKQRQIQVVEEVAKKTAATQLE 1787
Cdd:PTZ00121 1458 KaeeaKKKAEEakkadEAKKKAEEAKKADEAKKKA----EEAKKKADEAKK--AAEAKKKADEAKKAEEAKKADEAKKAE 1531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1788 SKQVAltarlEESLKNEQVMVIQLQEEAEHLKKqqAEADKAREQAEKELE---TWRQKANEALRLRLQAEEEANKKTAAQ 1864
Cdd:PTZ00121 1532 EAKKA-----DEAKKAEEKKKADELKKAEELKK--AEEKKKAEEAKKAEEdknMALRKAEEAKKAEEARIEEVMKLYEEE 1604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1865 EEAEKQKEEAKREAKKRA----KAEE-----AALKQKEAAEMELGNQRKMAEETAKQKlaAEQELIRLRADFEHAEQQRT 1935
Cdd:PTZ00121 1605 KKMKAEEAKKAEEAKIKAeelkKAEEekkkvEQLKKKEAEEKKKAEELKKAEEENKIK--AAEEAKKAEEDKKKAEEAKK 1682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1936 VLDDELQRLKNDVNSAVKQKKelEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVA 2015
Cdd:PTZ00121 1683 AEEDEKKAAEALKKEAEEAKK--AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIA 1760
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1207141724 2016 EEAKKQRQIAEEeaarQRAEAEKILKEKLTAINEATRLKTEAEI 2059
Cdd:PTZ00121 1761 HLKKEEEKKAEE----IRKEKEAVIEEELDEEDEKRRMEVDKKI 1800
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
232-329 |
2.26e-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: 100.47 E-value: 2.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 232 KTFTKWVNKHLVKA-QRHITDLYEDLRDGHNLISLLEVLSGETLPREK---GRMRFHKLQNVQIALDFLKHRQVKLVNIR 307
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 1207141724 308 NDDIADGnPKLTLGLIWTIILH 329
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
345-445 |
3.10e-24 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 100.19 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 424
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|....
gi 1207141724 425 EDV---DVphPDEKSIITYVSSMY 445
Cdd:cd21198 80 ADMvllSV--PDKLSVMTYLHQIR 101
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
332-445 |
4.27e-24 |
|
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: 100.53 E-value: 4.27e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 332 ISDIQVngqsDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSI 411
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 412 AERDLGVTRLLDPED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFY 111
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
344-450 |
6.64e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 99.28 E-value: 6.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 344 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY--RQTNLENLEQAFSIAERDLGVTR 420
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 1207141724 421 -LLDPEDVDvpHPDEKSIITYVSSMYDVMPR 450
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
229-332 |
7.90e-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: 7.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 229 VQKKTFTKWVNKHLVKAQRH--ITDLYEDLRDGHNLISLLEVLSGETLP-REKGRMRFHKLQNVQIALDFLKHRQ-VKLV 304
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
990-1056 |
8.30e-24 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 97.33 E-value: 8.30e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 990 QLKPRNpaQPIKGKLPVQAVCDFKQMEITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSICFIVP 1056
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
345-449 |
1.76e-23 |
|
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409094 Cd Length: 106 Bit Score: 97.94 E-value: 1.76e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 1207141724 425 EDVDVPHPDEKSIITYVSSMYDVMP 449
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1995-2879 |
3.36e-23 |
|
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: 109.68 E-value: 3.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1995 ESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRK 2074
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2075 AEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELK 2154
Cdd:pfam02463 232 LKLNEERIDLLQELLRDEQEEIESSKQEIEKEEE-KLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2155 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2234
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2235 KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQE-AEKAKDNAEKEAALLHKKAEEAERQ 2313
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGkLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2314 kkaaeaeaakqakaqedaEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDE 2393
Cdd:pfam02463 471 ------------------EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLG 532
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2394 tDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLA 2473
Cdd:pfam02463 533 -DLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKA 611
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2474 E-EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQR 2552
Cdd:pfam02463 612 TlEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAK 691
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2553 LDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEV 2632
Cdd:pfam02463 692 EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEE---EEEEKSRLKKEEKEEEKSE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2633 QRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQ--EKTILQQSFFAEKETLLKKEKAIEEEKK 2710
Cdd:pfam02463 769 LSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEeeQLLIEQEEKIKEEELEELALELKEEQKL 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2711 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQsamdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNL 2790
Cdd:pfam02463 849 EKLAEEELERLEEEITKEELLQELLLKEEELEEQK-------LKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEE 921
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2791 REKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGvKKDVPLAFDGIREKVPASRLHEIGVLS 2870
Cdd:pfam02463 922 RIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELG-KVNLMAIEEFEEKEERYNKDELEKERL 1000
|
....*....
gi 1207141724 2871 KKEYDKLKK 2879
Cdd:pfam02463 1001 EEEKKKLIR 1009
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
348-448 |
6.29e-23 |
|
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: 96.38 E-value: 6.29e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 348 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPEDV 427
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 1207141724 428 DVPHPDEKSIITYVSSMYDVM 448
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 ... |
1826-2685 |
6.32e-23 |
|
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: 108.91 E-value: 6.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1826 DKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1905
Cdd:pfam02463 168 KRKKKEALKKL---IEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1906 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNdvnsavKQKKELEEELIKVRKEMEILLQQKSKAEKETmS 1985
Cdd:pfam02463 245 LLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE------EELKLLAKEEEELKSELLKLERRKVDDEEKL-K 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1986 NTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 2065
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEEL 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2066 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSG 2145
Cdd:pfam02463 398 ELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKET 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2146 KQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGrlmKLAEE 2225
Cdd:pfam02463 478 QLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV---IVEVS 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2226 AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAlLHK 2305
Cdd:pfam02463 555 ATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILK-DTE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2306 KAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2385
Cdd:pfam02463 634 LTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELK 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2386 KVKVQLDETDKQKsvLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE 2465
Cdd:pfam02463 714 KLKLEAEELLADR--VQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEE 791
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2466 A-ENMKKLAEEAARLNIEAQEAA---RLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQK 2541
Cdd:pfam02463 792 KeEKLKAQEEELRALEEELKEEAellEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQE 871
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2542 LLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE-TEKHT 2620
Cdd:pfam02463 872 LLLKEEELEE-QKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEaDEKEK 950
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2621 SEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2685
Cdd:pfam02463 951 EENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEET 1015
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1930-2793 |
8.50e-23 |
|
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: 108.52 E-value: 8.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1930 AEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS-----KAEKETMSNTEKSKQL--LESEAAKMR 2002
Cdd:pfam02463 151 KPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQelklkEQAKKALEYYQLKEKLelEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2003 ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI-LKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 2081
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLaQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2082 RKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIAD 2161
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2162 ETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQV 2241
Cdd:pfam02463 391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKS 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2242 ILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEfEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEA 2321
Cdd:pfam02463 471 EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS-GLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAV 549
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2322 AKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKL-------AEKTLKQKSSVEEELVKVKVQLDET 2394
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLeidpilnLAQLDKATLEADEDDKRAKVVEGIL 629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2395 DKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEkenQELMKKDKDNTKKLLEEEAENMKKLAE 2474
Cdd:pfam02463 630 KDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ---ELQEKAESELAKEEILRRQLEIKKKEQ 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2475 EAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ-KLLEAKKEMQQRL 2553
Cdd:pfam02463 707 REKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKeKELAEEREKTEKL 786
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2554 DQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2633
Cdd:pfam02463 787 KVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKE 866
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2634 RLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLE 2713
Cdd:pfam02463 867 ELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEI------EERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2714 KQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDA-AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2792
Cdd:pfam02463 941 LLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLmAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLK 1020
|
.
gi 1207141724 2793 K 2793
Cdd:pfam02463 1021 E 1021
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2268-2846 |
1.25e-22 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 108.30 E-value: 1.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2268 DSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAallhKKAEEAERQKKAAEAEAAKQAkaqedAEKLRK-E----AEKEA 2342
Cdd:PTZ00121 1082 DAKEDNRADEATEEAFGKAEEAKKTETGKAEEA----RKAEEAKKKAEDARKAEEARK-----AEDARKaEearkAEDAK 1152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2343 SRRAEAEAAALKLKQEA-DSEMAKYKKLAEKTLKQKSSVE----EELVKVKV--------QLDETDKQKSVLDVELKRLK 2409
Cdd:PTZ00121 1153 RVEIARKAEDARKAEEArKAEDAKKAEAARKAEEVRKAEElrkaEDARKAEAarkaeeerKAEEARKAEDAKKAEAVKKA 1232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2410 QEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKEN----QELMKKDK----DNTKKLLEEEAENMKKLAEEAARLNI 2481
Cdd:PTZ00121 1233 EEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAaikaEEARKADElkkaEEKKKADEAKKAEEKKKADEAKKKAE 1312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2482 EAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQrLDQETEGFQ 2561
Cdd:PTZ00121 1313 EAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADA-AKKKAEEKK 1391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2562 KSLEAERKRQlEITAEAEKLKVKvtqlSDAQSKAEEEAKKF--KKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2639
Cdd:PTZ00121 1392 KADEAKKKAE-EDKKKADELKKA----AAAKKKADEAKKKAeeKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKA 1466
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2640 EadglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE--QLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFE 2717
Cdd:PTZ00121 1467 E----EAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEakKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKA 1542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2718 DEVKKAEALKAEQERQRKlmeEERKKLQSAmdaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLReklqql 2797
Cdd:PTZ00121 1543 EEKKKADELKKAEELKKA---EEKKKAEEA-----KKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMK------ 1608
|
570 580 590 600
....*....|....*....|....*....|....*....|....*....
gi 1207141724 2798 qsSQKASYTKEIEIQTDKVPEEELVQMTMVETTKKVLNGSTEVDGVKKD 2846
Cdd:PTZ00121 1609 --AEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKA 1655
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1522-2312 |
2.04e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.06 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1522 QEYVTLRTRYSEL-MTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEkqkqlaeTHAKAIAKAEQEANE 1600
Cdd:TIGR02168 213 ERYKELKAELRELeLALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLE-------ELRLEVSELEEEIEE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1601 LKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE 1680
Cdd:TIGR02168 286 LQKELYALANEISRL----EQQKQILRERLANL----ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1681 TELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaekdaakekkkaledlekfklqaeeAERHL 1760
Cdd:TIGR02168 358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER----------------------------LEARL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1761 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1840
Cdd:TIGR02168 410 ERLEDRRERLQQEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1841 QKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR----------------------------EAKKRAKAEEAALKQK 1892
Cdd:TIGR02168 489 ARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKKAIAFLKQN 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1893 E---AAEMELGNQRKMAEETAKQKLAAEQELIRLRADF--EHAEQQRTVLDDELQRLK--NDVNSAVKQKKELEEELIKV 1965
Cdd:TIGR02168 569 ElgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRKALSYLLGGVLvvDDLDNALELAKKLRPGYRIV 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1966 RKEMEILLQQKS---KAEKETMSNTEKSKQLLESEaAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 2042
Cdd:TIGR02168 649 TLDGDLVRPGGVitgGSAKTNSSILERRREIEELE-EKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2043 KLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEdQAAQHKQAIEEKIGQLKKssdtELDRQKKIVEETL 2122
Cdd:TIGR02168 728 ISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLE-EAEEELAEAEAEIEELEA----QIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2123 KQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAAE 2202
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA--------------EIEELEELI 868
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2203 EEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEF-EK 2281
Cdd:TIGR02168 869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLsEE 948
|
810 820 830
....*....|....*....|....*....|.
gi 1207141724 2282 AKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2312
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEEEARRRLKRLEN 979
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
228-333 |
3.81e-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: 95.15 E-value: 3.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
228-333 |
5.42e-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: 94.77 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 228 RVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR---EKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1748-2638 |
6.07e-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: 105.52 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1748 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKktaatQLES--KQVALTARLEEslkneqvmviqLQEEAEHLKKQQAEA 1825
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLEDILNELER-----QLKSleRQAEKAERYKE-----------LKAELRELELALLVL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1826 DKarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELgnqrkm 1905
Cdd:TIGR02168 233 RL--EELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQK------ 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1906 aEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtms 1985
Cdd:TIGR02168 305 -QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ--- 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1986 ntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIALKEK 2064
Cdd:TIGR02168 381 --------LETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEEL 452
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2065 EAENDRLKRKAEEegyqrkvLEDQAAQHKQAIEEKIGQLkkssdteldrqkkiveETLKQRKVVEEEihiLKLNFEKASS 2144
Cdd:TIGR02168 453 QEELERLEEALEE-------LREELEEAEQALDAAEREL----------------AQLQARLDSLER---LQENLEGFSE 506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2145 GKQELELELKKLKGIADETQKSKAKAEEEaekfrKLALEEEKKRKEAEAKVKQIQAAEEEAARQhkaAQEEVGRLMKLAE 2224
Cdd:TIGR02168 507 GVKALLKNQSGLSGILGVLSELISVDEGY-----EAAIEAALGGRLQAVVVENLNAAKKAIAFL---KQNELGRVTFLPL 578
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2225 EAKKQKEIAEKEAE--KQVILVQEAAQKCSAAEQKAQ--------NVLVQQNKDSmAQDKLKEEFEKAKKLAQEAEK--- 2291
Cdd:TIGR02168 579 DSIKGTEIQGNDREilKNIEGFLGVAKDLVKFDPKLRkalsyllgGVLVVDDLDN-ALELAKKLRPGYRIVTLDGDLvrp 657
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2292 ----AKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedaeklRKEAEKeasrraeaeaaalKLKQEADSEMAKYK 2367
Cdd:TIGR02168 658 ggviTGGSAKTNSSILERRRE--------------------------IEELEE-------------KIEELEEKIAELEK 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2368 KLAEkTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQME------DLLKLKL 2441
Cdd:TIGR02168 699 ALAE-LRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEeleerlEEAEEEL 777
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2442 KIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKL 2521
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESL 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2522 KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ---ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2598
Cdd:TIGR02168 858 AAEIEELEELIEELESELEALLNERASLEEALALlrsELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVR 937
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 1207141724 2599 AKKFKKQ-ADEIKIRLQETEKHTSEKHTVVEKLE--VQRLQSK 2638
Cdd:TIGR02168 938 IDNLQERlSEEYSLTLEEAEALENKIEDDEEEARrrLKRLENK 980
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
345-443 |
7.83e-22 |
|
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: 93.07 E-value: 7.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVY-RQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 1207141724 424 PEDVDVPHPDEKSIITYVSS 443
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 ... |
1589-2467 |
9.27e-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: 105.05 E-value: 9.27e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1589 KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrtRIEEEIHIIRLQ 1668
Cdd:pfam02463 200 LKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEK-----EEEKLAQVLKEN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1669 LETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEK 1748
Cdd:pfam02463 275 KEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESE-KEKKKAEKELKKEKEEIEELEKELKELEIKREA 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1749 FKLQAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKqqaEADKA 1828
Cdd:pfam02463 354 EEEEEEELE---KLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK---EEKKE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1829 REQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEE 1908
Cdd:pfam02463 428 ELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARS 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1909 TAKQKLAAEQELIRLRADFEHAEQQR---TVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL-QQKSKAEKETM 1984
Cdd:pfam02463 508 GLKVLLALIKDGVGGRIISAHGRLGDlgvAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLgARKLRLLIPKL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1985 SNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALKEK 2064
Cdd:pfam02463 588 KLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKES-GLRKGVSLEEGLAEKSEVKA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2065 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIgqlKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKass 2144
Cdd:pfam02463 667 SLSELTKELLEIQELQEKAESELAKEEILRRQLEIK---KKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKL--- 740
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2145 gkqelelelkKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEvgrlmKLAE 2224
Cdd:pfam02463 741 ----------LKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEE-----ELRA 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2225 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA-KDNAEKEAALL 2303
Cdd:pfam02463 806 LEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLlKEEELEEQKLK 885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2304 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKssVEEE 2383
Cdd:pfam02463 886 DELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEE--ERNK 963
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2384 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE 2463
Cdd:pfam02463 964 RLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELG 1043
|
....
gi 1207141724 2464 EEAE 2467
Cdd:pfam02463 1044 GSAE 1047
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1522-2359 |
2.05e-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: 103.90 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1522 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1601
Cdd:pfam02463 166 RLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQEL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1602 KTKMKDEVSK---RQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNT 1678
Cdd:pfam02463 246 LRDEQEEIESskqEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKK 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1679 AETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1758
Cdd:pfam02463 326 AEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1759 HlKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ------LQEEAEHLKKQQAEADKAREQA 1832
Cdd:pfam02463 406 E-AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQelkllkDELELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1833 EKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR-AKAEEAALKQKEAAEMELGNQRKMAEETAK 1911
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDlGVAVENYKVAISTAVIVEVSATADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1912 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKND--VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEK 1989
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDpiLNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1990 SKQLLESEAAkMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEK-EAE 2067
Cdd:pfam02463 645 ESGLRKGVSL-EEGLAEKSEVKASLSELTKELLEIQELqEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAeELL 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2068 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ---LKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 2144
Cdd:pfam02463 724 ADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKkeeKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEEL 803
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2145 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2224
Cdd:pfam02463 804 RALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQK 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2225 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKaqNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2304
Cdd:pfam02463 884 LKDELESKEEKEKEEKKELEEESQKLNLLEEKE--NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEER 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2305 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEA 2359
Cdd:pfam02463 962 NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIEETC 1016
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1547-2629 |
2.63e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 103.37 E-value: 2.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1547 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK-QKQLAETHAKAIAKAEQeANELKTKMKdevskrqdvavdsekqKHN 1625
Cdd:NF041483 251 QARRQAAELSRAAEQRMQEAEEALREARAEAEKvVAEAKEAAAKQLASAES-ANEQRTRTA----------------KEE 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1626 IQRELQELKTLSEQeIKAKSQQVeealLSRTRIEEEihiiRLQLETTMKQKN-TAETELLQLRAKAVDADKLRNAAQEEA 1704
Cdd:NF041483 314 IARLVGEATKEAEA-LKAEAEQA----LADARAEAE----KLVAEAAEKARTvAAEDTAAQLAKAARTAEEVLTKASEDA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1705 EKLRKQVAEETQK-KRKAEEELKRkseaekdaakekkkaledlekFKLQAEEAERHLKQAELE--KQRQIQVVE--EVAK 1779
Cdd:NF041483 385 KATTRAAAEEAERiRREAEAEADR---------------------LRGEAADQAEQLKGAAKDdtKEYRAKTVElqEEAR 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1780 KT--AATQLESKQVALTARLEESLKNEQVMviQLQEEA----EHLKKQQAEADKAREQAEKELETWRQKANE-ALRLRLQ 1852
Cdd:NF041483 444 RLrgEAEQLRAEAVAEGERIRGEARREAVQ--QIEEAArtaeELLTKAKADADELRSTATAESERVRTEAIErATTLRRQ 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1853 AEEEANkktaaqeeaekqkeeakreaKKRAKAEEaalkqkeaaemelgnQRKMAEETA-KQKLAAEQELIRLRADFEHA- 1930
Cdd:NF041483 522 AEETLE--------------------RTRAEAER---------------LRAEAEEQAeEVRAAAERAARELREETERAi 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1931 EQQRTVLDDELQRLKNDVNSAVKQKkelEEELIKVRKEMEILlqqkskaEKETMSNTEKskqlLESEAA-KMRELAEEAT 2009
Cdd:NF041483 567 AARQAEAAEELTRLHTEAEERLTAA---EEALADARAEAERI-------RREAAEETER----LRTEAAeRIRTLQAQAE 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2010 klrsvaEEAKKQRQIAEEEAARQRAEAEkilkekltaiNEATRLKTEAeialkekEAENDRLKRKAEEEGyQRKVLEDQA 2089
Cdd:NF041483 633 ------QEAERLRTEAAADASAARAEGE----------NVAVRLRSEA-------AAEAERLKSEAQESA-DRVRAEAAA 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2090 AQHKQAIEEkiGQLKKSSDTELDRQKKIVEETLkqrkvveeeihilklnfekassgkqelelelkklkgiadetqkskak 2169
Cdd:NF041483 689 AAERVGTEA--AEALAAAQEEAARRRREAEETL----------------------------------------------- 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2170 aeeeaekfrklaleeekkrkeaeakvkqiQAAEEEAARQHKAAQEEVGRLMklaeeAKKQKEIAEKEAEKQViLVQEAAQ 2249
Cdd:NF041483 720 -----------------------------GSARAEADQERERAREQSEELL-----ASARKRVEEAQAEAQR-LVEEADR 764
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2250 KC----SAAEQKAQNVlvqqnKDSMA--QDKLKEEFekaKKLAQEAEKAKDNAEKEAallhkkAEEAERqkkaaeaeaak 2323
Cdd:NF041483 765 RAtelvSAAEQTAQQV-----RDSVAglQEQAEEEI---AGLRSAAEHAAERTRTEA------QEEADR----------- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2324 qakAQEDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELvkvkvQLDETDKQKSVLDV 2403
Cdd:NF041483 820 ---VRSDAYAERERASEDAN----------RLRREAQEETEAAKALAERTVSEAIAEAERL-----RSDASEYAQRVRTE 881
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2404 ELKRLKQEVSDAIKQKAQVEDELSKVK----IQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMK-KLAEEAAR 2478
Cdd:NF041483 882 ASDTLASAEQDAARTRADAREDANRIRsdaaAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRaDAAAQAEQ 961
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2479 LNIEAQ-EAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAklkAEAEKLqkqKDQAQVEAQKLL-EAKKEMQQRLDQE 2556
Cdd:NF041483 962 LIAEATgEAERLRAEAAETVGSAQQHAERIRTEAERVKAEAA---AEAERL---RTEAREEADRTLdEARKDANKRRSEA 1035
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141724 2557 TEGFQKSLEAERKRQLEITAEAEKLKVKVTqlSDAQSKAEEEAKKFKKQADEIkirlqeTEKHTSEKHTVVEK 2629
Cdd:NF041483 1036 AEQADTLITEAAAEADQLTAKAQEEALRTT--TEAEAQADTMVGAARKEAERI------VAEATVEGNSLVEK 1100
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1746-2679 |
3.60e-21 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 102.98 E-value: 3.60e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1746 LEKFKLQAEE----AERHLKQAELEKQRQIQvveEVAKKTAATQLESKQVALTARLE------------ESLKNEQVM-V 1808
Cdd:NF041483 78 LRNAQIQADQlradAERELRDARAQTQRILQ---EHAEHQARLQAELHTEAVQRRQQldqelaerrqtvESHVNENVAwA 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1809 IQLQEEAEH-----LKKQQAEADK----AREQAEKELETWRQK-ANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1878
Cdd:NF041483 155 EQLRARTESqarrlLDESRAEAEQalaaARAEAERLAEEARQRlGSEAESARAEAEAILRRARKDAERLLNAASTQAQEA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1879 KKRAK------AEEAALKQKEAAEMELGNQRKMAE-ETAKQKLAAEQELIRLRAD---------FEHAEQQRT-VLDDEL 1941
Cdd:NF041483 235 TDHAEqlrsstAAESDQARRQAAELSRAAEQRMQEaEEALREARAEAEKVVAEAKeaaakqlasAESANEQRTrTAKEEI 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1942 QRLkndVNSAVKQ----KKELEEELIKVRKEMEILLQQ-----KSKAEKETMSNTEKSKQLLESEAAKMRELAEEATklR 2012
Cdd:NF041483 315 ARL---VGEATKEaealKAEAEQALADARAEAEKLVAEaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKATT--R 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2013 SVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAI---------------NEATRLKTEAEIALKEKEAENDRLKRKAEE 2077
Cdd:NF041483 390 AAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGEAEQLRAEAVAEGERIRGEARR 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2078 EGYQR---------------KVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQkkiVEETLkQRKVVEEEihilKLNFEKA 2142
Cdd:NF041483 470 EAVQQieeaartaeelltkaKADADELRSTATAESERVRTEAIERATTLRRQ---AEETL-ERTRAEAE----RLRAEAE 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2143 SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRL-MK 2221
Cdd:NF041483 542 EQAEEVRAAAERAARELREETERAIAARQAEAA--EELTRLHTEAEERLTAAEEALADARAEAERIRREAAEETERLrTE 619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2222 LAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEF-EKAKKLAQEAEKAKDNAEKE 2299
Cdd:NF041483 620 AAERIRTLQAQAEQEAER---LRTEAAADASAARAEGENVAVRLRSEAAAEaERLKSEAqESADRVRAEAAAAAERVGTE 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2300 AA-LLHKKAEEAERQkkaaeaeaakqakaqedaeklRKEAEKEASRRaeaeaaalklKQEADSEMAKYKKLAEKTLKQ-K 2377
Cdd:NF041483 697 AAeALAAAQEEAARR---------------------RREAEETLGSA----------RAEADQERERAREQSEELLASaR 745
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2378 SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQ-KAQVEDELS-----------KVKIQMEDLLKLKLKIEK 2445
Cdd:NF041483 746 KRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGlQEQAEEEIAglrsaaehaaeRTRTEAQEEADRVRSDAY 825
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2446 ENQELMKKDKDNTKKLLEEEAENMKKLAE--------EAARLNIEAQE-AARLRQIAESDLAKQRELAEKMLEEkkqAIQ 2516
Cdd:NF041483 826 AERERASEDANRLRREAQEETEAAKALAErtvseaiaEAERLRSDASEyAQRVRTEASDTLASAEQDAARTRAD---ARE 902
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2517 EAAKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLE-----ITAEAEKLKVKVTQ-LS 2589
Cdd:NF041483 903 DANRIRSDaAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEqliaeATGEAERLRAEAAEtVG 982
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2590 DAQSKAE---EEAKKFKKQADEikirlqETEKHTSEKHTVVEKL--EVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2664
Cdd:NF041483 983 SAQQHAErirTEAERVKAEAAA------EAERLRTEAREEADRTldEARKDANKRRSEAAEQADTLITEAAAEADQLTAK 1056
|
1050
....*....|....*
gi 1207141724 2665 LQKQSKEMANVQQEQ 2679
Cdd:NF041483 1057 AQEEALRTTTEAEAQ 1071
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
349-447 |
4.09e-21 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 91.26 E-value: 4.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 349 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 427
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141724 428 DVPHPDEKSIITYVSSMYDV 447
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYEL 107
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1344-2057 |
1.05e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.17 E-value: 1.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1344 RSEAEGK-QATFDRLEEELQRATEVNKRMSQLHSERDVeLEHYRQLVGNLRERwqavfaQIELRQRELDLLNRQMQAyre 1422
Cdd:COG1196 174 KEEAERKlEATEENLERLEDILGELERQLEPLERQAEK-AERYRELKEELKEL------EAELLLLKLRELEAELEE--- 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1423 sydwlirwiadakqrqdklhavpiggskgLQEQLTQEKKLLEEIEKNKDKVEDcqkfakgyidaikdyelqlvtykalve 1502
Cdd:COG1196 244 -----------------------------LEAELEELEAELEELEAELAELEA--------------------------- 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1503 piasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEErkkmAEMQAELEKQKQ 1582
Cdd:COG1196 268 ------ELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEEL----AELEEELEELEE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1583 LAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEI 1662
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEA-LRAAAELAAQLEELEEAEEALLERL 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1663 HIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKA 1742
Cdd:COG1196 417 ERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1743 LEDLEKFKLQAEEA-ERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKneqvmviQLQEEAEHLKKQ 1821
Cdd:COG1196 497 LEAEADYEGFLEGVkAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDE-------VAAAAIEYLKAA 569
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1822 QA--------EADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE 1893
Cdd:COG1196 570 KAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREV 649
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1894 AAEMELGNQRKMAEETAKQKLAAEQELIRLRAdfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILL 1973
Cdd:COG1196 650 TLEGEGGSAGGSLTGGSRRELLAALLEAEAEL--EELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALE 727
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1974 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI-------AEEEAARQRAEAEKILKEK--- 2043
Cdd:COG1196 728 EQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELEERYDFLSEQRedl 807
|
730 740
....*....|....*....|.
gi 1207141724 2044 -------LTAINEATRLKTEA 2057
Cdd:COG1196 808 eearetlEEAIEEIDRETRER 828
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
345-442 |
6.26e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 87.92 E-value: 6.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 424
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90
....*....|....*....
gi 1207141724 425 ED-VDVPHPDEKSIITYVS 442
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLC 98
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1329-2143 |
7.22e-20 |
|
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: 98.89 E-value: 7.22e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1329 NEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQavfAQIELRQR 1408
Cdd:pfam02463 175 LKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQ---ELLRDEQE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1409 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1488
Cdd:pfam02463 252 EIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELK 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1489 dyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDE-----------EK 1557
Cdd:pfam02463 332 --KEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEElelkseeekeaQL 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1558 AAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQdvavdSEKQKHNIQRELQELKTLS 1637
Cdd:pfam02463 410 LLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDEL-----ELKKSEDLLKETQLVKLQE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1638 EQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR-KQVAEETQ 1716
Cdd:pfam02463 485 QLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAtADEVEERQ 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1717 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTAR 1796
Cdd:pfam02463 565 KLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAK 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1797 LEESLKNEQVMV---------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKktaaqEEA 1867
Cdd:pfam02463 645 ESGLRKGVSLEEglaeksevkASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLK-----LEA 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1868 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1947
Cdd:pfam02463 720 EELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQ 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1948 VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN-------------TEKSKQLLESEAAKMRELAEEATKLRSV 2014
Cdd:pfam02463 800 EEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELalelkeeqkleklAEEELERLEEEITKEELLQELLLKEEEL 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2015 AEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaEEEGYQRKVLEDQAAQHKQ 2094
Cdd:pfam02463 880 EEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPE--ELLLEEADEKEKEENNKEE 957
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 1207141724 2095 AIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 2143
Cdd:pfam02463 958 EEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKK 1006
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2273-2821 |
8.46e-20 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 98.47 E-value: 8.46e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2273 DKLKEEFEKAKK---LAQEAEKAK--------DNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKE 2341
Cdd:COG1196 203 EPLERQAEKAERyreLKEELKELEaellllklRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELE 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2342 ASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ 2421
Cdd:COG1196 283 LEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAE 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2422 VEDELSKVKIQMEDLLKLKLKIEKENQELMkKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQR 2501
Cdd:COG1196 363 AEEALLEAEAELAEAEEELEELAEELLEAL-RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2502 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDqetegfqksLEAERKRQLEITAEAEKL 2581
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLL---------LLLEAEADYEGFLEGVKA 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2582 KVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEAdglhKAIADLEKEKEKLKKE 2661
Cdd:COG1196 513 ALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAG----RATFLPLDKIRARAAL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2662 AADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEER 2741
Cdd:COG1196 589 AAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRR 668
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2742 KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEEL 2821
Cdd:COG1196 669 ELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELL 748
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1547-2434 |
1.25e-19 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 97.97 E-value: 1.25e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1547 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK---------QKQLAETHAKAIAKAEQEANELKTKMKDEVSK------ 1611
Cdd:NF041483 313 EIARLVGEATKEAEALKAEAEQALADARAEAEKlvaeaaekaRTVAAEDTAAQLAKAARTAEEVLTKASEDAKAttraaa 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1612 ------RQDVAVDSEK---QKHNIQRELQELKTLSEQEIKAKSQQV-EEALLSRTRIEE-------EIHIIRLQLETTMK 1674
Cdd:NF041483 393 eeaeriRREAEAEADRlrgEAADQAEQLKGAAKDDTKEYRAKTVELqEEARRLRGEAEQlraeavaEGERIRGEARREAV 472
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1675 QK-----NTAEtELLQlRAKAvDADKLRNAAQEEAEKLRKQVAEE-TQKKRKAEEELKRKSEAEKDAAKEKKKALedlEK 1748
Cdd:NF041483 473 QQieeaaRTAE-ELLT-KAKA-DADELRSTATAESERVRTEAIERaTTLRRQAEETLERTRAEAERLRAEAEEQA---EE 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1749 FKLQAEEAERHLKQaELEK---QRQIQVVEEVAKK--TAATQLESKQVALT-ARLE-ESLKNEQVmviqlqEEAEHLKKQ 1821
Cdd:NF041483 547 VRAAAERAARELRE-ETERaiaARQAEAAEELTRLhtEAEERLTAAEEALAdARAEaERIRREAA------EETERLRTE 619
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1822 QAEADKA-REQAEKELETWRQKA------------NEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKR------- 1881
Cdd:NF041483 620 AAERIRTlQAQAEQEAERLRTEAaadasaaraegeNVAVRLRSEAAAEAERLKSEAQESADRVRAEAAAAAERvgteaae 699
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1882 --AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELI---RLRADFEHAEQQRTVldDELQRLKNDVNSAVKQ-- 1954
Cdd:NF041483 700 alAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRKRVEEAQAEAQRLV--EEADRRATELVSAAEQta 777
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1955 ----------KKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLESEAAKMRELA-EEATKLRSVA-EEAKKQR 2022
Cdd:NF041483 778 qqvrdsvaglQEQAEEEIAGLRSAAE-------HAAERTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAK 850
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2023 QIAEEEAARQRAEAEKILKEkltAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGyqRKVLEDQAAQHKQAIEEKIGQ 2102
Cdd:NF041483 851 ALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADAREDA--NRIRSDAAAQADRLIGEATSE 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2103 LKKSSDTELDRQKKIVEETLKQRKvveeeihilKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLAl 2182
Cdd:NF041483 926 AERLTAEARAEAERLRDEARAEAE---------RVRADAAAQAEQLIAEATGEAERLRAEAAETVGSAQQHAERIRTEA- 995
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2183 eeekkrkeaeakvKQIQA-AEEEAARQHKAAQEEVGRLMKLAEE--AKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQ 2259
Cdd:NF041483 996 -------------ERVKAeAAAEAERLRTEAREEADRTLDEARKdaNKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2260 NVLV--QQNKDSMAQDKLKEefekAKKLAQEA--------EKAKDNAE-------KEAALLHKKAEEAeRQKKAAEAEAA 2322
Cdd:NF041483 1063 RTTTeaEAQADTMVGAARKE----AERIVAEAtvegnslvEKARTDADellvgarRDATAIRERAEEL-RDRITGEIEEL 1137
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2323 KQAKAQEDAEKLRKEAEK-------EASRRAEAEAAALKLKQEADSEMAKYK----KLAEKTLKQKSSVEEELVKvkvql 2391
Cdd:NF041483 1138 HERARRESAEQMKSAGERcdalvkaAEEQLAEAEAKAKELVSDANSEASKVRiaavKKAEGLLKEAEQKKAELVR----- 1212
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*..
gi 1207141724 2392 dETDKQKSVLDVELKRL----KQEVSDAIKQKAQVEDELSKVKIQME 2434
Cdd:NF041483 1213 -EAEKIKAEAEAEAKRTveegKRELDVLVRRREDINAEISRVQDVLE 1258
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
345-445 |
2.69e-19 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 85.86 E-value: 2.69e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDP 424
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 1207141724 425 EDVDV--PHPDEKSIITYVSSMY 445
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
230-330 |
3.54e-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: 85.71 E-value: 3.54e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 230 QKKTFTKWVNKHLVKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPREKGR--MRFHKLQNVQIALDFLKHRQVKLVN 305
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 1207141724 306 IRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
345-441 |
4.14e-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: 85.67 E-value: 4.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERdLGVTRLLDP 424
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90
....*....|....*...
gi 1207141724 425 ED-VDVPHPDEKSIITYV 441
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYL 97
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
341-448 |
4.62e-19 |
|
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: 85.38 E-value: 4.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 341 SDDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTR 420
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*....
gi 1207141724 421 LLDPEDV-DVPHPDEKSIITYVSSMYDVM 448
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYEMF 109
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
348-444 |
5.66e-19 |
|
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: 85.06 E-value: 5.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 348 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN----LENLEQAFSIAERDLGVTRLLD 423
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 1207141724 424 PEDVDVPHPDEKSIITYVSSM 444
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1330-1975 |
9.93e-19 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 95.12 E-value: 9.93e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1330 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRE 1409
Cdd:TIGR02168 315 ERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ 394
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1410 LDLLNRQMQAYRE----SYDWLIRWIADAKQRQDKLHAVPIggsKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYID 1485
Cdd:TIGR02168 395 IASLNNEIERLEArlerLEDRRERLQQEIEELLKKLEEAEL---KELQAELEELEEELEELQEELERLEEALEELREELE 471
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1486 ----AIKDYELQLVTYKALV--------------EPIASPLKKAKMESASDDIIQEYVTLRTRYS------------ELM 1535
Cdd:TIGR02168 472 eaeqALDAAERELAQLQARLdslerlqenlegfsEGVKALLKNQSGLSGILGVLSELISVDEGYEaaieaalggrlqAVV 551
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1536 TLSSQYIKFIIETQRRlQDEEKAA-----EKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAE--------------- 1595
Cdd:TIGR02168 552 VENLNAAKKAIAFLKQ-NELGRVTflpldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRkalsyllggvlvvdd 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1596 -QEANELKTKMK----------DEVSKRQDVAVDSEKQKHNIQ------RELQELKTLSEQEIKAKSQQVEEALLSRTRI 1658
Cdd:TIGR02168 631 lDNALELAKKLRpgyrivtldgDLVRPGGVITGGSAKTNSSILerrreiEELEEKIEELEEKIAELEKALAELRKELEEL 710
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1659 EEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE 1738
Cdd:TIGR02168 711 EEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ 790
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1739 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT--------ARLEESLKNEQVMVIQ 1810
Cdd:TIGR02168 791 IEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQieelsediESLAAEIEELEELIEE 870
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1811 LQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTaaqeeaekQKEEAKREAKKRAKAEEAALK 1890
Cdd:TIGR02168 871 LESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELR--------EKLAQLELRLEGLEVRIDNLQ 942
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1891 QK--EAAEMELGNQRKMAEETAKQKLAAEQELIRLR--------------ADFEHAEQQRtvldDELQRLKNDVNSAVKQ 1954
Cdd:TIGR02168 943 ERlsEEYSLTLEEAEALENKIEDDEEEARRRLKRLEnkikelgpvnlaaiEEYEELKERY----DFLTAQKEDLTEAKET 1018
|
730 740
....*....|....*....|.
gi 1207141724 1955 kkeLEEELIKVRKEMEILLQQ 1975
Cdd:TIGR02168 1019 ---LEEAIEEIDREARERFKD 1036
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1711-2585 |
1.07e-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: 94.75 E-value: 1.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1711 VAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-QAELEKQRQIQVVEEvaKKTAATQLESK 1789
Cdd:TIGR02169 165 VAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQAlLKEKREYEGYELLKE--KEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1790 QVALtARLEESLKneqvmviQLQEEAEHLKKQQAEADKAREQAEKELEtwRQKANEALRLRLQAEEEANKKTAAQEEAEK 1869
Cdd:TIGR02169 243 ERQL-ASLEEELE-------KLTEEISELEKRLEEIEQLLEELNKKIK--DLGEEEQLRVKEKIGELEAEIASLERSIAE 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1870 QKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1949
Cdd:TIGR02169 313 KERELEDAEERLAKLEAEIDKLLAEIE----ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1950 SAVKQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATklrSVAEEAKKQRQIAEEEA 2029
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEELQRLSEEL----ADLNAAIAGIEAKINELEEEKE---DKALEIKKQEWKLEQLA 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2030 ArQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ--------------AAQHKQA 2095
Cdd:TIGR02169 462 A-DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASiqgvhgtvaqlgsvGERYATA 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2096 IEEKIGQLKKS--SDTELDRQKKIveETLKQRKVveEEIHILKLNfEKASSGKQELELELKKLKGIA-------DETQKS 2166
Cdd:TIGR02169 541 IEVAAGNRLNNvvVEDDAVAKEAI--ELLKRRKA--GRATFLPLN-KMRDERRDLSILSEDGVIGFAvdlvefdPKYEPA 615
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2167 KAKAEEEAEKFRKLALEEEKKRK-----------EAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEK 2235
Cdd:TIGR02169 616 FKYVFGDTLVVEDIEAARRLMGKyrmvtlegelfEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKRELSSLQS 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2236 EAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkk 2315
Cdd:TIGR02169 696 ELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE--- 772
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2316 aaeaeaakqakaqeDAEKLRKEAEKEASRraeaeaaalklkqEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETD 2395
Cdd:TIGR02169 773 --------------DLHKLEEALNDLEAR-------------LSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLT 825
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2396 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnMKKLAEE 2475
Cdd:TIGR02169 826 LEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ-LRELERK 904
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2476 AARLNIEAQEA-ARLRQIAESDLAKQRELAEkmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-------LEAKK 2547
Cdd:TIGR02169 905 IEELEAQIEKKrKRLSELKAKLEALEEELSE--IEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALepvnmlaIQEYE 982
|
890 900 910
....*....|....*....|....*....|....*...
gi 1207141724 2548 EMQQRLDqETEGFQKSLEAERKRQLEITAEAEKLKVKV 2585
Cdd:TIGR02169 983 EVLKRLD-ELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
231-328 |
1.60e-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: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 231 KKTFTKWVNKHL-VKAQRHITDLYEDLRDGHNLISLLEVLSGETLPRE--KGRMRFHKLQNVQIALDFLKHRQV-KLVNI 306
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 1207141724 307 RNDDI-ADGNPKLTLGLIWTIIL 328
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1987-2650 |
3.47e-17 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 89.61 E-value: 3.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1987 TEKSKQL--LESEAAKmrelAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLtainEATRLKTEAEIALKEK 2064
Cdd:COG1196 196 GELERQLepLERQAEK----AERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2065 EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKigqlkkssdtELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS 2144
Cdd:COG1196 268 ELEELRLELEELELELEEAQAEEYELLAELARLEQ----------DIARLEERRRELEERLEELEEELAELEEELEELEE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2145 GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAE 2224
Cdd:COG1196 338 ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2225 EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLH 2304
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2305 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEEL 2384
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2385 vkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVkIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2464
Cdd:COG1196 578 -----PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV-LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTL 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2465 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLE 2544
Cdd:COG1196 652 EGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLE 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2545 AKKEMQQRLDQETEGFqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSK-------AEEEAkkfkkqaDEIKIRLQEte 2617
Cdd:COG1196 732 AEREELLEELLEEEEL---LEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEY-------EELEERYDF-- 799
|
650 660 670
....*....|....*....|....*....|...
gi 1207141724 2618 khtsekhtvvekLEVQRLQSKQEADGLHKAIAD 2650
Cdd:COG1196 800 ------------LSEQREDLEEARETLEEAIEE 820
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1876-2796 |
3.58e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 89.73 E-value: 3.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1876 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFEHAE-----QQRTVLDDELQRLKNDVNS 1950
Cdd:TIGR02168 175 KETERKLERTRENLDRLEDILNELERQLKSLERQAEKA----ERYKELKAELRELElallvLRLEELREELEELQEELKE 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1951 AVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqlLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 2030
Cdd:TIGR02168 251 AEEELEELTAELQELEEKLEELRLEVSELEEE-----------IEELQKELYALANEISRLEQQKQILRERLANLERQLE 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2031 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEgyqrkvleDQAAQHKQAIEEKIGQLKKssdtE 2110
Cdd:TIGR02168 320 ELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAEL--------EELESRLEELEEQLETLRS----K 387
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2111 LDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELElelkklkgiadetqkskakaeeeaekfRKLALEEEKKRKE 2190
Cdd:TIGR02168 388 VAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL---------------------------KKLEEAELKELQA 440
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2191 AEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSM 2270
Cdd:TIGR02168 441 ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2271 AQDKLKEEFEKAKKLAQEAEKA-----------KDNAEKEAALLHKKAEE-----------AERQKKAAEAEAAKQAKAQ 2328
Cdd:TIGR02168 521 ILGVLSELISVDEGYEAAIEAAlggrlqavvveNLNAAKKAIAFLKQNELgrvtflpldsiKGTEIQGNDREILKNIEGF 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2329 EDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKqkSSVEEELVKVK-VQLDETDKQKSVL---DVE 2404
Cdd:TIGR02168 601 LGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRI--VTLDGDLVRPGgVITGGSAKTNSSIlerRRE 678
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2405 LKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ 2484
Cdd:TIGR02168 679 IEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE-LSRQISALRKDLARLEAEVEQLEERIAQLSKELT 757
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2485 EAARLRQIAESDLAKQRElaekmleEKKQAIQEAAKLKAEAEKLQKQKDQ---AQVEAQKLLEAKKEMQQRLDQETEGFQ 2561
Cdd:TIGR02168 758 ELEAEIEELEERLEEAEE-------ELAEAEAEIEELEAQIEQLKEELKAlreALDELRAELTLLNEEAANLRERLESLE 830
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2562 KSLEAERKRQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQR 2634
Cdd:TIGR02168 831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEeleelieELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2635 LQSKQEADGLHKAIADlekekeklkkeaadlqkqskemANVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklek 2714
Cdd:TIGR02168 911 SELRRELEELREKLAQ----------------------LELRLEGLEVRIDNLQERLSEEYSLTLEE------------- 955
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2715 qFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2794
Cdd:TIGR02168 956 -AEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEIDREARERF 1034
|
..
gi 1207141724 2795 QQ 2796
Cdd:TIGR02168 1035 KD 1036
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
349-447 |
3.91e-17 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a nuclear [F-actin]-monooxygenase that promotes depolymerization of F-actin by mediating oxidation of specific methionine residues on actin to form methionine-sulfoxide, resulting in actin filament disassembly and preventing repolymerization. In the absence of actin, it also functions as a NADPH oxidase producing H(2)O(2). MICAL-2 acts as a key regulator of the serum response factor (SRF) signaling pathway elicited by nerve growth factor and serum. It mediates oxidation and subsequent depolymerization of nuclear actin, leading to the increased MKL1/MRTF-A presence in the nucleus, promoting SRF:MKL1/MRTF-A-dependent gene transcription. MICAL-2 contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409099 [Multi-domain] Cd Length: 110 Bit Score: 79.92 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 349 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLD-PEDV 427
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90 100
....*....|....*....|
gi 1207141724 428 DVPHPDEKSIITYVSSMYDV 447
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYEL 107
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1518-2298 |
3.99e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 89.73 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1518 DDIIQEyvtLRTRYSELMTLSSQYIKFiietqRRLQDEEKAAE-----KLKEEERKKMAEMQAELEKQKQLAETHAKAIA 1592
Cdd:TIGR02168 192 EDILNE---LERQLKSLERQAEKAERY-----KELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQ 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1593 KAEQEANELKTKMKdEVSKRQDVavdsekqkhnIQRELQELKtlseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETT 1672
Cdd:TIGR02168 264 ELEEKLEELRLEVS-ELEEEIEE----------LQKELYALA----NEISRLEQQKQILRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1673 MKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKekkkaleDLEKFKLQ 1752
Cdd:TIGR02168 329 ESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL-------QIASLNNE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1753 AEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALtARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA 1832
Cdd:TIGR02168 402 IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAEL-EELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1833 EKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKR----------------------------EAKKRAKA 1884
Cdd:TIGR02168 481 ERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVlselisvdegyeaaieaalggrlqavvvENLNAAKK 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1885 EEAALKQKE---AAEMELGNQRKMAEETAKQKLAAEQELIRLRADF--EHAEQQRTVLDDELQRLK--NDVNSAVKQKKE 1957
Cdd:TIGR02168 561 AIAFLKQNElgrVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDlvKFDPKLRKALSYLLGGVLvvDDLDNALELAKK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1958 LEEE---------------------------LIKVRKEMEILLQQKSKAEketmSNTEKSKQLLESEAAKMRELAEEATK 2010
Cdd:TIGR02168 641 LRPGyrivtldgdlvrpggvitggsaktnssILERRREIEELEEKIEELE----EKIAELEKALAELRKELEELEEELEQ 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2011 LRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAA 2090
Cdd:TIGR02168 717 LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKE 796
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2091 QHKQAIEE----------------KIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELK 2154
Cdd:TIGR02168 797 ELKALREAldelraeltllneeaaNLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELE 876
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2155 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEA-ARQHKAAQEEVGRLMKLAEEAKKQKEIA 2233
Cdd:TIGR02168 877 ALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLeLRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2234 EKEAEKQVILVQEAAQKCSAAEQKAQNvLVQQNKDSMAQ-DKLKEEFEKAKKLAQEAEKAKDNAEK 2298
Cdd:TIGR02168 957 EALENKIEDDEEEARRRLKRLENKIKE-LGPVNLAAIEEyEELKERYDFLTAQKEDLTEAKETLEE 1021
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1315-2130 |
4.97e-17 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 89.35 E-value: 4.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1315 KYENQLREVnKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRE 1394
Cdd:TIGR02168 217 ELKAELREL-ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1395 RWQAVFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLhavpiggskglQEQLTQEKKLLEEIEKNkdkVE 1474
Cdd:TIGR02168 296 EISRLEQQKQILRERLANLERQLEELEAQ-------LEELESKLDEL-----------AEELAELEEKLEELKEE---LE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1475 DCQKFAKGYIDAIKDYELQLVTykalvepiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQyIKFIIETQRRLQD 1554
Cdd:TIGR02168 355 SLEAELEELEAELEELESRLEE------------LEEQLETLRSKVAQLELQIASLNNEIERLEAR-LERLEDRRERLQQ 421
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1555 EEKAAEKLKEEERkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQELK 1634
Cdd:TIGR02168 422 EIEELLKKLEEAE--LKELQAELEELEEELEELQEELERLEEALEELR----EELEEAEQALDAAERELAQLQARLDSLE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1635 TLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETeLLQLRAKAV-----DADKLRNAAQEEAEKLRK 1709
Cdd:TIGR02168 496 RL-QENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEA-ALGGRLQAVvvenlNAAKKAIAFLKQNELGRV 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1710 QVAEETQKKrkaEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA--------------ERHLKQAELEKQRQIQVVE 1775
Cdd:TIGR02168 574 TFLPLDSIK---GTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKAlsyllggvlvvddlDNALELAKKLRPGYRIVTL 650
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1776 E---VAKKTAATQLESKQVALT-------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1845
Cdd:TIGR02168 651 DgdlVRPGGVITGGSAKTNSSIlerrreiEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA 730
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1846 A----LRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEE---AALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1918
Cdd:TIGR02168 731 LrkdlARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEelaEAEAEIEELEAQIEQLKEELKALREALDELRA 810
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1919 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA 1998
Cdd:TIGR02168 811 ELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALA 890
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1999 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALkeKEAENDRLKRKAEEE 2078
Cdd:TIGR02168 891 LLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTL--EEAEALENKIEDDEE 968
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2079 GYQRKVledqaAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEE 2130
Cdd:TIGR02168 969 EARRRL-----KRLENKIKE-LGPVNLAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1883-2820 |
6.90e-17 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 89.08 E-value: 6.90e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1883 KAEEAALK-QKEAAEMELGNQRKMAEETAKQ-KLAAEQELirlradFEHAEQQRTVL---DDELQRLKNDVNSAVKQKKE 1957
Cdd:pfam01576 16 KVKERQQKaESELKELEKKHQQLCEEKNALQeQLQAETEL------CAEAEEMRARLaarKQELEEILHELESRLEEEEE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1958 LEEELIKVRKEMeillQQKSKAEKETMSNTEKSKQLLESEA----AKMRELAEEATKLRSVAEEAKKQRQIAEE---EAA 2030
Cdd:pfam01576 90 RSQQLQNEKKKM----QQHIQDLEEQLDEEEAARQKLQLEKvtteAKIKKLEEDILLLEDQNSKLSKERKLLEErisEFT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2031 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEA---ENDRLKRKAEEEGYQrkvLEDQAAQHKQAIEEKIGQLKKSS 2107
Cdd:pfam01576 166 SNLAEEEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqELEKAKRKLEGESTD---LQEQIAELQAQIAELRAQLAKKE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2108 DTELDRQKKIVEETLK----QRKVVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQkskakaeeeaekfrklALE 2183
Cdd:pfam01576 243 EELQAALARLEEETAQknnaLKKIRELEAQISELQ-EDLESERAARNKAEKQRRDLGEELE----------------ALK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2184 eekkrkeaeakvkqiqaAEEEAARQHKAAQEEVgrlmklaeEAKKQKEIAEkeaekqvilvqeaAQKCSAAEQKAQNVLV 2263
Cdd:pfam01576 306 -----------------TELEDTLDTTAAQQEL--------RSKREQEVTE-------------LKKALEEETRSHEAQL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2264 QQ--NKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK-------AEEAERQKKAAEAEAAKQAKAQEDAEKL 2334
Cdd:pfam01576 348 QEmrQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlqqaKQDSEHKRKKLEGQLQELQARLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2335 RKEAEKEASRRAEAEAAALKLKQEADSEmakykklAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD 2414
Cdd:pfam01576 428 RAELAEKLSKLQSELESVSSLLNEAEGK-------NIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2415 AIKQ-------KAQVEDELSKVKIQMEDLLKLKLKIEKENQEL------MKKDKDNTKKLLEEEAENMKKLAEEAARLNI 2481
Cdd:pfam01576 501 LQEQleeeeeaKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALeegkkrLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ 580
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2482 EAQEAA----RLRQIAeSDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQV----EAQKLLEAKKEM---- 2549
Cdd:pfam01576 581 ELDDLLvdldHQRQLV-SNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREKETRALslarALEEALEAKEELertn 659
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2550 -QQRLD---------------QETEGFQKSLEA---ERKRQLE------ITAEAEKLKVKVT----------QLSDAQSK 2594
Cdd:pfam01576 660 kQLRAEmedlvsskddvgknvHELERSKRALEQqveEMKTQLEeledelQATEDAKLRLEVNmqalkaqferDLQARDEQ 739
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2595 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2674
Cdd:pfam01576 740 GEEKRRQLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARA 819
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2675 VQQEQLQQEKTILQQSFFAEKETL-----LKKEKAIEEEKKKLEKQFEDEVKKAEALK-AEQERQRKL------MEEERK 2742
Cdd:pfam01576 820 SRDEILAQSKESEKKLKNLEAELLqlqedLAASERARRQAQQERDELADEIASGASGKsALQDEKRRLeariaqLEEELE 899
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2743 KLQSAMDAAIKKQKEAEE-------EMNGKQKEMQDLEKKRIEQEKllaeENKNLREKLQQLQSSQKASYTKEIEIQTDK 2815
Cdd:pfam01576 900 EEQSNTELLNDRLRKSTLqveqlttELAAERSTSQKSESARQQLER----QNKELKAKLQEMEGTVKSKFKSSIAALEAK 975
|
....*
gi 1207141724 2816 VPEEE 2820
Cdd:pfam01576 976 IAQLE 980
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
347-445 |
3.84e-16 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 77.34 E-value: 3.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 1207141724 427 -VDVPHPDEKSIITYVSSMY 445
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
227-326 |
8.44e-16 |
|
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: 76.42 E-value: 8.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 227 DRVQKKTFTKWVNKHLVKAQ-RHITDLYEDLRDGHNLISLLEVLSGETLPRE---KGRMRFHKLQNVQIALDFL-KHRQV 301
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIeEDLKI 81
|
90 100
....*....|....*....|....*
gi 1207141724 302 KLVNIRNDDIADGNPKLTLGLIWTI 326
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
347-446 |
1.03e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 75.77 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 1207141724 427 VDV--PHPDEKSIITYVSSMYD 446
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
814-1004 |
1.10e-15 |
|
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: 79.03 E-value: 1.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 814 QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAF 893
Cdd:cd00176 1 KLQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQER 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 894 TAALQTQWSWILQLCCCIETHLKENTAYFQFFSDVKEAEDRMKKMEDTMKKKYVCDrsiTVTRLEDLLQDAVEEKEQLNE 973
Cdd:cd00176 81 LEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEA 157
|
170 180 190
....*....|....*....|....*....|.
gi 1207141724 974 FKTHLEGLNRRAKTIIQLKPRNPAQPIKGKL 1004
Cdd:cd00176 158 HEPRLKSLNELAEELLEEGHPDADEEIEEKL 188
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1812-2785 |
1.54e-15 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 84.49 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1812 QEEAEHLKKQQAEADKAREQAEK----------ELETWRQKANEALR------------LRLQAEEEANKKTAAQEEAEK 1869
Cdd:NF041483 11 RADDDHLSRFEAEMDRLKTEREKavqhaedlgyQVEVLRAKLHEARRslasrpaydgadIGYQAEQLLRNAQIQADQLRA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1870 QKEEAKREAKKRAK------AEEAALKQKE----------AAEMELGNQRKMAEETAKQKLA--------AEQELIRL-- 1923
Cdd:NF041483 91 DAERELRDARAQTQrilqehAEHQARLQAElhteavqrrqQLDQELAERRQTVESHVNENVAwaeqlrarTESQARRLld 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1924 --RADFEH------AEQQRtVLDDELQRLKNDVNSAvkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTE--KSKQL 1993
Cdd:NF041483 171 esRAEAEQalaaarAEAER-LAEEARQRLGSEAESA---RAEAEAILRRARKDAERLLNAASTQAQEATDHAEqlRSSTA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1994 LESEAAKMR----------ELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE-------KILKEKLT-----AINEAT 2051
Cdd:NF041483 247 AESDQARRQaaelsraaeqRMQEAEEALREARAEAEKVVAEAKEAAAKQLASAEsaneqrtRTAKEEIArlvgeATKEAE 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2052 RLKTEAEIALKEKEAENDRLKRKAEEEGyQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEE 2131
Cdd:NF041483 327 ALKAEAEQALADARAEAEKLVAEAAEKA-RTVAAEDTAAQLAKAARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2132 IHilKLNFEKASSGKQelelelkkLKGIA-DETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQA-AEEEAARQ- 2208
Cdd:NF041483 406 AD--RLRGEAADQAEQ--------LKGAAkDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGeARREAVQQi 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2209 HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQKAQNVLvqqnkdsmaqDKLKEEFEKAKKLAQE 2288
Cdd:NF041483 476 EEAARTAEELLTKAKADADELRSTATAESER---VRTEAIERATTLRRQAEETL----------ERTRAEAERLRAEAEE 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2289 -AEKAKDNAEKEAALLHkkaEEAERqkkaaeAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAaalklkqEADSEMAKYK 2367
Cdd:NF041483 543 qAEEVRAAAERAARELR---EETER------AIAARQAEAAEELTRLHTEAEERLTAAEEALA-------DARAEAERIR 606
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2368 K-LAEKTLKQKSSVEEELVKVKVQLDEtdkqksvldvELKRLKQEVSdAIKQKAQVEDELSKVKIQMEdllklklkIEKE 2446
Cdd:NF041483 607 ReAAEETERLRTEAAERIRTLQAQAEQ----------EAERLRTEAA-ADASAARAEGENVAVRLRSE--------AAAE 667
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2447 NQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQ-EAARLRQIAESDLAKQRELAEkmlEEKKQAIQEAAKLKAEA 2525
Cdd:NF041483 668 AERLKSEAQESADRVRAEAAAAAERVGTEAAEALAAAQeEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA 744
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2526 eklQKQKDQAQVEAQKLLE------------AKKEMQQRLD----------QETEGFQKSLE--AERKRQlEITAEAEKL 2581
Cdd:NF041483 745 ---RKRVEEAQAEAQRLVEeadrratelvsaAEQTAQQVRDsvaglqeqaeEEIAGLRSAAEhaAERTRT-EAQEEADRV 820
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2582 KvkvtqlSDAQS---KAEEEAKKFKKQADEikirlqETE--KHTSEKhTVVEKL-EVQRLQSkQEADGLHKAIADLEKEK 2655
Cdd:NF041483 821 R------SDAYAereRASEDANRLRREAQE------ETEaaKALAER-TVSEAIaEAERLRS-DASEYAQRVRTEASDTL 886
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2656 EKLKKEAADLQKQSKEMANvqqeqlqqektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2735
Cdd:NF041483 887 ASAEQDAARTRADAREDAN------------RIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRAD 954
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2736 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQkemQDLEKKRIEQEKLLAE 2785
Cdd:NF041483 955 AAAQAEQLIAEATGEAERLRAEAAETVGSAQ---QHAERIRTEAERVKAE 1001
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
345-442 |
3.26e-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: 74.34 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-LENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCPDWETWDPNDaLENATEAMQLAEDWLGVPQLIT 77
|
90
....*....|....*....
gi 1207141724 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21230 78 PEEIINPNVDEMSVMTYLS 96
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2189-2749 |
3.36e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.45 E-value: 3.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2189 KEAEAKVKQIQAAEEEAARQHKAAQEEVGRLmkLAEEAKKQKEIAEKEAEKQVilvqeaaqkcsaAEQKAQNVLVQQNKD 2268
Cdd:COG1196 256 EELEAELAELEAELEELRLELEELELELEEA--QAEEYELLAELARLEQDIAR------------LEERRRELEERLEEL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2269 SMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEA 2348
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2349 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSK 2428
Cdd:COG1196 402 LEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2429 VKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKL------AEEAARLNIEAQEAARLRQIAESDLAKQRE 2502
Cdd:COG1196 482 LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAvavligVEAAYEAALEAALAAALQNIVVEDDEVAAA 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2503 LAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL-----LEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAE 2577
Cdd:COG1196 562 AIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVdlvasDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2578 AEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETekhtsekhtvvEKLEVQRLQSKQEADGLHKAIADLEKEKEK 2657
Cdd:COG1196 642 LAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAE-----------LEELAERLAEEELELEEALLAEEEEERELA 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2658 LKKEAADLQKQSKEMANVQQEQLQQEKTILQQsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-------------- 2723
Cdd:COG1196 711 EAEEERLEEELEEEALEEQLEAEREELLEELL----EEEELLEEEALEELPEPPDLEELERELERLereiealgpvnlla 786
|
570 580 590
....*....|....*....|....*....|...
gi 1207141724 2724 -EALKAEQER------QRKLMEEERKKLQSAMD 2749
Cdd:COG1196 787 iEEYEELEERydflseQREDLEEARETLEEAIE 819
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1309-1975 |
3.42e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.06 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1309 AEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkrmsqlhserdvELEHYRQL 1388
Cdd:COG1196 251 LEAELEELEAELAEL------EAELEELRLELEELELELEEAQAEEYELLAELARLEQ--------------DIARLEER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1389 VGNLRERwqavfaQIELRQRELDLLNRQMQAYREsydwLIRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK 1468
Cdd:COG1196 311 RRELEER------LEELEEELAELEEELEELEEE----LEELEEELEEAEEELEE--------AEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1469 NKDKVEdcqkfakgyidaikdyELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRyselmtlssqyikfIIET 1548
Cdd:COG1196 373 ELAEAE----------------EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLER--------------LEEE 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1549 QRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDvavdsEKQKHNIQR 1628
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-----AAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1629 ELQELKTLSEQEIKAKSQQVEEALLSRTrieeeihiIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1708
Cdd:COG1196 498 EAEADYEGFLEGVKAALLLAGLRGLAGA--------VAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAA 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1709 KQVAEEtqkkRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1788
Cdd:COG1196 570 KAGRAT----FLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1789 KQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1868
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1869 KQKEEAKREAKKRAKAEEAALKQKEAAEMELgnQRKMAEETAKQKLA-AEQELIRL-----RADFEHAEQQRTVldDELQ 1942
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEEL--PEPPDLEELERELErLEREIEALgpvnlLAIEEYEELEERY--DFLS 801
|
650 660 670
....*....|....*....|....*....|...
gi 1207141724 1943 RLKNDVNSAvkqKKELEEELIKVRKEMEILLQQ 1975
Cdd:COG1196 802 EQREDLEEA---RETLEEAIEEIDRETRERFLE 831
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1577-2512 |
5.32e-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: 82.79 E-value: 5.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1577 LEKQKQLAETHAKAIAKAEQEANELKT------KMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSE--QEIKAKSQQV 1648
Cdd:TIGR00606 188 LETLRQVRQTQGQKVQEHQMELKYLKQykekacEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKeiEHNLSKIMKL 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1649 EEALLSRTRIEEEIHIIRLQLETTMKQ--KNTAE--TELLQLRAKAV-DADKLRNAAQEEAEKLRKQVAEETQKKRKAEE 1723
Cdd:TIGR00606 268 DNEIKALKSRKKQMEKDNSELELKMEKvfQGTDEqlNDLYHNHQRTVrEKERELVDCQRELEKLNKERRLLNQEKTELLV 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1724 ELKRKSEAEKDAAKEKKKALEDLEKFKLQAE--------EAERHLKQA-ELEKQRQIQVVEEVAKKTA--ATQLESKQVA 1792
Cdd:TIGR00606 348 EQGRLQLQADRHQEHIRARDSLIQSLATRLEldgfergpFSERQIKNFhTLVIERQEDEAKTAAQLCAdlQSKERLKQEQ 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1793 LT------ARLEESLKNEQVMVIQLQEEAEHLKKQQAEAdkarEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEE 1866
Cdd:TIGR00606 428 ADeirdekKGLGRTIELKKEILEKKQEELKFVIKELQQL----EGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1867 AEKQKEEAKREAKKRAKAEEAALKQKEA---AEMELGNQRKMA--EETAKQKLAAEQELIRLRADFEHAEQqrtvLDDEL 1941
Cdd:TIGR00606 504 KSLQNEKADLDRKLRKLDQEMEQLNHHTttrTQMEMLTKDKMDkdEQIRKIKSRHSDELTSLLGYFPNKKQ----LEDWL 579
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1942 QRLKNDvnsavkqKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLES--EAAKMRELAEEATKLRSVAEEAK 2019
Cdd:TIGR00606 580 HSKSKE-------INQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfDVCGSQDEESDLERLKEEIEKSS 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2020 KQRQIAEEEAARQRAEAEKILKEKLTAINEATR-LKTEAEIALKEKEAENDRLKRKAEEEGyqrkvLEDQAAQHKQAIEE 2098
Cdd:TIGR00606 653 KQRAMLAGATAVYSQFITQLTDENQSCCPVCQRvFQTEAELQEFISDLQSKLRLAPDKLKS-----TESELKKKEKRRDE 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2099 KIGqLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2178
Cdd:TIGR00606 728 MLG-LAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVER 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2179 KLA-LEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKqviLVQEAAQKCSAAEQK 2257
Cdd:TIGR00606 807 KIAqQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNE---LKSEKLQIGTNLQRR 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2258 AQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEaerqkkaaeaeaakqakaqedaeklRKE 2337
Cdd:TIGR00606 884 QQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETS-------------------------NKK 938
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2338 AEKEASRRAEaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2417
Cdd:TIGR00606 939 AQDKVNDIKE------KVKNIHGYMKDIENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKI 1012
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2418 QKAQVEDELSKVKIQMEdllklklkIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAArlNIEAQEAARLRQIAESDl 2497
Cdd:TIGR00606 1013 QERWLQDNLTLRKRENE--------LKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENID--LIKRNHVLALGRQKGYE- 1081
|
970
....*....|....*
gi 1207141724 2498 aKQRELAEKMLEEKK 2512
Cdd:TIGR00606 1082 -KEIKHFKKELREPQ 1095
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
347-450 |
6.82e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 73.54 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 1207141724 427 VDV--PHPDEKSIITYVSSMYDVMPR 450
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4239-4277 |
7.83e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.82 E-value: 7.83e-15
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 4239 LLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEMNGIL 4277
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2274-2809 |
8.28e-15 |
|
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: 81.69 E-value: 8.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2274 KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASrraeaeaaal 2353
Cdd:pfam05483 216 KLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK--------------DLTFLLEESRDKAN---------- 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2354 KLKQEADSEMAKYKKLAEKtlkqKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQM 2433
Cdd:pfam05483 272 QLEEKTKLQDENLKELIEK----KDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAH 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2434 EDLLKLKLKIEKENQELMKKDKDNtkklLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQREL---AEKMLEE 2510
Cdd:pfam05483 348 SFVVTEFEATTCSLEELLRTEQQR----LEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKIlaeDEKLLDE 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2511 KKQAIQEAAKLKAEAEKL-----QKQKDQAQVEAQklLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKV 2585
Cdd:pfam05483 424 KKQFEKIAEELKGKEQELifllqAREKEIHDLEIQ--LTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2586 TQLSDAQS-------KAEEEAKKFKKQADEIKIR---LQETEKH-TSEKHTVVEKLEVQRLQ-------SKQEADGLHKA 2647
Cdd:pfam05483 502 KELTQEASdmtlelkKHQEDIINCKKQEERMLKQienLEEKEMNlRDELESVREEFIQKGDEvkckldkSEENARSIEYE 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2648 IADLEKEKEKLKKEAADLQKQSkEMANVQQEQLQQEKTILQQSFFAEKETLLK---KEKAIEEEKKKLEKQFEDEVKKAE 2724
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQI-ENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQ 660
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2725 ALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKN---LREKLQQLQSSQ 2801
Cdd:pfam05483 661 KEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEERDSelgLYKNKEQEQSSA 740
|
....*...
gi 1207141724 2802 KASYTKEI 2809
Cdd:pfam05483 741 KAALEIEL 748
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
347-445 |
9.12e-15 |
|
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: 73.58 E-value: 9.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|
gi 1207141724 427 -VDVPHPDEKSIITYVSSMY 445
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELY 102
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
230-330 |
1.10e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 72.72 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 230 QKKTFTKWVNKHLVK--AQRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMRfhklQNVQIALDFLKHRQV 301
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 1207141724 302 KLVNIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
350-445 |
1.10e-14 |
|
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: 73.16 E-value: 1.10e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 350 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDPED-VD 428
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 1207141724 429 VPHPDEKSIITYVSSMY 445
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1547-2642 |
1.24e-14 |
|
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: 81.37 E-value: 1.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1547 ETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKaEQEANELKTKMKDEVSKRQDVAVDSEKQKHNI 1626
Cdd:pfam01576 23 KAESELKELEKKHQQLCEEKNALQEQLQAETELCAEAEEMRARLAAR-KQELEEILHELESRLEEEEERSQQLQNEKKKM 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1627 QRELQELKT-LSEQEIKAKSQQVEEALLSRT--RIEEEIHIIRLQLETTMKQKNTAE-------TELLQLRAKAVDADKL 1696
Cdd:pfam01576 102 QQHIQDLEEqLDEEEAARQKLQLEKVTTEAKikKLEEDILLLEDQNSKLSKERKLLEeriseftSNLAEEEEKAKSLSKL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1697 RNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKkkaledLEKFKLQAEEAERHLKQAELEKQR-QIQVVE 1775
Cdd:pfam01576 182 KNKHEAMISDLEERLKKE-EKGRQELEKAKRKLEGESTDLQEQ------IAELQAQIAELRAQLAKKEEELQAaLARLEE 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1776 EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-------LQEEAEHLKKQ----------QAEADKAREQAEKELEt 1838
Cdd:pfam01576 255 ETAQKNNALKKIRELEAQISELQEDLESERAARNKaekqrrdLGEELEALKTEledtldttaaQQELRSKREQEVTELK- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1839 wRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKE--AAEMELGNQRKMAEETAKQKLaa 1916
Cdd:pfam01576 334 -KALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAelQAELRTLQQAKQDSEHKRKKL-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1917 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLles 1996
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNL--- 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1997 eAAKMRELAEEATKLRSVAEEAKKQRQIAEEE---AARQRAEAEKILKEKLTAINEATRLKTEAEialKEKEAENDRLKR 2073
Cdd:pfam01576 488 -STRLRQLEDERNSLQEQLEEEEEAKRNVERQlstLQAQLSDMKKKLEEDAGTLEALEEGKKRLQ---RELEALTQQLEE 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2074 KAEEegYQRkvLEDQAAQHKQAIEEKIgqlkkssdTELDRQKKIVEETLKQRKVVEEeihilKLNFEKASSGKqelelel 2153
Cdd:pfam01576 564 KAAA--YDK--LEKTKNRLQQELDDLL--------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISAR------- 619
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2154 kklkgIADETQKSKAKAEEEAEKFRKLAleeekkrkeaeAKVKQIQAAEEEAARQHKAAQEEVGRLM-------KLAEEA 2226
Cdd:pfam01576 620 -----YAEERDRAEAEAREKETRALSLA-----------RALEEALEAKEELERTNKQLRAEMEDLVsskddvgKNVHEL 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2227 KKQKEIAEKEAEKQVILVQEAAQKCSAAEQ------------KAQNVLVQQNKDSMAQDKLKEEFEKAKKLaqEAEKAKD 2294
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQATEDaklrlevnmqalKAQFERDLQARDEQGEEKRRQLVKQVREL--EAELEDE 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2295 NAEKEAALLHKKAEEAErqkkaaeaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTL 2374
Cdd:pfam01576 762 RKQRAQAVAAKKKLELD---------LKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESE 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2375 KQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenqelmkkd 2454
Cdd:pfam01576 833 KKLKNLEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQL------------------ 894
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2455 kdntKKLLEEEAENMKKLAEEAARLNIEAqEAARLRQIAESDLAKQRELAEKMLEEKKQAIQeaAKLkAEAEKLQKQKDQ 2534
Cdd:pfam01576 895 ----EEELEEEQSNTELLNDRLRKSTLQV-EQLTTELAAERSTSQKSESARQQLERQNKELK--AKL-QEMEGTVKSKFK 966
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2535 AQVEAqklLEAK-KEMQQRLDQETEGFQKSLEAERKRQleitaeaEKLKVKVTQLSDAQSKAEEeakkFKKQADEIKIRL 2613
Cdd:pfam01576 967 SSIAA---LEAKiAQLEEQLEQESRERQAANKLVRRTE-------KKLKEVLLQVEDERRHADQ----YKDQAEKGNSRM 1032
|
1130 1140
....*....|....*....|....*....
gi 1207141724 2614 QETEKHTSEKHTVVEKLEVQRLQSKQEAD 2642
Cdd:pfam01576 1033 KQLKRQLEEAEEEASRANAARRKLQRELD 1061
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2464-2824 |
2.21e-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: 2.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2464 EEAEnmKKLaeEAARLNIEaqeaaRL--------RQIAEsdLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQK 2532
Cdd:COG1196 175 EEAE--RKL--EATEENLE-----RLedilgeleRQLEP--LERQAEKAERYRElkeELKELEAELLLLKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2533 DQAQVEAQKLLEAKKEMQQRLDQETegfqksLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIR 2612
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAE------LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2613 LQETEKhtsekhtVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFF 2692
Cdd:COG1196 318 LEELEE-------ELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2693 AEKETLlkkekaieeekkklekqfedevkKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDL 2772
Cdd:COG1196 391 ALRAAA-----------------------ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2773 EKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQM 2824
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEA 499
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3260-3298 |
6.90e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 68.12 E-value: 6.90e-14
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 3260 LLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPELHEKL 3298
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
347-442 |
6.95e-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: 70.49 E-value: 6.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 347 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLDPE 425
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 1207141724 426 DVDVPHPDEKSIITYVS 442
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1330-2098 |
8.00e-14 |
|
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: 78.68 E-value: 8.00e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1330 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQR-ATEVNKRMSQLHSERDV--ELEHYRQLVGNLRERWQAVFAQIELR 1406
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQlCEEKNALQEQLQAETELcaEAEEMRARLAARKQELEEILHELESR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1407 QRELDLLNRQMQAYRESydwLIRWIADAKQRQDKLHAvpigGSKGLQ-EQLTQE---KKLLEEIEKNKDKVEDCQKFAKG 1482
Cdd:pfam01576 84 LEEEEERSQQLQNEKKK---MQQHIQDLEEQLDEEEA----ARQKLQlEKVTTEakiKKLEEDILLLEDQNSKLSKERKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1483 YIDAIKDYELQLvtykalvepiASPLKKAKMesasddiiqeyvtlrtryseLMTLSSQYIKFIIETQRRLQDEEK----- 1557
Cdd:pfam01576 157 LEERISEFTSNL----------AEEEEKAKS--------------------LSKLKNKHEAMISDLEERLKKEEKgrqel 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1558 -----AAEKLKEEERKKMAEMQAELEKQK-QLA---ETHAKAIAKAEQEAN-----------------ELKTKMKDEVSK 1611
Cdd:pfam01576 207 ekakrKLEGESTDLQEQIAELQAQIAELRaQLAkkeEELQAALARLEEETAqknnalkkireleaqisELQEDLESERAA 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1612 RQdvavDSEKQKHNIQRELQELKTLSE---------QEIKAKSQQvEEALLSRTrIEEEIHIIRLQLEtTMKQKNTAETE 1682
Cdd:pfam01576 287 RN----KAEKQRRDLGEELEALKTELEdtldttaaqQELRSKREQ-EVTELKKA-LEEETRSHEAQLQ-EMRQKHTQALE 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1683 -----LLQLRAKAVDADKLRNAAQEEAEKLRKQV-------AEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1750
Cdd:pfam01576 360 elteqLEQAKRNKANLEKAKQALESENAELQAELrtlqqakQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1751 LQAEEAERHLKQAElekQRQIQVVEEVAkkTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKARE 1830
Cdd:pfam01576 440 SELESVSSLLNEAE---GKNIKLSKDVS--SLESQLQDTQELLQEETRQKLNLST-RLRQLEDERNSLQEQLEEEEEAKR 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1831 QAEKELETWRQ------KANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK-EAAEMELGNQR 1903
Cdd:pfam01576 514 NVERQLSTLQAqlsdmkKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQElDDLLVDLDHQR 593
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1904 KMAEETAKQ-----KLAAEQELIRLRA--DFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1976
Cdd:pfam01576 594 QLVSNLEKKqkkfdQMLAEEKAISARYaeERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSK 673
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1977 SKAEKeTMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAK------------------KQRQIAEEEAARQRA---- 2034
Cdd:pfam01576 674 DDVGK-NVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKlrlevnmqalkaqferdlQARDEQGEEKRRQLVkqvr 752
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2035 EAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 2098
Cdd:pfam01576 753 ELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEE 816
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1288-2072 |
1.41e-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: 77.85 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1288 LSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNKVP-VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE 1366
Cdd:pfam15921 119 LQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKcLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSILVDFEE 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1367 VNKRmsQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYREsydwlirwiadakQRQDKLHAVpi 1446
Cdd:pfam15921 199 ASGK--KIYEHDSMSTMHFRSLGSAISKILRELDTEISYLKGRIFPVEDQLEALKS-------------ESQNKIELL-- 261
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1447 ggskglqeqltqekklleeIEKNKDKVEDCqkfakgyidaIKDYELQLVtykALVEPIASPLKKAKMESASDDIIQEYVT 1526
Cdd:pfam15921 262 -------------------LQQHQDRIEQL----------ISEHEVEIT---GLTEKASSARSQANSIQSQLEIIQEQAR 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1527 LRT-----RYSELMTLSSQYIKFIIETQRRLQDEEKaaeklkeeerkkmaemqaELEKQKQLAETHakaIAKAEQEANEL 1601
Cdd:pfam15921 310 NQNsmymrQLSDLESTVSQLRSELREAKRMYEDKIE------------------ELEKQLVLANSE---LTEARTERDQF 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1602 KTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIkAKSQQVEEalLSRTRIEEEIHIIRLQ-LETTMKQKNTAE 1680
Cdd:pfam15921 369 SQESGNLDDQLQKLLADLHKREKELSLEKEQNKRLWDRDT-GNSITIDH--LRRELDDRNMEVQRLEaLLKAMKSECQGQ 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1681 TEllqlraKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlekfKLQAEEAER-- 1758
Cdd:pfam15921 446 ME------RQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELTAK---------------------KMTLESSERtv 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1759 -HLKQAELEKQRQIQvveevAKKTAATQLESKqVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELE 1837
Cdd:pfam15921 499 sDLTASLQEKERAIE-----ATNAEITKLRSR-VDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1838 TWRQKANEALRL-------RLQAEEEANKKtaAQEEAEKQKEEAKREAKKRA-KAEEAALKQKEAAEMELGNQRKMAEET 1909
Cdd:pfam15921 573 NMTQLVGQHGRTagamqveKAQLEKEINDR--RLELQEFKILKDKKDAKIRElEARVSDLELEKVKLVNAGSERLRAVKD 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1910 AKQKL--------AAEQELIRLRADFE--------HAEQQRTVLD----------DELQRLKNDVNS-------AVKQKK 1956
Cdd:pfam15921 651 IKQERdqllnevkTSRNELNSLSEDYEvlkrnfrnKSEEMETTTNklkmqlksaqSELEQTRNTLKSmegsdghAMKVAM 730
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1957 ELEEELIKVRKEMEIlLQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatKLRSVAEEakKQRQIAEEEAARQRaea 2036
Cdd:pfam15921 731 GMQKQITAKRGQIDA-LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ------ELSTVATE--KNKMAGELEVLRSQ--- 798
|
810 820 830 840
....*....|....*....|....*....|....*....|
gi 1207141724 2037 EKILKEKLT----AINEATRLKTEAEIALKEKEAENDRLK 2072
Cdd:pfam15921 799 ERRLKEKVAnmevALDKASLQFAECQDIIQRQEQESVRLK 838
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
223-329 |
1.71e-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: 69.62 E-value: 1.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 223 ADERDrvqKKTFTKWVNKHLVKAQrhITDLYEDLRDGhnlISLLEVL--------SGETLPREKGRMRFHKLQNVQIALD 294
Cdd:cd21219 1 EGSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVLdkiqpgcvNWKKVNKPKPLNKFKKVENCNYAVD 72
|
90 100 110
....*....|....*....|....*....|....*
gi 1207141724 295 FLKHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 329
Cdd:cd21219 73 LAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
345-445 |
2.61e-13 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 69.33 E-value: 2.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 424
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 1207141724 425 ED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1381-2079 |
2.92e-13 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 76.93 E-value: 2.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1381 ELEHYRQLVGNLRERWQAVFAQIELRQRELDLL----NRQMQAYRESYDWLIRWIADAKQRQDKLhavpiggsKGLQEQL 1456
Cdd:TIGR00618 174 PLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLtlctPCMPDTYHERKQVLEKELKHLREALQQT--------QQSHAYL 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1457 TQEKKLLEEIEKNkdkvedcQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDIIQ-------EYVTLRT 1529
Cdd:TIGR00618 246 TQKREAQEEQLKK-------QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQieqqaqrIHTELQS 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1530 RYSELMTLSSQYIKFI-----IETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAEtHAKAIAKAEQEANELKTK 1604
Cdd:TIGR00618 319 KMRSRAKLLMKRAAHVkqqssIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQS 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1605 MKDEVSKRQDVAVDSEKQkHNIQRELQELKTLSEQEIKAksqQVEEALLSRTRIEEE--IHIIRLQLETTMKQKNTAETE 1682
Cdd:TIGR00618 398 LCKELDILQREQATIDTR-TSAFRDLQGQLAHAKKQQEL---QQRYAELCAAAITCTaqCEKLEKIHLQESAQSLKEREQ 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1683 LLQLRAKAVDADKlRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQ 1762
Cdd:TIGR00618 474 QLQTKEQIHLQET-RKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLT 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1763 AELEkqrQIQVVEEvaKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEhlKKQQAEADKAREQAEKELETWRQK 1842
Cdd:TIGR00618 553 SERK---QRASLKE--QMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTE--KLSEAEDMLACEQHALLRKLQPEQ 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1843 ANEALRLRLQ--AEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1920
Cdd:TIGR00618 626 DLQDVRLHLQqcSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTL 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1921 IR-----LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLE 1995
Cdd:TIGR00618 706 LRelethIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAA 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1996 SEAAKMRELAEEATKLRSVAEEAKKQ-------RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEN 2068
Cdd:TIGR00618 786 EIQFFNRLREEDTHLLKTLEAEIGQEipsdediLNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLT 865
|
730
....*....|.
gi 1207141724 2069 DRLKRKAEEEG 2079
Cdd:TIGR00618 866 QEQAKIIQLSD 876
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2041-2839 |
3.03e-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: 77.02 E-value: 3.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2041 KEKLTAINEA---TRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvLEDqaaqhkqAIEEKIGQLKKssdteLDRQKKI 2117
Cdd:TIGR02168 155 EERRAIFEEAagiSKYKERRKETERKLERTRENLDR-----------LED-------ILNELERQLKS-----LERQAEK 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2118 VEETLKQRKVVEE-EIHILKLNFEKASSGKQELELELKKLKGIADETQKskakaeeeaekfrklaleeekkrkeaeaKVK 2196
Cdd:TIGR02168 212 AERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEELEELTA----------------------------ELQ 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2197 QIQAAEEEAARQHKAAQEEVGRLMKLAEEAKkqKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmaqDKLK 2276
Cdd:TIGR02168 264 ELEEKLEELRLEVSELEEEIEELQKELYALA--NEISRLEQQKQILRERLANLERQLEELEAQLEELESKL-----DELA 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2277 EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEK----LRKEAEKEASRRAEAEAAA 2352
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELqiasLNNEIERLEARLERLEDRR 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2353 LKLKQEADSEMAKYKKLAEKTLKQK-SSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKI 2431
Cdd:TIGR02168 417 ERLQQEIEELLKKLEEAELKELQAElEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2432 QME--DLLKLKLKIEKENQELMKKDKDNTKKLLEEEA-----------ENMKKLA---EEAARLNIEAQEAARL--RQIA 2493
Cdd:TIGR02168 497 LQEnlEGFSEGVKALLKNQSGLSGILGVLSELISVDEgyeaaieaalgGRLQAVVvenLNAAKKAIAFLKQNELgrVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2494 ESDLAKQRELAEKMLEEKK-------------------------------------QAIQEAAKL--------------- 2521
Cdd:TIGR02168 577 PLDSIKGTEIQGNDREILKniegflgvakdlvkfdpklrkalsyllggvlvvddldNALELAKKLrpgyrivtldgdlvr 656
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2522 -------------------KAEAEKLQKQKDQAQV---EAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAE 2579
Cdd:TIGR02168 657 pggvitggsaktnssilerRREIEELEEKIEELEEkiaELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2580 KLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEkekeklk 2659
Cdd:TIGR02168 737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELR------- 809
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2660 keaADLQKQSKEMANVQQEQLQQEKTIlqqsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEE 2739
Cdd:TIGR02168 810 ---AELTLLNEEAANLRERLESLERRI------AATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2740 ERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEenknLREKLQQLQSsqkasytkEIEIQTDKVPEE 2819
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ----LELRLEGLEV--------RIDNLQERLSEE 948
|
890 900
....*....|....*....|
gi 1207141724 2820 ELVQMTMVETTKKVLNGSTE 2839
Cdd:TIGR02168 949 YSLTLEEAEALENKIEDDEE 968
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3920-3958 |
3.66e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 3.66e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 3920 LLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEFHDKL 3958
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2933-2971 |
4.12e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 4.12e-13
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 2933 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPELHTKL 2971
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
248-327 |
4.95e-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: 68.39 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 248 HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM----RFHKLQNVQIALDFLKHRQV----KLVNIRNDDIADGNPKLT 319
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 1207141724 320 LGLIWTII 327
Cdd:cd21223 105 LALLWRII 112
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
232-333 |
9.23e-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: 67.65 E-value: 9.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 232 KTFTKWVNKHLVKAqrHITDLYEDLRDGHNLISLLEVL-------SGETLPREKGRMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21298 9 KTYRNWMNSLGVNP--FVNHLYSDLRDGLVLLQLYDKIkpgvvdwSRVNKPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1823-2610 |
1.05e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.10 E-value: 1.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1823 AEADKAREQAEKELETWRQKANealRLRLQAEEEANKktaaqeeaekqkeeAKREAKKRAKAEEAALKQKEAAEMELGNQ 1902
Cdd:TIGR02169 166 AEFDRKKEKALEELEEVEENIE---RLDLIIDEKRQQ--------------LERLRREREKAERYQALLKEKREYEGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1903 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRKEMEILLQQKSKAEK 1981
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1982 ETMSNTEKSKQLLESEA---AKMRELAEEATKL-RSVAEEAKKQRQIAEEEAARQ------RAEAEKILKEKLTAINEAT 2051
Cdd:TIGR02169 309 SIAEKERELEDAEERLAkleAEIDKLLAEIEELeREIEEERKRRDKLTEEYAELKeeledlRAELEEVDKEFAETRDELK 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2052 RLKTEAEIALKEKEAENDRLKRKAEEegyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKI------VEETLKQR 2125
Cdd:TIGR02169 389 DYREKLEKLKREINELKRELDRLQEE----LQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIkkqewkLEQLAADL 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2126 KVVEEEIHILKLNF---EKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-----------------LALEEE 2185
Cdd:TIGR02169 465 SKYEQELYDLKEEYdrvEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQgvhgtvaqlgsvgeryaTAIEVA 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2186 KKRKEAEAKVKQIQAAEE--EAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLV 2263
Cdd:TIGR02169 545 AGNRLNNVVVEDDAVAKEaiELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEF-------DPKYEPAFK 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2264 QQNKDSMaqdkLKEEFEKAKKLAQEAEKAKDNAEkeaalLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEAS 2343
Cdd:TIGR02169 618 YVFGDTL----VVEDIEAARRLMGKYRMVTLEGE-----LFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERLEGLKR 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2344 RRAEAEAAALKLKQEADSEMAKYKKLAEKT---LKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA 2420
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIgeiEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2421 QVEDELSKVKIQMEDllklklKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQ 2500
Cdd:TIGR02169 769 ELEEDLHKLEEALND------LEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2501 RELAEKMLEEKkqaiQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEK 2580
Cdd:TIGR02169 843 IDLKEQIKSIE----KEIENLNGKKEELEEELEELEAALRDLESRLGD----LKKERDELEAQLRELERKIEELEAQIEK 914
|
810 820 830
....*....|....*....|....*....|
gi 1207141724 2581 LKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2610
Cdd:TIGR02169 915 KRKRLSELKAKLEALEEELSEIEDPKGEDE 944
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
345-445 |
1.42e-12 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 66.98 E-value: 1.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAErDLGVTRLLDP 424
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 1207141724 425 ED-VDVPHPDEKSIITYVSSMY 445
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3336-3374 |
2.00e-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: 2.00e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 3336 LLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEMNQNL 3374
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
719-908 |
2.05e-12 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 69.78 E-value: 2.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 719 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 795
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIeegHPDAEEIQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 796 LQYAKLLTSSKTRLRSLD---QLHAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNV 872
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 1207141724 873 QMTGDKLLKDGHP-ARKTIEAFTAALQTQWSWILQLC 908
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1876-2585 |
3.70e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 73.17 E-value: 3.70e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1876 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvldDELQRLKNDVNSAVKQK 1955
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEV----KELEELKEEIEELEKEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1956 KELEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLEsEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 2035
Cdd:PRK03918 248 ESLEGSK----RKLEEKIRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEE 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2036 AEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegYQR-KVLEDQAAQHKqaieekigqlKKSSDTELDRQ 2114
Cdd:PRK03918 323 INGI-EERIKELEEKEERLEELKKKLKELEKRLEELEERHEL--YEEaKAKKEELERLK----------KRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2115 KKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRK-LALEEEKKRKEAEA 2193
Cdd:PRK03918 390 EKELEELEKAKEEIEEEISKIT---ARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEHRKeLLEEYTAELKRIEK 466
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2194 KVKQIQAAEEEAarqhKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQD 2273
Cdd:PRK03918 467 ELKEIEEKERKL----RKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIK 542
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2274 KLKEEFEKAKKLAQEA---EKAKDNAEKEAALLHKKAEEaerqkkaaeaeaakqakaqedaeklrkeaekeasrraeaea 2350
Cdd:PRK03918 543 SLKKELEKLEELKKKLaelEKKLDELEEELAELLKELEE----------------------------------------- 581
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2351 AALKLKQEADSEMAKYKKLAEKTLKQKSSVEEelvkvkvqLDETDKqksvldvELKRLKQEVSDAIKQKAQVEDELSKVK 2430
Cdd:PRK03918 582 LGFESVEELEERLKELEPFYNEYLELKDAEKE--------LEREEK-------ELKKLEEELDKAFEELAETEKRLEELR 646
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2431 IQMEdllklklkiekenqELMKKDKDNTKKLLEEEaenMKKLAEEAARLNIEAQEAARLRQIAESDLAKqrelaekmLEE 2510
Cdd:PRK03918 647 KELE--------------ELEKKYSEEEYEELREE---YLELSRELAGLRAELEELEKRREEIKKTLEK--------LKE 701
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2511 KKQAIQEAAKlkaEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAE---RKRQ-LEITAEAEKLKVKV 2585
Cdd:PRK03918 702 ELEEREKAKK---ELEKLEKALERVEELREKVKKYKALLKERALSKVGEIASEIFEElteGKYSgVRVKAEENKVKLFV 777
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1555-2312 |
3.98e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 73.18 E-value: 3.98e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1555 EEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQ--------DVAVDSEKQKHNI 1626
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1627 QRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvdaDKLRNAAQEEAEK 1706
Cdd:TIGR02169 311 AEKERELEDAEERLAKLEAE--------IDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL---EDLRAELEEVDKE 379
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1707 LRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEKFKLQAEEAERHLKQAELEKQrqIQVVEEvAKKTAATQL 1786
Cdd:TIGR02169 380 FAETR-DELKDYREKLEKLKREINELKR------------ELDRLQEELQRLSEELADLNAA--IAGIEA-KINELEEEK 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1787 ESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAA 1863
Cdd:TIGR02169 444 EDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQG 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1864 QEEAEKQKEEAKREakkRAKAEEAA----------------------LKQKEAAEMELGNQRKMAEETAKQKLAAEQELI 1921
Cdd:TIGR02169 523 VHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavakeaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVI 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1922 RLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE-----LEEELIK---------VRKEMEILLQQKSKAEKE 1982
Cdd:TIGR02169 600 GFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKyrmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQ 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1983 TMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE----EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlK 2054
Cdd:TIGR02169 678 RLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkigEIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---I 753
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2055 TEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHI 2134
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTL 826
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2135 LKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEKFRKLALEEEkkrkeaeakVKQIQAAEEEAARQHKAAQE 2214
Cdd:TIGR02169 827 EKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLNGKKEELEEE---------LEELEAALRDLESRLGDLKK 889
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2215 EVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL------------------VQQNKDSMAQD--- 2273
Cdd:TIGR02169 890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEdpkgedeeipeeelsledVQAELQRVEEEira 969
|
810 820 830 840
....*....|....*....|....*....|....*....|....*
gi 1207141724 2274 ------KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2312
Cdd:TIGR02169 970 lepvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1571-2087 |
3.99e-12 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 73.15 E-value: 3.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1571 AEMQAELEKQKQLAETHAKAIAKAEQEANELKtkmkDEVSKRQDVAVDSEKQKHNIQRELQelktLSEQEIKAKSQQVEE 1650
Cdd:PRK02224 247 EERREELETLEAEIEDLRETIAETEREREELA----EEVRDLRERLEELEEERDDLLAEAG----LDDADAEAVEARREE 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1651 ALLSRTRIEEEIHIIRLQLETTmkqKNTAETellqLRAKAVDADKLRNAAQEEAEKLRKQV--AEETQKKRKAE-EELKR 1727
Cdd:PRK02224 319 LEDRDEELRDRLEECRVAAQAH---NEEAES----LREDADDLEERAEELREEAAELESELeeAREAVEDRREEiEELEE 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1728 KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEES-----LK 1802
Cdd:PRK02224 392 EIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSphvetIE 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1803 NEQVMVIQLQEEAEHLKKQQAEADKAREQA------EKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakr 1876
Cdd:PRK02224 472 EDRERVEELEAELEDLEEEVEEVEERLERAedlveaEDRIERLEERREDLEELIAERRETIE------------------ 533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1877 eakkrAKAEEAALKQKEAAEMELGNQRKmAEETAKQKLAAEQELIRLRAdfehAEQQRTVLDDELQRLkNDVNSAVKQKK 1956
Cdd:PRK02224 534 -----EKRERAEELRERAAELEAEAEEK-REAAAEAEEEAEEAREEVAE----LNSKLAELKERIESL-ERIRTLLAAIA 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1957 ELEEELIKVRKemeillQQKSKAEKEtmsntEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARqraea 2036
Cdd:PRK02224 603 DAEDEIERLRE------KREALAELN-----DERRERLAEKRERKRELEAEFDEAR--IEEAREDKERAEEYLEQ----- 664
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2037 ekiLKEKLTAINEA-TRLKTE---AEIALKEKEAENDRLKRKAEEEGYQRKVLED 2087
Cdd:PRK02224 665 ---VEEKLDELREErDDLQAEigaVENELEELEELRERREALENRVEALEALYDE 716
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2230-2810 |
4.61e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.79 E-value: 4.61e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2230 KEIAEKEAEKQVILVQEA--AQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKD---NAEKEAALLH 2304
Cdd:PRK03918 172 KEIKRRIERLEKFIKRTEniEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEeieELEKELESLE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2305 KKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAeaaaLKLKQEadseMAKYKKLAEKTLKQKSSVEEEL 2384
Cdd:PRK03918 252 GSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEY----IKLSEF----YEEYLDELREIEKRLSRLEEEI 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2385 VKVKVQLDETDKQKSVLDvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEE 2464
Cdd:PRK03918 324 NGIEERIKELEEKEERLE-ELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEKAKEE 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2465 EAENMKKLAEEAARLNIEAQEaaRLRQIAESDLAKQ------RELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQKDQ 2534
Cdd:PRK03918 403 IEEEISKITARIGELKKEIKE--LKKAIEELKKAKGkcpvcgRELTEehrkELLEEYTAELKRIEKELKEIEEKERKLRK 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2535 AQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITA-EAEKLKVKVTQLSDAQSKAEEEAKK---FKKQADE 2608
Cdd:PRK03918 481 ELRELEKVLKKESELikLKELAEQLKELEEKLKKYNLEELEKKAeEYEKLKEKLIKLKGEIKSLKKELEKleeLKKKLAE 560
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2609 IKIRLQETEKHTSEKHTvveKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIlq 2688
Cdd:PRK03918 561 LEKKLDELEEELAELLK---ELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEEL-- 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2689 qsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME-EERKKLQSAMDAAIKKQKEAEEEMNGKQK 2767
Cdd:PRK03918 636 ----AETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAElEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 1207141724 2768 EMQDLEKKRieqekllaEENKNLREKLQQLQSSQKASYTKEIE 2810
Cdd:PRK03918 712 ELEKLEKAL--------ERVEELREKVKKYKALLKERALSKVG 746
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1886-2792 |
6.83e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 72.41 E-value: 6.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1886 EAALKQKEAAEMELGNQRKMAEETAKQklaaeqeLIRLRADFEHAEQQRTVLDD----ELQRLKNDVNSAVKQKKELEEE 1961
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQQ-------LERLRREREKAERYQALLKEkreyEGYELLKEKEALERQKEAIERQ 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1962 LIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEatklrsvaEEAKKQRQIAEEEAarQRAEAEKILK 2041
Cdd:TIGR02169 246 LASLEEELEKLTEEISELEKRL----EEIEQLLEELNKKIKDLGEE--------EQLRVKEKIGELEA--EIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2042 EKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQ---AIEEKIGQLKKSSDTELDRQKKIV 2118
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEeleDLRAELEEVDKEFAETRDELKDYR 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2119 EETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLaleeekkrkeaEAKVKQI 2198
Cdd:TIGR02169 392 EKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQ-----------EWKLEQL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2199 QAAEEEAARQHKAAQEEVGRLMKlaEEAKKQKEIAEKEAEKQVIlvqEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKE 2277
Cdd:TIGR02169 461 AADLSKYEQELYDLKEEYDRVEK--ELSKLQRELAEAEAQARAS---EERVRGGRAVEEVLKASIQGVHGTVAQlGSVGE 535
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2278 EFEKAKKLAQEAEKA----KDNAEKEAALLHKKAEEAERQKKAaeaeaakqakaqedaeKLRKEAEKEASRRAEAEAAAL 2353
Cdd:TIGR02169 536 RYATAIEVAAGNRLNnvvvEDDAVAKEAIELLKRRKAGRATFL----------------PLNKMRDERRDLSILSEDGVI 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2354 KLKQEADSEMAKYKKlAEKTLKQKSSVEEELVKVKVQLDETdkQKSVLDVEL-----------KRLKQEVSDAIKQKAQV 2422
Cdd:TIGR02169 600 GFAVDLVEFDPKYEP-AFKYVFGDTLVVEDIEAARRLMGKY--RMVTLEGELfeksgamtggsRAPRGGILFSRSEPAEL 676
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2423 E---DELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEnmkklaeeaarlnieaqeaarlRQIAESDLAK 2499
Cdd:TIGR02169 677 QrlrERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKE----------------------IEQLEQEEEK 734
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2500 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLD----QETEGFQKSLEAERKRQLEIT 2575
Cdd:TIGR02169 735 LKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsriPEIQAELSKLEEEVSRIEARL 814
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2576 AEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvqrlqskQEADGLHKAIADLEKEK 2655
Cdd:TIGR02169 815 REIEQ---KLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELE-------EELEELEAALRDLESRL 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2656 EKLKKEAADLQKQSKEMANVQQEQ-LQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERqr 2734
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELeAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQR-- 962
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2735 klMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2792
Cdd:TIGR02169 963 --VEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3587-3625 |
7.12e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.73 E-value: 7.12e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 3587 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPEVHEKL 3625
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4163-4201 |
7.48e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 7.48e-12
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 4163 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEFKDKL 4201
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1810-2794 |
8.49e-12 |
|
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: 72.13 E-value: 8.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1810 QLQEEAEHLKKQQAEADKArEQAEKELETWRQKANE---ALRLRLQAEEE----ANKKTAAQEEAEKQKEEAKREAKKRA 1882
Cdd:pfam01576 6 EMQAKEEELQKVKERQQKA-ESELKELEKKHQQLCEeknALQEQLQAETElcaeAEEMRARLAARKQELEEILHELESRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1883 KAEE------AALKQKEAAEMELGNQRKMAEETAKQKL-----AAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSA 1951
Cdd:pfam01576 85 EEEEersqqlQNEKKKMQQHIQDLEEQLDEEEAARQKLqlekvTTEAKIKKLEEDILLLEDQNSKLSKERKLLEERISEF 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1952 VKQKKELEEE---LIKVRKEMEIL---LQQKSKAEKETMSNTEKSKQLLESEAAKMRElaeeatklrsvaEEAKKQRQIA 2025
Cdd:pfam01576 165 TSNLAEEEEKaksLSKLKNKHEAMisdLEERLKKEEKGRQELEKAKRKLEGESTDLQE------------QIAELQAQIA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2026 EEEAARQRAEAEkiLKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRkvleDQAAQHKQAIEEKIGQLKK 2105
Cdd:pfam01576 233 ELRAQLAKKEEE--LQAALARLEEETAQKNNALKKIRELEAQISELQEDLESERAAR----NKAEKQRRDLGEELEALKT 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2106 SSDTELDRQKkiVEETLKQRKvvEEEIHILKLNFEKASSGKQELELELKKLKGIA-DETQKSKAKAEEEAEKFRKLALEE 2184
Cdd:pfam01576 307 ELEDTLDTTA--AQQELRSKR--EQEVTELKKALEEETRSHEAQLQEMRQKHTQAlEELTEQLEQAKRNKANLEKAKQAL 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2185 EKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQK-EIAEK----------------EAEKQVILVQEA 2247
Cdd:pfam01576 383 ESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRaELAEKlsklqselesvssllnEAEGKNIKLSKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2248 AQKCSAAEQKAQNVLVQQNKDSMAQD----KLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEA----ERQKKAAEA 2319
Cdd:pfam01576 463 VSSLESQLQDTQELLQEETRQKLNLStrlrQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMkkklEEDAGTLEA 542
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2320 EAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEAD-------------SEMAKYKKLAEKTLKQKSSVEEELVK 2386
Cdd:pfam01576 543 LEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDdllvdldhqrqlvSNLEKKQKKFDQMLAEEKAISARYAE 622
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2387 VKVQLDETDKQKSVLDVELKRlkqEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKkdkdnTKKLLEEEA 2466
Cdd:pfam01576 623 ERDRAEAEAREKETRALSLAR---ALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKNVHELER-----SKRALEQQV 694
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2467 ENMKKLAEEA---------ARL----NIEAQEAARLRQIAESD---------LAKQ-RELAEKMLEEKKQAIQEAA---- 2519
Cdd:pfam01576 695 EEMKTQLEELedelqatedAKLrlevNMQALKAQFERDLQARDeqgeekrrqLVKQvRELEAELEDERKQRAQAVAakkk 774
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2520 ------KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-------------ETEGFQKSLEAERKRQLEITAEAEK 2580
Cdd:pfam01576 775 leldlkELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEarasrdeilaqskESEKKLKNLEAELLQLQEDLAASER 854
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2581 LKVKVTQLSDA-QSKAEEEAKKFKKQADE---IKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKE 2656
Cdd:pfam01576 855 ARRQAQQERDElADEIASGASGKSALQDEkrrLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQ 934
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2657 KLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSF------FAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQ 2730
Cdd:pfam01576 935 KSESARQQLERQNKELKAKLQEMEGTVKSKFKSSIaaleakIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDE 1014
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 2731 ERQRKLMEEERKKLQSAMDAAIKKQKEAEEE---MNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2794
Cdd:pfam01576 1015 RRHADQYKDQAEKGNSRMKQLKRQLEEAEEEasrANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2109-2823 |
1.00e-11 |
|
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: 71.92 E-value: 1.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2109 TELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASS-GKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLA--LEEE 2185
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTqkREAQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2186 KKRKEAEAKVKQIQAAEEEAARQ---HKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL--VQEAAQKCSAAEQKAQN 2260
Cdd:TIGR00618 253 EEQLKKQQLLKQLRARIEELRAQeavLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHteLQSKMRSRAKLLMKRAA 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2261 VLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKA---KDNAEKEAALLHK-KAEEAERQKKAAEAEAAKQAKAQEDAEKLRK 2336
Cdd:TIGR00618 333 HVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQATI 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2337 EAEKEASRRAEAEAAALKLKQEADSEMAKYKKLA-EKTLKQKSSVEEELVKVKVQLDETD---KQKSVLDVELKRLKQEV 2412
Cdd:TIGR00618 413 DTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAiTCTAQCEKLEKIHLQESAQSLKEREqqlQTKEQIHLQETRKKAVV 492
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2413 SDAIKQKAQVEDELSKVKIQMEdLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQi 2492
Cdd:TIGR00618 493 LARLLELQEEPCPLCGSCIHPN-PARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQ- 570
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2493 AESDLAKQRElaekmleekkqaiqeaaKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrldqetegfqKSLEAERKRQL 2572
Cdd:TIGR00618 571 SFSILTQCDN-----------------RSKEDIPNLQNITVRLQDLTEKLSEAED--------------MLACEQHALLR 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2573 EITAEAEKLKVKVTQlsdaQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLE 2652
Cdd:TIGR00618 620 KLQPEQDLQDVRLHL----QQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYW 695
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2653 KEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLlkkekaieEEKKKLEKQFEDEVKKAEALKAEQER 2732
Cdd:TIGR00618 696 KEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDAL--------NQSLKELMHQARTVLKARTEAHFNNN 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2733 QRKLMEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2811
Cdd:TIGR00618 768 EEVTAALQTgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEI 847
|
730
....*....|..
gi 1207141724 2812 QTDKVPEEELVQ 2823
Cdd:TIGR00618 848 THQLLKYEECSK 859
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4509-4547 |
1.08e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.96 E-value: 1.08e-11
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 4509 LLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMVDRI 4547
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2214-2828 |
1.17e-11 |
|
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: 71.54 E-value: 1.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2214 EEVGRLMKLAEEAKKQKEIAEKEAEKQV----ILVQEAAQKCSAAEQKAQnvlVQQNKDSMAQDKLKEEFEKAKKLAQEA 2289
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTlrsqLLTLCTPCMPDTYHERKQ---VLEKELKHLREALQQTQQSHAYLTQKR 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2290 EKAKDNAEKEAALLHKKAEEAE-RQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkQEADSEMAKYKK 2368
Cdd:TIGR00618 250 EAQEEQLKKQQLLKQLRARIEElRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTEL-QSKMRSRAKLLM 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2369 LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQevsdaikqKAQVEDELSKVKIQMEDLLKLKLKIEKENQ 2448
Cdd:TIGR00618 329 KRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREI--------SCQQHTLTQHIHTLQQQKTTLTQKLQSLCK 400
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2449 ELMKKDKDNTKKLLEEEAENmkklAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQaIQEAAKLKAEAEKL 2528
Cdd:TIGR00618 401 ELDILQREQATIDTRTSAFR----DLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHL-QESAQSLKEREQQL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2529 QKQKDQAQVEAQK--LLEAKKEMQQRLDQETEGFQKSLEAERKRQLEitaeAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2606
Cdd:TIGR00618 476 QTKEQIHLQETRKkaVVLARLLELQEEPCPLCGSCIHPNPARQDIDN----PGPLTRRMQRGEQTYAQLETSEEDVYHQL 551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2607 DEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTI 2686
Cdd:TIGR00618 552 TSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVR 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2687 LQQSFFAEKETLLKKEKAIEEEKKKLEKQFED--EVKKAEALKAEQeRQRKLMEEERKKLQSAMDAAIKKQK-----EAE 2759
Cdd:TIGR00618 632 LHLQQCSQELALKLTALHALQLTLTQERVREHalSIRVLPKELLAS-RQLALQKMQSEKEQLTYWKEMLAQCqtllrELE 710
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2760 EEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMTMVE 2828
Cdd:TIGR00618 711 THIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAE 779
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
347-446 |
1.31e-11 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 63.90 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN---LENLEQAFSIAER-DLGVTRLL 422
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 1207141724 423 DPEDVdVPHPDEKSIITYVSSMYD 446
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
225-324 |
1.43e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 64.37 E-value: 1.43e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 225 ERDRvQKKTFTKWVNKHLVKAQrhITDLYEDLRDGHNLISLLE-VLSGE-------TLPREKGRMRFHKLQNVQIALDFL 296
Cdd:cd21300 4 EGER-EARVFTLWLNSLDVEPA--VNDLFEDLRDGLILLQAYDkVIPGSvnwkkvnKAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 1207141724 297 KHRQVKLVNIRNDDIADGNPKLTLGLIW 324
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1312-2103 |
1.50e-11 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 71.25 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1312 ILNKYENQLREVNKVPVNEKEIEASQTQLQKLRSEAEgkqatfDRLEEELQRATEVNKRMSQLHSERDVElehyrqlvgn 1391
Cdd:TIGR02169 228 LLKEKEALERQKEAIERQLASLEEELEKLTEEISELE------KRLEEIEQLLEELNKKIKDLGEEEQLR---------- 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1392 LRERWQAVFAQIELRQRELDLLNRQMQAyresydwlirwiADAKQRQDKLhavpiggskglqeqltQEKKLLEEIEKNKD 1471
Cdd:TIGR02169 292 VKEKIGELEAEIASLERSIAEKERELED------------AEERLAKLEA----------------EIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1472 KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASddiiqeyvtLRTRYSELmtlsSQYIKFIIETQRR 1551
Cdd:TIGR02169 344 EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------YREKLEKL----KREINELKRELDR 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1552 LQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEvskrqdvavdsEKQKHNIQRELQ 1631
Cdd:TIGR02169 411 LQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKY-----------EQELYDLKEEYD 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1632 ELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQ---LETTMKQKNTAETELLQLRAKAVDAdkLRNAAqeeAEKLR 1708
Cdd:TIGR02169 480 RV----EKELSKLQRELAEAEAQARASEERVRGGRAVeevLKASIQGVHGTVAQLGSVGERYATA--IEVAA---GNRLN 550
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1709 KQVAEETQKKRKAEEELKRK-----------------SEAEKDAAKEKKKALEDLEKFKLQ-----------------AE 1754
Cdd:TIGR02169 551 NVVVEDDAVAKEAIELLKRRkagratflplnkmrderRDLSILSEDGVIGFAVDLVEFDPKyepafkyvfgdtlvvedIE 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1755 EAERHLKQAelekqRQIQVVEEVAKKT--------AATQLESKQVALTARLEESLKNEQVMVIQ---LQEEAEHLKKQQA 1823
Cdd:TIGR02169 631 AARRLMGKY-----RMVTLEGELFEKSgamtggsrAPRGGILFSRSEPAELQRLRERLEGLKRElssLQSELRRIENRLD 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1824 EADKAREQAEKELETWRQKANealrlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAE-EAALKQKEAAEMELgnq 1902
Cdd:TIGR02169 706 ELSQELSDASRKIGEIEKEIE-----QLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKElEARIEELEEDLHKL--- 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1903 rKMAEETAKQKLaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSaVKQKKELEEELIKVRKEMEILLQQKSKAEKE 1982
Cdd:TIGR02169 778 -EEALNDLEARL-SHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNR-LTLEKEYLEKEIQELQEQRIDLKEQIKSIEK 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1983 TMSNTEKSKQLLESEAAK----MRELAEEATKLRSVAEEAKKQR---QIAEEEAARQRAEAEKILKEkltaineatrLKT 2055
Cdd:TIGR02169 855 EIENLNGKKEELEEELEEleaaLRDLESRLGDLKKERDELEAQLrelERKIEELEAQIEKKRKRLSE----------LKA 924
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 1207141724 2056 EAEiALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKIGQL 2103
Cdd:TIGR02169 925 KLE-ALEEELSEIEDPKGEDEEIPEEELSLEDVQAE-LQRVEEEIRAL 970
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1630-1943 |
2.05e-11 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 70.54 E-value: 2.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1630 LQELKTLSEQEIKAKSQQVEEallSRTRIEEEIHIIRLQLETTMKQKNTAETELLQlRAKAVDADKLRNAAQEEAEKLRK 1709
Cdd:pfam17380 278 VQHQKAVSERQQQEKFEKMEQ---ERLRQEKEEKAREVERRRKLEEAEKARQAEMD-RQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1710 QvaeetQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK-----LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1784
Cdd:pfam17380 354 R-----QEERKRELERIRQEEIAMEISRMRELERLQMERQQknervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAE 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1785 QLESKQVALTaRLEESLKNEQVMV----IQLQEEAEHLKKQQAEADKAREQAEKELETwRQKANEALRLRLQAEEEANK- 1859
Cdd:pfam17380 429 QEEARQREVR-RLEEERAREMERVrleeQERQQQVERLRQQEEERKRKKLELEKEKRD-RKRAEEQRRKILEKELEERKq 506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1860 -------KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgnQRKMAEETAKqklaAEQELIRLRADFEHAEQ 1932
Cdd:pfam17380 507 amieeerKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEE-----RRRIQEQMRK----ATEERSRLEAMEREREM 577
|
330
....*....|.
gi 1207141724 1933 QRTVLDDELQR 1943
Cdd:pfam17380 578 MRQIVESEKAR 588
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3663-3699 |
2.32e-11 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 61.19 E-value: 2.32e-11
10 20 30
....*....|....*....|....*....|....*..
gi 1207141724 3663 LLDAQVATGGIIDPVNSHRLPNDVAIERGYFSKQLAK 3699
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQ 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1571-2028 |
5.02e-11 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 69.03 E-value: 5.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1571 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAvDSEKQKHNIQRELQELKtlSEQEIKAKSQQVEE 1650
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELE-ELEEELEELEAELEELR--EELEKLEKLLQLLP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1651 ALLSRTRIEEEIHIIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKse 1730
Cdd:COG4717 130 LYQELEALEAELAELPERLEE-------LEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEE-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1731 aEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQiQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVM--- 1807
Cdd:COG4717 201 -LEELQQRLAELEEELEEAQEELEELEEELEQLENELEAA-ALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIagv 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1808 ------VIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKkTAAQEEAEKQKEEAKREAKKR 1881
Cdd:COG4717 279 lflvlgLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-EELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1882 AKAEEAALKQKEAAEMELGNQRKMA-EETAKQKLAAEQELIRLRADFEHAEQQ----------------RTVLDDELQRL 1944
Cdd:COG4717 358 ELEEELQLEELEQEIAALLAEAGVEdEEELRAALEQAEEYQELKEELEELEEQleellgeleellealdEEELEEELEEL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1945 KNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskQLLESEAAKMRELAEEATKLRSVAEEAKKQRQI 2024
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQLEEDGELAELL---------QELEELKAELRELAEEWAALKLALELLEEAREE 508
|
....
gi 1207141724 2025 AEEE 2028
Cdd:COG4717 509 YREE 512
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1426-2099 |
5.30e-11 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 69.37 E-value: 5.30e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1426 WLIRWIADAKQRQDKLH---AVPIGGSKGLQE-QLTQEK---KLLEEIEKNKDKV--------------EDCQKFAKGYI 1484
Cdd:pfam05483 93 WKVSIEAELKQKENKLQenrKIIEAQRKAIQElQFENEKvslKLEEEIQENKDLIkennatrhlcnllkETCARSAEKTK 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1485 DAIKDYELQLVTYKAL---VEPIASPLKKAKMEsASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRR-----LQDEE 1556
Cdd:pfam05483 173 KYEYEREETRQVYMDLnnnIEKMILAFEELRVQ-AENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQvslllIQITE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1557 KAAEKLKEEERKKMAEMQA-ELEKQKQLAETHAKAIAKAE----QEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQ 1631
Cdd:pfam05483 252 KENKMKDLTFLLEESRDKAnQLEEKTKLQDENLKELIEKKdhltKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTE 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1632 ELKTLSEQEIKAKSQQ---VEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLR 1708
Cdd:pfam05483 332 EKEAQMEELNKAKAAHsfvVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELK 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1709 KQVAE------ETQKKRKAEEELKRKSEAEKdaakekkkaledlekFKLQAEEAERHLKQAEL-----EKQRQIQVVEEV 1777
Cdd:pfam05483 412 KILAEdeklldEKKQFEKIAEELKGKEQELI---------------FLLQAREKEIHDLEIQLtaiktSEEHYLKEVEDL 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1778 akKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA 1857
Cdd:pfam05483 477 --KTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVR 554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1858 NKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVL 1937
Cdd:pfam05483 555 EEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAY 634
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1938 DDELQRLKNDVNSAvkqKKELEEELIKVRKEMEIllqqKSKAEKETMSNTEKSKQlleseaakmreLAEEATKLRSVAEE 2017
Cdd:pfam05483 635 EIKVNKLELELASA---KQKFEEIIDNYQKEIED----KKISEEKLLEEVEKAKA-----------IADEAVKLQKEIDK 696
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2018 aKKQRQIAEEEA--ARQRAEAEKILKEKLTAI-------NEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQ 2088
Cdd:pfam05483 697 -RCQHKIAEMVAlmEKHKHQYDKIIEERDSELglyknkeQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKME 775
|
730
....*....|.
gi 1207141724 2089 AAQHKQAIEEK 2099
Cdd:pfam05483 776 AKENTAILKDK 786
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1597-1917 |
8.96e-11 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 68.50 E-value: 8.96e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1597 EANELKTKMKDEV-----SKRQDVAVDSEKQKH----NIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRL 1667
Cdd:NF033838 51 SGNESQKEHAKEVeshleKILSEIQKSLDKRKHtqnvALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1668 QLETTMKQKNTAET----ELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakeKKKAL 1743
Cdd:NF033838 131 KKDTLEPGKKVAEAtkkvEEAEKKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKE----------EAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1744 EDLEKFKlqAEEAERHLKQAELEKQRQIQV----VEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1819
Cdd:NF033838 201 RDEEKIK--QAKAKVESKKAEATRLEKIKTdrekAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVLGEPATPDK 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1820 KQQ-------------------------AEADKAREQAEKELETWRQK------ANEALRLRLQ-AEEEAN-KKTAAQEE 1866
Cdd:NF033838 279 KENdakssdssvgeetlpspslkpekkvAEAEKKVEEAKKKAKDQKEEdrrnypTNTYKTLELEiAESDVKvKEAELELV 358
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 1867 AEKQKEEAKREAKKRAKAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAE 1917
Cdd:NF033838 359 KEEAKEPRNEEKIKQAKAKVES-KKAEATRLEkIKTDRKKAEEEAKRKAAEE 409
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
347-445 |
9.18e-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: 61.60 E-value: 9.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 347 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSIAERDLGVTRLLDPED 426
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90
....*....|....*....
gi 1207141724 427 VdVPHPDEKSIITYVSSMY 445
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFH 102
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2201-2558 |
9.38e-11 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 68.00 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2201 AEEEAARQHKAAQEEVGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL----VQQNKDSMAQDKL 2275
Cdd:pfam07888 67 DREQWERQRRELESRVAELKEeLRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEArireLEEDIKTLTQRVL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2276 KEEfekakklaQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKL 2355
Cdd:pfam07888 147 ERE--------TELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTL 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2356 KQEADSEMAKYKKLaEKTLKQKSSVEEELvkvkvqldETDKQKSVLdvelkrLKQEVSDAIKQKAQVEDELSKVKI---Q 2432
Cdd:pfam07888 219 TQKLTTAHRKEAEN-EALLEELRSLQERL--------NASERKVEG------LGEELSSMAAQRDRTQAELHQARLqaaQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2433 MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKK 2512
Cdd:pfam07888 284 LTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESR 363
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1207141724 2513 QAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETE 2558
Cdd:pfam07888 364 RELQE---LKASLRVAQKEKEQLQAEKQELLEYIRQLEQRLETVAD 406
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1170-1957 |
1.12e-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: 1.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1170 EQEPALIQKDSTSGEQDESVCKSyitQIKDLRLRLEGCESRTVN----RLRQMVDKEPL-KACTQRATEQKKVQTELEGI 1244
Cdd:TIGR02169 286 EEEQLRVKEKIGELEAEIASLER---SIAEKERELEDAEERLAKleaeIDKLLAEIEELeREIEEERKRRDKLTEEYAEL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1245 KKDLDKVVEKSEAVLATSQQSSSAPV-LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ----GAEDILNKYENQ 1319
Cdd:TIGR02169 363 KEELEDLRAELEEVDKEFAETRDELKdYREKLEKLKREINELKRELDRLQEELQRLSEELADLNaaiaGIEAKINELEEE 442
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1320 LREVN-KVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELqraTEVNKRMSQLHSERDV---ELEHYRQLVGNLRER 1395
Cdd:TIGR02169 443 KEDKAlEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKEL---SKLQRELAEAEAQARAseeRVRGGRAVEEVLKAS 519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1396 WQAVFAQIelrqreldllnRQMQAYRESYDWLIRWIADAKqrqdkLHAVPIGGSKGLQE--QLTQEKKL--LEEIEKNKD 1471
Cdd:TIGR02169 520 IQGVHGTV-----------AQLGSVGERYATAIEVAAGNR-----LNNVVVEDDAVAKEaiELLKRRKAgrATFLPLNKM 583
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1472 KVEDCQKfAKGYIDAIKDYELQLVTYKALVEPI-----ASPLKKAKMESASDDIIQ-EYVTLRTRYSE---LMTLSSQYI 1542
Cdd:TIGR02169 584 RDERRDL-SILSEDGVIGFAVDLVEFDPKYEPAfkyvfGDTLVVEDIEAARRLMGKyRMVTLEGELFEksgAMTGGSRAP 662
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1543 KFIIETQRRLQDEEkaaeklkeeerkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQ 1622
Cdd:TIGR02169 663 RGGILFSRSEPAEL--------------QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQL 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1623 KHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdadklrnaaQE 1702
Cdd:TIGR02169 729 EQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEI---------QA 798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1703 EAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhlKQAELEKQrqiqvveevaKKTA 1782
Cdd:TIGR02169 799 ELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK--EIENLNGK----------KEEL 866
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1783 ATQLESKQVALtARLEESLKNeqvmviqLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANK--- 1859
Cdd:TIGR02169 867 EEELEELEAAL-RDLESRLGD-------LKKERDELEAQLRELERKIEELEAQIEKKRKRLSE-LKAKLEALEEELSeie 937
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1860 KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMelgnqrkmaeetakqklAAEQELIRLRADFEHAEQQRTVLDD 1939
Cdd:TIGR02169 938 DPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM-----------------LAIQEYEEVLKRLDELKEKRAKLEE 1000
|
810
....*....|....*...
gi 1207141724 1940 ELQRLKNDVNSAVKQKKE 1957
Cdd:TIGR02169 1001 ERKAILERIEEYEKKKRE 1018
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3996-4034 |
1.26e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.88 E-value: 1.26e-10
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 3996 LLEAQVATGGLMDPEYYFRLPIDIAMQRGYMNKETSERI 4034
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2528-2796 |
1.71e-10 |
|
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: 67.46 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2528 LQKQKDQAQVEAQKLLEakKEMQQRLDQETEgfQKSLEAERKRQLEitaEAEKLKvKVTQLSDAQSKAEEEAKKFKKQAD 2607
Cdd:pfam17380 278 VQHQKAVSERQQQEKFE--KMEQERLRQEKE--EKAREVERRRKLE---EAEKAR-QAEMDRQAAIYAEQERMAMERERE 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2608 EIKIRLQETEKHTS-----------EKHTVVEKLEVQRLQS----KQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEM 2672
Cdd:pfam17380 350 LERIRQEERKRELErirqeeiameiSRMRELERLQMERQQKnervRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQ 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2673 ANVQQEQLQQektiLQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQ-------RKLMEEERKKLQ 2745
Cdd:pfam17380 430 EEARQREVRR----LEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRkraeeqrRKILEKELEERK 505
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 2746 SAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2796
Cdd:pfam17380 506 QAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQE 556
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1542-2256 |
1.72e-10 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 67.79 E-value: 1.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1542 IKFIIETQRRLQDEE-------------------------KAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQ 1596
Cdd:TIGR02169 193 IDEKRQQLERLRRERekaeryqallkekreyegyellkekEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQ 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1597 EANELKTKMKDEVSKRQ--------DVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQqveeallsRTRIEEEIHIIRLQ 1668
Cdd:TIGR02169 273 LLEELNKKIKDLGEEEQlrvkekigELEAEIASLERSIAEKERELEDAEERLAKLEAE--------IDKLLAEIEELERE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1669 LETTMKQKNTAETELLQLRAKavdADKLRNAAQEEAEKLRKQVaEETQKKRKAEEELKRKSEAEKDaakekkkaledlEK 1748
Cdd:TIGR02169 345 IEEERKRRDKLTEEYAELKEE---LEDLRAELEEVDKEFAETR-DELKDYREKLEKLKREINELKR------------EL 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1749 FKLQAEEAERHLKQAELEKqrQIQVVEEvAKKTAATQLESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1828
Cdd:TIGR02169 409 DRLQEELQRLSEELADLNA--AIAGIEA-KINELEEEKEDKALEIKK-QEWKLEQLAADLSKYEQELYDLKEEYDRVEKE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1829 REQAEKEL---ETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREakkRAKAEEAA----------------- 1888
Cdd:TIGR02169 485 LSKLQRELaeaEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGER---YATAIEVAagnrlnnvvveddavak 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1889 -----LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ-----RTVLDDELqrLKNDVNSAVKQKKE- 1957
Cdd:TIGR02169 562 eaielLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTL--VVEDIEAARRLMGKy 639
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1958 ----LEEELIK---------VRKEMEILLQQKSKAEKETMSNT----EKSKQLLESEAAKMRELAEEATKLRSVAE---- 2016
Cdd:TIGR02169 640 rmvtLEGELFEksgamtggsRAPRGGILFSRSEPAELQRLRERleglKRELSSLQSELRRIENRLDELSQELSDASrkig 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2017 EAKKQRQIAEEEAARQRAEAEKiLKEKLTAINEAtrlKTEAEIALKEKEAENDRLKRKAEEEgyqRKVLEDQAAQHKQAI 2096
Cdd:TIGR02169 720 EIEKEIEQLEQEEEKLKERLEE-LEEDLSSLEQE---IENVKSELKELEARIEELEEDLHKL---EEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2097 EEKIGQLKKSSDTELDRQKKIVEETlkqrKVVEEEIHILKLNFEKASSGKQELElelkklkgIADETQKSKAKAEEEAEK 2176
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREI----EQKLNRLTLEKEYLEKEIQELQEQR--------IDLKEQIKSIEKEIENLN 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2177 FRKLALeeekkrkeaEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQ 2256
Cdd:TIGR02169 861 GKKEEL---------EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEE 931
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1683-2113 |
2.28e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.67 E-value: 2.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1683 LLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELK------RKSEAEKDAAKEKKKALEDLEKFKLQAEE- 1755
Cdd:COG3096 287 ALELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQaasdhlNLVQTALRQQEKIERYQEDLEELTERLEEq 366
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1756 ----AERHLKQAELEKQRQiQVVEEVakKTAATQLESKQVALTARLEESLKNEQVmvIQLQEEAEHLkkqQAEADKAREQ 1831
Cdd:COG3096 367 eevvEEAAEQLAEAEARLE-AAEEEV--DSLKSQLADYQQALDVQQTRAIQYQQA--VQALEKARAL---CGLPDLTPEN 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1832 AEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEETAK 1911
Cdd:COG3096 439 AEDYLAAFRAKEQQATEEVLELEQKLS----------------VADAARRQFEKAYELVCKIAGEVE----RSQAWQTAR 498
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1912 qklaaeqELIRLRADFEHAEQQRTVLDDELQRLkndvnsavkqkkeleEELIKVRKEMEILLQQKSKAEKETMSNTEKSK 1991
Cdd:COG3096 499 -------ELLRRYRSQQALAQRLQQLRAQLAEL---------------EQRLRQQQNAERLLEEFCQRIGQQLDAAEELE 556
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1992 QLLESEAAKMRELAEEAtklRSVAEEAKKQRQiAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 2071
Cdd:COG3096 557 ELLAELEAQLEELEEQA---AEAVEQRSELRQ-QLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAM 632
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1207141724 2072 KRKAEEEgYQRKVLEDQAAQHKQAIEEKIGQLKK---SSDTELDR 2113
Cdd:COG3096 633 QQLLERE-REATVERDELAARKQALESQIERLSQpggAEDPRLLA 676
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
223-330 |
3.42e-10 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 60.68 E-value: 3.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 223 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLP----REKGRMRFHKLQNVQIALDFLKH 298
Cdd:cd21222 10 APEKLAEVKELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMED 89
|
90 100 110
....*....|....*....|....*....|..
gi 1207141724 299 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21222 90 AGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2256-2639 |
3.50e-10 |
|
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: 66.69 E-value: 3.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2256 QKAQNVLVQQNK-DSMAQDKLKEEFEKakkLAQEAEKAKDNAEKEAAllhkKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2334
Cdd:pfam17380 281 QKAVSERQQQEKfEKMEQERLRQEKEE---KAREVERRRKLEEAEKA----RQAEMDRQAAIYAEQERMAMERERELERI 353
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2335 RKEAEKEASRRAEaeaaalklKQEADSEMAKYKKLAektlkqkssveeelvkvKVQLDETDKQKsvldvelkRLKQEVSD 2414
Cdd:pfam17380 354 RQEERKRELERIR--------QEEIAMEISRMRELE-----------------RLQMERQQKNE--------RVRQELEA 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2415 AIKQKAQVEDELSKVKIQMEDllklklkiekenQELMKKDKDNTKKlleeeaENMKKLAEEAARlnieaqEAARLRQiae 2494
Cdd:pfam17380 401 ARKVKILEEERQRKIQQQKVE------------MEQIRAEQEEARQ------REVRRLEEERAR------EMERVRL--- 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2495 SDLAKQRElaekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEakKEMQQRLdqetegfQKSLEAERKRQLeI 2574
Cdd:pfam17380 454 EEQERQQQ-----VERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILE--KELEERK-------QAMIEEERKRKL-L 518
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2575 TAEAEKlkvKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQ 2639
Cdd:pfam17380 519 EKEMEE---RQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQ 580
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1700-1919 |
5.13e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.83 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1700 AQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledLEKFKLQA-EEAERHLKQAELEKQRQIQVVEEVA 1778
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQ-----------------LEKERLAAqEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1779 KKTAATQLESKQVAltARLEESLKneqvmviqlQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRlRLQAEEEA 1857
Cdd:PRK09510 140 KAAAAAKAKAEAEA--KRAAAAAK---------KAAAEAKKKAEAEAAkKAAAEAKKKAEAEAAAKAAAEA-KKKAEAEA 207
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 1858 NKKTaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1919
Cdd:PRK09510 208 KKKA-------------AAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2368-2799 |
5.94e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 65.56 E-value: 5.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2368 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkieken 2447
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAE------------- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2448 qelmkkdkdntkklLEEEAENMKKL-AEEAARLNIEAQEAARLRQIAEsdlaKQRELAEKMLEEKKQAIQEAAKLKAEAE 2526
Cdd:COG4717 141 --------------LAELPERLEELeERLEELRELEEELEELEAELAE----LQEELEELLEQLSLATEEELQDLAEELE 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2527 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQ-SKAEEEAKKFKKQ 2605
Cdd:COG4717 203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLlSLILTIAGVLFLV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2606 ADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKT 2685
Cdd:COG4717 283 LGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2686 ILQQSFFAEKETLLKKEKAIEEEK-KKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ-KEAEEEMN 2763
Cdd:COG4717 363 LQLEELEQEIAALLAEAGVEDEEElRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELE 442
|
410 420 430
....*....|....*....|....*....|....*...
gi 1207141724 2764 GKQKEMQDL--EKKRIEQEKLLAEENKNLREKLQQLQS 2799
Cdd:COG4717 443 ELEEELEELreELAELEAELEQLEEDGELAELLQELEE 480
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1699-2132 |
6.07e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.86 E-value: 6.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1699 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1778
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1779 KKTAATQLESKQVALTARLEESLKneqvmviQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEAN 1858
Cdd:PRK03918 266 ERIEELKKEIEELEEKVKELKELK-------EKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING-IEERIKELEEKE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1859 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK--------QKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHA 1930
Cdd:PRK03918 338 ERLEELKKKLKELEKRLEELEERHELYEEAKAkkeelerlKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1931 EQQRTVLDDELQRLKNDVNSAVKQKKELEE------------ELIKVRKEMEILLQQKSKAEKEtMSNTEKsKQLLESEA 1998
Cdd:PRK03918 418 KKEIKELKKAIEELKKAKGKCPVCGRELTEehrkelleeytaELKRIEKELKEIEEKERKLRKE-LRELEK-VLKKESEL 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1999 AKMRELAEEatkLRSVAEEAKKqrqIAEEEAARQRAEAEK-------------ILKEKLTAINEATRLKTEAEIALKEKE 2065
Cdd:PRK03918 496 IKLKELAEQ---LKELEEKLKK---YNLEELEKKAEEYEKlkekliklkgeikSLKKELEKLEELKKKLAELEKKLDELE 569
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2066 AENDRLKRKAEEEGYqrKVLEDqaaqhkqaIEEKIGQLKKSSD--TELDRQKKIVEETLKQRKVVEEEI 2132
Cdd:PRK03918 570 EELAELLKELEELGF--ESVEE--------LEERLKELEPFYNeyLELKDAEKELEREEKELKKLEEEL 628
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1747-2521 |
6.80e-10 |
|
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: 66.02 E-value: 6.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1747 EKFKLQAEEAERHLKQAELekqrqIQVVEEVAKKTAATQLESKQVaLTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAD 1826
Cdd:pfam12128 214 PKSRLNRQQVEHWIRDIQA-----IAGIMKIRPEFTKLQQEFNTL-ESAELRLSHLHFGYKSDETLIASRQEERQETSAE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1827 KAREQAEKELEtWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA---KKRAKAEEAALKQKEAAEME----- 1898
Cdd:pfam12128 288 LNQLLRTLDDQ-WKEKRDE-LNGELSAADAAVAKDRSELEALEDQHGAFLDAdieTAAADQEQLPSWQSELENLEerlka 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1899 -LGNQRKMAEETAKQKLAAEQELIR--------LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKK---ELEEELIKVR 1966
Cdd:pfam12128 366 lTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELREQLEAGKlefNEEEYRLKSR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1967 KEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA 2046
Cdd:pfam12128 446 LGELKLRLNQATATPELLLQLENFDERIE----RAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSA 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2047 INEATRLKTEAEIALKEkeaendrlkrkaeeegyqrkVLEDQAAQHKQAIEEKIgqlkkssDTELDRQKKIVEETLKQRK 2126
Cdd:pfam12128 522 LDELELQLFPQAGTLLH--------------------FLRKEAPDWEQSIGKVI-------SPELLHRTDLDPEVWDGSV 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2127 VVEEEIHILKLNFEKAS-----SGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeaKVKQIQAA 2201
Cdd:pfam12128 575 GGELNLYGVKLDLKRIDvpewaASEEELRERLDKAEEALQSAREKQAAAEEQLVQANG--------------ELEKASRE 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2202 EEEAARQHKAAQEEVGRL--MKLAEEAKKQKEIAEKEAEKQVILVQEAAQKcSAAEQKAQNVLVQQNKD----SMAQDKL 2275
Cdd:pfam12128 641 ETFARTALKNARLDLRRLfdEKQSEKDKKNKALAERKDSANERLNSLEAQL-KQLDKKHQAWLEEQKEQkreaRTEKQAY 719
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2276 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER------------QKKAAEAEAAKQAKAQEDAEKLRKEA-EKEA 2342
Cdd:pfam12128 720 WQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYkrdlaslgvdpdVIAKLKREIRTLERKIERIAVRRQEVlRYFD 799
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2343 SRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQK--- 2419
Cdd:pfam12128 800 WYQETWLQRRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLRGLRCEMSKLATLKeda 879
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2420 --AQVEDELSKVKIQMED-LLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNieaqeAARLRQIAESD 2496
Cdd:pfam12128 880 nsEQAQGSIGERLAQLEDlKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREEDHYQN-----DKGIRLLDYRK 954
|
810 820
....*....|....*....|....*.
gi 1207141724 2497 LAKQRE-LAEKMLEEKKQAIQEAAKL 2521
Cdd:pfam12128 955 LVPYLEqWFDVRVPQSIMVLREQVSI 980
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1747-2095 |
7.07e-10 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 65.42 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1747 EKFKLQAEEAERHLK------QAELEKQRQIQVVE----------------EVAKKTAATQLESK-QVALTARLEESLKN 1803
Cdd:NF033838 54 ESQKEHAKEVESHLEkilseiQKSLDKRKHTQNVAlnkklsdikteylyelNVLKEKSEAELTSKtKKELDAAFEQFKKD 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1804 eqvmVIQLQEEAEHLKKQQAEAD-KAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRA 1882
Cdd:NF033838 134 ----TLEPGKKVAEATKKVEEAEkKAKDQKEEDRRNYPTNTYKTLELEIAESDVEVKKAELELVKEEAKEPRDEEKIKQA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1883 KAEEAAlKQKEAAEME-LGNQRKMAEETAKQKLAAEQE--LIRLRADFEHAEQQRTVLDDELQRL------KNDVNS--- 1950
Cdd:NF033838 210 KAKVES-KKAEATRLEkIKTDREKAEEEAKRRADAKLKeaVEKNVATSEQDKPKRRAKRGVLGEPatpdkkENDAKSsds 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1951 ----------AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSkqlLESEAAKMRELAEEAtKLRSVAEEAKK 2020
Cdd:NF033838 289 svgeetlpspSLKPEKKVAEAEKKVEEAKKKAKDQKEEDRRNYPTNTYKT---LELEIAESDVKVKEA-ELELVKEEAKE 364
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2021 QRQIAEEEAARQRAEAEKIlkekltainEATRL-KTEAEIALKEKEAendrlKRKAEEEgyqRKVLEDQAAQHKQA 2095
Cdd:NF033838 365 PRNEEKIKQAKAKVESKKA---------EATRLeKIKTDRKKAEEEA-----KRKAAEE---DKVKEKPAEQPQPA 423
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1302-2027 |
8.09e-10 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.47 E-value: 8.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1302 VIRSTQGAEDILNKYENqLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQatfDRLEEELQRATEVNKRMSQLHSERDvE 1381
Cdd:PRK03918 150 VVRQILGLDDYENAYKN-LGEV------IKEIKRRIERLEKFIKRTENIE---ELIKEKEKELEEVLREINEISSELP-E 218
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1382 LEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYdwlirwiadakqrqdklhavpiggsKGLQEQLTQEKK 1461
Cdd:PRK03918 219 LREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKI-------------------------RELEERIEELKK 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1462 LLEEIEKNKDKVEDCQKFAKGYIDAIKDYElqlvtykalvepiasplkkaKMESASDDIIQEYVTLRTRYSELmtlssqy 1541
Cdd:PRK03918 274 EIEELEEKVKELKELKEKAEEYIKLSEFYE--------------------EYLDELREIEKRLSRLEEEINGI------- 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1542 ikfiietQRRLQDEEKaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKdevskrqdvavdsek 1621
Cdd:PRK03918 327 -------EERIKELEE------------KEERLEELKKKLKELEKRLEELEERHELYEEAKAKKE--------------- 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1622 qkhNIQRELQELKTLSEQEIKAKSQQVEEAllsRTRIEEEIHII---RLQLETTMKQKNTAETELLQLRAKAV------- 1691
Cdd:PRK03918 373 ---ELERLKKRLTGLTPEKLEKELEELEKA---KEEIEEEISKItarIGELKKEIKELKKAIEELKKAKGKCPvcgrelt 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1692 --DADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQR 1769
Cdd:PRK03918 447 eeHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRE-----LEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELE 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1770 qiqvveevAKKTAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL 1849
Cdd:PRK03918 522 --------KKAEEYEKLKEKLIKLKGEI-KSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEE 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1850 RLQAEEEANKKTAaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEH 1929
Cdd:PRK03918 593 RLKELEPFYNEYL--------------ELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEKKYSE 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1930 AEQQRtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlqqksKAEKETMSNTEKSKQLLESEAAKMRELAEEAT 2009
Cdd:PRK03918 659 EEYEE--LREEYLELSRELAGLRAELEELEKRREEIKKTLEKL-----KEELEEREKAKKELEKLEKALERVEELREKVK 731
|
730 740
....*....|....*....|
gi 1207141724 2010 KLRSVAEEA--KKQRQIAEE 2027
Cdd:PRK03918 732 KYKALLKERalSKVGEIASE 751
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2451-2613 |
8.97e-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: 64.10 E-value: 8.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2451 MKKDKDNTKKLLEEEAENMKK--LAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKL 2528
Cdd:TIGR02794 62 AAKKEQERQKKLEQQAEEAEKqrAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAE 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2529 QKQKDQAQveAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT--AEAEKLKVKVTQlsdAQSKAEEEAKKFKKQA 2606
Cdd:TIGR02794 142 RKAKEEAA--KQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEakAKAEEAKAKAEA---AKAKAAAEAAAKAEAE 216
|
....*..
gi 1207141724 2607 DEIKIRL 2613
Cdd:TIGR02794 217 AAAAAAA 223
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1112-1920 |
9.85e-10 |
|
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: 65.38 E-value: 9.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1112 KTLRVEEYRLTLKNLEQHYQAFLRDSQDSGLFGADDRMQAENSYNKATQHYDNLLRSVEQEPALIQKDSTSGEQDESVCK 1191
Cdd:pfam02463 217 EKLELEEEYLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1192 SYITQIKDLRLRLEGCESRTVNRLRQMVDKEplkactqraTEQKKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVL 1271
Cdd:pfam02463 297 ELKSELLKLERRKVDDEEKLKESEKEKKKAE---------KELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEK 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1272 RSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNKVpvNEKEIEASQTQLQKLRSEAEGKQ 1351
Cdd:pfam02463 368 LEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLK--EEKKEELEILEEEEESIELKQGK 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1352 ATFDRLEEELQRATEVNKRMS------QLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAY----- 1420
Cdd:pfam02463 446 LTEEKEELEKQELKLLKDELElkksedLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVggrii 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1421 RESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEE----------IEKNKDKVEDCQKFAKGYIDAIKDY 1490
Cdd:pfam02463 526 SAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALtelplgarklRLLIPKLKLPLKSIAVLEIDPILNL 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1491 EL---------QLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEK 1561
Cdd:pfam02463 606 AQldkatleadEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKA 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1562 LKEEERkkmAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQdvAVDSEKQKHNIQRELQELKTLSEQEI 1641
Cdd:pfam02463 686 ESELAK---EEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKI--NEELKLLKQKIDEEEEEEEKSRLKKE 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1642 KAKSQQVEEALLSRTRIEEEIHIIRLQLEttmKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKA 1721
Cdd:pfam02463 761 EKEEEKSELSLKEKELAEEREKTEKLKVE---EEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1722 EEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESL 1801
Cdd:pfam02463 838 LALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKEN 917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1802 KNEQVMV------IQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL------RLQAEEEANKKTAAQEEAEK 1869
Cdd:pfam02463 918 EIEERIKeeaeilLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEElgkvnlMAIEEFEEKEERYNKDELEK 997
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 1870 QKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEL 1920
Cdd:pfam02463 998 ERLEEEKKKLIRAIIEETCQRLKEFLELFVSINKGWNKVFFYLELGGSAEL 1048
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1810-2137 |
1.04e-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: 65.14 E-value: 1.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1810 QLQEEAEHLKKQ---QAEADKAREQAEK----ELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREaKKRA 1882
Cdd:pfam17380 288 QQQEKFEKMEQErlrQEKEEKAREVERRrkleEAEKARQAEMDR-QAAIYAEQERMAMERERELERIRQEERKRE-LERI 365
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1883 KAEEAALKQKEAAEME-LGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK--KELE 1959
Cdd:pfam17380 366 RQEEIAMEISRMRELErLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRleEERA 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1960 EELIKVRKEmEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEeaaRQRAEAEKI 2039
Cdd:pfam17380 446 REMERVRLE-EQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE---RKRKLLEKE 521
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2040 LKEKLTAINEATRLKTEAEIALKEKEAENDR----LKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 2115
Cdd:pfam17380 522 MEERQKAIYEEERRREAEEERRKQQEMEERRriqeQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPITTIK 601
|
330 340
....*....|....*....|..
gi 1207141724 2116 KIVEETLKQRKVVEEEIHILKL 2137
Cdd:pfam17380 602 PIYRPRISEYQPPDVESHMIRF 623
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
231-327 |
1.09e-09 |
|
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: 58.74 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 231 KKTFTKWVNKHLVKaQRHIT----------DLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 295
Cdd:cd21217 3 KEAFVEHINSLLAD-DPDLKhllpidpdgdDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 1207141724 296 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 327
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1330-2012 |
1.15e-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: 65.09 E-value: 1.15e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1330 EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE-----VNKRMSQLHSER---DVELEHYRQLVGNLRERWQAVFA 1401
Cdd:TIGR02169 250 EEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEeeqlrVKEKIGELEAEIaslERSIAEKERELEDAEERLAKLEA 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1402 QIELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAK 1481
Cdd:TIGR02169 330 EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELD 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1482 GYID--------------AIKDYELQLVTYKALVEPIASPLKKA--KMESASDDII---QEYVTLRTRYS----ELMTLS 1538
Cdd:TIGR02169 410 RLQEelqrlseeladlnaAIAGIEAKINELEEEKEDKALEIKKQewKLEQLAADLSkyeQELYDLKEEYDrvekELSKLQ 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1539 SQYIKfiIETQRRLQDEE----KAAEKLKEEERKKMAEMQAELEKQKqlaETHAKAI----------------AKAEQEA 1598
Cdd:TIGR02169 490 RELAE--AEAQARASEERvrggRAVEEVLKASIQGVHGTVAQLGSVG---ERYATAIevaagnrlnnvvveddAVAKEAI 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1599 NELK------------TKMKDE-----VSKRQDVA------VDSEKQKHN----------IQRELQELKTLS-------- 1637
Cdd:TIGR02169 565 ELLKrrkagratflplNKMRDErrdlsILSEDGVIgfavdlVEFDPKYEPafkyvfgdtlVVEDIEAARRLMgkyrmvtl 644
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1638 EQEIKAKS------------------QQVEEALLSRTRIEEeihiIRLQLETTMKQKNTAETELLQLRAKAVDADKL--- 1696
Cdd:TIGR02169 645 EGELFEKSgamtggsraprggilfsrSEPAELQRLRERLEG----LKRELSSLQSELRRIENRLDELSQELSDASRKige 720
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1697 ----RNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL-EKQRQI 1771
Cdd:TIGR02169 721 iekeIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIpEIQAEL 800
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1772 QVVEEVAkktaatqleSKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELetwrqkanEALRLRL 1851
Cdd:TIGR02169 801 SKLEEEV---------SRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEI--------ENLNGKK 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1852 QAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEaaemelgNQRKMAEETAKQKLAaeqeliRLRADFEHAE 1931
Cdd:TIGR02169 864 EELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI-------EELEAQIEKKRKRLS------ELKAKLEALE 930
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1932 QQRTVLDDELQRLKNDVNSA------VKQKKELEEELIKVrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELA 2005
Cdd:TIGR02169 931 EELSEIEDPKGEDEEIPEEElsledvQAELQRVEEEIRAL-EPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERI 1009
|
....*..
gi 1207141724 2006 EEATKLR 2012
Cdd:TIGR02169 1010 EEYEKKK 1016
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3009-3047 |
1.19e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 56.18 E-value: 1.19e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 3009 LLDCQYATGGIIDPVNSHHVPVQLACTQGQLDEDLSKIL 3047
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1489-2136 |
1.61e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 64.36 E-value: 1.61e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1489 DYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKE---E 1565
Cdd:pfam05483 38 DPAFQKLNFLPMLEQVANSGDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKiieA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1566 ERKKMAEMQAELEKqkqlaethakaiakaeqeaneLKTKMKDEVSKRQDVAVDSEKQKHnIQRELQELKTLSEQEIKAKS 1645
Cdd:pfam05483 118 QRKAIQELQFENEK---------------------VSLKLEEEIQENKDLIKENNATRH-LCNLLKETCARSAEKTKKYE 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1646 QQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETEL-LQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE 1724
Cdd:pfam05483 176 YEREETRQVYMDLNNNIEKMILAFEELRVQAENARLEMhFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLLIQITEKENK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1725 LKRKSEAEKDAAKEKKKALedlEKFKLQAEeaerHLKQAELEKQRQIQVVEEVakKTAATQLESKQVAltarLEESLKNE 1804
Cdd:pfam05483 256 MKDLTFLLEESRDKANQLE---EKTKLQDE----NLKELIEKKDHLTKELEDI--KMSLQRSMSTQKA----LEEDLQIA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1805 QVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRL---RLQAEEEANKKTAAQEEAEKQKEEAKREAKKR 1881
Cdd:pfam05483 323 TKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKIITMELQKKSSELEEMTKFKNN 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1882 AKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRL----RADFEHAEQQRTVLD-------DELQRLKNDVNS 1950
Cdd:pfam05483 403 KEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlqarEKEIHDLEIQLTAIKtseehylKEVEDLKTELEK 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1951 AVKQKKELEEELIKVRKEMEILLQQKS------KAEKETMSNTEKSKQ--------LLESEAAKMRELAEEATKLRSVAE 2016
Cdd:pfam05483 483 EKLKNIELTAHCDKLLLENKELTQEASdmtlelKKHQEDIINCKKQEErmlkqienLEEKEMNLRDELESVREEFIQKGD 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2017 EAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKV-------LE 2086
Cdd:pfam05483 563 EVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKnknIEELHQENKALKKKGSAENKQLNAyeikvnkLE 642
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2087 DQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 2136
Cdd:pfam05483 643 LELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQK 692
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2357-2578 |
1.69e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.24 E-value: 1.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2357 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2436
Cdd:COG4942 37 AELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2437 LKLKLKIEKENQElmkkDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQ 2516
Cdd:COG4942 117 GRQPPLALLLSPE----DFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2517 EAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegfqksLEAERKRQLEITAEA 2578
Cdd:COG4942 193 LKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR--------LEAEAAAAAERTPAA 246
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2273-2792 |
1.88e-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: 64.27 E-value: 1.88e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2273 DKLKEEFEKAKKLAQEAEKAKD-------NAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRR 2345
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDkflteikKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2346 AEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEE---ELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQ- 2421
Cdd:TIGR04523 200 ELLLSNLKKKIQKNKSLESQISELKKQNNQLKDNIEKkqqEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQn 279
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2422 ------VEDELSKVKIQMEDLLKLKlkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQI--- 2492
Cdd:TIGR04523 280 nkkikeLEKQLNQLKSEISDLNNQK------EQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKEltn 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2493 AESD-LAKQRELAEKmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQ 2571
Cdd:TIGR04523 354 SESEnSEKQRELEEK-QNEIEKLKKENQSYKQEIKNLESQINDLE---SKIQNQEKLNQQ-KDEQIKKLQQEKELLEKEI 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2572 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADL 2651
Cdd:TIGR04523 429 ERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKEL 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2652 EKEKEklkkeaaDLQKQSKEMaNVQQEQLQQEKTILQQSFFAEKETLLKKekaieeekkklekqfeDEVKKAEALKAE-Q 2730
Cdd:TIGR04523 509 EEKVK-------DLTKKISSL-KEKIEKLESEKKEKESKISDLEDELNKD----------------DFELKKENLEKEiD 564
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2731 ERQRKLmeeerKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLRE 2792
Cdd:TIGR04523 565 EKNKEI-----EELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEK 621
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4585-4623 |
2.25e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.41 E-value: 2.25e-09
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 4585 FLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTAQKL 4623
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
345-442 |
2.35e-09 |
|
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: 58.16 E-value: 2.35e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90
....*....|....*....
gi 1207141724 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLS 106
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
232-326 |
2.77e-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: 57.35 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 232 KTFTKWVNKHLVKA--QRHITDLYEDLRDGHNLISLLEVLSGETL------PREKGRMrfhkLQNVQIALDFLKHRQVKL 303
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEKVedingcPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 1207141724 304 VNIRNDDIADGNPKLTLGLIWTI 326
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1747-2414 |
2.97e-09 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 63.59 E-value: 2.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1747 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALtaRLEESLKNEQVMVIQ----------LQE--- 1813
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSL--KLEEEIQENKDLIKEnnatrhlcnlLKEtca 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1814 -EAEHLKKQQAEADKARE-------------QAEKELETWRQKANEALRLRLQA--------EEEANKKTAAQEEAEKQK 1871
Cdd:pfam05483 166 rSAEKTKKYEYEREETRQvymdlnnniekmiLAFEELRVQAENARLEMHFKLKEdhekiqhlEEEYKKEINDKEKQVSLL 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1872 EEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ----RTVLDDELQRLKND 1947
Cdd:pfam05483 246 LIQITEKENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRsmstQKALEEDLQIATKT 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1948 VNSAVKQKKELEEELIKVRKEMEIL----------LQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLrsvaee 2017
Cdd:pfam05483 326 ICQLTEEKEAQMEELNKAKAAHSFVvtefeattcsLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKF------ 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2018 aKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK-TEAEIAL----KEKEAENDRLK---RKAEEEGYQRKVLEDQA 2089
Cdd:pfam05483 400 -KNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKgKEQELIFllqaREKEIHDLEIQltaIKTSEEHYLKEVEDLKT 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2090 AQHKQAIE---------------EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfEKASSGKQELELELK 2154
Cdd:pfam05483 479 ELEKEKLKnieltahcdklllenKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLE---EKEMNLRDELESVRE 555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2155 KLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE 2234
Cdd:pfam05483 556 EFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYE 635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2235 KEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAAllHKKAEEAERQk 2314
Cdd:pfam05483 636 IKVNKLELELASAKQK---FEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQ--HKIAEMVALM- 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2315 kaaeaeaakqakaqedaEKLRKEAEkeasrraeaeaaalKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDET 2394
Cdd:pfam05483 710 -----------------EKHKHQYD--------------KIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSL 758
|
730 740
....*....|....*....|
gi 1207141724 2395 DKQKSVLDVELKRLKQEVSD 2414
Cdd:pfam05483 759 KKQLEIEKEEKEKLKMEAKE 778
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1574-2115 |
5.63e-09 |
|
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: 62.93 E-value: 5.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1574 QAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEAL 1652
Cdd:pfam12128 353 QSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQnNRDIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1653 LsRTRIEEEIHIIRL-QLETTMKQKNTAETELLQLRAKavdaDKLRNAAQEEAEKLRKQVaeetqkkrkaeEELKRksea 1731
Cdd:pfam12128 433 L-EFNEEEYRLKSRLgELKLRLNQATATPELLLQLENF----DERIERAREEQEAANAEV-----------ERLQS---- 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1732 ekdaakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQiqvveevakKTAATQLESKQVALTARLEESLKNEqvmviqL 1811
Cdd:pfam12128 493 -------------ELRQARKRRDQASEALRQASRRLEER---------QSALDELELQLFPQAGTLLHFLRKE------A 544
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1812 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEAL---RLRLQAEEeankktaaQEEAEKQKEEAKREAKKRAKAEEAA 1888
Cdd:pfam12128 545 PDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvKLDLKRID--------VPEWAASEEELRERLDKAEEALQSA 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1889 LKQKEAAEMELGNQRKMAEEtakqklaAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKEL-EEELIKVRK 1967
Cdd:pfam12128 617 REKQAAAEEQLVQANGELEK-------ASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSaNERLNSLEA 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1968 EMEIL---LQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklRSVAEEAKKQRQIAEEEAARQRAEA-EKILKEK 2043
Cdd:pfam12128 690 QLKQLdkkHQAWLEEQKEQKREARTEKQ------AYWQVVEGA----LDAQLALLKAAIAARRSGAKAELKAlETWYKRD 759
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2044 LTA--INEATRLKTEAEIALKEKEAENDRLKRKA---------EEEGYQRKVLEDQAAQHKQAIEEKIGQL-KKSSDTEL 2111
Cdd:pfam12128 760 LASlgVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqETWLQRRPRLATQLSNIERAISELQQQLaRLIADTKL 839
|
....
gi 1207141724 2112 DRQK 2115
Cdd:pfam12128 840 RRAK 843
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1669-1913 |
6.37e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.40 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1669 LETTMKQKNTAETELLQLRAKAVDADKlrnaAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaledlEK 1748
Cdd:TIGR02794 38 IQAVLVDPGAVAQQANRIQQQKKPAAK----KEQERQKKLEQQAEEAEKQRAAEQARQKE------------------LE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1749 FKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNeqvmviqlQEEAEHLKKQQAEADKA 1828
Cdd:TIGR02794 96 QRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--------QAEEEAKAKAAAEAKKK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1829 REQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAalkQKEAAEMELGNQRKMAEE 1908
Cdd:TIGR02794 168 AEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEA---ERKADEAELGDIFGLASG 243
|
....*
gi 1207141724 1909 TAKQK 1913
Cdd:TIGR02794 244 SNAEK 248
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1196-1926 |
6.66e-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: 62.78 E-value: 6.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1196 QIKDLRLRLEGCESR------TVNRLRQMVDKEPLKACTQRATEQKKVQTELEGIKKDLDKVvEKSEAVLATSQQSSSAP 1269
Cdd:TIGR02169 245 QLASLEEELEKLTEEiselekRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASL-ERSIAEKERELEDAEER 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1270 V--LRSEIDITQKKMEhvyGLSSVYLDKLKTIDLVIRSTQGAEDILNKYENQLREVNK-VPVNEKEIEASQTQLQKLRSE 1346
Cdd:TIGR02169 324 LakLEAEIDKLLAEIE---ELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKeFAETRDELKDYREKLEKLKRE 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1347 AEGKQATFDRLEEELQRATE-----------VNKRMSQLHSERDV-----------------ELEHYRQLVGNLRERWQA 1398
Cdd:TIGR02169 401 INELKRELDRLQEELQRLSEeladlnaaiagIEAKINELEEEKEDkaleikkqewkleqlaaDLSKYEQELYDLKEEYDR 480
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1399 VFAQIELRQRELDLLNRQMQAYRESydwlirwIADAKQRQDKLHAvPIGGSKGLQEQLTQ-EKKLLEEIE---------- 1467
Cdd:TIGR02169 481 VEKELSKLQRELAEAEAQARASEER-------VRGGRAVEEVLKA-SIQGVHGTVAQLGSvGERYATAIEvaagnrlnnv 552
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1468 --KNKDKVEDCQKFAK------------------------GYIDAIKDYELQLVTYKALVEPI-----ASPLKKAKMESA 1516
Cdd:TIGR02169 553 vvEDDAVAKEAIELLKrrkagratflplnkmrderrdlsiLSEDGVIGFAVDLVEFDPKYEPAfkyvfGDTLVVEDIEAA 632
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1517 SDDIIQ-EYVTLRTRYSE---LMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkmAEMQAELEKQKQLAETHAKAIA 1592
Cdd:TIGR02169 633 RRLMGKyRMVTLEGELFEksgAMTGGSRAPRGGILFSRSEPAEL--------------QRLRERLEGLKRELSSLQSELR 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1593 KAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETT 1672
Cdd:TIGR02169 699 RIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEEL-EEDLSSLEQEIENVKSELKELEARIEELEEDLHKL 777
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1673 MKQKNTAETELLQLRAKAVdadklrnaaQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQ 1752
Cdd:TIGR02169 778 EEALNDLEARLSHSRIPEI---------QAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1753 AEEAERhlKQAELEKQrqiqvveevaKKTAATQLESKQVALtARLEESLKNeqvmviqLQEEAEHLKKQQAEADKAREQA 1832
Cdd:TIGR02169 849 IKSIEK--EIENLNGK----------KEELEEELEELEAAL-RDLESRLGD-------LKKERDELEAQLRELERKIEEL 908
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1833 EKELETWRQKANEaLRLRLQAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEET 1909
Cdd:TIGR02169 909 EAQIEKKRKRLSE-LKAKLEALEEELSeieDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKR 987
|
810 820
....*....|....*....|...
gi 1207141724 1910 ------AKQKLAAEQELIRLRAD 1926
Cdd:TIGR02169 988 ldelkeKRAKLEEERKAILERIE 1010
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4507-4544 |
7.28e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 7.28e-09
10 20 30
....*....|....*....|....*....|....*...
gi 1207141724 4507 QRLLEAQACTGGIIDPNTGEKFSVADAQNKGLVDKIMV 4544
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2381-2608 |
8.83e-09 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 61.00 E-value: 8.83e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2381 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekeNQELmkkdkdntKK 2460
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKL----------QAEI--------AE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2461 LLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES----DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQ 2536
Cdd:COG3883 77 AEAEIEERREELGERARALYRSGGSVSYLDVLLGSesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKL 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2537 VEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2608
Cdd:COG3883 157 AELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1221-2075 |
8.87e-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: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1221 KEPLKACTQRATEQKKVQT---ELEGIKKDLDKVVEKSEAVLATSQQSSS--APVLRSEIDITQKKMEHVYGlssvyldk 1295
Cdd:TIGR02169 230 KEKEALERQKEAIERQLASleeELEKLTEEISELEKRLEEIEQLLEELNKkiKDLGEEEQLRVKEKIGELEA-------- 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1296 lkTIDLVIRSTQGAEDILNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ-RATEVNKRMSQL 1374
Cdd:TIGR02169 302 --EIASLERSIAEKERELEDAEERLAKL------EAEIDKLLAEIEELEREIEEERKRRDKLTEEYAeLKEELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1375 HSErDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQE 1454
Cdd:TIGR02169 374 EEV-DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKK 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1455 QLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPI--ASPLKKAKMESASDDIIQEYVTLRtrys 1532
Cdd:TIGR02169 453 QEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASeeRVRGGRAVEEVLKASIQGVHGTVA---- 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1533 ELMTLSSQYIKFI-IETQRRLQ-----DEEKAAEKLkeeerkkmaemqaELEKQKQLAETHAKAIAKAEQEANELKTKMK 1606
Cdd:TIGR02169 529 QLGSVGERYATAIeVAAGNRLNnvvveDDAVAKEAI-------------ELLKRRKAGRATFLPLNKMRDERRDLSILSE 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1607 DEVSKRQDVAVDSEKQKHNIQRE-------LQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKnta 1679
Cdd:TIGR02169 596 DGVIGFAVDLVEFDPKYEPAFKYvfgdtlvVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGGSRAPRGGILFSRSE--- 672
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1680 ETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaaKEKKKALEDLEKFKLQAEEAERH 1759
Cdd:TIGR02169 673 PAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIE-------KEIEQLEQEEEKLKERLEELEED 745
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1760 LKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMviQLQEEAEHLKKQQAEADKAREQAEKELet 1838
Cdd:TIGR02169 746 LSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlNDLEARLSHSRIP--EIQAELSKLEEEVSRIEARLREIEQKL-- 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1839 wrqkaNEALRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAKAEEAALkqkEAAEMELGNQRKMAEETAKQKLAAEQ 1918
Cdd:TIGR02169 822 -----NRLTLEKEYLEKEIQEL-----------QEQRIDLKEQIKSIEKEI---ENLNGKKEELEEELEELEAALRDLES 882
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1919 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELikvrkemEILLQQKSKAEKETMSNTEKSKQLLESE- 1997
Cdd:TIGR02169 883 RLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKL-------EALEEELSEIEDPKGEDEEIPEEELSLEd 955
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 1998 -AAKMRELAEEATKLRSVAEEAKKQrqiAEEEAARQraeaeKILKEKLtaineaTRLKTEAEiALKEKEAENDRLKRKA 2075
Cdd:TIGR02169 956 vQAELQRVEEEIRALEPVNMLAIQE---YEEVLKRL-----DELKEKR------AKLEEERK-AILERIEEYEKKKREV 1019
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
2357-2635 |
1.27e-08 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 60.89 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2357 QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQldetdkqksvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDL 2436
Cdd:pfam03528 14 EKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEE-------------DLKRQNAVLQEAQVELDALQNQLALARAEMENI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2437 LKLKLKIEKENQELMkkdkDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQ 2516
Cdd:pfam03528 81 KAVATVSENTKQEAI----DEVKSQWQEEVASLQAIMKETVR-EYEVQFHRRLEQ-ERAQWNQYRESAEREIADLRRRLS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2517 EAAklkaEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ------ETEGFQKSLEAERKRQLEITAEAEK-----LKVKV 2585
Cdd:pfam03528 155 EGQ----EEENLEDEMKKAQEDAEKLRSVVMPMEKEIAAlkakltEAEDKIKELEASKMKELNHYLEAEKscrtdLEMYV 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2586 TQLSDAQSKAEEEAKKFKKQADEIKIRL-QETEKHTSEKHTVVEK----LEVQRL 2635
Cdd:pfam03528 231 AVLNTQKSVLQEDAEKLRKELHEVCHLLeQERQQHNQLKHTWQKAndqfLESQRL 285
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1868-2077 |
1.28e-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: 1.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1868 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKmaeetakqklAAEQELIRLRADFEHAEQQRTVLDDELQRLKND 1947
Cdd:COG4942 22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA----------ALERRIAALARRIRALEQELAALEAELAELEKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1948 VNSAVKQKKELEEELIKV---------RKEMEILLQQKSKAEKETMSNTEKS-KQLLESEAAKMRELAEEATKLRSVAEE 2017
Cdd:COG4942 92 IAELRAELEAQKEELAELlralyrlgrQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2018 AKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE 2077
Cdd:COG4942 172 ERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
230-329 |
1.35e-08 |
|
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: 55.59 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 230 QKKTFTKWVNKhlVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKG-----RMRFHKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILH 329
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1896-2639 |
1.92e-08 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 61.29 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1896 EMELGNQRKMAEETAKQKLAaeqeliRLRADFEHAEQqrtvlddELQRLKNDVNSA-VKQKKELEEELIKVRKEMeillq 1974
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEHIE------RVLEEYSHQVK-------DLQRRLNESNELhEKQKFYLRQSVIDLQTKL----- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1975 QKSKAEKETMSNTEKSkqllesEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLK 2054
Cdd:pfam15921 120 QEMQMERDAMADIRRR------ESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQEIRSIL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2055 TEAEIALKEKEAENDRL-----KRKAEEEGYQRKVLEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRk 2126
Cdd:pfam15921 194 VDFEEASGKKIYEHDSMstmhfRSLGSAISKILRELDTEISYLKGRIfpvEDQLEALKSESQNKIELLLQQHQDRIEQL- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2127 VVEEEIHILKLNfEKASSGKQELELELKKLKGIADETQKskakaeEEAEKFRKLAleeekkrkEAEAKVKQIQAAEEEAA 2206
Cdd:pfam15921 273 ISEHEVEITGLT-EKASSARSQANSIQSQLEIIQEQARN------QNSMYMRQLS--------DLESTVSQLRSELREAK 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2207 RQHKAAQEEVGRLMKLAE----EAKKQKEIAEKEA-------EKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2275
Cdd:pfam15921 338 RMYEDKIEELEKQLVLANseltEARTERDQFSQESgnlddqlQKLLADLHKREKELSLEKEQNKRLWDRDTGNSITIDHL 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2276 KEEFEKAKKLAQEAE--------KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKL--RKEAEKEASRR 2345
Cdd:pfam15921 418 RRELDDRNMEVQRLEallkamksECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEMLRKVVEELtaKKMTLESSERT 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2346 AEAEAAALKLKQEA----DSEMAKYK-----KLAE-KTLKQKS----SVEEELVKVKVQLDETDKQKSVLDVELKRLKQE 2411
Cdd:pfam15921 498 VSDLTASLQEKERAieatNAEITKLRsrvdlKLQElQHLKNEGdhlrNVQTECEALKLQMAEKDKVIEILRQQIENMTQL 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2412 V------SDAIK-QKAQVEDELSKVKIQMEDLlklklkiekenqELMKKDKDNTKKLLEEEAENMkklaeEAARLNIEAQ 2484
Cdd:pfam15921 578 VgqhgrtAGAMQvEKAQLEKEINDRRLELQEF------------KILKDKKDAKIRELEARVSDL-----ELEKVKLVNA 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2485 EAARLRqiAESDLAKQRElaeKMLEEKKQAIQEAAKLKAEAEKLQK----QKDQAQVEAQKLLEAKKEMQQRLDQeTEGF 2560
Cdd:pfam15921 641 GSERLR--AVKDIKQERD---QLLNEVKTSRNELNSLSEDYEVLKRnfrnKSEEMETTTNKLKMQLKSAQSELEQ-TRNT 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2561 QKSLEAERKR--------QLEITA---EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEK 2629
Cdd:pfam15921 715 LKSMEGSDGHamkvamgmQKQITAkrgQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLS---QELSTVATEKNKMAGE 791
|
810
....*....|
gi 1207141724 2630 LEVQRLQSKQ 2639
Cdd:pfam15921 792 LEVLRSQERR 801
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
345-442 |
1.93e-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: 1.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 345 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGVTRLLD 423
Cdd:cd21315 16 TPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDVPQLIK 92
|
90
....*....|....*....
gi 1207141724 424 PEDVDVPHPDEKSIITYVS 442
Cdd:cd21315 93 PEEMVNPKVDELSMMTYLS 111
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1937-2690 |
2.07e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.14 E-value: 2.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1937 LDDELQRLKNDVNSAVKQKKELEEELIKV--RKEMEILLQQKSKAEKETMSNT--------EKSKQLLESEAAK-MRELA 2005
Cdd:TIGR00618 83 LGTKIYRVHRTLRCTRSHRKTEQPEQLYLeqKKGRGRILAAKKSETEEVIHDLlkldyktfTRVVLLPQGEFAQfLKAKS 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2006 EEATKLRSVAEEAKKQRQIAeeeaarqrAEAEKILKEkltaineatrLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVL 2085
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLA--------LMEFAKKKS----------LHGKAELLTLRSQLLTLCTPCMPDTYHERKQVL 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2086 EDQAAQhkqaIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL-NFEKASSGKQELELELKKLKGIADETQ 2164
Cdd:TIGR00618 225 EKELKH----LREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELrAQEAVLEETQERINRARKAAPLAAHIK 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2165 ----------------KSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAA---QEEVGRLMKLAEE 2225
Cdd:TIGR00618 301 avtqieqqaqrihtelQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAtsiREISCQQHTLTQH 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2226 AKKQKEIAEKEAEKQVILVQE-----AAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEA 2300
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKEldilqREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIH 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2301 ALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSV 2380
Cdd:TIGR00618 461 LQESAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQL 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2381 EEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVK---------IQMEDLLKLKLKIEKENQELM 2451
Cdd:TIGR00618 541 ETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQnitvrlqdlTEKLSEAEDMLACEQHALLRK 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2452 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEA--------QEAARLRQIAESDLAKQRELAEKMLEEKKQAI-------- 2515
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQltltqervREHALSIRVLPKELLASRQLALQKMQSEKEQLtywkemla 700
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2516 QEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgFQKSLEAERKRQLEITAEAEKLK----VKVTQLSDA 2591
Cdd:TIGR00618 701 QCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQ-SLKELMHQARTVLKARTEAHFNNneevTAALQTGAE 779
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2592 QSKAEEEAKKFKKQADEIKIRLQETE-KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKeaadLQKQSK 2670
Cdd:TIGR00618 780 LSHLAAEIQFFNRLREEDTHLLKTLEaEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLGEITH----QLLKYE 855
|
810 820
....*....|....*....|
gi 1207141724 2671 EMANVQQEQLQQEKTILQQS 2690
Cdd:TIGR00618 856 ECSKQLAQLTQEQAKIIQLS 875
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2296-2799 |
2.54e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.82 E-value: 2.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2296 AEKEAALLHKKAEEAErqkkaaeaeaakQAKAQEDAEKLRKEAEKEASRRAeaeaaalklKQEADSEMAKYkklaEKTLK 2375
Cdd:PRK02224 197 EEKEEKDLHERLNGLE------------SELAELDEEIERYEEQREQARET---------RDEADEVLEEH----EERRE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2376 QKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSD-----------------AIKQKAQVEDELSKVKIQMEDLLK 2438
Cdd:PRK02224 252 ELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEEleeerddllaeaglddaDAEAVEARREELEDRDEELRDRLE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2439 LKLKIEKENQELMKKDKDNTKKlLEEEAenmKKLAEEAARLNIEAQEAARLRQIAESDLAK-----------------QR 2501
Cdd:PRK02224 332 ECRVAAQAHNEEAESLREDADD-LEERA---EELREEAAELESELEEAREAVEDRREEIEEleeeieelrerfgdapvDL 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2502 ELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2581
Cdd:PRK02224 408 GNAEDFLEELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDL 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2582 KVKVTQLSDAQSKAeEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEvQRLQSKQEADGLHKAIADLEKEKEKLKKE 2661
Cdd:PRK02224 488 EEEVEEVEERLERA-EDLVEAEDRIERLEERREDLEELIAERRETIEEKR-ERAEELRERAAELEAEAEEKREAAAEAEE 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2662 AADLQKQSKEMANVQQEQLQQEKTILqqsffAEKETLLKKEKAIEEEKKKLEKQFED----EVKKAEALKAEQERQRKL- 2736
Cdd:PRK02224 566 EAEEAREEVAELNSKLAELKERIESL-----ERIRTLLAAIADAEDEIERLREKREAlaelNDERRERLAEKRERKRELe 640
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2737 --MEEER-KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKK------RIEQEKLLAEENKNLREKLQQLQS 2799
Cdd:PRK02224 641 aeFDEARiEEAREDKERAEEYLEQVEEKLDELREERDDLQAEigavenELEELEELRERREALENRVEALEA 712
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1886-2573 |
2.60e-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: 2.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1886 EAALKQKEAAEMELGNQRKmaEETAKQKLAAEQELIRLRADFEHAEQQRTvLDDELQRLKNDVNSavkQKKELEEELIKV 1965
Cdd:pfam12128 247 QQEFNTLESAELRLSHLHF--GYKSDETLIASRQEERQETSAELNQLLRT-LDDQWKEKRDELNG---ELSAADAAVAKD 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1966 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEE----ATKLRSVAEEAKKQRQIAEEEAARQRAEaekiLK 2041
Cdd:pfam12128 321 RSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERlkalTGKHQDVTAKYNRRRSKIKEQNNRDIAG----IK 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2042 EKLTAINEA-TRLKTEAEIALKEKEA----ENDRLKRKAEEEGYQrkvledqaaqhkqaIEEKIGQLKKSSDteldrQKK 2116
Cdd:pfam12128 397 DKLAKIREArDRQLAVAEDDLQALESelreQLEAGKLEFNEEEYR--------------LKSRLGELKLRLN-----QAT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2117 IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQkskakaeeeaekfRKLALeeekkrkeAEAKVK 2196
Cdd:pfam12128 458 ATPELLLQLENFDERIERAREEQEAANAEVERLQSELRQARKRRDQAS-------------EALRQ--------ASRRLE 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2197 QIQAAEEEAARQHKAAQeevGRLMK-LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVL---------VQQN 2266
Cdd:pfam12128 517 ERQSALDELELQLFPQA---GTLLHfLRKEAPDWEQSIGKVISPELLHRTDLDPEVWDGSVGGELNLygvkldlkrIDVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2267 KDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakAQEDAEKLRKEAEkeasrra 2346
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASR--------------EETFARTALKNAR------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2347 eaeaaaLKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDEL 2426
Cdd:pfam12128 653 ------LDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGA 726
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2427 SKVKI-QMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES---------- 2495
Cdd:pfam12128 727 LDAQLaLLKAAIAARRSGAKAELKALETWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRyfdwyqetwl 806
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2496 ----DLAKQRELAEKMLEEKKQ---AIQEAAKLK-AEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL-----DQETEGFQK 2562
Cdd:pfam12128 807 qrrpRLATQLSNIERAISELQQqlaRLIADTKLRrAKLEMERKASEKQQVRLSENLRGLRCEMSKLatlkeDANSEQAQG 886
|
730
....*....|.
gi 1207141724 2563 SLeAERKRQLE 2573
Cdd:pfam12128 887 SI-GERLAQLE 896
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1879-2615 |
3.02e-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: 60.51 E-value: 3.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1879 KKRAKAEEAALKQKEAaemELGNQRKM--AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR-----LKNDVNSA 1951
Cdd:pfam05483 91 KKWKVSIEAELKQKEN---KLQENRKIieAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRhlcnlLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1952 VKQKKELEEELIKVRkemEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAAR 2031
Cdd:pfam05483 168 AEKTKKYEYEREETR---QVYMDLNNNIEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSL 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2032 ---QRAEAEKILKEkLTAINEATRLKTEAeiaLKEK-EAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIeekigqlkkSS 2107
Cdd:pfam05483 245 lliQITEKENKMKD-LTFLLEESRDKANQ---LEEKtKLQDENLKELIEKKDHLTKELEDIKMSLQRSM---------ST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2108 DTELDRQKKIVEETLKQRkVVEEEIHILKLNfeKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKK 2187
Cdd:pfam05483 312 QKALEEDLQIATKTICQL-TEEKEAQMEELN--KAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQK 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2188 RKEAEAKVKQIQAAEEEAARQHKAAqeeVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQNK 2267
Cdd:pfam05483 389 KSSELEEMTKFKNNKEVELEELKKI---LAEDEKLLDEKKQFEKIAEELKGKE----QELIFLLQAREKEIHDLEIQLTA 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2268 DSMAQDKLKEEFEKAKKlaqEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAE 2347
Cdd:pfam05483 462 IKTSEEHYLKEVEDLKT---ELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIEN 538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2348 AEAAALKLKQEADSemakykklAEKTLKQKSSveeelvKVKVQLDETDKQKsvldvelKRLKQEVSDAIKQKAQVEDELS 2427
Cdd:pfam05483 539 LEEKEMNLRDELES--------VREEFIQKGD------EVKCKLDKSEENA-------RSIEYEVLKKEKQMKILENKCN 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2428 KVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAE-NMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEk 2506
Cdd:pfam05483 598 NLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKvNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEE- 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2507 mLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLDQETE---GFQKSLEAERKR-QLEITAEAEKLK 2582
Cdd:pfam05483 677 -VEKAKAIADEAVKLQKEIDKRCQHK---IAEMVALMEKHKHQYDKIIEERDselGLYKNKEQEQSSaKAALEIELSNIK 752
|
730 740 750
....*....|....*....|....*....|...
gi 1207141724 2583 VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQE 2615
Cdd:pfam05483 753 AELLSLKKQLEIEKEEKEKLKMEAKENTAILKD 785
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2717-2901 |
3.24e-08 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 60.23 E-value: 3.24e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2717 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ--------KEAEEEMNGKQKEMQDLEKKRIEQ--EKLLAEE 2786
Cdd:PRK00409 533 EQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAekeaqqaiKEAKKEADEIIKELRQLQKGGYASvkAHELIEA 612
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2787 NKNLREKLQQLQSSQKASYTKEIEIQT-DKVPEEELVQMTMVETTKKvlngstevdgvKKDVPLAFDGIREKVPASRLHE 2865
Cdd:PRK00409 613 RKRLNKANEKKEKKKKKQKEKQEELKVgDEVKYLSLGQKGEVLSIPD-----------DKEAIVQAGIMKMKVPLSDLEK 681
|
170 180 190
....*....|....*....|....*....|....*.
gi 1207141724 2866 IGVLSKKEydklKKGKTTVQELSKNDKVKMCLKGKD 2901
Cdd:PRK00409 682 IQKPKKKK----KKKPKTVKPKPRTVSLELDLRGMR 713
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
340-442 |
4.06e-08 |
|
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409162 Cd Length: 110 Bit Score: 54.33 E-value: 4.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 340 QSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIAERDLGV 418
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....
gi 1207141724 419 TRLLDPEDVDVPHPDEKSIITYVS 442
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLS 103
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2196-2340 |
4.14e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.70 E-value: 4.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2196 KQIQAAEEE---AARQHKAAQEEvgrlMKLAEEAKKQKEIAEKEAEKQviLVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ 2272
Cdd:TIGR02794 81 EKQRAAEQArqkELEQRAAAEKA----AKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEE 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2273 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEK 2340
Cdd:TIGR02794 155 EAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAA 222
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2460-2810 |
4.26e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 60.07 E-value: 4.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2460 KLLEEEAENMKKLAEEAARLnieaqeaarlrqiaeSDLAKQRELAEKMLEEKKQAIQE----AAKLKAEAEKLQKQKDQA 2535
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAGI---------------SKYKERRKETERKLERTRENLDRlediLNELERQLKSLERQAEKA 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2536 QvEAQKLLEAKKEMQ--------QRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2607
Cdd:TIGR02168 213 E-RYKELKAELRELElallvlrlEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELY 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2608 EIKIRLQETEKhtsekhtvveklEVQRLQSKQEADglhkaiadlekekeklkkeaadlqKQSKEMANVQQEQLQQEKTIL 2687
Cdd:TIGR02168 292 ALANEISRLEQ------------QKQILRERLANL------------------------ERQLEELEAQLEELESKLDEL 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2688 QQSFfAEKETLLKKEKAIEEekkklekQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQK 2767
Cdd:TIGR02168 336 AEEL-AELEEKLEELKEELE-------SLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1207141724 2768 EMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIE 2810
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELE 450
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2459-2782 |
4.33e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 58.78 E-value: 4.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2459 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQrELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2538
Cdd:pfam13868 35 KAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQ-ELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2539 AQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA--DEIKIRLQET 2616
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNE-EQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEekEREIARLRAQ 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2617 EKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffAEKE 2696
Cdd:pfam13868 193 QEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREE--------EEFE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2697 TLLkkekaieeekkklekqfEDEVKKAEALKAEQERQRKLMEEERKKLQSAMD---AAIKKQKEAEEEMNGKQKEMQDLE 2773
Cdd:pfam13868 265 RML-----------------RKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEereEQRAAEREEELEEGERLREEEAER 327
|
....*....
gi 1207141724 2774 KKRIEQEKL 2782
Cdd:pfam13868 328 RERIEEERQ 336
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1625-2146 |
4.39e-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: 59.66 E-value: 4.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1625 NIQRELQELKTLSEQEIKAKSQQVEEaLLSRTRIEEEIhiiRLQLETTMKQKNTA--ETELLQLRAKAVD---ADKLRNA 1699
Cdd:pfam05701 46 KVQEEIPEYKKQSEAAEAAKAQVLEE-LESTKRLIEEL---KLNLERAQTEEAQAkqDSELAKLRVEEMEqgiADEASVA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1700 AQE--EAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKAledlekfklQAEEAERHLKQAElekqrqiQVVEEV 1777
Cdd:pfam05701 122 AKAqlEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIK---------RAEEAVSASKEIE-------KTVEEL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1778 AKKTAATQlESKQVALTARLEeslKNEQVMVIQLQEEAEHLKKQqaeadKAREQAEKELETWRQK------------ANE 1845
Cdd:pfam05701 186 TIELIATK-ESLESAHAAHLE---AEEHRIGAALAREQDKLNWE-----KELKQAEEELQRLNQQllsakdlkskleTAS 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1846 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKaeeAALKQKEAAEMElGNQRKMAEETAKQKLAAEQelirLRA 1925
Cdd:pfam05701 257 ALLLDLKAELAAYMESKLKEEADGEGNEKKTSTSIQAA---LASAKKELEEVK-ANIEKAKDEVNCLRVAAAS----LRS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1926 DFehaEQQRTVLdDELQRLKNDVNSAVKQkkeLEEELIKVRKEMEiLLQQKSKAEKETMSNTEKskqlleseaaKMRELA 2005
Cdd:pfam05701 329 EL---EKEKAEL-ASLRQREGMASIAVSS---LEAELNRTKSEIA-LVQAKEKEAREKMVELPK----------QLQQAA 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2006 EEATKLRSVAEEAKKQRQIAEEEAARQRAEA-------EKILKEKLtAINEATRLKTEAEIALKEKEAEndrlKRKAEEE 2078
Cdd:pfam05701 391 QEAEEAKSLAQAAREELRKAKEEAEQAKAAAstvesrlEAVLKEIE-AAKASEKLALAAIKALQESESS----AESTNQE 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2079 GYQRKV---LEDQAAQHKQA----------IEEKIGQLKKSSDTELDRQKKI--VEETLKQRKvveEEIHILKLNFEKAS 2143
Cdd:pfam05701 466 DSPRGVtlsLEEYYELSKRAheaeelankrVAEAVSQIEEAKESELRSLEKLeeVNREMEERK---EALKIALEKAEKAK 542
|
...
gi 1207141724 2144 SGK 2146
Cdd:pfam05701 543 EGK 545
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1522-2124 |
6.12e-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: 6.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1522 QEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEkaaeklkeeerkkMAEMQAELEKQKQLAETHAKAIAKAEQEANEL 1601
Cdd:COG4913 262 ERYAAARERLAELEYLRAALRLWFAQRRLELLEAE-------------LEELRAELARLEAELERLEARLDALREELDEL 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1602 KTKMKDevskrqdvavdsekqkhNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTmkqkntaET 1681
Cdd:COG4913 329 EAQIRG-----------------NGGDRLEQL----EREIERLERELEERERRRARLEALLAALGLPLPAS-------AE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1682 ELLQLRAKAVDadkLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA----- 1756
Cdd:COG4913 381 EFAALRAEAAA---LLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEAlglde 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1757 -------------------------------------ERHLKQA-------ELEKQRQIQVVEEVAKKTAATQLESKQVA 1792
Cdd:COG4913 458 aelpfvgelievrpeeerwrgaiervlggfaltllvpPEHYAAAlrwvnrlHLRGRLVYERVRTGLPDPERPRLDPDSLA 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1793 ---------LTARLEESLkNEQVMVIQLqEEAEHLKKqqaeADKA----------REQAEKELETWRQKA------NEAL 1847
Cdd:COG4913 538 gkldfkphpFRAWLEAEL-GRRFDYVCV-DSPEELRR----HPRAitragqvkgnGTRHEKDDRRRIRSRyvlgfdNRAK 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1848 RLRLQAEEEAnkktaaqeeaEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR---KMAEETAKQKLAAEQELIRLR 1924
Cdd:COG4913 612 LAALEAELAE----------LEEELAEAEERLEALEAELDALQERREALQRLAEYSwdeIDVASAEREIAELEAELERLD 681
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1925 ADFEHAEQqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMREL 2004
Cdd:COG4913 682 ASSDDLAA----LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAA 757
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2005 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE-KLTAINEATRLKTEAEiALKEKEAENDRLkrkaEEEGyqrk 2083
Cdd:COG4913 758 ALGDAVERELRENLEERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRL----EEDG---- 828
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 1207141724 2084 vLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 2124
Cdd:COG4913 829 -LPEYEERFKELLNENSIEFVADLLSKLRRAIREIKERIDP 868
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2195-2776 |
7.77e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 7.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2195 VKQIQAAEEEAARQHKAAQEEVGRLMKLAE---EAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQnVLVQQNKDSMA 2271
Cdd:PRK03918 209 INEISSELPELREELEKLEKEVKELEELKEeieELEKELESLEGSKRKLEEKIRELEERIEELKKEIE-ELEEKVKELKE 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2272 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAA 2351
Cdd:PRK03918 288 LKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIK--------------ELEEKEERLEELKKKLKELEKR 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2352 ALKLKQEADS-EMAKYKKLAEKTLKQKSSvEEELVKVKVQLDETDKQKSVLDVELKRLKQEvsdaikqKAQVEDELSKVK 2430
Cdd:PRK03918 354 LEELEERHELyEEAKAKKEELERLKKRLT-GLTPEKLEKELEELEKAKEEIEEEISKITAR-------IGELKKEIKELK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2431 IQMEDLLKLKLKIEKENQELmkkDKDNTKKLLEEEAENMKKLAEEAARL-NIEAQEAARLRQI-----AESDLAKQRELA 2504
Cdd:PRK03918 426 KAIEELKKAKGKCPVCGREL---TEEHRKELLEEYTAELKRIEKELKEIeEKERKLRKELRELekvlkKESELIKLKELA 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2505 EKMLE-EKKQAIQEAAKLKAEAEKLQKQKdqaqveaQKLLEAKKEmqqrldqetegfQKSLEAERKRQLEITAEAEKLKV 2583
Cdd:PRK03918 503 EQLKElEEKLKKYNLEELEKKAEEYEKLK-------EKLIKLKGE------------IKSLKKELEKLEELKKKLAELEK 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2584 KVTQLSDAQSKAEEEAKKFK-KQADEIKIRLQETEKHTSEKHTVVE-KLEVQRLQSKQE--ADGLHKAIADLEKEKEKLK 2659
Cdd:PRK03918 564 KLDELEEELAELLKELEELGfESVEELEERLKELEPFYNEYLELKDaEKELEREEKELKklEEELDKAFEELAETEKRLE 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2660 KEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKkklekqfedevKKAEALKAEQERqrklMEE 2739
Cdd:PRK03918 644 ELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIK-----------KTLEKLKEELEE----REK 708
|
570 580 590
....*....|....*....|....*....|....*..
gi 1207141724 2740 ERKKLQSamdaaIKKQKEAEEEMNGKQKEMQDLEKKR 2776
Cdd:PRK03918 709 AKKELEK-----LEKALERVEELREKVKKYKALLKER 740
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
225-332 |
7.86e-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: 54.24 E-value: 7.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 225 ERDRVQKKTFTKWVNKHLVKAqrHITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 295
Cdd:cd21331 18 EGETREERTFRNWMNSLGVNP--HVNHLYGDLQDALVILQLYEKIkvpvdwnkvNKPPYPKLGANMK--KLENCNYAVEL 93
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141724 296 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 332
Cdd:cd21331 94 GKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1274-2130 |
8.23e-08 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 59.29 E-value: 8.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1274 EIDITQKKMEHVYGLSSVYLDKLKTIDLVIRST--------QGAEDILNKYENQLREVNKvpvNEKEIEASQTQLQKLRS 1345
Cdd:TIGR00606 193 QVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQitskeaqlESSREIVKSYENELDPLKN---RLKEIEHNLSKIMKLDN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1346 EAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFaqielrQRELDLLNRQMQAYRESYD 1425
Cdd:TIGR00606 270 EIKALKSRKKQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDC------QRELEKLNKERRLLNQEKT 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1426 WLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKklLEEIEKNKDKVEDCQKFAKGYIDAIKDyelqlvtykalvepia 1505
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQEHIRARDSLIQSLATRLE--LDGFERGPFSERQIKNFHTLVIERQED---------------- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1506 splkKAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQR-RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLA 1584
Cdd:TIGR00606 406 ----EAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKeILEKKQEELKFVIKELQQLEGSSDRILELDQELR 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1585 ETHAKaIAKAEQEANeLKTKMKDEVSkRQDVAVDSEKQKHNIQRELQELKTLSEQEikaksQQVEEALLSRTRIEEEIHI 1664
Cdd:TIGR00606 482 KAERE-LSKAEKNSL-TETLKKEVKS-LQNEKADLDRKLRKLDQEMEQLNHHTTTR-----TQMEMLTKDKMDKDEQIRK 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1665 IRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKE------ 1738
Cdd:TIGR00606 554 IKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKlfdvcg 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1739 KKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALT-ARLEESLKNEQVMVIQLQEEAEH 1817
Cdd:TIGR00606 634 SQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTeAELQEFISDLQSKLRLAPDKLKS 713
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1818 LKKQQAEADKAREQAEKELETwrqKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1897
Cdd:TIGR00606 714 TESELKKKEKRRDEMLGLAPG---RQSI-IDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLT 789
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1898 ELGNQRKMAEETAK-----QKLAAEQELIRLRADFEHAEQQRTVLDDELQRlkndvnsaVKQKKELEEELIKVRKEMEIL 1972
Cdd:TIGR00606 790 DVTIMERFQMELKDverkiAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDT--------VVSKIELNRKLIQDQQEQIQH 861
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1973 LQQKS---KAEKETMS-NTEKSKQLLESEAAKMRELAEEATKLRSVAEE------AKKQRQIAEEEAARQRAEAEKILKE 2042
Cdd:TIGR00606 862 LKSKTnelKSEKLQIGtNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQdspletFLEKDQQEKEELISSKETSNKKAQD 941
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2043 KLTAINEATRLKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTElDRQKKIVEET 2121
Cdd:TIGR00606 942 KVNDIKEKVKNIHGYMKDIENKIQDGkDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQ-KIQERWLQDN 1020
|
....*....
gi 1207141724 2122 LKQRKVVEE 2130
Cdd:TIGR00606 1021 LTLRKRENE 1029
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2195-2399 |
9.61e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 57.55 E-value: 9.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2195 VKQIQAAEEEAArqhKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDsmAQDK 2274
Cdd:TIGR02794 52 ANRIQQQKKPAA---KKEQERQKKLEQQAEEAEKQRA-AEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA--EEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2275 LKEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEaeAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAL 2353
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAErKAKEEAAKQAEEEAKAKAAAEAKKKAEE--AKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141724 2354 KLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKS 2399
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQ 249
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1754-2312 |
9.72e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 9.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1754 EEAERHLKQAElEKQRQIQVVEEVAKK-TAATQLESKQVALTARLEesLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA 1832
Cdd:COG4913 238 ERAHEALEDAR-EQIELLEPIRELAERyAAARERLAELEYLRAALR--LWFAQRRLELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1833 EKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKq 1912
Cdd:COG4913 315 EARLDALREELDELEAQIRGNGGDR-----------------LEQLEREIERLERELEERERRRARLEALLAALGLPLP- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1913 klAAEQELIRLRADfehAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSkaeketmsntekskq 1992
Cdd:COG4913 377 --ASAEEFAALRAE---AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS--------------- 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1993 LLESEAAKMRELAEEATK-----LRSVAEEAkkqrQIAEEEAARQRAeAEKIL--------------KEKLTAINE---A 2050
Cdd:COG4913 437 NIPARLLALRDALAEALGldeaeLPFVGELI----EVRPEEERWRGA-IERVLggfaltllvppehyAAALRWVNRlhlR 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2051 TRLKTEaeialKEKEAENDRLKRKAEEEGYQRKVL-------------------------EDQAAQHKQAIEEKiGQLKK 2105
Cdd:COG4913 512 GRLVYE-----RVRTGLPDPERPRLDPDSLAGKLDfkphpfrawleaelgrrfdyvcvdsPEELRRHPRAITRA-GQVKG 585
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2106 SSDT-ELDRQKKIVEE------TLKQRKVVEEEIHILKLNFEKASSgkqelelELKKLKGIADETQKskakaeeeaekfR 2178
Cdd:COG4913 586 NGTRhEKDDRRRIRSRyvlgfdNRAKLAALEAELAELEEELAEAEE-------RLEALEAELDALQE------------R 646
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2179 KLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEiAEKEAEKQVILVQEAAQKCSAAEQKA 2258
Cdd:COG4913 647 REALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDDLAALEEQLEELEA-ELEELEEELDELKGEIGRLEKELEQA 725
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2259 QNVL--VQQNKDSMAQDKLKEEFEKAKKLAQEA------EKAKDNAEKEAALLHKKAEEAER 2312
Cdd:COG4913 726 EEELdeLQDRLEAAEDLARLELRALLEERFAAAlgdaveRELRENLEERIDALRARLNRAEE 787
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1626-2133 |
1.08e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 58.77 E-value: 1.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1626 IQRELQELKTLseQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAE-----TELLQLRAKAVDADKLRNAA 1700
Cdd:COG4913 244 LEDAREQIELL--EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAEleelrAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1701 QEEAEKLRKQVAE-ETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK 1779
Cdd:COG4913 322 REELDELEAQIRGnGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1780 K--TAATQLESKQVALTARLEEslkneqvmviqLQEEAEHLKKQQ----AEADKAREQAEKEL----------------- 1836
Cdd:COG4913 402 AleEALAEAEAALRDLRRELRE-----------LEAEIASLERRKsnipARLLALRDALAEALgldeaelpfvgelievr 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1837 ---ETWRQKANEAL---RLRL----QAEEEANK---KTAAQEEAEKQKEEAKREAKKRAKAEEAALKQK---------EA 1894
Cdd:COG4913 471 peeERWRGAIERVLggfALTLlvppEHYAAALRwvnRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKldfkphpfrAW 550
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1895 AEMELGNQRKMAeetakqKLAAEQELIRL-RA----------------DFEHAEQQRTVLddelqrlkndVNSAVKQKKE 1957
Cdd:COG4913 551 LEAELGRRFDYV------CVDSPEELRRHpRAitragqvkgngtrhekDDRRRIRSRYVL----------GFDNRAKLAA 614
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1958 LEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEE-AKKQRQIAE--------EE 2028
Cdd:COG4913 615 LEAELAELEEELAEAEERLEALEAE-LDALQERREALQ----RLAEYSWDEIDVASAEREiAELEAELERldassddlAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2029 AARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEegyqrkVLEDQAAQHKQAIEEKIGQLKKSsd 2108
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEA------AEDLARLELRALLEERFAAALGD-- 761
|
570 580
....*....|....*....|....*
gi 1207141724 2109 telDRQKKIVEETLKQRKVVEEEIH 2133
Cdd:COG4913 762 ---AVERELRENLEERIDALRARLN 783
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2359-2600 |
1.40e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2359 ADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlk 2438
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGER-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2439 lklkiekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARLN-IEAQEAARLRQIAEsdlakQRELAEKMLEEKKQAIQE 2517
Cdd:COG3883 92 --------ARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSkIADADADLLEELKA-----DKAELEAKKAELEAKLAE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2518 AAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEE 2597
Cdd:COG3883 159 LEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 238
|
...
gi 1207141724 2598 EAK 2600
Cdd:COG3883 239 AAA 241
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1643-2243 |
1.41e-07 |
|
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: 58.22 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1643 AKSQQVEeaLLSRT-----RIEEEIHIIRlqlETTMKQKNTAETELLQLRAKAVdADKlrnAAQEEAEKLRKQVAEETQK 1717
Cdd:pfam07111 60 ALSQQAE--LISRQlqelrRLEEEVRLLR---ETSLQQKMRLEAQAMELDALAV-AEK---AGQAEAEGLRAALAGAEMV 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1718 KRKAEEELKR-----KSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAA--TQLESKQ 1790
Cdd:pfam07111 131 RKNLEEGSQReleeiQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELlrKQLSKTQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1791 VALTAR--LEESLKN---EQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETWR-QKANEALRLRlqaEEEAN 1858
Cdd:pfam07111 211 EELEAQvtLVESLRKyvgEQVPPEVHSQTWELERQelldtmQHLQEDRADLQATVELLQVRvQSLTHMLALQ---EEELT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1859 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALK-QKEAAEMELGNQRKmaeeTAKQKLAAEQELIRLRAdfehaeQQRTVL 1937
Cdd:pfam07111 288 RKIQPSDSLEPEFPKKCRSLLNRWREKVFALMvQLKAQDLEHRDSVK----QLRGQVAELQEQVTSQS------QEQAIL 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1938 DDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE---TMSNTEKSKQLLESEAAKMRELAEEATKLRSV 2014
Cdd:pfam07111 358 QRALQDKAAEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQlkfVVNAMSSTQIWLETTMTRVEQAVARIPSLSNR 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2015 AEEAKKQRQIAEEEAARQRAEAEkILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRkaeeegyqrkvlEDQAAQHkq 2094
Cdd:pfam07111 438 LSYAVRKVHTIKGLMARKVALAQ-LRQESCPPPPPAPPVDADLSLELEQLREERNRLDA------------ELQLSAH-- 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2095 AIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEea 2174
Cdd:pfam07111 503 LIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQELTQQQEIYGQALQ-- 580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2175 ekfRKLALEEEKKRKEAEAKVKQIQAAEEEAAR--------QHKAAQEE--VGRLMKLAEEAKKQ------KEIAEKEAE 2238
Cdd:pfam07111 581 ---EKVAEVETRLREQLSDTKRRLNEARREQAKavvslrqiQHRATQEKerNQELRRLQDEARKEegqrlaRRVQELERD 657
|
....*
gi 1207141724 2239 KQVIL 2243
Cdd:pfam07111 658 KNLML 662
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2483-2618 |
1.47e-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: 1.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2483 AQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQK 2562
Cdd:TIGR02794 49 AQQANRIQQ-QKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2563 SlEAERKRQLEitAEAEKlkvkvTQLSDAQSKAEEEAKKfkKQADEIKIRLQETEK 2618
Cdd:TIGR02794 128 Q-AAEAKAKAE--AEAER-----KAKEEAAKQAEEEAKA--KAAAEAKKKAEEAKK 173
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4237-4273 |
1.65e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.17 E-value: 1.65e-07
10 20 30
....*....|....*....|....*....|....*..
gi 1207141724 4237 IRLLEAQIATGGIIDPEESHRLPVEMAYKRGLFDEEM 4273
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1931-2127 |
1.77e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 57.91 E-value: 1.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1931 EQQRTVLDDELQRLKNDVNSAVKQKKELEEElikvRKEMEILLQQkskAEKETMSNTEKSKQLLESEAAKMRELAEEATK 2010
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERELEQK----AEEAEALLKE---AEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQ 577
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2011 LRSVAEEAKKQ--RQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE---NDRLK-RKAEEEGYQRKV 2084
Cdd:PRK00409 578 AIKEAKKEADEiiKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEElkvGDEVKyLSLGQKGEVLSI 657
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1207141724 2085 LEDQAAQHKQAI---EEKIGQLKKSSDTELDRQKKIVEETLKQRKV 2127
Cdd:PRK00409 658 PDDKEAIVQAGImkmKVPLSDLEKIQKPKKKKKKKPKTVKPKPRTV 703
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1799-2038 |
1.98e-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: 1.98e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1799 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakREA 1878
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAEL-----------AEL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1879 KKRAKAEEAALKQKEA--AEMELGNQRKMAEETAKQKLAAE--QELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQ 1954
Cdd:COG4942 89 EKEIAELRAELEAQKEelAELLRALYRLGRQPPLALLLSPEdfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1955 KKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRA 2034
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGF 248
|
....
gi 1207141724 2035 EAEK 2038
Cdd:COG4942 249 AALK 252
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
349-442 |
2.20e-07 |
|
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: 53.07 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 349 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTN-------------------------- 401
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTqtvdraqdeaedfwvaefspstgdsg 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141724 402 -----LENLEQAFSIAE---RDLG-VTRLLDPEDVDVPHPDEKSIITYVS 442
Cdd:cd21224 82 lsselLANEKRNFKLVQqavAELGgVPALLRASDMSNTIPDEKVVILFLS 131
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1235-1769 |
2.23e-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: 57.82 E-value: 2.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1235 KKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVyLDKLKTIDLVIRSTQGAEDILn 1314
Cdd:pfam15921 227 RELDTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGL-TEKASSARSQANSIQSQLEII- 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1315 kyENQLREVNKVPVNE-KEIEASQTQLqklRSE-AEGKQATFDRLEEELQRATEVNKRMSQLHSERDveleHYRQLVGNL 1392
Cdd:pfam15921 305 --QEQARNQNSMYMRQlSDLESTVSQL---RSElREAKRMYEDKIEELEKQLVLANSELTEARTERD----QFSQESGNL 375
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1393 RERWQAVFAQIELRQRELDLLNRQMQAYRE-------SYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQE------ 1459
Cdd:pfam15921 376 DDQLQKLLADLHKREKELSLEKEQNKRLWDrdtgnsiTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQmaaiqg 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1460 -KKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAkmESASDDIIQEYVTLRTRYsELMTLS 1538
Cdd:pfam15921 456 kNESLEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEK--ERAIEATNAEITKLRSRV-DLKLQE 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1539 SQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVD 1618
Cdd:pfam15921 533 LQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKIL 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1619 SEKQKHNIQR--------ELQELKTLSE--------QEIKA-KSQQVEEALLSRTRIE---EEIHIIRL-------QLET 1671
Cdd:pfam15921 613 KDKKDAKIRElearvsdlELEKVKLVNAgserlravKDIKQeRDQLLNEVKTSRNELNslsEDYEVLKRnfrnkseEMET 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1672 TMK----QKNTAETELLQLR-------------------------AKAVDADKLRNAAQ-----------------EEAE 1705
Cdd:pfam15921 693 TTNklkmQLKSAQSELEQTRntlksmegsdghamkvamgmqkqitAKRGQIDALQSKIQfleeamtnankekhflkEEKN 772
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 1706 KLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQR 1769
Cdd:pfam15921 773 KLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVR 836
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1879-2079 |
2.64e-07 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 56.71 E-value: 2.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1879 KKRAKAEEAALKQKEAAEMElgnqrkmAEETAKQK-LAAEQELIRLRADFEhaeqqrtvlddelqrlkndvnsavKQKKE 1957
Cdd:PRK12704 31 AKIKEAEEEAKRILEEAKKE-------AEAIKKEAlLEAKEEIHKLRNEFE------------------------KELRE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1958 LEEELikvrKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA-KKQRQIAEEEAARQRAEA 2036
Cdd:PRK12704 80 RRNEL----QKLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEELiEEQLQELERISGLTAEEA 155
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1207141724 2037 EKILKEKLTAineatrlKTEAEIALKEKEAENdrlkrKAEEEG 2079
Cdd:PRK12704 156 KEILLEKVEE-------EARHEAAVLIKEIEE-----EAKEEA 186
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1340-2069 |
3.28e-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: 57.16 E-value: 3.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1340 LQKLRSEAEGKQATFDRLEEELQRATEVNK-------RMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELR------ 1406
Cdd:pfam12128 236 IMKIRPEFTKLQQEFNTLESAELRLSHLHFgyksdetLIASRQEERQETSAELNQLLRTLDDQWKEKRDELNGElsaada 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1407 -----QRELDLLNRQMQAYR----ESY----DWLIRWIADAKQRQDKLHAVPigGSKGLQEQLTQEKKLLEEiEKNKDKV 1473
Cdd:pfam12128 316 avakdRSELEALEDQHGAFLdadiETAaadqEQLPSWQSELENLEERLKALT--GKHQDVTAKYNRRRSKIK-EQNNRDI 392
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1474 EDCQKfakgYIDAIKD-YELQLVTYKALVEPIASPLKKaKMESASDDIIQEYVTLRTRYSELMTL--SSQYIKFIIETQR 1550
Cdd:pfam12128 393 AGIKD----KLAKIREaRDRQLAVAEDDLQALESELRE-QLEAGKLEFNEEEYRLKSRLGELKLRlnQATATPELLLQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1551 RLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMkDEVSKRQDvavdseKQKHNIQREL 1630
Cdd:pfam12128 468 NFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSAL-DELELQLF------PQAGTLLHFL 540
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1631 QELKTLSEQEIkakSQQVEEALLSRTRIEEEIhiirlqLETTMKQKNTAETelLQLRAKAVDADK---LRNAAQEEAEKL 1707
Cdd:pfam12128 541 RKEAPDWEQSI---GKVISPELLHRTDLDPEV------WDGSVGGELNLYG--VKLDLKRIDVPEwaaSEEELRERLDKA 609
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1708 RKQVAEETQKKRKAEEELKRKSEAekdaakekkkaledLEKFKLQAEEAERHLKQAElEKQRQIQVVEEVAKKTAATQLE 1787
Cdd:pfam12128 610 EEALQSAREKQAAAEEQLVQANGE--------------LEKASREETFARTALKNAR-LDLRRLFDEKQSEKDKKNKALA 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1788 SKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeea 1867
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRSG---------- 744
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1868 ekqkeeakreakkrAKAEEAALKQKEAAEMElgnqRKMAEETAKQKLAAE-QELIRLRADFEHAEQQRTVLDDELQrlkn 1946
Cdd:pfam12128 745 --------------AKAELKALETWYKRDLA----SLGVDPDVIAKLKREiRTLERKIERIAVRRQEVLRYFDWYQ---- 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1947 dvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKET-MSNTEKSKQLLESEAAKMReLAEEATKLRSVaeeakkQRQIA 2025
Cdd:pfam12128 803 --ETWLQRRPRLATQLSNIERAISELQQQLARLIADTkLRRAKLEMERKASEKQQVR-LSENLRGLRCE------MSKLA 873
|
730 740 750 760
....*....|....*....|....*....|....*....|....
gi 1207141724 2026 EEEAARQRAEAEKILKEKLTAINEaTRLKTEAEIALKEKEAEND 2069
Cdd:pfam12128 874 TLKEDANSEQAQGSIGERLAQLED-LKLKRDYLSESVKKYVEHF 916
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2452-2665 |
3.32e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.97 E-value: 3.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2452 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAE--SDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2529
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKqaEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2530 KQKDQAQVEAqkllEAKKemqqrldQETEGFQKSLEAERKRQleitAEAEklkvkvtqlsdAQSKAEEEAKKFKKQADEI 2609
Cdd:PRK09510 156 AAAAAKKAAA----EAKK-------KAEAEAAKKAAAEAKKK----AEAE-----------AAAKAAAEAKKKAEAEAKK 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2610 KIRLQETEKHTSEKHTVVEKLEVqrlQSKQEADGLHKAIADLEKEKEKLKKEAADL 2665
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1895-2099 |
3.47e-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: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1895 AEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM----- 1969
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELgerar 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1970 ------------EILLQQKSKAEkeTMSNTEKSKQLLESEAAKMRELAEEATKLrsvaEEAKKQRQIAEEEAARQRAEAE 2037
Cdd:COG3883 94 alyrsggsvsylDVLLGSESFSD--FLDRLSALSKIADADADLLEELKADKAEL----EAKKAELEAKLAELEALKAELE 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2038 KILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEK 2099
Cdd:COG3883 168 AAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAA 229
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2448-2610 |
3.52e-07 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 56.76 E-value: 3.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2448 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAE 2526
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKEAQQAiKEAKKEAD 587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2527 KLQK------QKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS------------------------LEAERKRQLEITA 2576
Cdd:PRK00409 588 EIIKelrqlqKGGYASVKAHELIEARKRLNKANEKKEKKKKKQkekqeelkvgdevkylslgqkgevLSIPDDKEAIVQA 667
|
170 180 190
....*....|....*....|....*....|....
gi 1207141724 2577 EAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2610
Cdd:PRK00409 668 GIMKMKVPLSDLEKIQKPKKKKKKKPKTVKPKPR 701
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1332-1860 |
3.58e-07 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 56.67 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1332 EIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELE-HYRQLVGNLRERWQAVFAQIELRQREL 1410
Cdd:pfam05557 3 ELIESKARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQkRIRLLEKREAEAEEALREQAELNRLKK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1411 DLLNRQMQAYRESYDWL-------------IRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQ 1477
Cdd:pfam05557 83 KYLEALNKKLNEKESQLadarevisclkneLSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEKQQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1478 KFAKGYIDAIKD--YELQLVTYKALVepiaspLKKAKMESAS-DDIIQEYVTLRTRYSELMTLSSQyiKFIIETQ----- 1549
Cdd:pfam05557 163 SSLAEAEQRIKEleFEIQSQEQDSEI------VKNSKSELARiPELEKELERLREHNKHLNENIEN--KLLLKEEvedlk 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1550 RRLQDEEKaAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDE-VSKRQDVAVDSE-KQKHNIQ 1627
Cdd:pfam05557 235 RKLEREEK-YREEAATLELEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRIEQLQQREiVLKEENSSLTSSaRQLEKAR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1628 RELQE-----LKTLSEQEIKAKSQQVEEALLSRTRI--EEEIHIIRLQL-----ETTMKQKNTAETELLQLRAKAVDADK 1695
Cdd:pfam05557 314 RELEQelaqyLKKIEDLNKKLKRHKALVRRLQRRVLllTKERDGYRAILesydkELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1696 LRNA--------AQEEAE--KLRKQVAEETQKKRKAEEELKRKSeaekDAAKEKKKALEDLEKFKLQAEEAERHLKQAEL 1765
Cdd:pfam05557 394 AHNEemeaqlsvAEEELGgyKQQAQTLERELQALRQQESLADPS----YSKEEVDSLRRKLETLELERQRLREQKNELEM 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1766 EKQRQIQVVEEVAKKTAATQLESKQvalTARLEESLKNeqvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN- 1844
Cdd:pfam05557 470 ELERRCLQGDYDPKKTKVLHLSMNP---AAEAYQQRKN---QLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFk 543
|
570
....*....|....*.
gi 1207141724 1845 EALRLRLQAeEEANKK 1860
Cdd:pfam05557 544 EVLDLRKEL-ESAELK 558
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1810-2066 |
3.72e-07 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 56.99 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1810 QLQEEAEHLkkqQAEADKAREQAEkELETWRQKANEALRL------RLQAEEEANKKTaaqeeaekqkeeakreakkrAK 1883
Cdd:PRK10929 117 QLLEKSRQA---QQEQDRAREISD-SLSQLPQQQTEARRQlneierRLQTLGTPNTPL--------------------AQ 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1884 AEEAALKQKEAAEMELGNQRKMAEETAKQKlaaeQELIRLRADFehAEQQRTVLDDELQRLKNDVNSAVKQK-------- 1955
Cdd:PRK10929 173 AQLTALQAESAALKALVDELELAQLSANNR----QELARLRSEL--AKKRSQQLDAYLQALRNQLNSQRQREaeralest 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1956 ---------------------KELEEELIKVRKEMEILLQQKSKAEKETM------------------SNT--------- 1987
Cdd:PRK10929 247 ellaeqsgdlpksivaqfkinRELSQALNQQAQRMDLIASQQRQAASQTLqvrqalntlreqsqwlgvSNAlgealraqv 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1988 ----EKSK-QLLESEAAKMR-------ELAEEATKLRSVAEE-----AKKQRQIAEEEAARQRAEAEKILKEKLTAINEA 2050
Cdd:PRK10929 327 arlpEMPKpQQLDTEMAQLRvqrlryeDLLNKQPQLRQIRQAdgqplTAEQNRILDAQLRTQRELLNSLLSGGDTLILEL 406
|
330 340
....*....|....*....|
gi 1207141724 2051 TRLK---TEAEIALKE-KEA 2066
Cdd:PRK10929 407 TKLKvanSQLEDALKEvNEA 426
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2240-2815 |
4.15e-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: 56.67 E-value: 4.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2240 QVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEkAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEA 2319
Cdd:pfam15921 239 RIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVE-ITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2320 EAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLkqeADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKS 2399
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVL---ANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELS 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2400 VLDVELKRL--------------KQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLlEEE 2465
Cdd:pfam15921 395 LEKEQNKRLwdrdtgnsitidhlRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQL-EST 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2466 AENMKKLAEE--AARLNIEAQEaarlRQIaeSDLAKQRELAEKMLEEKKQAI-----------QEAAKLKAEAEKLQKQk 2532
Cdd:pfam15921 474 KEMLRKVVEEltAKKMTLESSE----RTV--SDLTASLQEKERAIEATNAEItklrsrvdlklQELQHLKNEGDHLRNV- 546
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2533 dQAQVEAQKLLEAKKemqqrlDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIR 2612
Cdd:pfam15921 547 -QTECEALKLQMAEK------DKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAK 619
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2613 LQETEKHTSEKHtvVEKLEV-----QRLQS----KQEADGLHKAI----ADLEKEKEKLKKEAADLQKQSKEM---ANVQ 2676
Cdd:pfam15921 620 IRELEARVSDLE--LEKVKLvnagsERLRAvkdiKQERDQLLNEVktsrNELNSLSEDYEVLKRNFRNKSEEMettTNKL 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2677 QEQLQQEKTILQQSffaeKETLLKKekaieeekkklekqfedEVKKAEALKAEQERQRKLMEEerkklQSAMDAAIKKQK 2756
Cdd:pfam15921 698 KMQLKSAQSELEQT----RNTLKSM-----------------EGSDGHAMKVAMGMQKQITAK-----RGQIDALQSKIQ 751
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2757 EAEEEMNGKQKEMQDL--EKKRIEQE-KLLAEENKNLREKLQQLQSSQKASYTK--EIEIQTDK 2815
Cdd:pfam15921 752 FLEEAMTNANKEKHFLkeEKNKLSQElSTVATEKNKMAGELEVLRSQERRLKEKvaNMEVALDK 815
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1747-2067 |
4.45e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.49 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1747 EKFKLQAEEAERhlKQAELEKQRqiqvveevakktaatqLESKQvaltARLEEslkneqvmviqlqEEAEHLKKQQAEAD 1826
Cdd:PRK05035 434 AKAEIRAIEQEK--KKAEEAKAR----------------FEARQ----ARLER-------------EKAAREARHKKAAE 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1827 KAREQAEKELetwrQKANEALRLRlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEmelgNQRK-- 1904
Cdd:PRK05035 479 ARAAKDKDAV----AAALARVKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAA----DPKKaa 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1905 --MAEETAKQKLAAEQElirlradfEHAEQQRTVlDDELQRLKNDVNSAVKQKKELEEElikvrkemeillqQKSKAEKE 1982
Cdd:PRK05035 550 vaAAIARAKAKKAAQQA--------ANAEAEEEV-DPKKAAVAAAIARAKAKKAAQQAA-------------SAEPEEQV 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1983 TMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKqrqiAEEEAARQRAEAEKILKEKLTAINEAT----RLKTEAE 2058
Cdd:PRK05035 608 AEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRK----AAVAAAIARAKARKAAQQQANAEPEEAedpkKAAVAAA 683
|
330
....*....|
gi 1207141724 2059 IA-LKEKEAE 2067
Cdd:PRK05035 684 IArAKAKKAA 693
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1435-1770 |
4.66e-07 |
|
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: 56.29 E-value: 4.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1435 KQRQDKLHavpiggsKGLQEQLTQEKK-LLEEIEKNKdKVEDCQKFAKGYID---AI-KDYELQLVTYKALVEPIASPLK 1509
Cdd:pfam17380 287 RQQQEKFE-------KMEQERLRQEKEeKAREVERRR-KLEEAEKARQAEMDrqaAIyAEQERMAMERERELERIRQEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1510 KAKMESASDDIIQEYVTlRTRYSELMTLSSQyikfiiETQRRLQDEEKAAEKLKEEERkkmaEMQAELEKQKQLAEThak 1589
Cdd:pfam17380 359 KRELERIRQEEIAMEIS-RMRELERLQMERQ------QKNERVRQELEAARKVKILEE----ERQRKIQQQKVEMEQ--- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1590 aIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHniQRELQELKTlSEQEIKAKSQQVEEALLSRTRIEEEihiirlql 1669
Cdd:pfam17380 425 -IRAEQEEARQREVRRLEEERAREMERVRLEEQER--QQQVERLRQ-QEEERKRKKLELEKEKRDRKRAEEQ-------- 492
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1670 ettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF 1749
Cdd:pfam17380 493 -----RRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEE-ERRREAEEERRKQQEMEERRRIQEQMRKATEERS 566
|
330 340
....*....|....*....|...
gi 1207141724 1750 KLQAEEAERHLKQ--AELEKQRQ 1770
Cdd:pfam17380 567 RLEAMEREREMMRqiVESEKARA 589
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1903-2042 |
4.77e-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: 54.16 E-value: 4.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1903 RKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVR---------KEMEILL 1973
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRnnkeyealqKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 1974 QQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKE 2042
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1752-1961 |
4.97e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 55.24 E-value: 4.97e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1752 QAEEAErhlKQAELEKQRQIQVVEEVAKKTAATQLEskqvalTARLEESLKneqvmviqlQEEAEHLKKQQAEADKAREQ 1831
Cdd:TIGR02794 76 QAEEAE---KQRAAEQARQKELEQRAAAEKAAKQAE------QAAKQAEEK---------QKQAEEAKAKQAAEAKAKAE 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1832 AEKEletwRQKANEALRlrlQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAK 1911
Cdd:TIGR02794 138 AEAE----RKAKEEAAK---QAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAA 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1912 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1961
Cdd:TIGR02794 211 AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1613-1835 |
5.24e-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: 5.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1613 QDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAvd 1692
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAEL----EKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1693 aDKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLK-----QAELEK 1767
Cdd:COG4942 93 -AELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAelaalRAELEA 171
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 1768 QRQIQVV---EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKE 1835
Cdd:COG4942 172 ERAELEAllaELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1576-2058 |
5.70e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 56.23 E-value: 5.70e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1576 ELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIqRELQELKTLSEQ---------EIKAKSQ 1646
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKV-KELKELKEKAEEyiklsefyeEYLDELR 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1647 QVEEALlsrTRIEEEIHIIRLQL----------ETTMKQKNTAETELLQLRAKAVDADKLRnAAQEEAEKLRKQVAEETQ 1716
Cdd:PRK03918 311 EIEKRL---SRLEEEINGIEERIkeleekeerlEELKKKLKELEKRLEELEERHELYEEAK-AKKEELERLKKRLTGLTP 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1717 KKRKAE-EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQA---------ELEKQRQIQVVEEVAKKTAATql 1786
Cdd:PRK03918 387 EKLEKElEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAkgkcpvcgrELTEEHRKELLEEYTAELKRI-- 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1787 eSKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANK-KTAAQE 1865
Cdd:PRK03918 465 -EKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKlKGEIKS 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1866 EAEKQKEEAKREAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQR 1943
Cdd:PRK03918 544 LKKELEKLEELKKKLAELEKKLDELEEELAELlkELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKK 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1944 LKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQ 2023
Cdd:PRK03918 624 LEEELDKAFEELAETEKRLEELRKELEELEKKYSEEEYE---ELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLK 700
|
490 500 510
....*....|....*....|....*....|....*...
gi 1207141724 2024 IAEEEAARQRAEAEKILK--EKLTAINEATR-LKTEAE 2058
Cdd:PRK03918 701 EELEEREKAKKELEKLEKalERVEELREKVKkYKALLK 738
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2196-2338 |
6.01e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 55.20 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2196 KQIQAAEEEAARQHKAAQEEVgrlmklAEEAKKQKEIAEKEAEKQVILVQEAAQKcsAAEQKAQNVLVQQNKDSMAQDKL 2275
Cdd:PRK09510 114 QEQKKQAEEAAKQAALKQKQA------EEAAAKAAAAAKAKAEAEAKRAAAAAKK--AAAEAKKKAEAEAAKKAAAEAKK 185
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2276 KEEFEKAKKLAQEAE-KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEA 2338
Cdd:PRK09510 186 KAEAEAAAKAAAEAKkKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEK 249
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1925-2664 |
6.36e-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: 55.88 E-value: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1925 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKsKAEKETMSNTEKSKQLLESEAAKMREL 2004
Cdd:pfam05483 68 SDFENSEGLSRLYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQR-KAIQELQFENEKVSLKLEEEIQENKDL 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2005 AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIAlkEKEAENDRLKrkaeeegYQRKV 2084
Cdd:pfam05483 147 IKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL--RVQAENARLE-------MHFKL 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2085 LEDQaaqhkqaieEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAssgkQELELELKKLKGIADETQ 2164
Cdd:pfam05483 218 KEDH---------EKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMKDLTFLLEES----RDKANQLEEKTKLQDENL 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2165 KskakaeeeaekfrklalEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEV----GRLMKLAEEAKKQKEIAEKEAEKQ 2240
Cdd:pfam05483 285 K-----------------ELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLqiatKTICQLTEEKEAQMEELNKAKAAH 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2241 VILVQE-AAQKCSAAEQ-KAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAE 2318
Cdd:pfam05483 348 SFVVTEfEATTCSLEELlRTEQQRLEKNEDQLKI--ITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKK 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2319 AeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQK 2398
Cdd:pfam05483 426 Q-----------FEKIAEELKGKEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHC 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2399 SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ----------MEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAEN 2468
Cdd:pfam05483 495 DKLLLENKELTQEASDMTLELKKHQEDIINCKKQeermlkqienLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEEN 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2469 MKKLAEEAarlnIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiQEAAKLKAEAEklQKQKDQAQVEAQKLLEAKKE 2548
Cdd:pfam05483 575 ARSIEYEV----LKKEKQMKILENKCNNLKKQIENKNKNIEELHQE-NKALKKKGSAE--NKQLNAYEIKVNKLELELAS 647
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2549 MQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK-----------KFKKQADEIkIRLQETE 2617
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADEAVKLQKEIDKRCQhkiaemvalmeKHKHQYDKI-IEERDSE 726
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2618 -----KHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAD 2664
Cdd:pfam05483 727 lglykNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKE 778
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1911-2618 |
6.41e-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: 55.80 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1911 KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKeTMSNTEKS 1990
Cdd:TIGR04523 117 EQKNKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQK-NIDKIKNK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1991 KQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE---EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 2067
Cdd:TIGR04523 196 LLKLELLLSNLKKKIQKNKSLESQISELKKQNNQLKdniEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2068 NDRLKRKAEEegyqrkvLEDQAAQHKQAIE----EKIGQLKKSSDTELDRQKKIVEETlkQRKVVEEEIHILKLNfekas 2143
Cdd:TIGR04523 276 LEQNNKKIKE-------LEKQLNQLKSEISdlnnQKEQDWNKELKSELKNQEKKLEEI--QNQISQNNKIISQLN----- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2144 sgkqelelelkklkgiadetqkskakaeeeaekfrklaleeekkrkeaeakvKQIQAAEEEaarqhkaaqeevgRLMKLA 2223
Cdd:TIGR04523 342 ----------------------------------------------------EQISQLKKE-------------LTNSES 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2224 EEAKKQKEIAEKEAEKQVILVQEAAQKcsaaeQKAQNVLVQQNkdsmaqdKLKEEFEKAKKLAQEAEKAKDNAEKEAALL 2303
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENQSYK-----QEIKNLESQIN-------DLESKIQNQEKLNQQKDEQIKKLQQEKELL 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2304 HKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQEADSEMAKYKKLaEKTLKQKssvEEE 2383
Cdd:TIGR04523 425 EKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRE----------SLETQLKVLSRSINKI-KQNLEQK---QKE 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2384 LVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDllklklkiekENQELMKKDKDNTKKLLE 2463
Cdd:TIGR04523 491 LKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLESEKKEKESKISD----------LEDELNKDDFELKKENLE 560
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2464 EEAENMKKLAEEaarlnieaqeaarLRQIAESDLAKQRELAEKMLE---EKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ 2540
Cdd:TIGR04523 561 KEIDEKNKEIEE-------------LKQTQKSLKKKQEEKQELIDQkekEKKDLIKEIEEKEKKISSLEKELEKAKKENE 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2541 KLLEAKK---EMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2617
Cdd:TIGR04523 628 KLSSIIKnikSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDDIIELMKDWLKELSLHYKKYITRMIRIKDLP 707
|
.
gi 1207141724 2618 K 2618
Cdd:TIGR04523 708 K 708
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4340-4368 |
6.92e-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: 6.92e-07
10 20
....*....|....*....|....*....
gi 1207141724 4340 IVDPETGKEMSVYEAYRKGLIDHQTYIEL 4368
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1696-2137 |
7.00e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 55.54 E-value: 7.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1696 LRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVE 1775
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1776 EVAKKTAATQLESKQVALTARLEEsLKNEQVMVIQLQEEAEHLKKQQAEADKAREQA--------EKELETWRQKANEAL 1847
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEE-LEERLEELRELEEELEELEAELAELQEELEELleqlslatEEELQDLAEELEELQ 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1848 RLRLQAEEEANKKTAAQEEAEKQKEEAkrEAKKRAKAEEAALKQKE------AAEMELGNQRKMAEETAKQKLAAEQELI 1921
Cdd:COG4717 206 QRLAELEEELEEAQEELEELEEELEQL--ENELEAAALEERLKEARlllliaAALLALLGLGGSLLSLILTIAGVLFLVL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1922 RLRAD-FEHAEQQRTVLDDELQRLkndvNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAK 2000
Cdd:COG4717 284 GLLALlFLLLAREKASLGKEAEEL----QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEEL 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2001 MRELAEEAtkLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEND--RLKRKAEEE 2078
Cdd:COG4717 360 EEELQLEE--LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDeeELEEELEEL 437
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2079 GYQRKVLEDQAAQHKQAIEEKIGQLKK-SSDTELDRQKKIVEETLKQRKVVEEEIHILKL 2137
Cdd:COG4717 438 EEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKAELRELAEEWAALKL 497
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2196-2381 |
1.07e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2196 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKdsmAQDKL 2275
Cdd:PRK09510 93 QQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAA---AEAKK 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2276 KEEFEKAKKLAQEA-EKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALK 2354
Cdd:PRK09510 170 KAEAEAAKKAAAEAkKKAEAEAAAKAAAEAKKKAEAEA------------------KKKAAAEAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*..
gi 1207141724 2355 LKQEADSEMAKYKKLAEKTLKQKSSVE 2381
Cdd:PRK09510 232 AEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1930-2100 |
1.17e-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: 53.00 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1930 AEQQRTVLDdeLQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLLESEAAKMRELAEEAT 2009
Cdd:COG1579 3 PEDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTE-LEDLEKEIKRLELEIEEVEARIKKYE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2010 KLrsvAEEAKKQRQIA-----EEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKV 2084
Cdd:COG1579 80 EQ---LGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
170
....*....|....*.
gi 1207141724 2085 LEDQAAQHKQAIEEKI 2100
Cdd:COG1579 157 ELEELEAEREELAAKI 172
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1595-1939 |
1.31e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 54.49 E-value: 1.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1595 EQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSeqeikAKSQQVEEALLSRTRIEEEIHIIRLQlETTMK 1674
Cdd:pfam02029 12 RRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSG-----QGGLDEEEAFLDRTAKREERRQKRLQ-EALER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1675 QKNTAETellQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEE--LKRKSEAEKDAAKEKKKALEDLEKFKLQ 1752
Cdd:pfam02029 86 QKEFDPT---IADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEEteIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1753 AEEAERHLKQAEL-EKQRQIQVVEEVAKKTAATQLESKQVALTarlEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQ 1831
Cdd:pfam02029 163 SEEAEEVPTENFAkEEVKDEKIKKEKKVKYESKVFLDQKRGHP---EVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1832 AEKELETwrQKANEALRLRLQA--EEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMElgnqRKMAEET 1909
Cdd:pfam02029 240 AEVFLEA--EQKLEELRRRRQEkeSEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE----RKLREEE 313
|
330 340 350
....*....|....*....|....*....|
gi 1207141724 1910 AKQKLaaEQELIRLRAdfEHAEQQRTVLDD 1939
Cdd:pfam02029 314 EKRRM--KEEIERRRA--EAAEKRQKLPED 339
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2566-2788 |
1.44e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2566 AERKRQLEitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLH 2645
Cdd:COG4942 19 ADAAAEAE--AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2646 KAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQ--QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2723
Cdd:COG4942 97 AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylKYLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2724 EALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENK 2788
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
227-326 |
1.47e-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: 50.35 E-value: 1.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 227 DRVQKKTFTKWVNKHLVKA--QRHITDLYEDLRDGHNLISLLEVLSGETLPREKG--RMRFHKLQNVQIALDFLKHRQVK 302
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 1207141724 303 LVNIRNDDIADGNPKLTLGLIWTI 326
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1953-2100 |
1.56e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 54.11 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1953 KQKKELEEELIKVRKEMEILLQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSV---------AEEAKKQRQ 2023
Cdd:COG2268 216 IAQANREAEEAELEQEREIETARIAEAEAEL----AKKKAEERREAETARAEAEAAYEIAEAnaerevqrqLEIAERERE 291
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 2024 IAEEEAARQRAEAEKILKEKLTAinEATRLKTEAEialKEKEAENDRLKRKAEEEGYQRKVlEDQAAQHKQAIEEKI 2100
Cdd:COG2268 292 IELQEKEAEREEAELEADVRKPA--EAEKQAAEAE---AEAEAEAIRAKGLAEAEGKRALA-EAWNKLGDAAILLML 362
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2589-2804 |
1.60e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 54.00 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2589 SDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQ 2668
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2669 SKEmanvQQEQLQQEKTILQQSFFAEKETLL------KKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERK 2742
Cdd:COG4942 99 LEA----QKEELAELLRALYRLGRQPPLALLlspedfLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERA 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2743 KLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE---ENKNLREKLQQLQSSQKAS 2804
Cdd:COG4942 175 ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAElqqEAEELEALIARLEAEAAAA 239
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
816-908 |
1.63e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 49.25 E-value: 1.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 816 HAFVVAATKELMWLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTA 895
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 1207141724 896 ALQTQWSWILQLC 908
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1912-2107 |
1.64e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.07 E-value: 1.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1912 QKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSK 1991
Cdd:COG3883 17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEA-EAEIEERREELGERARAL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1992 Q-----------LLESEAAKmrELAEEATKLRSVAEEAKK---QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 2057
Cdd:COG3883 96 YrsggsvsyldvLLGSESFS--DFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2058 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSS 2107
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAA 223
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1936-2136 |
1.74e-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: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1936 VLDDelQRLKNDVNSAVKQKKEL---EEELIKVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAA--KMRELA 2005
Cdd:COG4913 217 MLEE--PDTFEAADALVEHFDDLeraHEALEDAREQIELLepireLAERYAAARERLAELEYLRAALRLWFAqrRLELLE 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2006 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTA----INEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ 2081
Cdd:COG4913 295 AELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrLEQLEREIERLERELEERERRRARLEALLAALGLP 374
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2082 ----RKVLEDQAAQHKQAIEEkIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILK 2136
Cdd:COG4913 375 lpasAEEFAALRAEAAALLEA-LEEELEALEEALAEAEAALRDLRRELRELEAEIASLE 432
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2465-2607 |
2.10e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.72 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2465 EAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAE----KMLEEKKQAIQEAAKLKAEAEKLQKQkDQAQVEA- 2539
Cdd:COG2268 187 DALGRRKIAEIIRDARIAEAEAERETEIAIAQANREAEEAEleqeREIETARIAEAEAELAKKKAEERREA-ETARAEAe 265
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2540 QKLLEAKKEMQQRLDQETEgfqkslEAERKRQLEItAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2607
Cdd:COG2268 266 AAYEIAEANAEREVQRQLE------IAEREREIEL-QEKEAEREEAELEADVRKPAEAEKQAAEAEAE 326
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1951-2820 |
2.79e-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: 54.28 E-value: 2.79e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1951 AVKQKKELEEELIKVRKEMEILlQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKlRSVAEEAKKQRQIAEEEAA 2030
Cdd:TIGR00606 170 ALKQKFDEIFSATRYIKALETL-RQVRQTQGQKVQEHQMELKYLKQYKEKACEIRDQITS-KEAQLESSREIVKSYENEL 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2031 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE-------------EGYQRKVLEDQaaQHKQAIE 2097
Cdd:TIGR00606 248 DPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvfqgtdeqlndlyHNHQRTVREKE--RELVDCQ 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2098 EKIGQLKKSSdTELDRQKK--IVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKA-KAEEEA 2174
Cdd:TIGR00606 326 RELEKLNKER-RLLNQEKTelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFERGPFSERQIKNFHTlVIERQE 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2175 EKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAK-KQKEIAEKEAEKQVILVQEAAQKCSA 2253
Cdd:TIGR00606 405 DEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKfVIKELQQLEGSSDRILELDQELRKAE 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2254 AEqkaqnvLVQQNKDSMAQDKLKEEF----EKA---KKLAQEAEK-AKDNAEKEA-----ALLHKKAEEAERQKKAAEAE 2320
Cdd:TIGR00606 485 RE------LSKAEKNSLTETLKKEVKslqnEKAdldRKLRKLDQEmEQLNHHTTTrtqmeMLTKDKMDKDEQIRKIKSRH 558
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2321 AAKQAKAQEDAEKlRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSv 2400
Cdd:TIGR00606 559 SDELTSLLGYFPN-KKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQD- 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2401 LDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD------NTKKLLEEEAENMKKLAE 2474
Cdd:TIGR00606 637 EESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAElqefisDLQSKLRLAPDKLKSTES 716
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2475 EAARLNIEAQEAARLRQIAESDLA-KQRELAEkmLEEKKQAI-QEAAKLKAEAEKLQKQKD--QAQVEAQKLLEAKKEMQ 2550
Cdd:TIGR00606 717 ELKKKEKRRDEMLGLAPGRQSIIDlKEKEIPE--LRNKLQKVnRDIQRLKNDIEEQETLLGtiMPEEESAKVCLTDVTIM 794
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2551 QRLDQETEGFQKSLEaerkrQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKL 2630
Cdd:TIGR00606 795 ERFQMELKDVERKIA-----QQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNEL 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2631 EVQRLQ-----------------SKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN-------VQQEQLQQEKTI 2686
Cdd:TIGR00606 870 KSEKLQigtnlqrrqqfeeqlveLSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISsketsnkKAQDKVNDIKEK 949
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2687 LQQSFFAEKETllkkEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQ----------- 2755
Cdd:TIGR00606 950 VKNIHGYMKDI----ENKIQDGKDDYLKQKETELNTVNAQLEECEKHQEKINEDMRLMRQDIDTQKIQErwlqdnltlrk 1025
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2756 -----KEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQTDKVPEEE 2820
Cdd:TIGR00606 1026 renelKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQ 1095
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2201-2745 |
3.15e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 53.57 E-value: 3.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2201 AEEEAARQHKAAQEEVGRLMKLAEEAkkQKEIAEKEAEKQVILVQEAAQKcsaAEQKAQNVLVQQNKDSMAQ-------- 2272
Cdd:pfam05483 206 AENARLEMHFKLKEDHEKIQHLEEEY--KKEINDKEKQVSLLLIQITEKE---NKMKDLTFLLEESRDKANQleektklq 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2273 -DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE---KEASRRAEA 2348
Cdd:pfam05483 281 dENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSfvvTEFEATTCS 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2349 EAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKVK----VQLDE-------------TDKQKSVLDVELKRLKQE 2411
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkeVELEElkkilaedeklldEKKQFEKIAEELKGKEQE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2412 VSDAIKQKaqvEDELSKVKIQMEDLLKLKLKIEKENQElMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQ 2491
Cdd:pfam05483 441 LIFLLQAR---EKEIHDLEIQLTAIKTSEEHYLKEVED-LKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELK 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2492 IAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2571
Cdd:pfam05483 517 KHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKC 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2572 LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD--EIKIRLQETEKHTSEK------HTVVEKLEVQRLQSKQEADG 2643
Cdd:pfam05483 597 NNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNayEIKVNKLELELASAKQkfeeiiDNYQKEIEDKKISEEKLLEE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2644 LHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKA 2723
Cdd:pfam05483 677 VEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIE-----ERDSELGLYKNKEQEQSSAKAALEIELSNI 751
|
570 580
....*....|....*....|..
gi 1207141724 2724 EALKAEQERQRKLMEEERKKLQ 2745
Cdd:pfam05483 752 KAELLSLKKQLEIEKEEKEKLK 773
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1847-2265 |
3.31e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 53.62 E-value: 3.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1847 LRLRLQAE-EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE------ETAKQKLAAEQE 1919
Cdd:COG4717 47 LLERLEKEaDELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEaeleelREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1920 LIRLRADFEHAEQQRTVLDDELQRLKN---DVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT--------- 1987
Cdd:COG4717 127 LLPLYQELEALEAELAELPERLEELEErleELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLaeeleelqq 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1988 --EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAArQRAEAEKILKEKLTAINEATRLKTEAEIAL---- 2061
Cdd:COG4717 207 rlAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLvlgl 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2062 ------------KEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDT-----ELDRQKKIVEETLkQ 2124
Cdd:COG4717 286 lallflllarekASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRieelqELLREAEELEEEL-Q 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2125 RKVVEEEIHILkLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEE 2204
Cdd:COG4717 365 LEELEQEIAAL-LAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEE 443
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 2205 AARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQvilvQEAAQKCSAAEQKAQNVLVQQ 2265
Cdd:COG4717 444 LEEELEELREELAELEAELEQLEEDGELAELLQELE----ELKAELRELAEEWAALKLALE 500
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2454-2650 |
3.52e-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: 3.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2454 DKDNTKKLLEEEAENMKKL--AEEAARlnIEAQEAARLRQI---------AESDLAKQREL--------AEKMLEEKKQA 2514
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLerAHEALE--DAREQIELLEPIrelaeryaaARERLAELEYLraalrlwfAQRRLELLEAE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2515 I----QEAAKLKAEAEKLQKQKDQAQveaQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKvkvTQLSD 2590
Cdd:COG4913 297 LeelrAELARLEAELERLEARLDALR---EELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---ALLAA 370
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2591 AQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAD 2650
Cdd:COG4913 371 LGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2484-2761 |
3.74e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 53.41 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2484 QEAARLRQIAE----SDLAKQR-ELAEKMLEEKKQAiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKemqqrlDQETE 2558
Cdd:PRK05035 433 QAKAEIRAIEQekkkAEEAKARfEARQARLEREKAA--REARHKKAAEARAAKDKDAVAAALARVKAKK------AAATQ 504
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2559 GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA----DEIKIRLQETEKHTSEKHTVVEKLEVQR 2634
Cdd:PRK05035 505 PIVIKAGARPDNSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAaiarAKAKKAAQQAANAEAEEEVDPKKAAVAA 584
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2635 LQSKQEAdglHKAIADLEKEKEKLKKEAADLQKQSKEMANVQ---QEQLQQEKTILQQSFFAEKETLlkkekaieeekkk 2711
Cdd:PRK05035 585 AIARAKA---KKAAQQAASAEPEEQVAEVDPKKAAVAAAIARakaKKAEQQANAEPEEPVDPRKAAV------------- 648
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2712 lekqfEDEVKKAEALKAEQER--QRKLMEEERKKLQSAMDAAIKKQKEAEEE 2761
Cdd:PRK05035 649 -----AAAIARAKARKAAQQQanAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1588-1828 |
4.14e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1588 AKAIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELktlsEQEIKAKSQQVEEallsrtrIEEEIHIIRL 1667
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAAL----KKEEKALLKQLAAL----ERRIAALARRIRA-------LEQELAALEA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1668 QLETTMKQKNTAETELLQLR---AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALE 1744
Cdd:COG4942 84 ELAELEKEIAELRAELEAQKeelAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1745 DLEKfKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQvmviQLQEEAEHLKKQQAE 1824
Cdd:COG4942 164 ALRA-ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAE----ELEALIARLEAEAAA 238
|
....
gi 1207141724 1825 ADKA 1828
Cdd:COG4942 239 AAER 242
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2330-2803 |
4.21e-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: 53.30 E-value: 4.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2330 DAEKLRKEAEKEASRRAEAEAAALKLK---------QEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqlDETDKQKSV 2400
Cdd:pfam12128 235 GIMKIRPEFTKLQQEFNTLESAELRLShlhfgyksdETLIASRQEERQETSAELNQLLRTLDDQWKEKR--DELNGELSA 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2401 LDVELKRLKQEVSDAIKQKAQVEDE-LSKVKIQMEDLLKLKLKIEKENQELmkkdkdntkKLLEEEAENMKKlAEEAARL 2479
Cdd:pfam12128 313 ADAAVAKDRSELEALEDQHGAFLDAdIETAAADQEQLPSWQSELENLEERL---------KALTGKHQDVTA-KYNRRRS 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2480 NIEAQEAARLRQIaESDLAKQRELAEKMLEEKKQAIQeaaKLKAE-AEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET- 2557
Cdd:pfam12128 383 KIKEQNNRDIAGI-KDKLAKIREARDRQLAVAEDDLQ---ALESElREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATa 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2558 --------EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEK-HTVVE 2628
Cdd:pfam12128 459 tpelllqlENFDERIERAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQaGTLLH 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2629 KLevqRLQSKQEADGLHKAIAdlekekeKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQ----SFFAEKETLlkkeka 2704
Cdd:pfam12128 539 FL---RKEAPDWEQSIGKVIS-------PELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRidvpEWAASEEEL------ 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2705 ieeekKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLA 2784
Cdd:pfam12128 603 -----RERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKK---NKALA 674
|
490
....*....|....*....
gi 1207141724 2785 EENKNLREKLQQLQSSQKA 2803
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQ 693
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2395-2610 |
4.57e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.50 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2395 DKQKSVLDVELKRLKQEvsdaikqkAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEE--AENMKKL 2472
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKE--------QQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQkqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2473 AEEAARLNIEAQeaarlrQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQr 2552
Cdd:PRK09510 141 AAAAAKAKAEAE------AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAA- 213
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2553 ldqetegfqkslEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2610
Cdd:PRK09510 214 ------------EAKKK------AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAA 253
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1643-1892 |
4.76e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.46 E-value: 4.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1643 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1722
Cdd:COG4942 17 AQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1723 EELK-RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE----LEKQRQIQVVEEVAKKTAATQLESKQVALTARL 1797
Cdd:COG4942 97 AELEaQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQylkyLAPARREQAEELRADLAELAALRAELEAERAEL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1798 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAnkktaaqeeaekqkeeaKRE 1877
Cdd:COG4942 177 EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEA-----------------AAA 239
|
250
....*....|....*
gi 1207141724 1878 AKKRAKAEEAALKQK 1892
Cdd:COG4942 240 AERTPAAGFAALKGK 254
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1697-1912 |
4.81e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.65 E-value: 4.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1697 RNAAQEEAEKLRKQVAE----ETQKKRKAEEELKRkseAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQaELEKQRQIQ 1772
Cdd:pfam15709 328 REQEKASRDRLRAERAEmrrlEVERKRREQEEQRR---LQQEQLERAEKMREELELEQQRRFEEIRLRKQ-RLEEERQRQ 403
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1773 VVEEvakKTAATQLESKQVALTARLEESLKNEQvmviQLQEeaehlKKQQAEADKAREQAEKELETWRQKANEALRLRLQ 1852
Cdd:pfam15709 404 EEEE---RKQRLQLQAAQERARQQQEEFRRKLQ----ELQR-----KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM 471
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1853 AEEEankktaaqeEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQ 1912
Cdd:pfam15709 472 AEEE---------RLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQARQ 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1810-2099 |
5.00e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1810 QLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLR-----LQ---AEEEANKKTAAQEEAEKQKEEAKREAKKR 1881
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEaeiedLRetiAETEREREELAEEVRDLRERLEELEEERD 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1882 AKAEEAAL----------------KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLK 1945
Cdd:PRK02224 297 DLLAEAGLddadaeavearreeleDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAR 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1946 NDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsnteksKQLLESEAAKMRE-LAEEATKLRSVAEEAKKQRQI 2024
Cdd:PRK02224 377 EAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDF--------LEELREERDELRErEAELEATLRTARERVEEAEAL 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2025 AEE-----------------EAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAEnDRLKRKAEeegyQRKVLED 2087
Cdd:PRK02224 449 LEAgkcpecgqpvegsphveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAE-DRIERLEE----RREDLEE 523
|
330
....*....|..
gi 1207141724 2088 QAAQHKQAIEEK 2099
Cdd:PRK02224 524 LIAERRETIEEK 535
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1599-2146 |
5.10e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 53.10 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1599 NELKTKmKDEVSKRQDVAVDSEKQKHNIQRELQELKTlSEQEIKAKSQQVEEALlsrTRIEEEIHIIRLQLETTMKQKNT 1678
Cdd:TIGR04523 47 NELKNK-EKELKNLDKNLNKDEEKINNSNNKIKILEQ-QIKDLNDKLKKNKDKI---NKLNSDLSKINSEIKNDKEQKNK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1679 AETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAER 1758
Cdd:TIGR04523 122 LEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1759 HLKQAELEKQRQIQVVEEVAK-----KTAATQLESKQVALTArLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAE 1833
Cdd:TIGR04523 202 LLSNLKKKIQKNKSLESQISElkkqnNQLKDNIEKKQQEINE-KTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1834 KELETWRQKANEalrlrlqaeeeankktaaqeeaekqkeeakreakkrAKAEEAALKQKEAAEMelgnQRKMAEETAKQk 1913
Cdd:TIGR04523 281 KKIKELEKQLNQ------------------------------------LKSEISDLNNQKEQDW----NKELKSELKNQ- 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1914 laaEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKaEKETMSNTEKSKQL 1993
Cdd:TIGR04523 320 ---EKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQS-YKQEIKNLESQIND 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1994 LESeaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEkltaINEATRLKTEAEIALKEKEAENDRLKR 2073
Cdd:TIGR04523 396 LES---KIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE----IKDLTNQDSVKELIIKNLDNTRESLET 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141724 2074 KAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKssdteLDRQKKIVEETLkqrKVVEEEIHILKLNFEKASSGK 2146
Cdd:TIGR04523 469 QLKVLSRSINKIKQNLEQKQKELKSKEKELKK-----LNEEKKELEEKV---KDLTKKISSLKEKIEKLESEK 533
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1510-2086 |
5.10e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 52.82 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1510 KAKMESASDDIIQEYVTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELE----KQKQLAE 1585
Cdd:pfam05557 8 KARLSQLQNEKKQMELEHKRARIELEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlKKKYLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1586 THAKAIAK--AEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEqEIKAKSQQVEEALLS-----RTRI 1658
Cdd:pfam05557 88 LNKKLNEKesQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLD-LLKAKASEAEQLRQNlekqqSSLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1659 EEEIHIIRLQLETTMKQKNTAETELLQLR-AKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAeEELKRKSEAEKDAAK 1737
Cdd:pfam05557 167 EAEQRIKELEFEIQSQEQDSEIVKNSKSElARIPELEKELERLREHNKHLNENIENKLLLKEEV-EDLKRKLEREEKYRE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1738 EKKKALEDLEKFKLQAEEAERhlkqaeLEKQRQIQVVEEVAKKTAATQLESKQVALTAR---LEESLKNEQVMVIQLQEE 1814
Cdd:pfam05557 246 EAATLELEKEKLEQELQSWVK------LAQDTGLNLRSPEDLSRRIEQLQQREIVLKEEnssLTSSARQLEKARRELEQE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1815 AEHLKKQQAEADKAREQAEKELETWRQKANEALRLR--LQAEEEANKKTAAQEEAEKQKEEAKREAKK---RAKAEEAAL 1889
Cdd:pfam05557 320 LAQYLKKIEDLNKKLKRHKALVRRLQRRVLLLTKERdgYRAILESYDKELTMSNYSPQLLERIEEAEDmtqKMQAHNEEM 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1890 K-QKEAAEMELGNQRKMAEetakqklAAEQELIRLRADFEHAEQQRTvlddelqrlKNDVNSAVKQKKELEEELIKVRKE 1968
Cdd:pfam05557 400 EaQLSVAEEELGGYKQQAQ-------TLERELQALRQQESLADPSYS---------KEEVDSLRRKLETLELERQRLREQ 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1969 MEILLQQKSKAEKETMSNTEKSK--QLLESEAAKMRE-LAEEATKLRsvaeeakkqrqiAEEEAARQRAEAEKILKEKLT 2045
Cdd:pfam05557 464 KNELEMELERRCLQGDYDPKKTKvlHLSMNPAAEAYQqRKNQLEKLQ------------AEIERLKRLLKKLEDDLEQVL 531
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 1207141724 2046 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLE 2086
Cdd:pfam05557 532 RLPETTSTMNFKEVLDLRKELESAELKNQRLKEVFQAKIQE 572
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2381-2810 |
5.13e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 53.12 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2381 EEELVKVKVQLDETDKQKSvldvELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKK 2460
Cdd:PRK02224 212 ESELAELDEEIERYEEQRE----QARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2461 LLEEEAENMKKLAE-EAARLNIEAQEAARlrqiaeSDLAKQRELAEKMLEEKKQAIQEAAKlkaEAEKLQKQKDQAQVEA 2539
Cdd:PRK02224 288 LEELEEERDDLLAEaGLDDADAEAVEARR------EELEDRDEELRDRLEECRVAAQAHNE---EAESLREDADDLEERA 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2540 QKLLEAKKEmqqrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKH 2619
Cdd:PRK02224 359 EELREEAAE----LESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEAT 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2620 TSEKHTVVEklEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAAdLQKQSKEMANVQQEQLQQEKTILQQSFFAEketll 2699
Cdd:PRK02224 435 LRTARERVE--EAEALLEAGKCPECGQPVEGSPHVETIEEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVE----- 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2700 kkekaieeekkkLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQ 2779
Cdd:PRK02224 507 ------------AEDRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEV 574
|
410 420 430
....*....|....*....|....*....|....*
gi 1207141724 2780 EKLLAE--ENKNLREKLQQLQSSQK--ASYTKEIE 2810
Cdd:PRK02224 575 AELNSKlaELKERIESLERIRTLLAaiADAEDEIE 609
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2463-2599 |
5.35e-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: 52.70 E-value: 5.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2463 EEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA------------KLKAEAEKLQK 2530
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtsspkedkqvaeNQKREIEKAQI 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 2531 QKDQAQVEAQKLLEAKKE--MQQRLDQETEGFQKSLEAERKRqLEITAEAEKLKVKVtqlsDAQSKAEEEA 2599
Cdd:pfam05262 289 EIKKNDEEALKAKDHKAFdlKQESKASEKEAEDKELEAQKKR-EPVAEDLQKTKPQV----EAQPTSLNED 354
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1876-2311 |
5.53e-06 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 52.60 E-value: 5.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1876 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1955
Cdd:COG5278 82 EEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLL 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1956 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAE 2035
Cdd:COG5278 162 ALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALA 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2036 AEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQK 2115
Cdd:COG5278 242 LALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAA 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2116 KIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKV 2195
Cdd:COG5278 322 AAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAA 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2196 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKL 2275
Cdd:COG5278 402 AAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAA 481
|
410 420 430
....*....|....*....|....*....|....*.
gi 1207141724 2276 KEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAE 2311
Cdd:COG5278 482 AALAEAEAAAALAAAAALSLALALAALLLAAAEAAL 517
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1762-1982 |
5.58e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1762 QAELEKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvmviQLQEEaehlKKQQAEADKAREQAEKELETWRQ 1841
Cdd:PRK09510 74 AKRAEEQRKKKE------QQQAEELQQKQAAEQERLKQLEKERL----AAQEQ----KKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1842 KANEALRLRLQAEEEAnkktaaqeeaekqkeeaKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQEli 1921
Cdd:PRK09510 140 KAAAAAKAKAEAEAKR-----------------AAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAK-- 200
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 1922 rlradfEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKE 1982
Cdd:PRK09510 201 ------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
334-442 |
5.70e-06 |
|
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: 48.26 E-value: 5.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 334 DIQVNGQSDDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHKHRPNLI-DINKVYRQTNLENLEQAFSIA 412
Cdd:cd21312 1 DEEEDEEAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQA 77
|
90 100 110
....*....|....*....|....*....|
gi 1207141724 413 ERDLGVTRLLDPEDVDVPHPDEKSIITYVS 442
Cdd:cd21312 78 DDWLGIPQVITPEEIVDPNVDEHSVMTYLS 107
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1309-1969 |
6.21e-06 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 53.13 E-value: 6.21e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1309 AEDILNKYENQLREVNKVPVNEKEI-EASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQ 1387
Cdd:TIGR00606 424 KQEQADEIRDEKKGLGRTIELKKEIlEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLKKEV 503
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1388 L------------VGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYD----------WLIRWIADAKQRQDKLHAVP 1445
Cdd:TIGR00606 504 KslqnekadldrkLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKiksrhsdeltSLLGYFPNKKQLEDWLHSKS 583
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1446 iGGSKGLQEQLTQEKKLLEEIEKNKD--------KVEDCQKFAKGYIDAIKDYELQlVTYKALVEPIASPLKKAKMESAS 1517
Cdd:TIGR00606 584 -KEINQTRDRLAKLNKELASLEQNKNhinnelesKEEQLSSYEDKLFDVCGSQDEE-SDLERLKEEIEKSSKQRAMLAGA 661
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1518 DDIIQEYVTLRTRYSE----LMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAK 1593
Cdd:TIGR00606 662 TAVYSQFITQLTDENQsccpVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDL 741
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1594 AEQEANELKTKMkdevskrQDVAVDSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTM 1673
Cdd:TIGR00606 742 KEKEIPELRNKL-------QKVNRDIQRLKNDIEEQETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK 814
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1674 KQKNTAETELLQLRAKAVDAD-KLRNAAQ--EEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFK 1750
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQhELDTVVSkiELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELS 894
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1751 LQAEEAERHLKQaeleKQRQIQVVEEVAKKtaatqLESKQVALTARLEESLKNEQVMVIQLQEEAEHL--------KKQQ 1822
Cdd:TIGR00606 895 TEVQSLIREIKD----AKEQDSPLETFLEK-----DQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdieNKIQ 965
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1823 AEADKAREQAEKELETWRQKANEALRLRLQAEEEankktaaqeeaekqkEEAKREAKKRAKAEEAALkQKEAAEMELGNQ 1902
Cdd:TIGR00606 966 DGKDDYLKQKETELNTVNAQLEECEKHQEKINED---------------MRLMRQDIDTQKIQERWL-QDNLTLRKRENE 1029
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 1903 RKMAEETAKQKLAAEQELIRLRADFEHAEqqrtvLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1969
Cdd:TIGR00606 1030 LKEVEEELKQHLKEMGQMQVLQMKQEHQK-----LEENIDLIKRNHVLALGRQKGYEKEIKHFKKEL 1091
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2448-2815 |
6.65e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2448 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAES--DLAKQRELAEKMLEEKKQAIQ------EAA 2519
Cdd:COG4717 56 DELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEEleELEAELEELREELEKLEKLLQllplyqELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2520 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2599
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2600 KKFKKQADEIKIRLQETEKhTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA--------------DL 2665
Cdd:COG4717 216 EEAQEELEELEEELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVlflvlgllallfllLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2666 QKQSKEMANVQQEQLQQEKTILQQsffAEKETLLKKEKAIEEEKKKLEKQFEDEVKKA-----EALKAEQERQRKLMEEE 2740
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEE---EELEELLAALGLPPDLSPEELLELLDRIEELqellrEAEELEEELQLEELEQE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2741 RKKLQSAMDA-----------AIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENknLREKLQQLQSSQKASYTKEI 2809
Cdd:COG4717 372 IAALLAEAGVedeeelraaleQAEEYQELKEELEELEEQLEELLGELEELLEALDEEE--LEEELEELEEELEELEEELE 449
|
....*.
gi 1207141724 2810 EIQTDK 2815
Cdd:COG4717 450 ELREEL 455
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
225-333 |
7.29e-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: 48.06 E-value: 7.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 225 ERDRVQKKTFTKWVNKhlVKAQRHITDLYEDLRDGHNLISLLEV---------LSGETLPREKGRMRfhKLQNVQIALDF 295
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141724 296 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1598-2058 |
7.58e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.65 E-value: 7.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1598 ANELKTKMKDEVSKRQDVA-----VDSEKQKHN-IQRELQELK---TLSEQEIKAKS---QQVEEALLSRTRIE---EEI 1662
Cdd:PRK04863 278 ANERRVHLEEALELRRELYtsrrqLAAEQYRLVeMARELAELNeaeSDLEQDYQAASdhlNLVQTALRQQEKIEryqADL 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1663 HIIRLQLETTMKQKNTAETELLQLRAKAvdadklrNAAQEEAEKLRKQVAEETQkkrkAEEELKRKSeaekdaakekkka 1742
Cdd:PRK04863 358 EELEERLEEQNEVVEEADEQQEENEARA-------EAAEEEVDELKSQLADYQQ----ALDVQQTRA------------- 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1743 ledlekfkLQAEEAerhlKQAeLEKQRQIQVVEEVAKKTAATQLEskqvALTARLEEslkneqvmviqLQEEAEHLKKQQ 1822
Cdd:PRK04863 414 --------IQYQQA----VQA-LERAKQLCGLPDLTADNAEDWLE----EFQAKEQE-----------ATEELLSLEQKL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1823 AEADKAREQAEKELETWRQKANEALRLrlQAEEEAnkktaaqeeaekqkeeakREAKKRAKAEEAALKQKEAAEMELGnq 1902
Cdd:PRK04863 466 SVAQAAHSQFEQAYQLVRKIAGEVSRS--EAWDVA------------------RELLRRLREQRHLAEQLQQLRMRLS-- 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1903 rkmaeeTAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEillQQKSKAEKE 1982
Cdd:PRK04863 524 ------ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALR---QQLEQLQAR 594
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1983 TMSNTEKSKQLLESEAA--KMRELAEEATK--------LRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR 2052
Cdd:PRK04863 595 IQRLAARAPAWLAAQDAlaRLREQSGEEFEdsqdvteyMQQLLERERELTVERDELAARKQALDEEIERLSQPGGSEDPR 674
|
....*.
gi 1207141724 2053 LKTEAE 2058
Cdd:PRK04863 675 LNALAE 680
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1793-2131 |
7.83e-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: 7.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1793 LTARLEESLKnEQVMVIQLQEEAehlkKQQAEADKAREQAEKEleTWRQKANEaLRLRLQAEEEANKKTaaqeeaekqke 1872
Cdd:pfam07888 32 LQNRLEECLQ-ERAELLQAQEAA----NRQREKEKERYKRDRE--QWERQRRE-LESRVAELKEELRQS----------- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1873 eakreakkRAKAEEAALKQKEAAEMelgnQRKMAEETA---KQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVN 1949
Cdd:pfam07888 93 --------REKHEELEEKYKELSAS----SEELSEEKDallAQRAAHEARIRELEEDIKTLTQRVLERETELERMKERAK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1950 SAVKQKKELEEElikvRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAkkQRQIAEEEA 2029
Cdd:pfam07888 161 KAGAQRKEEEAE----RKQLQAKLQQTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTA--HRKEAENEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2030 ARQRAEAekiLKEKLTAINEATR-LKTEaeiaLKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ------ 2102
Cdd:pfam07888 235 LLEELRS---LQERLNASERKVEgLGEE----LSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARwaqere 307
|
330 340 350
....*....|....*....|....*....|
gi 1207141724 2103 -LKKSSDTELDRQKKIVEETLKQRKVVEEE 2131
Cdd:pfam07888 308 tLQQSAEADKDRIEKLSAELQRLEERLQEE 337
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1310-2116 |
7.93e-06 |
|
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: 52.48 E-value: 7.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1310 EDILNKYENQLREVNKVPVN-EKEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATEvnkRMSQLHSERDVELEHYRQL 1388
Cdd:pfam01576 193 EERLKKEEKGRQELEKAKRKlEGESTDLQEQIAELQAQIAELRAQLAKKEEELQAALA---RLEEETAQKNNALKKIREL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1389 VGNLRE------RWQAVFAQIELRQREldlLNRQMQAYR-ESYDWLirwiaDAKQRQDKLHavpiggSKGLQEqLTQEKK 1461
Cdd:pfam01576 270 EAQISElqedleSERAARNKAEKQRRD---LGEELEALKtELEDTL-----DTTAAQQELR------SKREQE-VTELKK 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1462 LLEEIEKNKD-KVEDCQKFAKGYIDAIKDYELQLVTYKALVEPiasplKKAKMESASDDIIQEYVTLRTRYSELMTLSSQ 1540
Cdd:pfam01576 335 ALEEETRSHEaQLQEMRQKHTQALEELTEQLEQAKRNKANLEK-----AKQALESENAELQAELRTLQQAKQDSEHKRKK 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1541 YIKFIIETQRRLQDEEKAaeklKEEERKKMAEMQAELEK---------------QKQLA---------------ETHAK- 1589
Cdd:pfam01576 410 LEGQLQELQARLSESERQ----RAELAEKLSKLQSELESvssllneaegkniklSKDVSslesqlqdtqellqeETRQKl 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1590 ----AIAKAEQEANELKTKMKDEVSKRQDVavdsEKQKHNIQRELQELKTLSEQEikakSQQVEEALLSRTRIEEEIHII 1665
Cdd:pfam01576 486 nlstRLRQLEDERNSLQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEED----AGTLEALEEGKKRLQRELEAL 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1666 RLQLETTM-------KQKNTAETELLQLrakAVDADKLR---NAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDA 1735
Cdd:pfam01576 558 TQQLEEKAaaydkleKTKNRLQQELDDL---LVDLDHQRqlvSNLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1736 AKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKtaATQLESKQVALTARLEEslkneqvMVIQLQEEA 1815
Cdd:pfam01576 635 ETRALSLARALEEALEAKEELERTNKQLRAEMEDLVSSKDDVGKN--VHELERSKRALEQQVEE-------MKTQLEELE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1816 EHLkkqqaeadKAREQAEKELETWRQKANEALRLRLQAEEEANkktaaqeeaekqkeeakrEAKKRakaeeAALKQKEAA 1895
Cdd:pfam01576 706 DEL--------QATEDAKLRLEVNMQALKAQFERDLQARDEQG------------------EEKRR-----QLVKQVREL 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1896 EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRtvlDDELQRLKNdvnsAVKQKKELEEELIKVRKEM-EILLQ 1974
Cdd:pfam01576 755 EAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGR---EEAVKQLKK----LQAQMKDLQRELEEARASRdEILAQ 827
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1975 QKskaeketmsNTEKSKQLLESEAAKMRELAeeatklrSVAEEAKKQRQIAEEEAARQRAEAekiLKEKLTAINEATRLk 2054
Cdd:pfam01576 828 SK---------ESEKKLKNLEAELLQLQEDL-------AASERARRQAQQERDELADEIASG---ASGKSALQDEKRRL- 887
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2055 tEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKK 2116
Cdd:pfam01576 888 -EARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNK 948
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2363-2571 |
7.99e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 51.38 E-value: 7.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2363 MAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAikQKAQVEDELSKVKIQMEdllklklk 2442
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAE--KAAKQAEQAAKQAEEKQ-------- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2443 iekeNQELMKKDKDNTKKLLEEEAENMKKLAEEAARL-----NIEAQEAARLRQ-----IAESDLAKQRELAEKMLEEKK 2512
Cdd:TIGR02794 119 ----KQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQaeeeaKAKAAAEAKKKAeeakkKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2513 QAIQEAAKLKAEAEklQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQ 2571
Cdd:TIGR02794 195 KAKAEAAKAKAAAE--AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGG 251
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2449-2623 |
8.03e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.26 E-value: 8.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2449 ELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEA--E 2526
Cdd:pfam15709 351 ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2527 KLQKQKDQAQVEAQKLLEAKKEMQQRLDQEtegfqksLEAERKRQLEItAEAEKLKVKvTQLSDAQSKAEEEAKKFKKQA 2606
Cdd:pfam15709 431 KLQELQRKKQQEEAERAEAEKQRQKELEMQ-------LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLEAEERRQKE 501
|
170
....*....|....*...
gi 1207141724 2607 DE-IKIRLQETEKHTSEK 2623
Cdd:pfam15709 502 EEaARLALEEAMKQAQEQ 519
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1775-2032 |
8.10e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 52.26 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1775 EEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAE 1854
Cdd:pfam15709 317 EEDPSKALLEKREQEKASRDRLRAERAEMRRLEVERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRL 396
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1855 EEankktaaqeeaekqkeeakreakKRAKAEEAALKQKEaaemelgnQRKMAEETAKQKlaaEQELIRLRADFEHAEQQr 1934
Cdd:pfam15709 397 EE-----------------------ERQRQEEEERKQRL--------QLQAAQERARQQ---QEEFRRKLQELQRKKQQ- 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1935 tvldDELQRLKndvnsAVKQK-KELEEELIKVRK------EMEILLQQKSKAEKEtmsntEKSKQllesEAAKMRELAEE 2007
Cdd:pfam15709 442 ----EEAERAE-----AEKQRqKELEMQLAEEQKrlmemaEEERLEYQRQKQEAE-----EKARL----EAEERRQKEEE 503
|
250 260
....*....|....*....|....*
gi 1207141724 2008 ATKLrsVAEEAKKQRQiaeeEAARQ 2032
Cdd:pfam15709 504 AARL--ALEEAMKQAQ----EQARQ 522
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2666-2832 |
8.24e-06 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.88 E-value: 8.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2666 QKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQ 2745
Cdd:pfam15709 354 RREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQ 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2746 SAMDaaiKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKnlREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT 2825
Cdd:pfam15709 434 ELQR---KKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEMAE--EERLEYQRQKQEAEEKARLEAEERRQKEEEAARLA 508
|
....*..
gi 1207141724 2826 MVETTKK 2832
Cdd:pfam15709 509 LEEAMKQ 515
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1969-2301 |
8.31e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 52.43 E-value: 8.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1969 MEILLQQKSKAEKETMSNTEKSKQlleseaAKMRELAEEatklrsVAEEAKKQRQIAEEEAARQRAeaekiLKEKLTAIN 2048
Cdd:pfam17380 275 LHIVQHQKAVSERQQQEKFEKMEQ------ERLRQEKEE------KAREVERRRKLEEAEKARQAE-----MDRQAAIYA 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2049 EATRLKTEAE-----IALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQlkkssDTELDRQKKIVEETlK 2123
Cdd:pfam17380 338 EQERMAMERErelerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQ-----ELEAARKVKILEEE-R 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2124 QRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLalEEEKKRKEAEAKVKQIQAAEE 2203
Cdd:pfam17380 412 QRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQ--EEERKRKKLELEKEKRDRKRA 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2204 EAARQHKAAQEEVGRLMKLAEEAKKQKeIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ-DKLKEEFEKA 2282
Cdd:pfam17380 490 EEQRRKILEKELEERKQAMIEEERKRK-LLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQmRKATEERSRL 568
|
330
....*....|....*....
gi 1207141724 2283 KKLAQEAEKAKDNAEKEAA 2301
Cdd:pfam17380 569 EAMEREREMMRQIVESEKA 587
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2332-2604 |
8.44e-06 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 51.06 E-value: 8.44e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2332 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELVKV---KVQLDETDKQKSVLDVELKRL 2408
Cdd:COG1340 18 EELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelKEERDELNEKLNELREELDEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2409 KQEVSDAIKQKAQVeDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAAR 2488
Cdd:COG1340 98 RKELAELNKAGGSI-DKLRKEIERLEWRQQTEVLSPEEEKELVEKIKELEKEL--EKAKKALEKNEKLKELRAELKELRK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2489 LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAER 2568
Cdd:COG1340 175 EAEEIHKKIKELAEEAQELHEEMIELYKEADELRKEADELHKEIVEAQEKADELHEEIIELQKELRE----LRKELKKLR 250
|
250 260 270
....*....|....*....|....*....|....*.
gi 1207141724 2569 KRQLEITAEAEKlkvkvtqlSDAQSKAEEEAKKFKK 2604
Cdd:COG1340 251 KKQRALKREKEK--------EELEEKAEEIFEKLKK 278
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1747-2049 |
8.82e-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: 51.46 E-value: 8.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1747 EKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLK-NEQVMVIQLQEEAEHLKKQQAEA 1825
Cdd:pfam13868 43 RRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQeREQMDEIVERIQEEDQAEAEEKL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1826 DKaREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKM 1905
Cdd:pfam13868 123 EK-QRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1906 AEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMS 1985
Cdd:pfam13868 202 ERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREE--QIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQE 279
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 1986 NTEKSKQLLESEAAKMRELAEEATKLRsvAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINE 2049
Cdd:pfam13868 280 EAEKRRMKRLEHRRELEKQIEEREEQR--AAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
230-337 |
9.01e-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: 9.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 230 QKKTFTKWVNK---------HLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 296
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141724 297 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 337
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1579-1970 |
1.06e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 52.11 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1579 KQKQLAEThAKAIAKAEQEANELKTKMKDevsKRQDVavdSEKQKHniqreLQELKTLSEQEIKAKSQQVEEALL----- 1653
Cdd:PRK10246 438 QQKRLAQL-QVAIQNVTQEQTQRNAALNE---MRQRY---KEKTQQ-----LADVKTICEQEARIKDLEAQRAQLqagqp 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1654 -------SRTRIEE----EIHIIRLQLETTMKQKNTAETELLQLRAKaVDAdklrnaaqeeaekLRKQV---AEETQKKR 1719
Cdd:PRK10246 506 cplcgstSHPAVEAyqalEPGVNQSRLDALEKEVKKLGEEGAALRGQ-LDA-------------LTKQLqrdESEAQSLR 571
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1720 KAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT-QLESKQVALTARLE 1798
Cdd:PRK10246 572 QEEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLRLLSQRHELQGQIAAHNQQIIQYQqQIEQRQQQLLTALA 651
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1799 E-SLK-----NEQVMVIQLQEEAEHLKKQQAEADKAREQ---------------------AEKELETWRQKANEALRLR- 1850
Cdd:PRK10246 652 GyALTlpqedEEASWLATRQQEAQSWQQRQNELTALQNRiqqltplletlpqsddlphseETVALDNWRQVHEQCLSLHs 731
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1851 ---------LQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE---ETAKQKLAAEQ 1918
Cdd:PRK10246 732 qlqtlqqqdVLEAQRLQKAQAQFDTALQASVFDDQQAFLAALLDEETLTQLEQLKQNLENQRQQAQtlvTQTAQALAQHQ 811
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 1919 ----ELIRLRADFEHAEQQRTVLDDEL-----------QRLKNDVNSAvKQKKELEEELIKVRKEME 1970
Cdd:PRK10246 812 qhrpDGLDLTVTVEQIQQELAQLAQQLrenttrqgeirQQLKQDADNR-QQQQALMQQIAQATQQVE 877
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2371-2775 |
1.11e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 51.94 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2371 EKTLKQKSSVEEELVKVKVQLDETDKQK-----SVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEK 2445
Cdd:TIGR04523 277 EQNNKKIKELEKQLNQLKSEISDLNNQKeqdwnKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSES 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2446 ENQELMKKDKDNTKKLLEEEAEN------MKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAA 2519
Cdd:TIGR04523 357 ENSEKQRELEEKQNEIEKLKKENqsykqeIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2520 KLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQetegFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEA 2599
Cdd:TIGR04523 437 KNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKV----LSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKV 512
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2600 KKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQE--ADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQ 2677
Cdd:TIGR04523 513 KDLTKKISSLKEKIEKLESEKKEKESKISDLEDELNKDDFElkKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELID 592
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2678 EQLQQEKTILQQsfFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKE 2757
Cdd:TIGR04523 593 QKEKEKKDLIKE--IEEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKE 670
|
410
....*....|....*...
gi 1207141724 2758 AEEEMNGKQKEMQDLEKK 2775
Cdd:TIGR04523 671 SKTKIDDIIELMKDWLKE 688
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1915-2114 |
1.14e-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: 51.00 E-value: 1.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1915 AAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLL 1994
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAKKEQERQKKLEQQA----EEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1995 ESEA--AKMRELAEEATKLRSVAEEAKKQRQI-----AEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAE 2067
Cdd:TIGR02794 123 EAKAkqAAEAKAKAEAEAERKAKEEAAKQAEEeakakAAAEAKKKAEEAKKKAEAEAKAKAEAEA-KAKAEEAKAKAEAA 201
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141724 2068 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQ 2114
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1591-1857 |
1.17e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1591 IAKAEQEaNELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQElktlsEQEIKAKsQQVEEALLSRTRIEEEIhiirlqle 1670
Cdd:pfam15709 325 LEKREQE-KASRDRLRAERAEMRRLEVERKRREQEEQRRLQQ-----EQLERAE-KMREELELEQQRRFEEI-------- 389
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1671 ttmkqkntaetellQLRAKAVDADKLRNAAQEEAEKLRKQVAEEtqKKRKAEEELKRKSEAEKDaakekkkaledlekfK 1750
Cdd:pfam15709 390 --------------RLRKQRLEEERQRQEEEERKQRLQLQAAQE--RARQQQEEFRRKLQELQR---------------K 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1751 LQAEEAERhlkqAELEKQRQiqvveevakktaatqleskqvaltARLEESLKNEQVMVIQLQEEA--EHLKKQQAEADKA 1828
Cdd:pfam15709 439 KQQEEAER----AEAEKQRQ------------------------KELEMQLAEEQKRLMEMAEEErlEYQRQKQEAEEKA 490
|
250 260 270
....*....|....*....|....*....|....
gi 1207141724 1829 REQAEKEletwRQKANEALRLRL-----QAEEEA 1857
Cdd:pfam15709 491 RLEAEER----RQKEEEAARLALeeamkQAQEQA 520
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1331-2020 |
1.37e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.88 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1331 KEIEASQTQLQKLRSEAEGKQATFDRLEEELQRATE-VNKRMSQL-HSERdveLEHYRQLVGNLRERWQAVFAQIELRQR 1408
Cdd:COG3096 299 RQLAEEQYRLVEMARELEELSARESDLEQDYQAASDhLNLVQTALrQQEK---IERYQEDLEELTERLEEQEEVVEEAAE 375
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1409 ELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQeQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIK 1488
Cdd:COG3096 376 QLAEAEARLEAAEEEVDSLKSQLADYQQALDVQQTRAIQYQQAVQ-ALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1489 DYELQLVTY------------KA--LVEPIASPLKKAKMESASDDIIQEY----------VTLRTRYSELMTLSSQYikf 1544
Cdd:COG3096 455 EEVLELEQKlsvadaarrqfeKAyeLVCKIAGEVERSQAWQTARELLRRYrsqqalaqrlQQLRAQLAELEQRLRQQ--- 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1545 iiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQK-QLAETHAKAIAKA---EQEANELKTKMKdEVSKRQDVAVDSE 1620
Cdd:COG3096 532 --QNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLeELEEQAAEAVEQRselRQQLEQLRARIK-ELAARAPAWLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1621 KQKHNIQRELQELKTlSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTA----ETELLQLR--------A 1688
Cdd:COG3096 609 DALERLREQSGEALA-DSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPggaeDPRLLALAerlggvllS 687
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1689 KAVDADKLRNAAQEEA--------------EKLRKQVAE-------------------------ETQKKR---KAEEELK 1726
Cdd:COG3096 688 EIYDDVTLEDAPYFSAlygparhaivvpdlSAVKEQLAGledcpedlyliegdpdsfddsvfdaEELEDAvvvKLSDRQW 767
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1727 RKSEAEKDAAKEKKKALEDLEKFKLQAEE-AERHLKQA-ELEK-QR-----------QIQVVEEVAKKTAATQLESKQVA 1792
Cdd:COG3096 768 RYSRFPEVPLFGRAAREKRLEELRAERDElAEQYAKASfDVQKlQRlhqafsqfvggHLAVAFAPDPEAELAALRQRRSE 847
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1793 LTARLEESLKNEQvmviQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEA------NKKTAAQEE 1866
Cdd:COG3096 848 LERELAQHRAQEQ----QLRQQLDQLKEQLQLLNKLLPQANLLADETLADRLEELREELDAAQEAqafiqqHGKALAQLE 923
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1867 AEK-------QKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRK-MAEETAKQKLAAEQELI-RLRADFEHAEQQRTVL 1937
Cdd:COG3096 924 PLVavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQAEEARREA 1003
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1938 DDELQRLKNDVNSA------------VKQK--KELEEEL----IKVRKEMEIL-------LQQKSKAEKETMSNTEKSKQ 1992
Cdd:COG3096 1004 REQLRQAQAQYSQYnqvlaslkssrdAKQQtlQELEQELeelgVQADAEAEERarirrdeLHEELSQNRSRRSQLEKQLT 1083
|
810 820 830
....*....|....*....|....*....|..
gi 1207141724 1993 LLESEAA----KMRELAEEATKLRSVAEEAKK 2020
Cdd:COG3096 1084 RCEAEMDslqkRLRKAERDYKQEREQVVQAKA 1115
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1620-2099 |
1.38e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 51.31 E-value: 1.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1620 EKQKHNIQRELQELKTLSEQEIKAKSQQVEEAllsrTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNA 1699
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEA----EEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1700 AQ--EEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfklQAEEAERHLKQAELEKQRQIqvveev 1777
Cdd:COG4717 128 LPlyQELEALEAELAELPERLEELEERLEELR----------------------ELEEELEELEAELAELQEEL------ 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1778 akktaATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEK-ELETWRQKANEALR-------- 1848
Cdd:COG4717 180 -----EELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQlENELEAAALEERLKearlllli 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1849 ----------LRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQ 1918
Cdd:COG4717 255 aaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDL 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1919 ELIRLRADFEHAEQQRTvLDDELQRLKNDVNSAVkQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQL---LE 1995
Cdd:COG4717 335 SPEELLELLDRIEELQE-LLREAEELEEELQLEE-LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELeeqLE 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1996 SEAAKMRELAEEATKlrsvaEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKA 2075
Cdd:COG4717 413 ELLGELEELLEALDE-----EELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
490 500
....*....|....*....|....*
gi 1207141724 2076 EEEGYQRKVLEDQA-AQHKQAIEEK 2099
Cdd:COG4717 488 LAEEWAALKLALELlEEAREEYREE 512
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1816-2102 |
1.42e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 51.13 E-value: 1.42e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1816 EHLKKQQAEadKAREQAEKELetwrqKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAAL-KQKEA 1894
Cdd:PRK07735 8 EDLKKEAAR--RAKEEARKRL-----VAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAKAKAAALaKQKRE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1895 A-----EMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1969
Cdd:PRK07735 81 GteevtEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1970 EILLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKKqrqiaeeeAARQRAEAEKILKEKLTAIN- 2048
Cdd:PRK07735 161 DKEKAKAKAAAAAKAKAAALAKQ----KAAEAGEGTEEVTEEEKAKAKAKA--------AAAAKAKAAALAKQKASQGNg 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141724 2049 --EATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAA-------QHKQAIEEKIGQ 2102
Cdd:PRK07735 229 dsGDEDAKAKAIAAAKAKAAAAARAKTKGAEGKKEEEPKQEEPSvnqpylnKYVEVIKEKLGE 291
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2356-2551 |
1.46e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.98 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2356 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMED 2435
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2436 LLKLKLKIEK-----------ENQELMKKDKDNTKKLLEE------EAENMK-KLAEEAARLNIEAQEAARLRQIAESDL 2497
Cdd:COG3883 98 SGGSVSYLDVllgsesfsdflDRLSALSKIADADADLLEElkadkaELEAKKaELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2498 AKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQ 2551
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAA 231
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1751-2618 |
1.48e-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: 51.59 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1751 LQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvALTARlEESLKNEQVMVIQLQEEAEHLKKQQAEADKARE 1830
Cdd:TIGR00606 185 IKALETLRQVRQTQGQKVQEHQMELKYLKQYKEKACEIRD-QITSK-EAQLESSREIVKSYENELDPLKNRLKEIEHNLS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1831 ---QAEKELETWRQKANEALRLRLQAEEEAnKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEaaeMELGNQRKMAE 1907
Cdd:TIGR00606 263 kimKLDNEIKALKSRKKQMEKDNSELELKM-EKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRE---LEKLNKERRLL 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1908 ETAKQKLAAEQELIRLRADFEH-------AEQQRTVLDDELQRLKND------VNSAVKQKKELEEELIKVRKEMEILLQ 1974
Cdd:TIGR00606 339 NQEKTELLVEQGRLQLQADRHQehirardSLIQSLATRLELDGFERGpfserqIKNFHTLVIERQEDEAKTAAQLCADLQ 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1975 QKSKAEKETMSNTE-KSKQLLESEAAKMRELAEEATKLRSVAEEAKK----QRQIAEEEAARQRAEAEKILKEKltaiNE 2049
Cdd:TIGR00606 419 SKERLKQEQADEIRdEKKGLGRTIELKKEILEKKQEELKFVIKELQQlegsSDRILELDQELRKAERELSKAEK----NS 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2050 ATRLKTEAEIALKEKEAENDRLKRKAEEEGYQ-------RKVLEdQAAQHKQAIEEKIGQLKKSSDTELDRQ------KK 2116
Cdd:TIGR00606 495 LTETLKKEVKSLQNEKADLDRKLRKLDQEMEQlnhhtttRTQME-MLTKDKMDKDEQIRKIKSRHSDELTSLlgyfpnKK 573
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2117 IVEETL----KQRKVVEEEIHILKLNFEKASSGKQELELelkklkgiaDETQKSKAKAEEEAEKFRklaleeekkrkeae 2192
Cdd:TIGR00606 574 QLEDWLhsksKEINQTRDRLAKLNKELASLEQNKNHINN---------ELESKEEQLSSYEDKLFD-------------- 630
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2193 akvkqiqaaeeeaARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSA----------AEQKAQNVL 2262
Cdd:TIGR00606 631 -------------VCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSccpvcqrvfqTEAELQEFI 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2263 VQ-QNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEke 2341
Cdd:TIGR00606 698 SDlQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLG-- 775
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2342 asrraeAEAAALKLKQEADSEMAKYKKLAEKTlkqkSSVEEELVKVKVQLDETDKQKSVLDV-ELKRLKQEVSDAIKQKA 2420
Cdd:TIGR00606 776 ------TIMPEEESAKVCLTDVTIMERFQMEL----KDVERKIAQQAAKLQGSDLDRTVQQVnQEKQEKQHELDTVVSKI 845
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2421 QVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQ 2500
Cdd:TIGR00606 846 ELNRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEK 925
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2501 RELAEKMLEEKKQAIQEAAKLKAEAE--------------------KLQKQKDQAQVEAQklLEAKKEMQQRLDQETEGF 2560
Cdd:TIGR00606 926 EELISSKETSNKKAQDKVNDIKEKVKnihgymkdienkiqdgkddyLKQKETELNTVNAQ--LEECEKHQEKINEDMRLM 1003
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2561 QKSLEAERKR------QLEITAEAEKLK---------------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEK 2618
Cdd:TIGR00606 1004 RQDIDTQKIQerwlqdNLTLRKRENELKeveeelkqhlkemgqMQVLQMKQEHQKLEENIDLIKRNHVLALGRQKGYEK 1082
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1328-1498 |
1.56e-05 |
|
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: 49.37 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1328 VNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELQ----RATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQI 1403
Cdd:cd00176 16 LSEKEELLSSTDYGDDLESVEALLKKHEALEAELAaheeRVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1404 ELRQRELDLLNRQMQAYRESYDwLIRWIADAKQRQDKLhaVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGY 1483
Cdd:cd00176 96 EERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASE--DLGKDLESVEELLKKHKELEEELEAHEPRLKSLNELAEEL 172
|
170
....*....|....*
gi 1207141724 1484 IDAIKDYELQLVTYK 1498
Cdd:cd00176 173 LEEGHPDADEEIEEK 187
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1761-1917 |
1.56e-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: 50.61 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1761 KQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWR 1840
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1841 QKANEALRLRLQAE------EEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKL 1914
Cdd:TIGR02794 126 AKQAAEAKAKAEAEaerkakEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKA 205
|
...
gi 1207141724 1915 AAE 1917
Cdd:TIGR02794 206 AAE 208
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1208-1790 |
1.59e-05 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 51.68 E-value: 1.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1208 ESRTVNRLRQMVDKEPLKACTQRATEQKKVqtelEGIKKDLDKVVEKSEAVLATSQQSS-SAPVLRSEIDITQKKMEHVY 1286
Cdd:PTZ00121 1288 EKKKADEAKKAEEKKKADEAKKKAEEAKKA----DEAKKKAEEAKKKADAAKKKAEEAKkAAEAAKAEAEAAADEAEAAE 1363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1287 GLSSVylDKLKTIDlvirSTQGAEDILNKYEnqlrEVNKVPVNEKEIEASQTQLQKLRSEAEGKQATfdrleEELQRATE 1366
Cdd:PTZ00121 1364 EKAEA--AEKKKEE----AKKKADAAKKKAE----EKKKADEAKKKAEEDKKKADELKKAAAAKKKA-----DEAKKKAE 1428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1367 VNKRMSQLHSERDvELEHYRQLVGNLRERWQAVFAQIELRQ-RELDLLNRQMQAYRESyDWLIRWIADAKQRQDKLHAVP 1445
Cdd:PTZ00121 1429 EKKKADEAKKKAE-EAKKADEAKKKAEEAKKAEEAKKKAEEaKKADEAKKKAEEAKKA-DEAKKKAEEAKKKADEAKKAA 1506
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1446 IGGSKGLQEQLTQEKKLLEEIEK--NKDKVEDCQKF--AKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMESASDDII 1521
Cdd:PTZ00121 1507 EAKKKADEAKKAEEAKKADEAKKaeEAKKADEAKKAeeKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEA 1586
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1522 QEyvTLRTRYSELMTLSSQYIKFIIETQRRLQDEEKAAEKLKEEerkkmaemqaelEKQKQLAETHAKAIAKAEQEANEL 1601
Cdd:PTZ00121 1587 KK--AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA------------EEEKKKVEQLKKKEAEEKKKAEEL 1652
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1602 KTKMKDEVSKRQDVAVDSEKQKhniqRELQELKTLSEQEIKAKSQQVEEALLSRtRIEEeihiirlqlettMKQKNTAET 1681
Cdd:PTZ00121 1653 KKAEEENKIKAAEEAKKAEEDK----KKAEEAKKAEEDEKKAAEALKKEAEEAK-KAEE------------LKKKEAEEK 1715
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1682 EllqlrakavDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlEKFKLQAEEAERHLK 1761
Cdd:PTZ00121 1716 K---------KAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEE-----------------EKKKIAHLKKEEEKK 1769
|
570 580
....*....|....*....|....*....
gi 1207141724 1762 QAELEKQRQIQVVEEVAKKTAATQLESKQ 1790
Cdd:PTZ00121 1770 AEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1792-2098 |
1.68e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 51.50 E-value: 1.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1792 ALTARLE-----ESLKNEQVMVIQLQEEAEhlkkQQAEADKAREQAEKELETWRQKANEALRLRLQ---AEEEANKKTaa 1863
Cdd:PRK04863 288 ALELRRElytsrRQLAAEQYRLVEMARELA----ELNEAESDLEQDYQAASDHLNLVQTALRQQEKierYQADLEELE-- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1864 qeeaekqkeeakreakkrAKAEEAALKQKEAAEmelgnQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD 1938
Cdd:PRK04863 362 ------------------ERLEEQNEVVEEADE-----QQEENEA---RAEAAEEEVDELKsqlADYQQAldVQQTRAIQ 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1939 --------DELQRLKNDVNSAVKQKKELEEELikVRKEMEIL-----LQQKSKAEKETMSNTEKSKQLLESEAAKM---- 2001
Cdd:PRK04863 416 yqqavqalERAKQLCGLPDLTADNAEDWLEEF--QAKEQEATeellsLEQKLSVAQAAHSQFEQAYQLVRKIAGEVsrse 493
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2002 -----RELAEEATKLRSVAEEAK---------KQRQIAEEEAARQRAEAEKILKEKLTAINEATRLkteaeiaLKEKEAE 2067
Cdd:PRK04863 494 awdvaRELLRRLREQRHLAEQLQqlrmrlselEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQL-------QEELEAR 566
|
330 340 350
....*....|....*....|....*....|.
gi 1207141724 2068 NDRLKRKAEEEGYQRKVLEDQAAQHKQAIEE 2098
Cdd:PRK04863 567 LESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
367-443 |
1.76e-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: 46.53 E-value: 1.76e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 367 DNFTTSWRDGRLFNAIIHKHRPNLIDINKVYRQTNLENLEQAFSiAERDLGVTRLLDPEDVDVPHPDEKSIITYVSS 443
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLE-AGKSLGVEPVLTAEEMADPEVEHLGIMAYAAQ 95
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4333-4361 |
1.81e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.81e-05
10 20
....*....|....*....|....*....
gi 1207141724 4333 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4361
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1844-2076 |
1.86e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1844 NEALRLRLQAEEEANKKTAaqeeaEKQKEEAKREAKKRAKAEEAALKQkeaaEMELGNQRKMAEETAKQKLAAEQeliRL 1923
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEA-----EAERETEIAIAQANREAEEAELEQ----EREIETARIAEAEAELAKKKAEE---RR 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1924 RADFEHAEQQRTVlddELQRlkndvnsaVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsntekskqllESEAAKMRE 2003
Cdd:COG2268 256 EAETARAEAEAAY---EIAE--------ANAEREVQRQLEIAEREREIELQEKEAEREE------------AELEADVRK 312
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141724 2004 LAeeatklrsvaeEAKKQRQIAEEEaarqrAEAEKIlKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 2076
Cdd:COG2268 313 PA-----------EAEKQAAEAEAE-----AEAEAI-RAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE 368
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1570-1725 |
1.94e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1570 MAEMQAELEKQKQLAETHA-KAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKhniQRELQELKTLSEQEIKAKSQQV 1648
Cdd:COG2268 194 IAEIIRDARIAEAEAERETeIAIAQANREAEEAELEQEREIETARIAEAEAELAK---KKAEERREAETARAEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1649 EEALLSRTrIEEEIHIIRLQLETTMKQKNtAETELLQLRA---KAVDADKLRNAAQEEAE------KLRKQvAEETQKKR 1719
Cdd:COG2268 271 AEANAERE-VQRQLEIAEREREIELQEKE-AEREEAELEAdvrKPAEAEKQAAEAEAEAEaeairaKGLAE-AEGKRALA 347
|
....*.
gi 1207141724 1720 KAEEEL 1725
Cdd:COG2268 348 EAWNKL 353
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
229-330 |
2.09e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 47.03 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 229 VQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMRF----HKLQNVQIALDFLKHRQVKLV 304
Cdd:cd21306 16 VVKKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDAGLPKP 95
|
90 100
....*....|....*....|....*.
gi 1207141724 305 NIRNDDIADGNPKLTLGLIWTIILHF 330
Cdd:cd21306 96 KARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2222-2640 |
2.15e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 2.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2222 LAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNA---EK 2298
Cdd:PRK02224 277 LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDAddlEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2299 EAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYK-KLAEKTLKQK 2377
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELReREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2378 SsVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLklklkiekenqelmkkdkdn 2457
Cdd:PRK02224 437 T-ARERVEEAEALLEAGKCPECGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVE-------------------- 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2458 tKKLleEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEekkqaiqEAAKLKAEAEKLQKQKDQAQV 2537
Cdd:PRK02224 496 -ERL--ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELRE-------RAAELEAEAEEKREAAAEAEE 565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2538 EAQKLLEAKKEMQQRLdqetegfqksleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2617
Cdd:PRK02224 566 EAEEAREEVAELNSKL------------AELKERIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKR 633
|
410 420
....*....|....*....|...
gi 1207141724 2618 KHTSEKHTVVEKLEVQRLQSKQE 2640
Cdd:PRK02224 634 ERKRELEAEFDEARIEEAREDKE 656
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2470-2621 |
2.17e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2470 KKLAEEAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-----AKLKAEAEKLQKQKDQAQVEAQKLLE 2544
Cdd:COG4913 288 RRLELLEAELEELRAELARLEA-ELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERLERELEERERRRARLEA 366
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 2545 AKKEMQQRLDQETEGFQksleaerKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTS 2621
Cdd:COG4913 367 LLAALGLPLPASAEEFA-------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKS 436
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2389-2556 |
2.24e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 49.15 E-value: 2.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2389 VQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLE----E 2464
Cdd:COG1579 10 LDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNvrnnK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2465 EAENMKKlAEEAARLNIEAQEAARLrqiaesDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQAQVEAQKLL 2543
Cdd:COG1579 90 EYEALQK-EIESLKRRISDLEDEIL------ELMERIEELEEELAELEAELAELeAELEEKKAELDEELAELEAELEELE 162
|
170
....*....|...
gi 1207141724 2544 EAKKEMQQRLDQE 2556
Cdd:COG1579 163 AEREELAAKIPPE 175
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2489-2935 |
2.32e-05 |
|
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: 50.88 E-value: 2.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2489 LRQIAES-DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQK----------QKDQAQVEAQKLLEAKKEMQQRLDQET 2557
Cdd:pfam05483 50 LEQVANSgDCHYQEGLKDSDFENSEGLSRLYSKLYKEAEKIKKwkvsieaelkQKENKLQENRKIIEAQRKAIQELQFEN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2558 EGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQS 2637
Cdd:pfam05483 130 EKVSLKLEEEIQENKDLIKENNATRHLCNLLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEELRVQAENA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2638 KQEadgLHKAIADLEKEKEKlkkeaadLQKQSKEMANVQQEQLQqekTILQQSffAEKETLLKKEKAIEEEKKKLEKQFE 2717
Cdd:pfam05483 210 RLE---MHFKLKEDHEKIQH-------LEEEYKKEINDKEKQVS---LLLIQI--TEKENKMKDLTFLLEESRDKANQLE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2718 DEVK-KAEALKAEQERQRKLMEEeRKKLQSAMDAAIKKQKEAEEEMN-----------GKQKEMQDLEKKRIEQEKLLAE 2785
Cdd:pfam05483 275 EKTKlQDENLKELIEKKDHLTKE-LEDIKMSLQRSMSTQKALEEDLQiatkticqlteEKEAQMEELNKAKAAHSFVVTE 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2786 ENKN-------LREKLQQLQSSQKASYTKEIEIQTDKVPEEELVQMT-----MVETTKKVLNGSTEVDGVKKDvplaFDG 2853
Cdd:pfam05483 354 FEATtcsleelLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKnnkevELEELKKILAEDEKLLDEKKQ----FEK 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2854 IREKVPASRLHEIGVLSKKEYD------KLKKGKTTVQELSKNDKVKMCLKGKDCIGGVIVEPNQKMsiyQALKDKMITQ 2927
Cdd:pfam05483 430 IAEELKGKEQELIFLLQAREKEihdleiQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDK---LLLENKELTQ 506
|
....*...
gi 1207141724 2928 STAIMLLE 2935
Cdd:pfam05483 507 EASDMTLE 514
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2196-2602 |
2.43e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 50.82 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2196 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEK--QVI-----LVQEAAQKCSAAEQKAQNVLVQQNKD 2268
Cdd:PRK10929 26 KQITQELEQAKAAKTPAQAEIVEALQSALNWLEERKGSLERAKQyqQVIdnfpkLSAELRQQLNNERDEPRSVPPNMSTD 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2269 SMAQDKLK---EEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEeaerqkkaaeaeaakqakaqedAEKLRKEAEKEasrr 2345
Cdd:PRK10929 106 ALEQEILQvssQLLEKSRQAQQEQDRAREISDSLSQLPQQQTE----------------------ARRQLNEIERR---- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2346 aeaeaaaLKLKQEADS--EMAKYKKLAEKTLKQKSSVEE-ELVkvkvQLDETDKQksvldvELKRLKQEVsdAIKQKAQV 2422
Cdd:PRK10929 160 -------LQTLGTPNTplAQAQLTALQAESAALKALVDElELA----QLSANNRQ------ELARLRSEL--AKKRSQQL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2423 EDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLeeeAENMKKLAEEAARLNIEAQE----AARLRQIAESDLa 2498
Cdd:PRK10929 221 DAYLQALRNQLNSQRQREAERALESTELLAEQSGDLPKSI---VAQFKINRELSQALNQQAQRmdliASQQRQAASQTL- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2499 kQRELAEKMLEEKKQ------AIQEAakLKAEAEKL-------QKQKDQAQVEAQKL-LEAKKEMQQRLDQE-------- 2556
Cdd:PRK10929 297 -QVRQALNTLREQSQwlgvsnALGEA--LRAQVARLpempkpqQLDTEMAQLRVQRLrYEDLLNKQPQLRQIrqadgqpl 373
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 2557 TEGFQKSLEAERKRQ---------------LEITaeaeKLKVKVTQLSDAQSKAEEEAKKF 2602
Cdd:PRK10929 374 TAEQNRILDAQLRTQrellnsllsggdtliLELT----KLKVANSQLEDALKEVNEATHRY 430
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2455-2689 |
2.50e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 51.11 E-value: 2.50e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2455 KDNTKKLLEEEAENMKKLAEEAARLNIEAQEAAR----LRQ-IAESDLAKQR-----ELAEKMLEE--KKQAIQEAAKLK 2522
Cdd:COG3096 422 LEKARALCGLPDLTPENAEDYLAAFRAKEQQATEevleLEQkLSVADAARRQfekayELVCKIAGEveRSQAWQTARELL 501
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2523 AEAEKLQKQKDQAQVEAQKLLEAKKEM--QQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2600
Cdd:COG3096 502 RRYRSQQALAQRLQQLRAQLAELEQRLrqQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRS 581
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2601 KFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQeadglhkAIADLEKEKEKLKKEAADL--QKQSKEMANVQQE 2678
Cdd:COG3096 582 ELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGE-------ALADSQEVTAAMQQLLEREreATVERDELAARKQ 654
|
250
....*....|.
gi 1207141724 2679 QLQQEKTILQQ 2689
Cdd:COG3096 655 ALESQIERLSQ 665
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1571-1797 |
2.51e-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: 50.15 E-value: 2.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1571 AEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVEE 1650
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAAL----EAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1651 AllsRTRIEEEIHIIRLQLETTMKQKNTAETELL------------------QLRAKAVDADKLRnAAQEEAEKLRKQVA 1712
Cdd:COG4942 95 L---RAELEAQKEELAELLRALYRLGRQPPLALLlspedfldavrrlqylkyLAPARREQAEELR-ADLAELAALRAELE 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1713 EETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVA 1792
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAGFAA 250
|
....*
gi 1207141724 1793 LTARL 1797
Cdd:COG4942 251 LKGKL 255
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1932-2588 |
2.55e-05 |
|
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: 50.91 E-value: 2.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1932 QQRTVLDDELQRLKndvnsavkqkkELEEElikVRKEMEILLQQKSKAEKETMSntekskqlLESEAAKMRELAEEATKL 2011
Cdd:pfam07111 63 QQAELISRQLQELR-----------RLEEE---VRLLRETSLQQKMRLEAQAME--------LDALAVAEKAGQAEAEGL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2012 RSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEAtrlkteAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQ 2091
Cdd:pfam07111 121 RAALAGAEMVRKNLEEGSQRELEEIQRLHQEQLSSLTQA------HEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAE 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2092 HKQAIEEKIGQLKKSSDtELDRQKKIVEETlkqRKVVEE----EIHILKLNFEKassgKQELELELKKLKGIADETQKSK 2167
Cdd:pfam07111 195 AQKEAELLRKQLSKTQE-ELEAQVTLVESL---RKYVGEqvppEVHSQTWELER----QELLDTMQHLQEDRADLQATVE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2168 AKAEEEAEKFRKLALEEEKKRKEaeakVKQIQAAEEEAARQHKAA----QEEVGRLMKLAEEAKKQKEIAEKEAEKQVIL 2243
Cdd:pfam07111 267 LLQVRVQSLTHMLALQEEELTRK----IQPSDSLEPEFPKKCRSLlnrwREKVFALMVQLKAQDLEHRDSVKQLRGQVAE 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2244 VQEAAqkcsAAEQKAQNVLVQQNKDSMAQdkLKEEFEKAKKLAQEAEKAKDNAEKEaallHKKAEEAERQKKAAEAEAAK 2323
Cdd:pfam07111 343 LQEQV----TSQSQEQAILQRALQDKAAE--VEVERMSAKGLQMELSRAQEARRRQ----QQQTASAEEQLKFVVNAMSS 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2324 QAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKykKLAEKTLKQKSSVEEELV-----KVKVQLDETDKQK 2398
Cdd:pfam07111 413 TQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMAR--KVALAQLRQESCPPPPPAppvdaDLSLELEQLREER 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2399 SVLDVELKR----LKQEVSDAIKQKAQVEDELSKVKIQMEdllklklkiekenQELMKKdkdntkkllEEEAENMKKLAE 2474
Cdd:pfam07111 491 NRLDAELQLsahlIQQEVGRAREQGEAERQQLSEVAQQLE-------------QELQRA---------QESLASVGQQLE 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2475 EAARLNIEA-QEAARLRQiaesDLAKQRELAEKMLEEKKQAIQeaAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2553
Cdd:pfam07111 549 VARQGQQEStEEAASLRQ----ELTQQQEIYGQALQEKVAEVE--TRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRA 622
|
650 660 670
....*....|....*....|....*....|....*
gi 1207141724 2554 DQETEgfqKSLEAERKRQLEITAEAEKLKVKVTQL 2588
Cdd:pfam07111 623 TQEKE---RNQELRRLQDEARKEEGQRLARRVQEL 654
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1325-1799 |
2.59e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.54 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1325 KVPVNEKEIEASQTQLQklrsEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGN--LRERWQAVFAQ 1402
Cdd:COG4717 65 KPELNLKELKELEEELK----EAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1403 IELRQRELDLLNRQMQAYRESYDWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKG 1482
Cdd:COG4717 141 LAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1483 YIDAIKDyELQLVTYKALVEPIASPLKKAKMESASDDIIqeyVTLRTRYSELMTLSSQYIKFIIetqrrlqdeekAAEKL 1562
Cdd:COG4717 221 ELEELEE-ELEQLENELEAAALEERLKEARLLLLIAAAL---LALLGLGGSLLSLILTIAGVLF-----------LVLGL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1563 KEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKTLSEQEIK 1642
Cdd:COG4717 286 LALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQL 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1643 AKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAE 1722
Cdd:COG4717 366 EELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELE 445
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 1723 EELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQ-IQVVEEVAKKTAATQLESKQVALTARLEE 1799
Cdd:COG4717 446 EELEELREELAELEAELEQLEEDGELAELLQELEELKAELRELAEEWAaLKLALELLEEAREEYREERLPPVLERASE 523
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1708-1916 |
2.61e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.26 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1708 RKQVAEETQKKRKAEEELKRKSeaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQVVEeVAKKTAATQLE 1787
Cdd:COG2268 191 RRKIAEIIRDARIAEAEAERET--------------------EIAIAQANREAEEAELEQEREIETAR-IAEAEAELAKK 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1788 skqvaltarleeslkneqvmviqlQEEAEhlkkqqAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEA 1867
Cdd:COG2268 250 ------------------------KAEER------REAETARAEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEA 299
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1207141724 1868 EKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1916
Cdd:COG2268 300 EREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAE 348
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2473-2678 |
2.66e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2473 AEEAARLNIEAQEAARLRQIAESDLAKQ-RELAEKMLEEKkQAIQEAAKLKAEAEKLQKQKDQAqveAQKLLEAKKEMQQ 2551
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQaEELQQKQAAEQ-ERLKQLEKERLAAQEQKKQAEEA---AKQAALKQKQAEE 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2552 RLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQlSDAQSKAEEEAKkfKKQADEIKIRLQETEKHTSEKhtvvEKLE 2631
Cdd:PRK09510 137 AAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAE-AEAAKKAAAEAK--KKAEAEAAAKAAAEAKKKAEA----EAKK 209
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1207141724 2632 VQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQE 2678
Cdd:PRK09510 210 KAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAA 256
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3258-3293 |
2.73e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.01 E-value: 2.73e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1207141724 3258 LNLLEAQAGTGFIIDPVKNQKLTVDEAVKSGVVGPE 3293
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2199-2377 |
2.82e-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: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2199 QAAEEEAARQHK--AAQEEVGRLMKLAEEAKKQkeiAEKEAEKQvilVQEAAQKcSAAEQKAQnvlvqqnkdSMAQDKLK 2276
Cdd:TIGR02794 119 KQAEEAKAKQAAeaKAKAEAEAERKAKEEAAKQ---AEEEAKAK---AAAEAKK-KAEEAKKK---------AEAEAKAK 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2277 EEFE---KAKKLAQEAEKAKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEaeaaal 2353
Cdd:TIGR02794 183 AEAEakaKAEEAKAKAEAAKAKAAAEAA---AKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGAR------ 253
|
170 180
....*....|....*....|....
gi 1207141724 2354 klKQEADSEMAKYKKLAEKTLKQK 2377
Cdd:TIGR02794 254 --GAAAGSEVDKYAAIIQQAIQQN 275
|
|
| SH3_Tec_like |
cd11768 |
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed ... |
1006-1051 |
3.02e-05 |
|
Src Homology 3 domain of Tec-like Protein Tyrosine Kinases; The Tec (Tyrosine kinase expressed in hepatocellular carcinoma) subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) tyr kinases containing Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Most Tec subfamily members (except Rlk) also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. The function of Tec kinases in lymphoid cells have been studied extensively. They play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212702 [Multi-domain] Cd Length: 54 Bit Score: 44.19 E-value: 3.02e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1207141724 1006 VQAVCDFKQME---ITVHKGDECALVNNSQPYKWKVRDSSGNEAVVPSI 1051
Cdd:cd11768 2 VVALYDFQPIEpgdLPLEKGEEYVVLDDSNEHWWRARDKNGNEGYIPSN 50
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1798-1963 |
3.04e-05 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 50.00 E-value: 3.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1798 EESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAE-EEANKKTAAQEEAEKQKEEAKR 1876
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADtSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1877 EAKKRAkaeEAALKQKEAAEMELGNQRKMAEETAKQKLaaeqelirlradfEHAEQQRTVLDDELQRLKNDVNSavkQKK 1956
Cdd:pfam05262 289 EIKKND---EEALKAKDHKAFDLKQESKASEKEAEDKE-------------LEAQKKREPVAEDLQKTKPQVEA---QPT 349
|
....*..
gi 1207141724 1957 ELEEELI 1963
Cdd:pfam05262 350 SLNEDAI 356
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2595-2811 |
3.19e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2595 AEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMAN 2674
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2675 VQQEQLQQEKTIlqqsffaekETLLKKEkaieeekkklekQFEDEVKKAEALKAEQERQRKLMEE---ERKKLQSAMDAA 2751
Cdd:COG3883 94 ALYRSGGSVSYL---------DVLLGSE------------SFSDFLDRLSALSKIADADADLLEElkaDKAELEAKKAEL 152
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2752 IKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2811
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAA 212
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
1450-2108 |
3.73e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 50.02 E-value: 3.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1450 KGLQEQLTQEKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKAlvepiasplKKAKMESASDDIIQEYVTLRT 1529
Cdd:TIGR04523 131 KQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLEK---------EKLNIQKNIDKIKNKLLKLEL 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1530 RYSELMTLssqyikfiIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQlaethakAIAKAEQEANELK---TKMK 1606
Cdd:TIGR04523 202 LLSNLKKK--------IQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTT-------EISNTQTQLNQLKdeqNKIK 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1607 DEVSKRQDVAVDSEKQKHNIQRELQELKTlseqEIKAKSQQVEEALLSRtrieeeihiIRLQLETTMKQKNTAETELLQl 1686
Cdd:TIGR04523 267 KQLSEKQKELEQNNKKIKELEKQLNQLKS----EISDLNNQKEQDWNKE---------LKSELKNQEKKLEEIQNQISQ- 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1687 rakavdADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHL-KQAEL 1765
Cdd:TIGR04523 333 ------NNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIqNQEKL 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1766 EKQRQIQVveevakKTAATQLESKQVALTARLEESLKNEQvMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANE 1845
Cdd:TIGR04523 407 NQQKDEQI------KKLQQEKELLEKEIERLKETIIKNNS-EIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINK 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1846 ALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKrAKAEEAALKQKEaaemelgnqrkmaEETAKQKLAAEQELIRLRA 1925
Cdd:TIGR04523 480 IKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKD-LTKKISSLKEKI-------------EKLESEKKEKESKISDLED 545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1926 DFEHAEQQRTvlDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELA 2005
Cdd:TIGR04523 546 ELNKDDFELK--KENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQKEKEKKDLIKEIEEKEKKISSLEKELEKAK 623
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2006 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAE--IALKEKEAENDRLKRKAEEEGYQRK 2083
Cdd:TIGR04523 624 KENEKLSSIIKNIKSKKNKLKQEVKQIKETIKEIRNKWPEIIKKIKESKTKIDdiIELMKDWLKELSLHYKKYITRMIRI 703
|
650 660
....*....|....*....|....*
gi 1207141724 2084 VLEDQAAQHKQAIEEKIGQLKKSSD 2108
Cdd:TIGR04523 704 KDLPKLEEKYKEIEKELKKLDEFSK 728
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1550-1758 |
3.77e-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: 3.77e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1550 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRE 1629
Cdd:COG4942 30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAEL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1630 LQELKTLSEQ---EIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNtaetELLQLRAKAVDADKLRNAAQEEAEK 1706
Cdd:COG4942 110 LRALYRLGRQpplALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA----ELAALRAELEAERAELEALLAELEE 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 1707 LRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKF--KLQAEEAER 1758
Cdd:COG4942 186 ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAA 239
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1573-1728 |
4.03e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.38 E-value: 4.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1573 MQAELEKQKQLAETHAKaIAKAEQEANELK---TKMKDEVSKRQDVAVDSEKQKHNIQRELQELktlsEQEIKAKSQQVE 1649
Cdd:COG1579 2 MPEDLRALLDLQELDSE-LDRLEHRLKELPaelAELEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARIK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1650 --EALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKR 1727
Cdd:COG1579 77 kyEEQLGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEA 156
|
.
gi 1207141724 1728 K 1728
Cdd:COG1579 157 E 157
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
2196-2604 |
4.09e-05 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 49.76 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2196 KQIQAAEEEAARQHKAAQEEVgrlmKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAaeqKAQNVLVQQNKDSMAQDKl 2275
Cdd:pfam09731 89 VKIPRQSGVSSEVAEEEKEAT----KDAAEAKAQLPKSEQEKEKALEEVLKEAISKAE---SATAVAKEAKDDAIQAVK- 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2276 keefEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAerqkkaaeaeaakqakaqedAEKLRKEAEKEASRRAEAEAAALKL 2355
Cdd:pfam09731 161 ----AHTDSLKEASDTAEISREKATDSALQKAEAL--------------------AEKLKEVINLAKQSEEEAAPPLLDA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2356 KQEADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqLDETDKQksVLDVELKRLKQEVSDAIKQK-AQVEDELSKVkiqME 2434
Cdd:pfam09731 217 APETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKE-LVASERI--VFQQELVSIFPDIIPVLKEDnLLSNDDLNSL---IA 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2435 DLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARlNIEAQEAARLRQIAESdlakqrelaekmLEEKKQA 2514
Cdd:pfam09731 291 HAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSA-RLEEVRAADEAQLRLE------------FEREREE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2515 IQEAAKLKAEAEklqkQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKS-LEAERKRQLEITAEAeKLKVK-VTQLSDAQ 2592
Cdd:pfam09731 358 IRESYEEKLRTE----LERQAEAHEEHLKDVLVEQEIELQREFLQDIKEkVEEERAGRLLKLNEL-LANLKgLEKATSSH 432
|
410
....*....|..
gi 1207141724 2593 SKAEEEAKKFKK 2604
Cdd:pfam09731 433 SEVEDENRKAQQ 444
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
236-326 |
4.11e-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: 4.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 236 KWVNKHLVKAQR---HITDLYEDLRDGHNLISLLEVLSGETLPREKGRM---RFHKLQNVQIALDFLkhRQVKLVN-IRN 308
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAA--EKLGCKYfLTP 94
|
90
....*....|....*...
gi 1207141724 309 DDIADGNPKLTLGLIWTI 326
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| F-BAR_PSTPIP |
cd07647 |
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine ... |
2402-2636 |
4.40e-05 |
|
The F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain of Proline-Serine-Threonine Phosphatase-Interacting Proteins; F-BAR domains are dimerization modules that bind and bend membranes and are found in proteins involved in membrane dynamics and actin reorganization. Vetebrates contain two Proline-Serine-Threonine Phosphatase-Interacting Proteins (PSTPIPs), PSTPIP1 and PSTPIP2. PSTPIPs are mainly expressed in hematopoietic cells and are involved in the regulation of cell adhesion and motility. Mutations in PSTPIPs have been shown to cause autoinflammatory disorders. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, and a C-terminal SH3 domain, while PSTPIP2 contains only the N-terminal F-BAR domain. F-BAR domains form banana-shaped dimers with a positively-charged concave surface that binds to negatively-charged lipid membranes. They can induce membrane deformation in the form of long tubules.
Pssm-ID: 153331 [Multi-domain] Cd Length: 239 Bit Score: 48.24 E-value: 4.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2402 DVELKRLK------QEVSDAIKQKAQVEDELSKVKIQMEDLLKLklkiekenqelmkKDKDNTkklLEEEAENMKKLAEE 2475
Cdd:cd07647 8 DTLLQRLKegkkmcKELEDFLKQRAKAEEDYGKALLKLSKSAGP-------------GDEIGT---LKSSWDSLRKETEN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2476 AARLNIEaqeaarlrqiaesdLAKQ-RELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKdqaQVEAQKLLEAKKEMQQRLd 2554
Cdd:cd07647 72 VANAHIQ--------------LAQSlREEAEKLEEFREKQKEERKKTEDIMKRSQKNK---KELYKKTMKAKKSYEQKC- 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2555 QETEGFQKSleAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKLEVQR 2634
Cdd:cd07647 134 REKDKAEQA--YEKSSSGAQPKEAEKLKKKAAQCKTSAEEADSAYKSSIGCLEDAR---VEWESEHATACQVFQNMEEER 208
|
..
gi 1207141724 2635 LQ 2636
Cdd:cd07647 209 IK 210
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
1578-2012 |
4.73e-05 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 49.82 E-value: 4.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1578 EKQKQLaethakaiakaeQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQelkTLSEQeIKAKSQQVEEAllsRTR 1657
Cdd:pfam10174 363 KKTKQL------------QDLTEEKSTLAGEIRDLKDMLDVKERKINVLQKKIE---NLQEQ-LRDKDKQLAGL---KER 423
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1658 IEEeihiirLQLETTmkqknTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAK 1737
Cdd:pfam10174 424 VKS------LQTDSS-----NTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQPELT 492
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1738 EKKKALEDL-EKFKLQAEEA---ERHLKQAELEkqrqIQVVEEVAKKTAATQLESKQVALTARLEESLKNE-QVMVIQLQ 1812
Cdd:pfam10174 493 EKESSLIDLkEHASSLASSGlkkDSKLKSLEIA----VEQKKEECSKLENQLKKAHNAEEAVRTNPEINDRiRLLEQEVA 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1813 EEAEHLKKQQAEADK---AREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQeeaekqkeeakreakkraKAEEAAL 1889
Cdd:pfam10174 569 RYKEESGKAQAEVERllgILREVENEKNDKDKKIAELESLTLRQMKEQNKKVANI------------------KHGQQEM 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1890 KQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLradfehaEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEM 1969
Cdd:pfam10174 631 KKKGAQLLEEARRREDNLADNSQQLQLEELMGAL-------EKTRQELDATKARLSSTQQSLAEKDGHLTNLRAERRKQL 703
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1207141724 1970 EILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLR 2012
Cdd:pfam10174 704 EEILEMKQEALLAAISEKDANIALLELSSSKKKKTQEEVMALK 746
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1640-1918 |
5.10e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1640 EIKAKSQQVEEALLSRTRIEEEIhiIRLQLETtmkqkntAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKR 1719
Cdd:PRK05035 437 EIRAIEQEKKKAEEAKARFEARQ--ARLEREK-------AAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIV 507
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1720 KAEEELKRKSEAEKDAakekkkaleDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQvalTARLEE 1799
Cdd:PRK05035 508 IKAGARPDNSAVIAAR---------EARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANA---EAEEEV 575
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1800 SLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELetwRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAK 1879
Cdd:PRK05035 576 DPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDP---KKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAI 652
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141724 1880 KRAKAEEAALKQKEAAEMELGNQRKMAEETA----KQKLAAEQ 1918
Cdd:PRK05035 653 ARAKARKAAQQQANAEPEEAEDPKKAAVAAAiaraKAKKAAQQ 695
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1792-2224 |
5.12e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 5.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1792 ALTARLE-----ESLKNEQVMVIQLQEEAEHLkkqqaeadkarEQAEKELETWRQKANEALRLRLQAEEEANKKtaaqee 1866
Cdd:COG3096 287 ALELRRElfgarRQLAEEQYRLVEMARELEEL-----------SARESDLEQDYQAASDHLNLVQTALRQQEKI------ 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1867 aekqkeeakreAKKRAKAEEAALKQKEAAEM--ELGNQRKMAEEtakQKLAAEQELIRLR---ADFEHA--EQQRTVLD- 1938
Cdd:COG3096 350 -----------ERYQEDLEELTERLEEQEEVveEAAEQLAEAEA---RLEAAEEEVDSLKsqlADYQQAldVQQTRAIQy 415
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1939 -DELQRLKN----------DVNSAVKQKKELEEELIKVRKEMeILLQQKSKAEKETMSNTEKSKQLLESEAA-------- 1999
Cdd:COG3096 416 qQAVQALEKaralcglpdlTPENAEDYLAAFRAKEQQATEEV-LELEQKLSVADAARRQFEKAYELVCKIAGeversqaw 494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2000 -KMRELAEEATKLRSVAEEAKK-QRQIAE-EEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAE 2076
Cdd:COG3096 495 qTARELLRRYRSQQALAQRLQQlRAQLAElEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAA 574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2077 EEGYQRKVLEdqaaQHKQAIEEKIGQLKKS------SDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKqele 2150
Cdd:COG3096 575 EAVEQRSELR----QQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVER---- 646
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2151 lelkklkgiaDETQkskakaeeeaekFRKLALeeekkrkeaeakvkqiqaaEEEAARQHKAAQEEVGRLMKLAE 2224
Cdd:COG3096 647 ----------DELA------------ARKQAL-------------------ESQIERLSQPGGAEDPRLLALAE 679
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
230-338 |
5.19e-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: 46.59 E-value: 5.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 230 QKKTFTKWVNK---------HLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 296
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141724 297 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVN 338
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1812-2040 |
5.28e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.03 E-value: 5.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1812 QEEAEHLKKQQAEADKAREQAEKELETWRQKANEalRLRLQAEEEANKKtaaqeeaekqkEEAKREAKKRAK-AEEAALK 1890
Cdd:PRK09510 74 AKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLE--KERLAAQEQKKQA-----------EEAAKQAALKQKqAEEAAAK 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1891 QKEAAemelgnqrkmaeetakqKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKndvnSAVKQKKELEEElikVRKEME 1970
Cdd:PRK09510 141 AAAAA-----------------KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKK----AAAEAKKKAEAE---AAAKAA 196
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1971 ILLQQKSKAEKETMSNTEkSKQLLESEAAKMRELAEEATKlrSVAEEAKKQRQIAEEEAARQRAEAEKIL 2040
Cdd:PRK09510 197 AEAKKKAEAEAKKKAAAE-AKKKAAAEAKAAAAKAAAEAK--AAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1917-2077 |
5.64e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 5.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1917 EQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtMSNTEKSKQLles 1996
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ-LGNVRNNKEY--- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1997 eAAKMRELaEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEatrLKTEAEIALKEKEAENDRLKRKAE 2076
Cdd:COG1579 92 -EALQKEI-ESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEE---KKAELDEELAELEAELEELEAERE 166
|
.
gi 1207141724 2077 E 2077
Cdd:COG1579 167 E 167
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1877-2125 |
5.93e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 5.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1877 EAKKRAKAEEAALKQKEAAEMELGNQrkmAEETAKQKLAAEQELIRLRADFEHAEQQRTVlddELQRLKndvnsAVKQKK 1956
Cdd:TIGR02794 51 QANRIQQQKKPAAKKEQERQKKLEQQ---AEEAEKQRAAEQARQKELEQRAAAEKAAKQA---EQAAKQ-----AEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1957 ELEEELIKVRKEmeillqQKSKAEKEtmsntekSKQLLESEAAKMRElaEEATKlrSVAEEAKKQRQIAE---EEAARQR 2033
Cdd:TIGR02794 120 QAEEAKAKQAAE------AKAKAEAE-------AERKAKEEAAKQAE--EEAKA--KAAAEAKKKAEEAKkkaEAEAKAK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2034 AEAE-KILKEKLTAINEATRLKTEAEiALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQ-LKKSSDTEL 2111
Cdd:TIGR02794 183 AEAEaKAKAEEAKAKAEAAKAKAAAE-AAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGaRGAAAGSEV 261
|
250
....*....|....
gi 1207141724 2112 DRQKKIVEETLKQR 2125
Cdd:TIGR02794 262 DKYAAIIQQAIQQN 275
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2454-2615 |
5.98e-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: 5.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2454 DKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmleekkqAIQEAAKLKAEAEKLQKQKD 2533
Cdd:pfam05262 179 DKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADK-------AQQKADFAQDNADKQRDEVR 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2534 QAQVEAQKLLEAKKEMQQRLDQETEGFQKSlEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRL 2613
Cdd:pfam05262 252 QKQQEAKNLPKPADTSSPKEDKQVAENQKR-EIEKAQIEIKKNDEEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKR 330
|
..
gi 1207141724 2614 QE 2615
Cdd:pfam05262 331 EP 332
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1625-1964 |
6.34e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1625 NIQRELQELKTLsEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEA 1704
Cdd:COG4372 32 QLRKALFELDKL-QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1705 EKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAT 1784
Cdd:COG4372 111 EELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1785 QLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQ 1864
Cdd:COG4372 191 EANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVE 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1865 EEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRL 1944
Cdd:COG4372 271 KDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGL 350
|
330 340
....*....|....*....|
gi 1207141724 1945 KNDVNSAVKQKKELEEELIK 1964
Cdd:COG4372 351 LDNDVLELLSKGAEAGVADG 370
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2196-2334 |
6.67e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 48.65 E-value: 6.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2196 KQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQkeiAEKEAEKQVilvQEAAQKCSAAEQKAQNVLVQQNKdSMAQDKL 2275
Cdd:PRK09510 129 LKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK---AAAEAKKKA---EAEAAKKAAAEAKKKAEAEAAAK-AAAEAKK 201
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2276 KEEFEKAKKLAQEAEK-----AKDNAEKEAAllhKKAEEAERQKKAAEAEAAKQAKAQEDAEKL 2334
Cdd:PRK09510 202 KAEAEAKKKAAAEAKKkaaaeAKAAAAKAAA---EAKAAAEKAAAAKAAEKAAAAKAAAEVDDL 262
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2682-2811 |
8.65e-05 |
|
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: 48.05 E-value: 8.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2682 QEKTILQQsFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRklmeEERKKLQSAMDAAIKKQKEAEEE 2761
Cdd:pfam02841 173 KAEEVLQE-FLQSKEAVEEAILQTDQALTAKEKAIEAERAKAEAAEAEQELLR----EKQKEEEQMMEAQERSYQEHVKQ 247
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2762 MngKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEI 2811
Cdd:pfam02841 248 L--IEKMEAEREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQKEIQD 295
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1528-1944 |
8.71e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.75 E-value: 8.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1528 RTRYSELMTLSSQYIKF---IIETQRRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEANELKTK 1604
Cdd:COG5278 106 QARLDELEALIDQWLAEleqVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAAL 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1605 MKDEVSKRQDVAVDSEKQKHNIQRELQELkTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELL 1684
Cdd:COG5278 186 LALAELLLLALARALAALLLLLLLEAELA-AAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1685 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1764
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1765 LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKAN 1844
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1845 EALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLR 1924
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410 420
....*....|....*....|
gi 1207141724 1925 ADFEHAEQQRTVLDDELQRL 1944
Cdd:COG5278 505 LAALLLAAAEAALAAALAAA 524
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
1799-2083 |
8.76e-05 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 47.98 E-value: 8.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1799 ESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEaLRLRLQAEEEANKKTAAQEEAEKQKEEAKREA 1878
Cdd:COG1340 1 SKTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDE-LNAQVKELREEAQELREKRDELNEKVKELKEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1879 KKRAKAEEAALKQKEAaemELGNQRKMAEETAKQKLAAEQELIRLRAdfehaEQQRTVLD--------DELQRLKNDVNs 1950
Cdd:COG1340 80 RDELNEKLNELREELD---ELRKELAELNKAGGSIDKLRKEIERLEW-----RQQTEVLSpeeekelvEKIKELEKELE- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1951 AVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 2030
Cdd:COG1340 151 KAKKALEKNEKLKELRAELKELRKEAEEIHKKIKELAEEAQELHE----EMIELYKEADELRKEADELHKEIVEAQEKAD 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1207141724 2031 RQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRK 2083
Cdd:COG1340 227 ELHEEIIELQKELRELRKELKKLRKKQRALKREKEKEELEEKAEEIFEKLKKG 279
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2498-2765 |
9.30e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.22 E-value: 9.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2498 AKQRELAEKMLEEKKQAIQEaakLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLdQETEGFQKSLEAErkrqleitae 2577
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAE---LEKELAALKKEEKALLKQLAALERRIAALARRI-RALEQELAALEAE---------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2578 aeklkvkvtqLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVeklevqrLQSKQEADGLHKAIADLEKEKEK 2657
Cdd:COG4942 85 ----------LAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL-------LLSPEDFLDAVRRLQYLKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2658 LKKEAADLQKQSKEMANVQQEQLQQEKtilqqsffaEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLM 2737
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERA---------ELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
250 260
....*....|....*....|....*...
gi 1207141724 2738 EEERKKLQSAMDAAIKKQKEAEEEMNGK 2765
Cdd:COG4942 219 QQEAEELEALIARLEAEAAAAAERTPAA 246
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2462-2673 |
9.40e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 48.79 E-value: 9.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2462 LEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdlAKQRELAekmLEEKKQAIQEAAKLKAEA-EKLQKQKDQAQVEAQ 2540
Cdd:pfam15709 309 MESEEERSEEDPSKALLEKREQEKASRDRLRAER--AEMRRLE---VERKRREQEEQRRLQQEQlERAEKMREELELEQQ 383
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2541 KLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAEAEK-------LKVKVTQLS-DAQSKAEEEAKKFKKQADEIKIR 2612
Cdd:pfam15709 384 RRFEEIRLRKQRLEEER---QRQEEEERKQRLQLQAAQERarqqqeeFRRKLQELQrKKQQEEAERAEAEKQRQKELEMQ 460
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 2613 LQETEKHTSEKhTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMA 2673
Cdd:pfam15709 461 LAEEQKRLMEM-AEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQEQA 520
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1925-2298 |
1.05e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1925 ADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKetmsntekskqllESEAAKMR-E 2003
Cdd:PRK04863 272 ADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQ-------------DYQAASDHlN 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2004 LAEEAtklrsVAEEAKKQRQIAEEEAARQRAEAEKILKEkltainEATRLKTEAEIALKEKEAENDRLkrKAEEEGYQRK 2083
Cdd:PRK04863 339 LVQTA-----LRQQEKIERYQADLEELEERLEEQNEVVE------EADEQQEENEARAEAAEEEVDEL--KSQLADYQQA 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2084 --VLEDQAAQHKQAIE--EKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGI 2159
Cdd:PRK04863 406 ldVQQTRAIQYQQAVQalERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKI 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2160 ADETQKSkakaeEEAEKFRKLaLEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQeevgRLMKLAEEAKKQKEIAEKEAEK 2239
Cdd:PRK04863 486 AGEVSRS-----EAWDVAREL-LRRLREQRHLAEQLQQLRMRLSELEQRLRQQQ----RAERLLAEFCKRLGKNLDDEDE 555
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2240 QVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEK 2298
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALAR 614
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3918-3954 |
1.11e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.11e-04
10 20 30
....*....|....*....|....*....|....*..
gi 1207141724 3918 IDLLEAQAATGFMIDPVKDELLTVDEAVRKGLVGPEF 3954
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1969-2435 |
1.11e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 48.61 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1969 MEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEE-AKKQRQIAEEEAARQRAEAEKILKEKLTAI 2047
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2048 NEATRLKTEAEIALKEKEAENDRLKRKAEE-EGYQRKV--LEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQ 2124
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEElRELEEELeeLEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2125 RKVVEEEIHILKlnfEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAeee 2204
Cdd:COG4717 208 LAELEEELEEAQ---EELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFL--- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2205 aarqhkaaqeEVGRLMKLAEEAKKQKEIAEKEAEKqvilVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKK 2284
Cdd:COG4717 282 ----------VLGLLALLFLLLAREKASLGKEAEE----LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2285 LAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaAKQAKAQEDAEKLRKEAEKeasrrAEAEAAALKLKQEADSEMA 2364
Cdd:COG4717 348 ELQELLREAEELEEELQLEELEQEIAA----------LLAEAGVEDEEELRAALEQ-----AEEYQELKEELEELEEQLE 412
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2365 KYKKLAEKTLKQ--KSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQK--AQVEDELSKVKIQMED 2435
Cdd:COG4717 413 ELLGELEELLEAldEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGelAELLQELEELKAELRE 487
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2211-2424 |
1.15e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2211 AAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVilvQEAAQKCSAAEQKAQnvlvQQNKDSMAQDKLKEEFEKAKKLAQEAE 2290
Cdd:PRK09510 59 AVVEQYNRQQQQQKSAKRAEEQRKKKEQQQA---EELQQKQAAEQERLK----QLEKERLAAQEQKKQAEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2291 KAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAAlKLKQEADSEM-AKYKKL 2369
Cdd:PRK09510 132 KQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAA-KAAAEAKKKAeAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2370 AEKTLKQKSSVEEELVKVKvqldETDKQKSVLDVELKRLKQEVSDAIKQKAQVED 2424
Cdd:PRK09510 211 AAAEAKKKAAAEAKAAAAK----AAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDD 261
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1668-2091 |
1.16e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 48.36 E-value: 1.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1668 QLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLE 1747
Cdd:COG5278 111 ELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAE 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1748 KFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADK 1827
Cdd:COG5278 191 LLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1828 AREQAEKELETWRQKANEALRLRLQAEEEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAE 1907
Cdd:COG5278 271 AALLLALAAAAALAAAAALELAAAEALALA-----ELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1908 ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNT 1987
Cdd:COG5278 346 LLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELA 425
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1988 EKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAE 2067
Cdd:COG5278 426 EALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALAL 505
|
410 420
....*....|....*....|....
gi 1207141724 2068 NDRLKRKAEEEGYQRKVLEDQAAQ 2091
Cdd:COG5278 506 AALLLAAAEAALAAALAAALASAE 529
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1766-2083 |
1.17e-04 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 48.11 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1766 EKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKK------QQAEADKAREQAEKELETW 1839
Cdd:pfam15558 4 ERDRKIAALMLARHKEEQRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQsqeqwqAEKEQRKARLGREERRRAD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1840 RQKANEAL---RLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALkQKEAAEMELGNQRKMAE--------- 1907
Cdd:pfam15558 84 RREKQVIEkesRWREQAEDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL-QALREQNSLQLQERLEEachkrqlke 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1908 --------ETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKA 1979
Cdd:pfam15558 163 reeqkkvqENNLSELLNHQARKVLVDCQAKAEELLRRLSLEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRA 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1980 EKETMSNTEKSKQLLESEAAKMRelaeeatKLRSVAEEAKKQR--QIAEEEAARQRaeAEKILKEKLTAINEATRLKTEA 2057
Cdd:pfam15558 243 EEKEEERQEHKEALAELADRKIQ-------QARQVAHKTVQDKaqRARELNLEREK--NHHILKLKVEKEEKCHREGIKE 313
|
330 340
....*....|....*....|....*.
gi 1207141724 2058 EIALKEKEAENDRLKRKAEEEGYQRK 2083
Cdd:pfam15558 314 AIKKKEQRSEQISREKEATLEEARKT 339
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1745-2045 |
1.17e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.80 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1745 DLEKFKLQAEEAERHLKQAELEKQRQIQvveevakktAATQLEsKQVALTARLEEslkneQVMVIQ---LQEEAEHLKKQ 1821
Cdd:PRK04863 838 ELRQLNRRRVELERALADHESQEQQQRS---------QLEQAK-EGLSALNRLLP-----RLNLLAdetLADRVEEIREQ 902
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1822 QAEADKAR----------EQAEKELETWRQKANEALRLRLQAEEeankktaaqeeaekqkeeakreakkrAKAEEAALKQ 1891
Cdd:PRK04863 903 LDEAEEAKrfvqqhgnalAQLEPIVSVLQSDPEQFEQLKQDYQQ--------------------------AQQTQRDAKQ 956
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1892 KEAAEMELgNQRK--MAEETAKQKLAAEQEL-IRLRADFEHAEQQRTVLDDEL--------------QRLKNDVNSAVKQ 1954
Cdd:PRK04863 957 QAFALTEV-VQRRahFSYEDAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQM 1035
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1955 KKELEEEL--IKVR--KEMEILLQQKSKAEKETMSNT-------EKSKQLLESE----AAKMRELAEEATKLRSVAEEAK 2019
Cdd:PRK04863 1036 LQELKQELqdLGVPadSGAEERARARRDELHARLSANrsrrnqlEKQLTFCEAEmdnlTKKLRKLERDYHEMREQVVNAK 1115
|
330 340
....*....|....*....|....*.
gi 1207141724 2020 KqRQIAEEEAARQRAEAEKILKEKLT 2045
Cdd:PRK04863 1116 A-GWCAVLRLVKDNGVERRLHRRELA 1140
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2717-2809 |
1.19e-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: 47.84 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2717 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQ 2796
Cdd:COG4942 33 QQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRA 112
|
90
....*....|...
gi 1207141724 2797 LQSSQKASYTKEI 2809
Cdd:COG4942 113 LYRLGRQPPLALL 125
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1174-2147 |
1.24e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 48.89 E-value: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1174 ALIQKDSTSGEQDESVCKSYITQIKDLRLRLEGCESRTVNRLRQMVDKEPLKACTQRATEQKKVQTElegIKKDLDKVVE 1253
Cdd:TIGR01612 682 SIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQNMETATVELHLSNIENKKNELLDIIVEIKKHIHGE---INKDLNKILE 758
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1254 KSEAvlATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVYLDKLkTIDlvirsTQGAEDILNKYENQLREVNKVPVNEKEI 1333
Cdd:TIGR01612 759 DFKN--KEKELSNKINDYAKEKDELNKYKSKISEIKNHYNDQI-NID-----NIKDEDAKQNYDKSKEYIKTISIKEDEI 830
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1334 EASQTQLQKLRSEAEGKQATFDRLE---------EELQRATEVNKRMSQLHSERdveLEHYRQLVGNLRERWQAVFAQIE 1404
Cdd:TIGR01612 831 FKIINEMKFMKDDFLNKVDKFINFEnnckekidsEHEQFAELTNKIKAEISDDK---LNDYEKKFNDSKSLINEINKSIE 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1405 LRQRELDLLNRqmqayresYDWLIRWIADAKQRQDKLHavpiggskglqeqlTQEKKLLEEIEKNKDKVEDCQKFAKGYI 1484
Cdd:TIGR01612 908 EEYQNINTLKK--------VDEYIKICENTKESIEKFH--------------NKQNILKEILNKNIDTIKESNLIEKSYK 965
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1485 DaikDYELQLVTYKALVEPIASPLKKAKMESASDDIIQEYVTLRTRY--SELMTLSSQYI---KFIIETQRRLQDEEKAA 1559
Cdd:TIGR01612 966 D---KFDNTLIDKINELDKAFKDASLNDYEAKNNELIKYFNDLKANLgkNKENMLYHQFDekeKATNDIEQKIEDANKNI 1042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1560 EKLKEEERKKMAEMQAELEKQ--KQLAETHAKAIAKAEQEA---NELKTKMK----------------DEVSK-RQDVAV 1617
Cdd:TIGR01612 1043 PNIEIAIHTSIYNIIDEIEKEigKNIELLNKEILEEAEINItnfNEIKEKLKhynfddfgkeenikyaDEINKiKDDIKN 1122
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1618 DSEKQKHNIqRELQELKTLSEQ---EIKAKSQQVEEaLLSRTRIEEEIHIIRLQLETTM----KQKNTAE------TELL 1684
Cdd:TIGR01612 1123 LDQKIDHHI-KALEEIKKKSENyidEIKAQINDLED-VADKAISNDDPEEIEKKIENIVtkidKKKNIYDeikkllNEIA 1200
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1685 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEE--------------ELKRKSEAEKDAAKEKKKALEDLEKFK 1750
Cdd:TIGR01612 1201 EIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKKKSEhmikameayiedldEIKEKSPEIENEMGIEMDIKAEMETFN 1280
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1751 LQAEE-------AERHLKQAELEKQRQIQVVEEVAKKTAATQLESKqvaLTARLEESLKNEQVMVIQLQEEAE-----HL 1818
Cdd:TIGR01612 1281 ISHDDdkdhhiiSKKHDENISDIREKSLKIIEDFSEESDINDIKKE---LQKNLLDAQKHNSDINLYLNEIANiynilKL 1357
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1819 KKQQAEADKAREQAeKELETWRQKANEAL----RLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAK-------AEEA 1887
Cdd:TIGR01612 1358 NKIKKIIDEVKEYT-KEIEENNKNIKDELdkseKLIKKIKDDINLEECKSKIESTLDDKDIDECIKKIKelknhilSEES 1436
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1888 ALKQ--KEAAEME-----LGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVldDELQRLKNDVNSAVKQKKELEE 1960
Cdd:TIGR01612 1437 NIDTyfKNADENNenvllLFKNIEMADNKSQHILKIKKDNATNDHDFNINELKEHI--DKSKGCKDEADKNAKAIEKNKE 1514
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1961 ELIKVRKEMEILLQQKSKAE-KETMSNTEK-SKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEK 2038
Cdd:TIGR01612 1515 LFEQYKKDVTELLNKYSALAiKNKFAKTKKdSEIIIKEIKDAHKKFILEAEKSEQKIKEIKKEKFRIEDDAAKNDKSNKA 1594
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2039 ILKEKLTAINEATRL------KTEAEIALKEKEA------------ENDRLKRKAEEEGYQRKVLEDQAAQhKQAIEEKi 2100
Cdd:TIGR01612 1595 AIDIQLSLENFENKFlkisdiKKKINDCLKETESiekkissfsidsQDTELKENGDNLNSLQEFLESLKDQ-KKNIEDK- 1672
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 1207141724 2101 gqlKKSSDtELDRQKKIVEETLKQRK------VVEEEIHILKLNFEKASSGKQ 2147
Cdd:TIGR01612 1673 ---KKELD-ELDSEIEKIEIDVDQHKknyeigIIEKIKEIAIANKEEIESIKE 1721
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2467-2688 |
1.33e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 48.51 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2467 ENMKKLAEE-AARLNIEAQEAARLRQIAESDLAKQREL--AEKMLEEKKQAIQEAAKLKAEAEKLQkQKDQAQVEAQKLL 2543
Cdd:PRK10929 75 DNFPKLSAElRQQLNNERDEPRSVPPNMSTDALEQEILqvSSQLLEKSRQAQQEQDRAREISDSLS-QLPQQQTEARRQL 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2544 eakKEMQQRLdqETEGFQKSLEAERKRQLeITAEAEKLKVKVTQLSDAQSKAEE-------EAKKFKKQADEIKIRLQET 2616
Cdd:PRK10929 154 ---NEIERRL--QTLGTPNTPLAQAQLTA-LQAESAALKALVDELELAQLSANNrqelarlRSELAKKRSQQLDAYLQAL 227
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2617 EKH-TSEKHTVVEK-LEVQRLQSKQEADgLHKAIADLEKEKEKLkkeAADLQKQSKEMANVQQEQLQQEKTILQ 2688
Cdd:PRK10929 228 RNQlNSQRQREAERaLESTELLAEQSGD-LPKSIVAQFKINREL---SQALNQQAQRMDLIASQQRQAASQTLQ 297
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2207-2796 |
1.40e-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: 48.30 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2207 RQHKAA-QEEVGRLMKLAEEAKkQKEIAE------KEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQ--DKLKE 2277
Cdd:pfam12128 230 IQAIAGiMKIRPEFTKLQQEFN-TLESAElrlshlHFGYKSDETLIASRQEERQETSAELNQLLRTLDDQWKEkrDELNG 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2278 EfekakKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqakaqeDAEKLRKEAEKEASRRAEAEAaalkLKQ 2357
Cdd:pfam12128 309 E-----LSAADAAVAKDRSELEALEDQHGAFLDA------------------DIETAAADQEQLPSWQSELEN----LEE 361
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2358 EADSEMAKYKKLAEKTLKQKSSVEEELV-KVKVQLDETDKQKSVLDvelkRLKQEVSDAI-KQKAQVEDELSKVKIQMED 2435
Cdd:pfam12128 362 RLKALTGKHQDVTAKYNRRRSKIKEQNNrDIAGIKDKLAKIREARD----RQLAVAEDDLqALESELREQLEAGKLEFNE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2436 LlklklkiekenqelmkkdkdntKKLLEEEAENMKklaeeaARLNIEAQEAARLRQIAESDlakqrELAEKMLEEKKQAI 2515
Cdd:pfam12128 438 E----------------------EYRLKSRLGELK------LRLNQATATPELLLQLENFD-----ERIERAREEQEAAN 484
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2516 QEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ-ETEGFQKS------LEAE----RKRQLEITAEAEKLKVK 2584
Cdd:pfam12128 485 AEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDElELQLFPQAgtllhfLRKEapdwEQSIGKVISPELLHRTD 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2585 VTQLSDAQSKAEE-------------EAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADL 2651
Cdd:pfam12128 565 LDPEVWDGSVGGElnlygvkldlkriDVPEWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFA 644
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2652 EKEKEKLKKeaaDLQKQSKEManvQQEQLQQEKTILQQSFFAEKEtlLKKEKAIEEEKKKLEKQFEDEVKKaEALKAEQE 2731
Cdd:pfam12128 645 RTALKNARL---DLRRLFDEK---QSEKDKKNKALAERKDSANER--LNSLEAQLKQLDKKHQAWLEEQKE-QKREARTE 715
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 2732 RQ--RKLMEEERKKLQSAMDAAI-KKQKEAEEEMNGKQKEM-QDLEKKRIEQEKL--LAEENKNLREKLQQ 2796
Cdd:pfam12128 716 KQayWQVVEGALDAQLALLKAAIaARRSGAKAELKALETWYkRDLASLGVDPDVIakLKREIRTLERKIER 786
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
2474-2767 |
1.41e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 47.94 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2474 EEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRL 2553
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2554 DQETEGFQKSLEAERKrqleitAEAEKLKVKVTQLSDAQSKAEEE-----AKKFKKQADEIKIRLQETEKHTSEKHTVVE 2628
Cdd:pfam02029 140 YQENKWSTEVRQAEEE------GEEEEDKSEEAEEVPTENFAKEEvkdekIKKEKKVKYESKVFLDQKRGHPEVKSQNGE 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2629 KlEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAA----DLQKQSKEMANVQQEQLQQEktilQQSFFAEKETLLKKEKA 2704
Cdd:pfam02029 214 E-EVTKLKVTTKRRQGGLSQSQEREEEAEVFLEAEqkleELRRRRQEKESEEFEKLRQK----QQEAELELEELKKKREE 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2705 IEEEKKKLEKQFEDEvkKAEALKAEQERQRKLMEE-ERKKlqsaMDAAIKKQKEAEEEMNGKQK 2767
Cdd:pfam02029 289 RRKLLEEEEQRRKQE--EAERKLREEEEKRRMKEEiERRR----AEAAEKRQKLPEDSSSEGKK 346
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1890-2095 |
1.45e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.88 E-value: 1.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1890 KQKEAAEMElgNQRKMAEETAKQKLAAEQElirlradfehAEQQRtVLDDELQRLKndvnsAVKQKKELEEElikvrkEM 1969
Cdd:PRK09510 70 QQKSAKRAE--EQRKKKEQQQAEELQQKQA----------AEQER-LKQLEKERLA-----AQEQKKQAEEA------AK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1970 EILLQQKsKAEKETMSNTEKSKqlLESEAAKMReLAEEATKlrsvAEEAKKQRQIAE-----EEAARQRAEAEKILKEKL 2044
Cdd:PRK09510 126 QAALKQK-QAEEAAAKAAAAAK--AKAEAEAKR-AAAAAKK----AAAEAKKKAEAEaakkaAAEAKKKAEAEAAAKAAA 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 2045 TAINEATRLKTEAEIALKEKEAENDRlKRKAEEEGYQRKVLEDQAAQHKQA 2095
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAEA-KAAAAKAAAEAKAAAEKAAAAKAA 247
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4583-4620 |
1.49e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.49e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141724 4583 QRFLEVQYLTGGLIEPDVTGRVSLDEAVRKGSLDARTA 4620
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2400-2770 |
1.50e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2400 VLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARL 2479
Cdd:pfam07888 31 LLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2480 NIEAQEAARLRQIAESDLAKQRELAE--KMLEEKKQAIQ-EAAKLKAEAEKLQKQKDQAQVEaQKLLEAKKEMQQrldQE 2556
Cdd:pfam07888 111 EELSEEKDALLAQRAAHEARIRELEEdiKTLTQRVLEREtELERMKERAKKAGAQRKEEEAE-RKQLQAKLQQTE---EE 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2557 TEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKA---EEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQ 2633
Cdd:pfam07888 187 LRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAhrkEAENEALLEELRSLQERLNASERKVEGLGEELSSMAAQ 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2634 RLQSKQEadgLHKAiadlekekeklKKEAADLQKQSKEMANVQQE---QLQQEKTILQQSFFAEKETLLKKEKAIEEEKK 2710
Cdd:pfam07888 267 RDRTQAE---LHQA-----------RLQAAQLTLQLADASLALREgraRWAQERETLQQSAEADKDRIEKLSAELQRLEE 332
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2711 KLEKQFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQ 2770
Cdd:pfam07888 333 RLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLE 392
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1629-1962 |
1.68e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1629 ELQELKTLSEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKavdadklRNAAQEEAEKLR 1708
Cdd:COG4372 14 SLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSE-------LEQLEEELEELN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1709 KQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLES 1788
Cdd:COG4372 87 EQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEEL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1789 KQVALTARLEESLKNEQVmVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAE 1868
Cdd:COG4372 167 AALEQELQALSEAEAEQA-LDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELE 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1869 KQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDV 1948
Cdd:COG4372 246 EDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELA 325
|
330
....*....|....
gi 1207141724 1949 NSAVKQKKELEEEL 1962
Cdd:COG4372 326 KKLELALAILLAEL 339
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2475-2611 |
1.68e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 47.90 E-value: 1.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2475 EAARLNIeAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQEAAKLKaeaEKLQKQKDQAQ-VEAQKLLEAKKEMQQRL 2553
Cdd:PRK00409 505 EEAKKLI-GEDKEKLNELIASLEELERELEQK-AEEAEALLKEAEKLK---EELEEKKEKLQeEEDKLLEEAEKEAQQAI 579
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2554 DQETEgfqkslEAERK-RQLEITAEAEKLKVKVTQLSDAQS-------KAEEEAKKFKKQADEIKI 2611
Cdd:PRK00409 580 KEAKK------EADEIiKELRQLQKGGYASVKAHELIEARKrlnkaneKKEKKKKKQKEKQEELKV 639
|
|
| CH_PARV_rpt1 |
cd21221 |
first calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
231-296 |
1.69e-04 |
|
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: 43.80 E-value: 1.69e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 231 KKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREK----GRMRFHKLQNVQIALDFL 296
Cdd:cd21221 3 VRVLTEWINEELADDRIVVRDLEEDLFDGQVLQALLEKLANEKLEVPEvaqsEEGQKQKLAVVLACVNFL 72
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
230-337 |
1.69e-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: 45.00 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 230 QKKTFTKWVNK---------HLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 296
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1207141724 297 KHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 337
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2499-2812 |
1.72e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 1.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2499 KQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL---LEAKKEMQQRLDQETEGFQKSLEAERKRQLEIT 2575
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLeeeLEQARSELEQLEEELEELNEQLQAAQAELAQAQ 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2576 AEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIAdlEKEK 2655
Cdd:COG4372 101 EELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ--ALSE 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2656 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRK 2735
Cdd:COG4372 179 AEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILK 258
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 2736 LMEEERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSSQKASYTKEIEIQ 2812
Cdd:COG4372 259 EIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1941-2110 |
1.82e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 47.49 E-value: 1.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1941 LQRLKNDVNSAVKQKKELEEElikvrKEMEilLQQKSKAEKETMSNTEKSKQllesEAAKMRELAEEATKLRSVAEEAKK 2020
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ-----QAEE--LQQKQAAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2021 QRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENdrlKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 2100
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEA---KKKAEAEAAAKAAAEAKKKAEAEAKKKAA 212
|
170
....*....|
gi 1207141724 2101 GQLKKSSDTE 2110
Cdd:PRK09510 213 AEAKKKAAAE 222
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2722-2823 |
1.86e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 1.86e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2722 KAEALKAEQERQRKLMEEER-------KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKL 2794
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKeaeaikkEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELLEKRE 109
|
90 100
....*....|....*....|....*....
gi 1207141724 2795 QQLQSSQKASYTKEIEIQTDKVPEEELVQ 2823
Cdd:PRK12704 110 EELEKKEKELEQKQQELEKKEEELEELIE 138
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1163-1528 |
1.91e-04 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 48.14 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1163 DNLLRSVEQEPALIQKDSTSGEQDESVCKSYITQIKDLRLRLEGCESRTVNRLRQMVDKepLKACTQRATEQKKVQTELE 1242
Cdd:TIGR02169 687 KRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEED--LSSLEQEIENVKSELKELE 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1243 GIKKDLDKVVEKSEAVLATSQQSSSapvlRSEIDITQKKMEHVYglssvylDKLKTIDLVIRSTQG-----------AED 1311
Cdd:TIGR02169 765 ARIEELEEDLHKLEEALNDLEARLS----HSRIPEIQAELSKLE-------EEVSRIEARLREIEQklnrltlekeyLEK 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1312 ILNKYENQLREV-NKVPVNEKEIEASQTQLQKLRSEAEGKQATFDRLEEELqratevnkrmSQLHSERDVELEHYRQlvg 1390
Cdd:TIGR02169 834 EIQELQEQRIDLkEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRL----------GDLKKERDELEAQLRE--- 900
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1391 nLRERWQAVFAQIELRQRELDLLNRQMQAyresydwlirwiadAKQRQDKlhavpIGGSKGLQEQLTQEKKLLEEIEKNK 1470
Cdd:TIGR02169 901 -LERKIEELEAQIEKKRKRLSELKAKLEA--------------LEEELSE-----IEDPKGEDEEIPEEELSLEDVQAEL 960
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 1471 DKVE-DCQKFAKGYIDAIKDYELQLVTYKALVEpiasplKKAKMESASDDI---IQEYVTLR 1528
Cdd:TIGR02169 961 QRVEeEIRALEPVNMLAIQEYEEVLKRLDELKE------KRAKLEEERKAIlerIEEYEKKK 1016
|
|
| Mitofilin |
pfam09731 |
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ... |
1754-2130 |
2.24e-04 |
|
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.
Pssm-ID: 430783 [Multi-domain] Cd Length: 618 Bit Score: 47.44 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1754 EEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESlkneqvmviqlqeeaEHLKKQQAEADKAREQAE 1833
Cdd:pfam09731 52 GEDPPLAPKPKTFRPLQPSVVSAVTGESKEPKEEKKQVKIPRQSGVS---------------SEVAEEEKEATKDAAEAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1834 KELETWRQKANEALRLRLQ-AEEEANKKTAAQEEAekqkeeakrEAKKRAKAEEAALKQKEAAEMELGNQRKMaEETAKQ 1912
Cdd:pfam09731 117 AQLPKSEQEKEKALEEVLKeAISKAESATAVAKEA---------KDDAIQAVKAHTDSLKEASDTAEISREKA-TDSALQ 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1913 KLAAEQELIRLRADFEHAEQQrTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ 1992
Cdd:pfam09731 187 KAEALAEKLKEVINLAKQSEE-EAAPPLLDAAPETPPKLPEHLDNVEEKVEKAQSLAKLVDQYKELVASERIVFQQELVS 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1993 LLESEAAKMREL-AEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRL 2071
Cdd:pfam09731 266 IFPDIIPVLKEDnLLSNDDLNSLIAHAHREIDQLSKKLAELKKREEKHIERALEKQKEELDKLAEELSARLEEVRAADEA 345
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2072 KRKAEeegYQRKVLEDQaaqhkQAIEEKIgqlkkssDTELDRQKKIVEETLKQRKVVEE 2130
Cdd:pfam09731 346 QLRLE---FEREREEIR-----ESYEEKL-------RTELERQAEAHEEHLKDVLVEQE 389
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2489-2648 |
2.29e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.47 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2489 LRQIAESDLAKQRELAEKMLEE--------KKQAIQEA----AKLKAEAEKLQKQKDQaqvEAQKLLEAKKEMQQRLDQE 2556
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEakkeaeaiKKEALLEAkeeiHKLRNEFEKELRERRN---ELQKLEKRLLQKEENLDRK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2557 TEGFQK---SLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFkkQADEIK-IRLQETEKHTSEK--HTVVEKL 2630
Cdd:PRK12704 102 LELLEKreeELEKKEKELEQKQQELEKKEEELEELIEEQLQELERISGL--TAEEAKeILLEKVEEEARHEaaVLIKEIE 179
|
170
....*....|....*...
gi 1207141724 2631 EvqrlQSKQEADGLHKAI 2648
Cdd:PRK12704 180 E----EAKEEADKKAKEI 193
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2357-2590 |
2.72e-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: 47.33 E-value: 2.72e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2357 QEADSEMAKYKKLAEKTLKQKSsvEEELVKVKVQLDETDKQKSVLDVELKRLKQEVsdaikqkAQVEDELSKVKIQMEdl 2436
Cdd:pfam05667 312 APAATSSPPTKVETEEELQQQR--EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE-- 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2437 lklklkIEKENQELMKKdkdnTKKLLEEEAENMKKL----AEEAARL-NIEAQ-EAARlrqiaESDLAKQRELAEKMLEE 2510
Cdd:pfam05667 381 ------ELEKQYKVKKK----TLDLLPDAEENIAKLqalvDASAQRLvELAGQwEKHR-----VPLIEEYRALKEAKSNK 445
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2511 KKqaiqEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSleAERKRQLEITAEAEKLKVKVTQ-LS 2589
Cdd:pfam05667 446 ED----ESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVSRS--AYTRRILEIVKNIKKQKEEITKiLS 519
|
.
gi 1207141724 2590 D 2590
Cdd:pfam05667 520 D 520
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2969-3006 |
2.77e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 2.77e-04
10 20 30
....*....|....*....|....*....|....*...
gi 1207141724 2969 TKLLSAERAVTGFKDPFTGDTISVFEAMKKGLITEDQA 3006
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2486-2690 |
3.14e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 3.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2486 AARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLE 2565
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2566 AERKRQ-----LEITAEAEKLK------VKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKL--EV 2632
Cdd:COG3883 94 ALYRSGgsvsyLDVLLGSESFSdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2633 QRLQSKQEADgLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQS 2690
Cdd:COG3883 174 EAQQAEQEAL-LAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAA 230
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3335-3370 |
3.21e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.21e-04
10 20 30
....*....|....*....|....*....|....*.
gi 1207141724 3335 RLLEAQLATGGIIDPEKSYRITPDIAYKRGHLNEEM 3370
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1685-1846 |
3.36e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 3.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1685 QLRAKAVDADKLRN--AAQEEAEKLRKQVAE-----ETQKKRKAEEELKRKSEAEKDAAKEKKKALED-----LEKFKLQ 1752
Cdd:PRK09510 69 QQQKSAKRAEEQRKkkEQQQAEELQQKQAAEqerlkQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEaaakaAAAAKAK 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1753 AEEAERHL----KQAELEKQRQIQvvEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKA 1828
Cdd:PRK09510 149 AEAEAKRAaaaaKKAAAEAKKKAE--AEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAA 226
|
170
....*....|....*...
gi 1207141724 1829 REQAEKELETWRQKANEA 1846
Cdd:PRK09510 227 AAKAAAEAKAAAEKAAAA 244
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
1831-2143 |
3.38e-04 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 46.82 E-value: 3.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1831 QAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQ--RKMAEE 1908
Cdd:pfam15964 321 SSLAEAQQRESSAYEQVKQAVQMTEEANFEKTKALIQCEQLKSELERQKERLEKELASQQEKRAQEKEALRKemKKEREE 400
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1909 TAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQrlkndvnSAVKQKKELEEELIKVRKEMEILLQQkSKAEKEtmsntE 1988
Cdd:pfam15964 401 LGATMLALSQNVAQLEAQVEKVTREKNSLVSQLE-------EAQKQLASQEMDVTKVCGEMRYQLNQ-TKMKKD-----E 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1989 KSKQLLESEAAKMRELA---EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKIlkekltaineaTRLKTEAEIALKEKE 2065
Cdd:pfam15964 468 AEKEHREYRTKTGRQLEikdQEIEKLGLELSESKQRLEQAQQDAARAREECLKL-----------TELLGESEHQLHLTR 536
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2066 AENDRLKRKAEEEGyqrKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKAS 2143
Cdd:pfam15964 537 LEKESIQQSFSNEA---KAQALQAQQREQELTQKMQQMEAQHDKTVNEQYSLLTSQNTFIAKLKEECCTLAKKLEEIT 611
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4473-4506 |
3.51e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.51e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141724 4473 EETGPVAGILDTDTLEKVSVTEAMHRNLVDNITG 4506
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2368-2645 |
3.65e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2368 KLAEKTLKQKSSVEEelvkVKVQLDETDKQKSVLDVELKRLKQEVSD-----------AIkQKAQVEDELSKVKIQMEDL 2436
Cdd:PRK04863 359 ELEERLEEQNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLADyqqaldvqqtrAI-QYQQAVQALERAKQLCGLP 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2437 LKLKLKIEKENQELMKKDKDNTKKLLEEE-----AENMKKLAEEAARL------NIEAQEAARLRQIAESDLAKQRELAE 2505
Cdd:PRK04863 434 DLTADNAEDWLEEFQAKEQEATEELLSLEqklsvAQAAHSQFEQAYQLvrkiagEVSRSEAWDVARELLRRLREQRHLAE 513
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2506 KM---------LEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITA 2576
Cdd:PRK04863 514 QLqqlrmrlseLEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQLEQLQA 593
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 2577 EAEKLKVKVTQLSDAQSKAEE------EAKKFKKQADEIKIRLQETEKHTSEkhtVVEKLEVQRLQSKQEADGLH 2645
Cdd:PRK04863 594 RIQRLAARAPAWLAAQDALARlreqsgEEFEDSQDVTEYMQQLLERERELTV---ERDELAARKQALDEEIERLS 665
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2396-2647 |
3.65e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.22 E-value: 3.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2396 KQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLkiekenqelmkkdkdntkklLEEEAENMKKLAEE 2475
Cdd:COG4913 610 AKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAE--------------------YSWDEIDVASAERE 669
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2476 AARLNieaQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQ 2555
Cdd:COG4913 670 IAELE---AELERLDA-SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2556 ETEgfqKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKirlQETEKHTSEKHTVVEKL-EVQR 2634
Cdd:COG4913 746 ELR---ALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN---REWPAETADLDADLESLpEYLA 819
|
250
....*....|...
gi 1207141724 2635 LQSKQEADGLHKA 2647
Cdd:COG4913 820 LLDRLEEDGLPEY 832
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1637-1888 |
3.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.36 E-value: 3.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1637 SEQEIKAKSQQVEEALLSRTRIEEEIHIIRLQLETTMKQKNTAETELlqlrakavdadklrNAAQEEAEKLRKQVAEETQ 1716
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL--------------EALQAEIDKLQAEIAEAEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1717 KKRKAEEELKRkseaeKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQ---RQIQVVEEVakKTAATQLESKQval 1793
Cdd:COG3883 80 EIEERREELGE-----RARALYRSGGSVSYLDVLLGSESFSDFLDRLSALSKiadADADLLEEL--KADKAELEAKK--- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1794 tARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEE 1873
Cdd:COG3883 150 -AELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
250
....*....|....*
gi 1207141724 1874 AKREAKKRAKAEEAA 1888
Cdd:COG3883 229 AAAAAAAAAAAAAAA 243
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1926-2810 |
3.89e-04 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 46.96 E-value: 3.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1926 DFEHAEQQRTVLDDELQRLKNDVNSAVK-QKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQ-LLESEAAKMRE 2003
Cdd:TIGR00606 55 DFPPGTKGNTFVHDPKVAQETDVRAQIRlQFRDVNGEECAVVRSMVCTQKTKKTEFKTLEGVITRYKHgEKVSLSSKCAE 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2004 LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATR----LKTEAEIAL------KEKEAENDRLKR 2073
Cdd:TIGR00606 135 IDREMISHLGVSKAVLNNVIFCHQEDSNWPLSEGKALKQKFDEIFSATRyikaLETLRQVRQtqgqkvQEHQMELKYLKQ 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2074 KAEEEGYQRKVLEDQAAQhkQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekasSGKQELELEL 2153
Cdd:TIGR00606 215 YKEKACEIRDQITSKEAQ--LESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKALK-------SRKKQMEKDN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2154 KKLKGIADETQKSKAKAEEEAEKFRKlaleeekkrkeaeakvKQIQAAEEEAARQHKaaqeEVGRLMKLAEEAKKQKeiA 2233
Cdd:TIGR00606 286 SELELKMEKVFQGTDEQLNDLYHNHQ----------------RTVREKERELVDCQR----ELEKLNKERRLLNQEK--T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2234 EKEAEKQVILVQEAAQKCsaaEQKAQNVLVQQNKDSMAQDKLKE------EFEKAKKLAQE--AEKAKDNAEKEAALLHK 2305
Cdd:TIGR00606 344 ELLVEQGRLQLQADRHQE---HIRARDSLIQSLATRLELDGFERgpfserQIKNFHTLVIErqEDEAKTAAQLCADLQSK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2306 KAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEKTLKQKSSVEEELV 2385
Cdd:TIGR00606 421 ERLKQEQADEIRDEKKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELDQELRKAERELSKAEKNSLTETLK 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2386 KVKVQLDEtdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKD--NTKKL-- 2461
Cdd:TIGR00606 501 KEVKSLQN---EKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLLGYfpNKKQLed 577
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2462 -LEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLaKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQ 2540
Cdd:TIGR00606 578 wLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNEL-ESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRA 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2541 KLLEAKKEMQQRLDQETEGFQKSL---EAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIR----- 2612
Cdd:TIGR00606 657 MLAGATAVYSQFITQLTDENQSCCpvcQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLapgrq 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2613 --LQETEKHTSEKHTVVEKL--EVQRLQSKQEADglhkaiADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQ 2688
Cdd:TIGR00606 737 siIDLKEKEIPELRNKLQKVnrDIQRLKNDIEEQ------ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIAQ 810
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2689 QSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALK---------------------------AEQERQRKLMEEER 2741
Cdd:TIGR00606 811 QAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRkliqdqqeqiqhlksktnelkseklqiGTNLQRRQQFEEQL 890
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 2742 KKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQSS--QKASYTKEIE 2810
Cdd:TIGR00606 891 VELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKvkNIHGYMKDIE 961
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1753-2078 |
4.42e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 46.40 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1753 AEEAERHLKQAELEKQRQIQVVEEVAK------KTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEAd 1826
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGqvtesvEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1827 karEQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKeeakreaKKRAKAEEAALKQKEAAEMELGNQRKMA 1906
Cdd:pfam02029 83 ---LERQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSR-------LGRYKEEETEIREKEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1907 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSN 1986
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1987 T----EKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQiaeEEAARQRAEAEKILKEKlTAINEATRLKTEAEIALK 2062
Cdd:pfam02029 233 SqereEEAEVFLEAEQ-KLEELRRRRQEKESEEFEKLRQKQ---QEAELELEELKKKREER-RKLLEEEEQRRKQEEAER 307
|
330
....*....|....*.
gi 1207141724 2063 EKEAENDRLKRKAEEE 2078
Cdd:pfam02029 308 KLREEEEKRRMKEEIE 323
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1271-1475 |
4.78e-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: 45.91 E-value: 4.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1271 LRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQGAediLNKYENQLREVnkvpvnEKEIEASQTQLQKLRSEAEGK 1350
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARR---IRALEQELAAL------EAELAELEKEIAELRAELEAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1351 QATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESYDWLIRW 1430
Cdd:COG4942 103 KEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAE 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1207141724 1431 IADAKQRQDKLHAVPIGGSKGLQEQLTQEKKLLEEIEKNKDKVED 1475
Cdd:COG4942 183 LEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2207-2531 |
4.90e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.48 E-value: 4.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2207 RQHKAAQEEVGRLMKLAEEAK-----KQ----KEIAEKEAEKqvilvQEAAQKCSAAEQKAqnvlVQQNKDSMAQDKLKE 2277
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKarfeaRQarleREKAAREARH-----KKAAEARAAKDKDA----VAAALARVKAKKAAA 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2278 EFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAErqkkaaeaeaakqaKAQEDAEKLRKEAekeasrraeaeaaalklkQ 2357
Cdd:PRK05035 503 TQPIVIKAGARPDNSAVIAAREARKAQARARQAE--------------KQAAAAADPKKAA------------------V 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2358 EADSEMAKYKKLAEKTLKQKSSVEEELVKVKVqldetdkQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLL 2437
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEAEEEVDPKKAAV-------AAAIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIAR 623
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2438 KLKLKIEKENQElmkkdkdntkklLEEEAENMKKLAEEAARlnieAQEAARLRQIAESDLAKQRElaekmLEEKKQAIqE 2517
Cdd:PRK05035 624 AKAKKAEQQANA------------EPEEPVDPRKAAVAAAI----ARAKARKAAQQQANAEPEEA-----EDPKKAAV-A 681
|
330
....*....|....
gi 1207141724 2518 AAKLKAEAEKLQKQ 2531
Cdd:PRK05035 682 AAIARAKAKKAAQQ 695
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2721-2810 |
5.00e-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: 45.65 E-value: 5.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2721 KKAEALKAEQ-ERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMngKQKEMQDLEKKRIEQEKLLAEENKNLREKLQQLQS 2799
Cdd:cd16269 200 IEAERAKAEAaEQERKLLEEQQRELEQKLEDQERSYEEHLRQL--KEKMEEERENLLKEQERALESKLKEQEALLEEGFK 277
|
90
....*....|.
gi 1207141724 2800 SQKASYTKEIE 2810
Cdd:cd16269 278 EQAELLQEEIR 288
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2469-2608 |
5.54e-04 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 46.24 E-value: 5.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2469 MKKLAEEAARLNIEAQEAARlRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKL--LEAK 2546
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAE-EKLEAALLEAKELLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLdnLENQ 106
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2547 KEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2608
Cdd:PRK12705 107 LEEREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEE 168
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
2388-2630 |
5.62e-04 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 46.16 E-value: 5.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2388 KVQLDETDKQKSVLDVELKRLKQEVsdAIKQKAQVE-DELSKVKIQ----MEDLLKLKLKIEKENQELMKKDKDNTKKLL 2462
Cdd:PHA02562 173 KDKIRELNQQIQTLDMKIDHIQQQI--KTYNKNIEEqRKKNGENIArkqnKYDELVEEAKTIKAEIEELTDELLNLVMDI 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2463 EEEAENMKKLAEEAARLNIEAQEAARLrqiaesdlakqrelaEKMLEEK------KQAIQEAAKLkaeAEKLQKQKDQAQ 2536
Cdd:PHA02562 251 EDPSAALNKLNTAAAKIKSKIEQFQKV---------------IKMYEKGgvcptcTQQISEGPDR---ITKIKDKLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2537 VEAQKLLEAKKEMQQRLDQETE------GFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIK 2610
Cdd:PHA02562 313 HSLEKLDTAIDELEEIMDEFNEqskkllELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|
gi 1207141724 2611 IRLQETEKHTSEKHTVVEKL 2630
Cdd:PHA02562 393 KTKSELVKEKYHRGIVTDLL 412
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1886-2129 |
6.60e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 45.66 E-value: 6.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1886 EAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKV 1965
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1966 RKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLT 2045
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2046 AINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQR 2125
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
....
gi 1207141724 2126 KVVE 2129
Cdd:COG4372 288 LEEA 291
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
719-813 |
6.84e-04 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 41.93 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 719 LKYIQDLLSWVEENQRRIEGAEWGEDLPSVESQLGSHRGLHQSIEEFKYKIDRARADENQLT---PVSKGAYREYLGKLD 795
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIeegHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 1207141724 796 LQYAKLLTSSKTRLRSLD 813
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2480-2759 |
6.88e-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: 46.37 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2480 NIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAiqEAAKLKAEAEKlQKQKDqAQVEAQKLLEAKKemQQRLDQETEG 2559
Cdd:NF012221 1533 NVVATSESSQQADAVSKHAKQDDAAQNALADKERA--EADRQRLEQEK-QQQLA-AISGSQSQLESTD--QNALETNGQA 1606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2560 FQKSLEAERKrqlEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQ-ADEIKIRLQEteKHTSEKHTVVEKLEVQRLQSK 2638
Cdd:NF012221 1607 QRDAILEESR---AVTKELTTLAQGLDALDSQATYAGESGDQWRNPfAGGLLDRVQE--QLDDAKKISGKQLADAKQRHV 1681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2639 QEADGLHKAIADLEkekeklkkeaADLQKQSKEMANVQQEqLQQEKTilqQSFFAEKETLLKKEKAIEEEkkklekqfed 2718
Cdd:NF012221 1682 DNQQKVKDAVAKSE----------AGVAQGEQNQANAEQD-IDDAKA---DAEKRKDDALAKQNEAQQAE---------- 1737
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1207141724 2719 evKKAEAL--KAEQERQRKLMEEERKKLQSAMDAAIKKQKEAE 2759
Cdd:NF012221 1738 --SDANAAanDAQSRGEQDASAAENKANQAQADAKGAKQDESD 1778
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
1939-2612 |
6.96e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 46.20 E-value: 6.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1939 DELQRLKNDVNSaVKQK-----KELEEELIKVRKEMEILLQQKSKAEK---ETMSN-----TEKSKQLLESEAAKMRELA 2005
Cdd:TIGR01612 1111 DEINKIKDDIKN-LDQKidhhiKALEEIKKKSENYIDEIKAQINDLEDvadKAISNddpeeIEKKIENIVTKIDKKKNIY 1189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2006 EEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRlKTEAEIALKEKEAEN-DRLKRKAEEEGYQRKV 2084
Cdd:TIGR01612 1190 DEIKKLLNEIAEIEKDKTSLEEVKGINLSYGKNLGKLFLEKIDEEKK-KSEHMIKAMEAYIEDlDEIKEKSPEIENEMGI 1268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2085 LEDQAAQ--------------------HKQAI----------------EEKIGQLKKSSDTELDRQKKIVEETLKQRKVV 2128
Cdd:TIGR01612 1269 EMDIKAEmetfnishdddkdhhiiskkHDENIsdirekslkiiedfseESDINDIKKELQKNLLDAQKHNSDINLYLNEI 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2129 EEEIHILKLNFEKA--SSGKQELELELKKLKGIADETQKSKAKAEEEAEkfrKLALEEEKKRKEAEAKVKQIqaaeEEAA 2206
Cdd:TIGR01612 1349 ANIYNILKLNKIKKiiDEVKEYTKEIEENNKNIKDELDKSEKLIKKIKD---DINLEECKSKIESTLDDKDI----DECI 1421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2207 RQHKAAQEEVgrlmkLAEEAKKQKEIAE-KEAEKQVILVqeaAQKCSAAEQKAQNVLVQQnKDSMAQD------KLKEEF 2279
Cdd:TIGR01612 1422 KKIKELKNHI-----LSEESNIDTYFKNaDENNENVLLL---FKNIEMADNKSQHILKIK-KDNATNDhdfninELKEHI 1492
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2280 EKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER--QKKAAEAEAAKQAKAQEDAEKLRKEAEKEASrraeaeaaalKLKQ 2357
Cdd:TIGR01612 1493 DKSKGCKDEADKNAKAIEKNKELFEQYKKDVTEllNKYSALAIKNKFAKTKKDSEIIIKEIKDAHK----------KFIL 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2358 EADSEMAKYKKLAektlKQKSSVEEELVKV-KVQLDETDKQKSVLDVELKRLK-----QEVSDAIKQKAQVEDELSKVKI 2431
Cdd:TIGR01612 1563 EAEKSEQKIKEIK----KEKFRIEDDAAKNdKSNKAAIDIQLSLENFENKFLKisdikKKINDCLKETESIEKKISSFSI 1638
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2432 QMEDLLKLKLKIEKEN-QELMKKDKDNtKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEK-MLE 2509
Cdd:TIGR01612 1639 DSQDTELKENGDNLNSlQEFLESLKDQ-KKNIEDKKKELDELDSEIEKIEIDVDQHKKNYEIGIIEKIKEIAIANKeEIE 1717
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2510 EKKQAIQEAAKLKAEA------------EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETegfQKSLEAERKRQLEITAE 2577
Cdd:TIGR01612 1718 SIKELIEPTIENLISSfntndlegidpnEKLEEYNTEIGDIYEEFIELYNIIAGCLETVS---KEPITYDEIKNTRINAQ 1794
|
730 740 750
....*....|....*....|....*....|....*
gi 1207141724 2578 AEKLKVKvtqlsdaqskaeEEAKKFKKQADEIKIR 2612
Cdd:TIGR01612 1795 NEFLKII------------EIEKKSKSYLDDIEAK 1817
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
2264-2610 |
7.08e-04 |
|
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: 45.77 E-value: 7.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2264 QQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKA----EEAERQKKAAEAEAAKQAKAQEDAEKLRKEAE 2339
Cdd:NF033838 112 EAELTSKTKKELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAkdqkEEDRRNYPTNTYKTLELEIAESDVEVKKAELE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2340 --KEASRRAEAEAAALKLKQEADSEMAKYKKLaEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIK 2417
Cdd:NF033838 192 lvKEEAKEPRDEEKIKQAKAKVESKKAEATRL-EKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGVL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2418 QKAQVEDElSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLleEEAENMKKLAEEAARLNIEAQEAARLR-QIAESD 2496
Cdd:NF033838 271 GEPATPDK-KENDAKSSDSSVGEETLPSPSLKPEKKVAEAEKKV--EEAKKKAKDQKEEDRRNYPTNTYKTLElEIAESD 347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2497 LAKQRELAEKMLEEKKQAIQEAAKLKAEAEklqkqkdqaqveaqklLEAKKEMQQRLDQ-ETEGFQKSLEAERKrqleiT 2575
Cdd:NF033838 348 VKVKEAELELVKEEAKEPRNEEKIKQAKAK----------------VESKKAEATRLEKiKTDRKKAEEEAKRK-----A 406
|
330 340 350
....*....|....*....|....*....|....*..
gi 1207141724 2576 AEAEKLKVKVTQLSDAQS--KAEEEAKKFKKQADEIK 2610
Cdd:NF033838 407 AEEDKVKEKPAEQPQPAPapQPEKPAPKPEKPAEQPK 443
|
|
| DUF2968 |
pfam11180 |
Protein of unknown function (DUF2968); This family of proteins has no known function. |
2466-2542 |
7.65e-04 |
|
Protein of unknown function (DUF2968); This family of proteins has no known function.
Pssm-ID: 431707 [Multi-domain] Cd Length: 180 Bit Score: 43.52 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2466 AENMKKLAE-EAARLNIEAQEAARLRQIAES---------DLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2535
Cdd:pfam11180 88 ARQTAQLADvEIRRAQLEAQKAQTERQIAASearaarlqaDLQVARQQEQQVASRQKQTRQEAAALEAQRQAAQAQLRAL 167
|
....*..
gi 1207141724 2536 QVEAQKL 2542
Cdd:pfam11180 168 QRQIRQL 174
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3587-3620 |
7.78e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 7.78e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141724 3587 LLEAQAATGYIIDPIRNEMFTVDDAVKAGIVGPE 3620
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1678-1910 |
7.93e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1678 TAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKseaekdaakekkkaLEDLEKFKLQAEEAe 1757
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL--------------QAEIDKLQAEIAEA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1758 rhlkQAELEKQRqiqvvEEVAKKTAATQLESKQVALTARLEES----------------LKNEQVMVIQLQEEAEHLKKQ 1821
Cdd:COG3883 78 ----EAEIEERR-----EELGERARALYRSGGSVSYLDVLLGSesfsdfldrlsalskiADADADLLEELKADKAELEAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1822 QAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGN 1901
Cdd:COG3883 149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
....*....
gi 1207141724 1902 QRKMAEETA 1910
Cdd:COG3883 229 AAAAAAAAA 237
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2390-2623 |
7.93e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 44.90 E-value: 7.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2390 QLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKL------LE 2463
Cdd:COG1340 2 KTDELSSSLEELEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKVkelkeeRD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2464 EEAENMKKLAEEAARLNIEAQEAARLR-----------------QIAESDLAKQRELAEKM------LEEKKQAIQEAAK 2520
Cdd:COG1340 82 ELNEKLNELREELDELRKELAELNKAGgsidklrkeierlewrqQTEVLSPEEEKELVEKIkelekeLEKAKKALEKNEK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2521 LKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKsLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAK 2600
Cdd:COG1340 162 LKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKE-ADELRKEADELHKEIVEAQEKADELHEEIIELQKELR 240
|
250 260
....*....|....*....|...
gi 1207141724 2601 KFKKQADEIKIRLQETEKHTSEK 2623
Cdd:COG1340 241 ELRKELKKLRKKQRALKREKEKE 263
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2933-2966 |
8.25e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 8.25e-04
10 20 30
....*....|....*....|....*....|....
gi 1207141724 2933 LLEAQAASGYIIDPIKNRRLSVSESVKDGLIGPE 2966
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2357-2561 |
8.52e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 8.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2357 QEADSEMAKYKK---------LAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKA--QVEDE 2425
Cdd:COG3206 192 EEAEAALEEFRQknglvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPViqQLRAQ 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2426 LSKVKIQMedllklklkiekenQELMKKDKDNT---KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQre 2502
Cdd:COG3206 272 LAELEAEL--------------AELSARYTPNHpdvIALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQ-- 335
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2503 laekmLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQ 2561
Cdd:COG3206 336 -----LAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVR 389
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
230-327 |
8.88e-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: 42.65 E-value: 8.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 230 QKKTFTKWVN---------KHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPR----EKGRMRFHKLQNVQIALDFL 296
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 1207141724 297 KHRQVKLVNIRNDDIADGNPKLTLGLIWTII 327
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| Nop14 |
pfam04147 |
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the ... |
1926-2095 |
9.26e-04 |
|
Nop14-like family; Emg1 and Nop14 are novel proteins whose interaction is required for the maturation of the 18S rRNA and for 40S ribosome production.
Pssm-ID: 461196 Cd Length: 835 Bit Score: 45.69 E-value: 9.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1926 DFEHAEQQRTVLDDELQRL---------KNDVNSAVKQKKELEEELIkvrkemeillqQKSKAEKetmsnTEKSKQLLES 1996
Cdd:pfam04147 126 DDDSEEEEDGQLDLKRVRRahfgggeddEEEEPERKKSKKEVMEEVI-----------AKSKLHK-----YERQKAKEED 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1997 EAakMRE-----LAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAE--KILKEkLTAINEAT---RLKTEAEIALKEKE- 2065
Cdd:pfam04147 190 EE--LREeldkeLKDLRSLLSGSKRPKPEQAKKPEEKPDRKKPDDDydKLVRE-LAFDKRAKpsdRTKTEEELAEEEKEr 266
|
170 180 190
....*....|....*....|....*....|....
gi 1207141724 2066 ---AENDRLKR-KAEEEGYQRKvlEDQAAQHKQA 2095
Cdd:pfam04147 267 lekLEEERLRRmRGEEDEEEED--GKKKKKHKSA 298
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2366-2581 |
9.57e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 45.18 E-value: 9.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2366 YKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiek 2445
Cdd:PRK09510 64 YNRQQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQA--------- 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2446 enQELMKKDKDNTKKLLEEEAenmKKLAEEAARlnieAQEAARLRQIAESDlAKQRELAEKMLEEKKQAiQEAAKLKAEA 2525
Cdd:PRK09510 135 --EEAAAKAAAAAKAKAEAEA---KRAAAAAKK----AAAEAKKKAEAEAA-KKAAAEAKKKAEAEAAA-KAAAEAKKKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2526 EKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKL 2581
Cdd:PRK09510 204 EAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1685-1976 |
9.58e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.91 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1685 QLRAKAVDADKLRNAAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAE 1764
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1765 LEKQRQIQVVEEVAKKTAATQLESKQVALTAR----LEESLKNEQVMVIQLQ----EEAEHLKKQQAEADKAREQ----A 1832
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKelekEEEREEDERILEYLKEkaerEEEREAEREEIEEEKEREIarlrA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1833 EKELETWRQKANEALRLRLQAEE---EANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEET 1909
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEqerKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 1910 AKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQK 1976
Cdd:pfam13868 272 EDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
2460-2690 |
9.89e-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: 44.43 E-value: 9.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2460 KLLEEEAENMKKLAEEaarlniEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ-KQKDQAQVE 2538
Cdd:pfam17045 38 DIREEELLSARNTLER------KHKEIGLLRQQLEELEKGKQELVAKYEQQLQKLQEELSKLKRSYEKLQrKQLKEAREE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2539 AQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLeitaeaekLKVKVTQLsDAQSKA-EEEAKKFKKQADEIKI--RLQE 2615
Cdd:pfam17045 112 AKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQ--------YQQQVASL-EAQRKAlAEQSSLIQSAAYQVQLegRKQC 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2616 TEKHTSEKHTVVEKLEVQR---LQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKeMANVQQEQLQQEKTILQQS 2690
Cdd:pfam17045 183 LEASQSEIQRLRSKLERAQdslCAQELELERLRMRVSELGDSNRKLLEEQQRLLEELR-MSQRQLQVLQNELMELKAT 259
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1804-1970 |
1.00e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 44.15 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1804 EQVMVIQLQE---EAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKtaaqeeAEKQKEEAKREAKK 1880
Cdd:COG1579 5 DLRALLDLQEldsELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL------ELEIEEVEARIKKY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1881 RAKAEEAA-LKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELE 1959
Cdd:COG1579 79 EEQLGNVRnNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
170
....*....|.
gi 1207141724 1960 EELIKVRKEME 1970
Cdd:COG1579 159 EELEAEREELA 169
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1818-2137 |
1.15e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.89 E-value: 1.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1818 LKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEM 1897
Cdd:COG4372 8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1898 ELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKS 1977
Cdd:COG4372 88 QLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1978 KAEKEtmsNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEA 2057
Cdd:COG4372 168 ALEQE---LQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALEL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2058 EIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKL 2137
Cdd:COG4372 245 EEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLEL 324
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1506-1856 |
1.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 45.33 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1506 SPLKKA--KMESASD------DIIQEYVTLRTRYSELMTLSSQYIK---FIIETQRRLQDEEK--------AAEKLKEEE 1566
Cdd:PRK04863 226 SGVRKAfqDMEAALRenrmtlEAIRVTQSDRDLFKHLITESTNYVAadyMRHANERRVHLEEAlelrrelyTSRRQLAAE 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1567 RKKMAEMQAELEKQK--------------------QLAETHAKAIAKAEQEANELKTKMKD--EVSKRQDVAVD-SEKQK 1623
Cdd:PRK04863 306 QYRLVEMARELAELNeaesdleqdyqaasdhlnlvQTALRQQEKIERYQADLEELEERLEEqnEVVEEADEQQEeNEARA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1624 HNIQRELQELKT--------LSEQEIKA-KSQQVEEAL-----------LSRTRIEEEIHIIRLQLEttmkqknTAETEL 1683
Cdd:PRK04863 386 EAAEEEVDELKSqladyqqaLDVQQTRAiQYQQAVQALerakqlcglpdLTADNAEDWLEEFQAKEQ-------EATEEL 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1684 LQLRAKAVDADKLRNAAQEEAEKLRKQVAE--ETQKKRKAEEELK--RKSEAEKDAAKEKKKALEDLEKFKLQAEEAERH 1759
Cdd:PRK04863 459 LSLEQKLSVAQAAHSQFEQAYQLVRKIAGEvsRSEAWDVARELLRrlREQRHLAEQLQQLRMRLSELEQRLRQQQRAERL 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1760 LKQAElekQRQIQVVEevakktAATQLESKQVALTARLeESLKNEQVMVIQLQEEAEHlkkQQAEADKAREQAEKELETW 1839
Cdd:PRK04863 539 LAEFC---KRLGKNLD------DEDELEQLQEELEARL-ESLSESVSEARERRMALRQ---QLEQLQARIQRLAARAPAW 605
|
410
....*....|....*...
gi 1207141724 1840 RQkANEAL-RLRLQAEEE 1856
Cdd:PRK04863 606 LA-AQDALaRLREQSGEE 622
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3624-3660 |
1.25e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.25e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141724 3624 KLLSAEKAVTGYKDPYTGNKISLLQAMQKQLVLREHA 3660
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1699-2028 |
1.31e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1699 AAQEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1778
Cdd:COG4372 42 KLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQ 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1779 KktAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEEEAN 1858
Cdd:COG4372 122 K--ERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1859 KKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLD 1938
Cdd:COG4372 200 EELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELE 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1939 DELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA 2018
Cdd:COG4372 280 IAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELL 359
|
330
....*....|
gi 1207141724 2019 KKQRQIAEEE 2028
Cdd:COG4372 360 SKGAEAGVAD 369
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1876-2132 |
1.36e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.51 E-value: 1.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1876 REAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQK 1955
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1956 KELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEA---AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQ 2032
Cdd:COG4372 83 EELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQdleQQRKQLEAQIAELQSEIAEREEELKELEEQLESL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2033 RAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELD 2112
Cdd:COG4372 163 QEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDAL 242
|
250 260
....*....|....*....|
gi 1207141724 2113 RQKKIVEETLKQRKVVEEEI 2132
Cdd:COG4372 243 ELEEDKEELLEEVILKEIEE 262
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
283-327 |
1.38e-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: 1.38e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1207141724 283 FHKLQNVQIALDFLKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 327
Cdd:cd21294 78 FQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
225-333 |
1.38e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 41.90 E-value: 1.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 225 ERDRVQKKTFTKWVNKHLVKAQrhITDLYEDLRDGHNLISLLEVL---------SGETLPREKGRMRfhKLQNVQIALDF 295
Cdd:cd21330 9 EGETREERTFRNWMNSLGVNPR--VNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 1207141724 296 LKHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 333
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1701-1916 |
1.41e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 44.59 E-value: 1.41e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1701 QEEAEKLRKQVAEETQKKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERhLKQAELEKQRQIQVVE----- 1775
Cdd:PRK07735 11 KKEAARRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAAK-AKAAALAKQKREGTEEvteee 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1776 -EVAKKTAATQLESKQVALTArleeslkneqvmviQLQEEAEHLKKQQAEADKAREQAEKeletwRQKANEALRLRLQAE 1854
Cdd:PRK07735 90 kAKAKAKAAAAAKAKAAALAK--------------QKREGTEEVTEEEKAAAKAKAAAAA-----KAKAAALAKQKREGT 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 1855 EEAnkktaAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAA 1916
Cdd:PRK07735 151 EEV-----TEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKA 207
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
223-331 |
1.50e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 41.90 E-value: 1.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 223 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 298
Cdd:cd21337 14 APDKLNVVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
|
90 100 110
....*....|....*....|....*....|...
gi 1207141724 299 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 331
Cdd:cd21337 94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1352-1947 |
1.57e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1352 ATFDRLEEELQRATE---VNKRMSQLHSERDVELEHYRQLVGnLRERWQAVFAQielrqRELDLLNRQMQAYRESYDWLI 1428
Cdd:COG4913 235 DDLERAHEALEDAREqieLLEPIRELAERYAAARERLAELEY-LRAALRLWFAQ-----RRLELLEAELEELRAELARLE 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1429 RWIADAKQRQDKLHAVpiggSKGLQEQLTQ-----EKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVT----YKA 1499
Cdd:COG4913 309 AELERLEARLDALREE----LDELEAQIRGnggdrLEQLEREIERLERELEERERRRARLEALLAALGLPLPAsaeeFAA 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1500 LVEPIASplKKAKMESASDDIIQEYVTLRTRYSELMtlssqyikfiiETQRRLQDEEKAAEKLKEEERKKMAEMQAELEK 1579
Cdd:COG4913 385 LRAEAAA--LLEALEEELEALEEALAEAEAALRDLR-----------RELRELEAEIASLERRKSNIPARLLALRDALAE 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1580 QKQLAETHAKAIA-----KAEQEA---------NELKTKM------KDEVSKrqdvAVDSEKQKHNIQ-------RELQE 1632
Cdd:COG4913 452 ALGLDEAELPFVGelievRPEEERwrgaiervlGGFALTLlvppehYAAALR----WVNRLHLRGRLVyervrtgLPDPE 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1633 LKTLSEQ----EIKAKSQQVEEALlsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAV-----DADKLR------ 1697
Cdd:COG4913 528 RPRLDPDslagKLDFKPHPFRAWL--EAELGRRFDYVCVDSPEELRRHPRAITRAGQVKGNGTrhekdDRRRIRsryvlg 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1698 --NAAQEEAekLRKQVAEETQKKRKAEEELKrkseaekdaakekkkaledlekfKLQAEEAERHLKQAELEKQRQIQvVE 1775
Cdd:COG4913 606 fdNRAKLAA--LEAELAELEEELAEAEERLE-----------------------ALEAELDALQERREALQRLAEYS-WD 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1776 EVAKKTAATQLESKQVALtarleESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQAEE 1855
Cdd:COG4913 660 EIDVASAEREIAELEAEL-----ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1856 EANKKTAAQEEAEKQkeeakrEAKKRAKAEEAALKQKEAAEmELGNQRKMAEETAKQklaAEQELIRLRADF------EH 1929
Cdd:COG4913 735 RLEAAEDLARLELRA------LLEERFAAALGDAVERELRE-NLEERIDALRARLNR---AEEELERAMRAFnrewpaET 804
|
650 660
....*....|....*....|...
gi 1207141724 1930 AEQQRTVLD-----DELQRLKND 1947
Cdd:COG4913 805 ADLDADLESlpeylALLDRLEED 827
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
232-324 |
1.58e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 44.93 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 232 KTFTKWVNKHLVKAQrhITDLYEDLRDGHNLISLLEVLSGE---TLPREKGR-------MRFHKLQNVQIALDFLKHRQV 301
Cdd:COG5069 382 RVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYAVDLGITEGF 459
|
90 100
....*....|....*....|...
gi 1207141724 302 KLVNIRNDDIADGNpKLTLGLIW 324
Cdd:COG5069 460 SLVGIKGLEILDGI-RLKLTLVW 481
|
|
| Agg_substance |
NF033875 |
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, ... |
1876-2086 |
1.69e-03 |
|
LPXTG-anchored aggregation substance; Aggregation substances, as described in Enterococcus, are LPXTG-anchored large surface proteins that contribute to virulence. Several closely related paralogs may be found in a single strain.
Pssm-ID: 411439 [Multi-domain] Cd Length: 1306 Bit Score: 45.09 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1876 REAKKRAKAEEAALkQKEAAemelgNQRKMAEETAKQKLAAEQE---------LIRLRADFEHAEQQRTVLD-------- 1938
Cdd:NF033875 66 SETPKTAVSEEATV-QKDTT-----SQPTKVEEVASEKNGAEQSsatpndttnAQQPTVGAEKSAQEQPVVSpettnepl 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1939 ---DELQRLKNDVNSAVKQKKELE-----EELIKVRKEMEILLQQKSKaekETMSNTEkSKQLleseAAKMRElaeeatk 2010
Cdd:NF033875 140 gqpTEVAPAENEANKSTSIPKEFEtpdvdKAVDEAKKDPNITVVEKPA---EDLGNVS-SKDL----AAKEKE------- 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2011 lrsVAEEAKKQRQIAEEEAARQRAEAEKILKEKltaineatrlkteAEIALKEkeaendrlkrKAEEEGYQRKVLE 2086
Cdd:NF033875 205 ---VDQLQKEQAKKIAQQAAELKAKNEKIAKEN-------------AEIAAKN----------KAEKERYEKEVAE 254
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2378-2618 |
2.00e-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: 44.56 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2378 SSVEEELVKVKVQLDETDKQKSVLDVEL-KRLKQEVSDAIKQKAQVEDELSKVkiqMEDLLKLKLKIEKENQELMKKdkd 2456
Cdd:COG5185 206 SIKESETGNLGSESTLLEKAKEIINIEEaLKGFQDPESELEDLAQTSDKLEKL---VEQNTDLRLEKLGENAESSKR--- 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2457 ntkklLEEEAENMKKLAEEAARLNIEAQEAARLRQ-IAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2534
Cdd:COG5185 280 -----LNENANNLIKQFENTKEKIAEYTKSIDIKKaTESLEEQLAAAEAEQELEESKRETETGiQNLTAEIEQGQESLTE 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2535 AQVEAQKLLEAKKEMQQ--RLDQETEGFQKSLEAERKRQLEITAEAEK-LKVKVTQLSDAQSKAEEEAKKFKKQADEIKI 2611
Cdd:COG5185 355 NLEAIKEEIENIVGEVElsKSSEELDSFKDTIESTKESLDEIPQNQRGyAQEILATLEDTLKAADRQIEELQRQIEQATS 434
|
....*..
gi 1207141724 2612 RLQETEK 2618
Cdd:COG5185 435 SNEEVSK 441
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4200-4231 |
2.10e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.10e-03
10 20 30
....*....|....*....|....*....|..
gi 1207141724 4200 KLLSAERAVTGYKDPYSGKVISLFQAMKKGLI 4231
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2273-2581 |
2.12e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2273 DKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERQKKAAEAEAAKQAKAQEDAEKLRKEAEKEASRRAEAEAAA 2352
Cdd:pfam13868 25 DAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMD 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2353 LKLKQEADSEMAKYKKLAEKTLKQKSSVEEelvkvkvQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQ 2432
Cdd:pfam13868 105 EIVERIQEEDQAEAEEKLEKQRQLREEIDE-------FNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2433 MEDLLKLKLKIEKENQELMKKDKDN-----TKKLLEEEAENMKKLAEEAARLNIEAQEA---ARLRQIAESDLAKQRElA 2504
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAErdelrAKLYQEEQERKERQKEREEAEKKARQRQElqqAREEQIELKERRLAEE-A 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2505 EKMLEEKKQAIQEAAKL----KAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQET-EGFQKSLEAERKRQLEITAEAE 2579
Cdd:pfam13868 257 EREEEEFERMLRKQAEDeeieQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEElEEGERLREEEAERRERIEEERQ 336
|
..
gi 1207141724 2580 KL 2581
Cdd:pfam13868 337 KK 338
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1559-1795 |
2.20e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.05 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1559 AEKLKEEERKKMAEMQAELEK-QKQLAETHAKaIAKAEQEANELKTKMKDEVSKRQDVAVDSEKQKHNIQRELQELKT-L 1636
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAaQAELDALQAE-LEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGErA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1637 SEQEIKAKSQQVEEALLSRTRIEEEIHiiRLQLETTMKQKNTAETELLQLRAKAVDADKlrNAAQEEAEKLRKQVAEETQ 1716
Cdd:COG3883 93 RALYRSGGSVSYLDVLLGSESFSDFLD--RLSALSKIADADADLLEELKADKAELEAKK--AELEAKLAELEALKAELEA 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 1717 KKRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQLESKQVALTA 1795
Cdd:COG3883 169 AKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1994-2124 |
2.24e-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: 41.70 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1994 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEEEAarqRAEAEKILKEkltAINEATRLKTEaeiALKEKEAENDRLKR 2073
Cdd:COG0711 29 LDERQEKIADGLAEAERAKEEAEAALAEYEEKLAEA---RAEAAEIIAE---ARKEAEAIAEE---AKAEAEAEAERIIA 99
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2074 KAEEEGYQ-----RKVLEDQAAQHKQAIEEKIgqLKKSSDTelDRQKKIVEETLKQ 2124
Cdd:COG0711 100 QAEAEIEQerakaLAELRAEVADLAVAIAEKI--LGKELDA--AAQAALVDRFIAE 151
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1815-2039 |
2.28e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1815 AEHLKKQQAEADKAREQAEKELETWRQKANEAlRLRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEeAALKQKEA 1894
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEA-EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAR-AELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1895 AEMELGNQRKMAEETAKQkLAAEQELIRLRADFEHAEQQRTVL-------DDELQRLKNDVNSAVKQ-KKELEEELIKVR 1966
Cdd:COG3206 241 RLAALRAQLGSGPDALPE-LLQSPVIQQLRAQLAELEAELAELsarytpnHPDVIALRAQIAALRAQlQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141724 1967 KEMEILLQQKSKAEKETMSNTEKSKQLLESEAaKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKI 2039
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAEALTVGNVRVI 391
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1907-2037 |
2.28e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 44.56 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1907 EETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKEtmsN 1986
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQE---R 214
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1207141724 1987 TEKSKQLLEsEAAKMRELAEEAT------KLRSVAEEAKKQR----QIAEEEAARQRAEAE 2037
Cdd:PRK11448 215 KQKRKEITD-QAAKRLELSEEETrilidqQLRKAGWEADSKTlrfsKGARPEKGRNLAIAE 274
|
|
| CH_AtFIM_like_rpt1 |
cd21293 |
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
230-327 |
2.48e-03 |
|
first calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, and are probably involved in the cell cycle, cell division, cell elongation, and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409142 Cd Length: 116 Bit Score: 40.97 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 230 QKKTFTKWVNKHLVK---------AQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR-----FHKLQNVQIALDF 295
Cdd:cd21293 2 EKGSYVDHINRYLGDdpflkqflpIDPSTNDLFDLVKDGVLLCKLINVAVPGTIDERAINTKkvlnpWERNENHTLCLNS 81
|
90 100 110
....*....|....*....|....*....|..
gi 1207141724 296 LKHRQVKLVNIRNDDIADGNPKLTLGLIWTII 327
Cdd:cd21293 82 AKAIGCSVVNIGTQDLAEGRPHLVLGLISQII 113
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3297-3333 |
2.48e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.48e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1207141724 3297 KLLSAERAVCGYKDPYTGKTVSLFEAMQKDLIKKEQG 3333
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1333-1859 |
2.50e-03 |
|
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: 44.40 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1333 IEASQTQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVELEHYRQLVGNLrERWQAVFAQIELRQRELDL 1412
Cdd:pfam01576 540 LEALEEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNL-EKKQKKFDQMLAEEKAISA 618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1413 lnrqmqAYRESYDwliRWIADAKQRQDKLHAvpiggskgLQEQLTQEKKLLEEIEK-NKDKVEDCQKFAKGYIDAIKDYE 1491
Cdd:pfam01576 619 ------RYAEERD---RAEAEAREKETRALS--------LARALEEALEAKEELERtNKQLRAEMEDLVSSKDDVGKNVH 681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1492 lQLVTYKALVEPIASPLkKAKMESASDDI-IQEYVTLRTRYSeLMTLSSQYikfiietQRRLQDEEKAAEKLKEEERKKM 1570
Cdd:pfam01576 682 -ELERSKRALEQQVEEM-KTQLEELEDELqATEDAKLRLEVN-MQALKAQF-------ERDLQARDEQGEEKRRQLVKQV 751
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1571 AEMQAELE---KQKQLAETHAKaiaKAEQEANELKTKMkDEVSKRQDVAVDSEK----QKHNIQRELQELKtLSEQEIKA 1643
Cdd:pfam01576 752 RELEAELEderKQRAQAVAAKK---KLELDLKELEAQI-DAANKGREEAVKQLKklqaQMKDLQRELEEAR-ASRDEILA 826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1644 KSQQVEEALLSrtrIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEKLRKQVA---EETQKKRK 1720
Cdd:pfam01576 827 QSKESEKKLKN---LEAELLQLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAqleEELEEEQS 903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1721 AEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAK---KTAATQLESKQVALTARL 1797
Cdd:pfam01576 904 NTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQLERQNKELKAKLQEMEGTVKskfKSSIAALEAKIAQLEEQL 983
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1798 EESLKNEQVMVIQLQEEAEHLKK-------QQAEADKAREQAEKELETWRQkaneaLRLRL-QAEEEANK 1859
Cdd:pfam01576 984 EQESRERQAANKLVRRTEKKLKEvllqvedERRHADQYKDQAEKGNSRMKQ-----LKRQLeEAEEEASR 1048
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1919-2067 |
2.55e-03 |
|
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.
Pssm-ID: 461778 [Multi-domain] Cd Length: 859 Bit Score: 44.28 E-value: 2.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1919 ELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAE----KETMSNTEKSKQLL 1994
Cdd:pfam05911 682 ENKRLKEEFEQLKSEKENLEVELASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAEtqlkCMAESYEDLETRLT 761
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1995 ESEaAKMRELAEEATKLRSVAEEakkQRQIAEEEAAR--------QRAEAEKILKEklTAINEATRLKTEAEI-ALKEKE 2065
Cdd:pfam05911 762 ELE-AELNELRQKFEALEVELEE---EKNCHEELEAKclelqeqlERNEKKESSNC--DADQEDKKLQQEKEItAASEKL 835
|
..
gi 1207141724 2066 AE 2067
Cdd:pfam05911 836 AE 837
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2370-2687 |
2.59e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2370 AEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkiekenQE 2449
Cdd:COG4372 33 LRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQA-----------QE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2450 LMKKDKDNTKKLLEEeaenMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQ 2529
Cdd:COG4372 102 ELESLQEEAEELQEE----LEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2530 KQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEI 2609
Cdd:COG4372 178 EAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVIL 257
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2610 KIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2687
Cdd:COG4372 258 KEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAIL 335
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2459-2606 |
2.64e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2459 KKLLEEEAENMKKLAEEAARLNIEAQEAAR---LRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQA 2535
Cdd:PRK12705 28 RQRLAKEAERILQEAQKEAEEKLEAALLEAkelLLRERNQQRQEARREREELQREEERLVQKEEQLDARAEKLDNLENQL 107
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2536 QVEAQKLLEAKKEMQQRLDQETEGFQK--SLEAERKRQ-----LEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQA 2606
Cdd:PRK12705 108 EEREKALSARELELEELEKQLDNELYRvaGLTPEQARKlllklLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4125-4163 |
2.67e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 38.46 E-value: 2.67e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 4125 YLEGISSIAGVFVEATKDRLSVYQAMKKTMIRPGTAFEL 4163
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
1948-2485 |
2.73e-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: 43.79 E-value: 2.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1948 VNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEA---KKQRQI 2024
Cdd:COG5185 3 QRSKFLQVKNPLAKEGNANKELIEILLESSKSEGKTLVFITILFFPLGISRDSLRVTLRSVINVLDGLNYQndvKKSESS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2025 AEEEAARQRA-EAEKILKEKLTAINEATRLKTEAEIA---LKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKI 2100
Cdd:COG5185 83 VKARKFLKEKkLDTKILQEYVNSLIKLPNYEWSADILislLYLYKSEIVALKDELIKVEKLDEIADIEASYGEVETGIIK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2101 GQLKKSSDTELDRQKK--IVEETLKQRKVVEEEihiLKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFR 2178
Cdd:COG5185 163 DIFGKLTQELNQNLKKleIFGLTLGLLKGISEL---KKAEPSGTVNSIKESETGNLGSESTLLEKAKEIINIEEALKGFQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2179 KLALEEEKKRKEA---EAKVKQIQAAEEEAARQH----KAAQEEVGRLMKLAEEAKKQkeIAEKEAEKQVILVQEAAQKC 2251
Cdd:COG5185 240 DPESELEDLAQTSdklEKLVEQNTDLRLEKLGENaessKRLNENANNLIKQFENTKEK--IAEYTKSIDIKKATESLEEQ 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2252 SAAEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaaeaeaakqakaqedA 2331
Cdd:COG5185 318 LAAAEAEQELEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGEVELSKSSEE------------------L 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2332 EKLRKEAEKEASRRAEAEAAALKLKQEADSEMAKYKKLAEK-------TLKQKSSVEEELVKVKVQLDE--TDKQKSVLD 2402
Cdd:COG5185 380 DSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAADRqieelqrQIEQATSSNEEVSKLLNELISelNKVMREADE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2403 VELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIE 2482
Cdd:COG5185 460 ESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHIL 539
|
...
gi 1207141724 2483 AQE 2485
Cdd:COG5185 540 ALE 542
|
|
| DUF3450 |
pfam11932 |
Protein of unknown function (DUF3450); This family of proteins are functionally ... |
2528-2610 |
2.77e-03 |
|
Protein of unknown function (DUF3450); This family of proteins are functionally uncharacterized. This protein is found in bacteria and eukaryotes. Proteins in this family are about 260 amino acids in length.
Pssm-ID: 432198 [Multi-domain] Cd Length: 238 Bit Score: 42.60 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2528 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEgfQKSLEAERKRQLeiTAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2607
Cdd:pfam11932 11 LAATLDQALDLAEKAVAAAAQSQKKIDKWDD--EKQELLAEYRAL--KAELESLEVYNRQLERLVASQEQEIASLERQIE 86
|
...
gi 1207141724 2608 EIK 2610
Cdd:pfam11932 87 EIE 89
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1876-2312 |
2.80e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.87 E-value: 2.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1876 REAKKRAKAEEAALKQKEAAEMElgnQRKMAEETAKQKLAAEQELIRLRADFEHAEQQrtvlddelqrlkndvnsAVKQK 1955
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEE-----------------AREAK 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1956 KELEEELIKVRKEMEillQQKSKAEKETmsntEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQRQIAE----EEAAR 2031
Cdd:COG3064 62 AEAEQRAAELAAEAA---KKLAEAEKAA----AEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAkrkaEEEAK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2032 QRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTEL 2111
Cdd:COG3064 135 RKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADA 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2112 DRQKKIVEETLKQRKVVEEEIHILKLNFEKASSGKQELELELKKLKGIADETQKSKAKAEEEAEKFRKLALEEEKKRKEA 2191
Cdd:COG3064 215 ALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2192 EAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMA 2271
Cdd:COG3064 295 LVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGA 374
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1207141724 2272 QDKLKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAER 2312
Cdd:COG3064 375 LLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAA 415
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2379-2617 |
2.96e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.12 E-value: 2.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2379 SVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEdllklklKIEKENQELMKKDKDnt 2458
Cdd:PRK01156 194 SSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLED-------MKNRYESEIKTAESD-- 264
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2459 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVE 2538
Cdd:PRK01156 265 LSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDYNDYIKK 344
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1207141724 2539 AQKLLEAKKEMQQrLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQETE 2617
Cdd:PRK01156 345 KSRYDDLNNQILE-LEGYEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDIS 422
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1550-1860 |
3.33e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.37 E-value: 3.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1550 RRLQDEEKAAEKLKEEERKKMAEMQAELEKQKQLAETHAKAIAKAEQEAN---ELKTKMKDEVSKRQDVAVDSEKQKHNI 1626
Cdd:pfam13868 24 RDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRyrqELEEQIEEREQKRQEEYEEKLQEREQM 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1627 QRELQELKTLSEQEIKAKSQQVEEALlsrtriEEEIHIIRLQLEttMKQKNTAETELLQLRAKAVDADKLRNAAQEEAEK 1706
Cdd:pfam13868 104 DEIVERIQEEDQAEAEEKLEKQRQLR------EEIDEFNEEQAE--WKELEKEEEREEDERILEYLKEKAEREEEREAER 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1707 LRKQVAEETQKKRKAEEELKRKseaekdaakeKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAATQL 1786
Cdd:pfam13868 176 EEIEEEKEREIARLRAQQEKAQ----------DEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQI 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1207141724 1787 ESKQVALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELE-TWRQKANEALRLRLQAEEEANKK 1860
Cdd:pfam13868 246 ELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEkQIEEREEQRAAEREEELEEGERL 320
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2459-2608 |
3.39e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2459 KKLLEEEAENMKKLAE---EAARLNIEAQEAARLRQiAESDLAKQRELAEKMLEEKKQAIQEA-AKLKAEAEKLQKQKDQ 2534
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKrilEEAKKEAEAIKKEALLE-AKEEIHKLRNEFEKELRERRNELQKLeKRLLQKEENLDRKLEL 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2535 AQVEAQKLLEAKKEMQQRLDQ--ETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2608
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQEleKKEEELEELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEAAVLIKEIEE 180
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1951-2077 |
3.42e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 40.29 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1951 AVKQKKELEEELIKVRKEMEillqqksKAEKETMSNTEKSKQLLEseaaKMRELAEEATKLRSVAEEAKKQRQIAEEEAA 2030
Cdd:pfam20492 4 AEREKQELEERLKQYEEETK-------KAQEELEESEETAEELEE----ERRQAEEEAERLEQKRQEAEEEKERLEESAE 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1207141724 2031 RQRAEAEKILKEKLTAINEATRLKTEAEialkEKEAENDRLKRKAEE 2077
Cdd:pfam20492 73 MEAEEKEQLEAELAEAQEEIARLEEEVE----RKEEEARRLQEELEE 115
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4479-4509 |
3.51e-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: 3.51e-03
10 20 30
....*....|....*....|....*....|.
gi 1207141724 4479 AGILDTDTLEKVSVTEAMHRNLVDNITGQRL 4509
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
2368-2698 |
3.53e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.35 E-value: 3.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2368 KLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQEVSDAIKQKAQVEDELSKVKIQMEDLlklklkieken 2447
Cdd:COG4372 3 RLGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQA----------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2448 QELMKKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKMLEEKKQAIQEAAKLKAEAEK 2527
Cdd:COG4372 72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2528 LQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQAD 2607
Cdd:COG4372 152 LKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2608 EIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTIL 2687
Cdd:COG4372 232 GLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIG 311
|
330
....*....|.
gi 1207141724 2688 QQSFFAEKETL 2698
Cdd:COG4372 312 ALEDALLAALL 322
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
2462-2608 |
3.75e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 43.43 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2462 LEEEAENMKKLAEEAARLNIEAQE--AARLRQIAESDLAKQ-RELAEKMLEEKKQAIQ----EAAKLKAEAEKLQKQKDQ 2534
Cdd:PRK07735 37 LEEENREKEKALPKNDDMTIEEAKrrAAAAAKAKAAALAKQkREGTEEVTEEEKAKAKakaaAAAKAKAAALAKQKREGT 116
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2535 AQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEEAKKFKKQADE 2608
Cdd:PRK07735 117 EEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGE 190
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1228-1651 |
3.89e-03 |
|
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: 43.56 E-value: 3.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1228 TQRATEQKKVQTELEGIKKDLDKVVEKSEAVLATSQQSSSAPVLRSEIDITQKKMEHVYGLSSVYLDKLKTIDLVIRSTQ 1307
Cdd:pfam05483 356 ATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELK 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1308 GAE-DILNKYENQLREVNKVPVNEKEIEASQ----TQLQKLRSEAEGKQATFDRLEEELQRATEVNKRMSQLHSERDVEL 1382
Cdd:pfam05483 436 GKEqELIFLLQAREKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLEL 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1383 EHYRQLVGNLRERWQAVFAQIELRQRELDLLNRQMQAYRESY----DWLIRWIADAKQRQDKLHAVPIGGSKGLQEQLTQ 1458
Cdd:pfam05483 516 KKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFiqkgDEVKCKLDKSEENARSIEYEVLKKEKQMKILENK 595
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1459 EKKLLEEIEKNKDKVEDCQKFAKGYIDAIKDYELQLVTYKALVEPIASPLKKAKMEsasddiIQEYVTLRTRYSELMTLS 1538
Cdd:pfam05483 596 CNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQK------FEEIIDNYQKEIEDKKIS 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1539 SQYIKFIIETQRRLQDEE-KAAEKLKEEERKKMAEMQAELEKQKQlaeTHAKAIAKAEQEANELKTKMKDEVSKRqdvaV 1617
Cdd:pfam05483 670 EEKLLEEVEKAKAIADEAvKLQKEIDKRCQHKIAEMVALMEKHKH---QYDKIIEERDSELGLYKNKEQEQSSAK----A 742
|
410 420 430
....*....|....*....|....*....|....
gi 1207141724 1618 DSEKQKHNIQRELQELKTLSEQEIKAKSQQVEEA 1651
Cdd:pfam05483 743 ALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEA 776
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1999-2142 |
4.03e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 43.35 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1999 AKMRELAEEATKLRSVAEEAKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEEE 2078
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2079 GYQRKVLEDQAAQHKQAIEE------KIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKLNFEKA 2142
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQT 183
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2576-2785 |
4.11e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2576 AEAEKLKVKVtqlsdAQSKAEEEAKKFKKQADEIKIRLQETEKHTSEKHTVVEKLEVQRLQSKQEADGLHKAIADLEKEK 2655
Cdd:PRK09510 75 KRAEEQRKKK-----EQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2656 EKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQSFFAEKEtllkkekaieeekkkLEKQFEDEVKKaealKAEQERQRK 2735
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAE---------------AAAKAAAEAKK----KAEAEAKKK 210
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2736 LMEEERKKlqSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRIEQEKLLAE 2785
Cdd:PRK09510 211 AAAEAKKK--AAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2462-2797 |
4.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.79 E-value: 4.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2462 LEEEAENMKKLAEE----AARLNIeAQEAARLR-QI--AESDLAkqrELAEKmLEEKKQAIQEAAKLKAEAEKlqkQKDQ 2534
Cdd:PRK04863 316 LAELNEAESDLEQDyqaaSDHLNL-VQTALRQQeKIerYQADLE---ELEER-LEEQNEVVEEADEQQEENEA---RAEA 387
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2535 AQveaQKLLEAKKEM---QQRLD-QETEG--FQKSLEA-ERKRQL----------------EITAEAEKLKVKV----TQ 2587
Cdd:PRK04863 388 AE---EEVDELKSQLadyQQALDvQQTRAiqYQQAVQAlERAKQLcglpdltadnaedwleEFQAKEQEATEELlsleQK 464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2588 LSDAQSKAEEEAKKFK---KQADEI-KIRLQETEKHTSEKHTVvEKLEVQRLQSKQEAdglHKAIADLEKEKEKLKKEAA 2663
Cdd:PRK04863 465 LSVAQAAHSQFEQAYQlvrKIAGEVsRSEAWDVARELLRRLRE-QRHLAEQLQQLRMR---LSELEQRLRQQQRAERLLA 540
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2664 DLQKQSKEMANVQQ--EQLQQEKTILQQSFFAEKETLLKKEKAIEEEKKKLEKQFEDEVKKAEALKAEQERQRKLME--- 2738
Cdd:PRK04863 541 EFCKRLGKNLDDEDelEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsg 620
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 2739 ---EERKKLQSAMDAAIKKQKEAEEEMNGKQKEMQDLEKKRieqEKLLAEENKNLrEKLQQL 2797
Cdd:PRK04863 621 eefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEI---ERLSQPGGSED-PRLNAL 678
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1618-1829 |
4.43e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.94 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1618 DSEKQKHNIQRElqelktlSEQEIKAKSQQVEEAllsRTRIEEEIHIIRLQLETTMKQKNTAETELLQLRAKAVdADKlr 1697
Cdd:COG2268 200 DARIAEAEAERE-------TEIAIAQANREAEEA---ELEQEREIETARIAEAEAELAKKKAEERREAETARAE-AEA-- 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1698 nAAQEEAEKLRKQVAEETQKKRKAEE-ELKRKseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQRQIQVVE- 1775
Cdd:COG2268 267 -AYEIAEANAEREVQRQLEIAEREREiELQEK------------------EAEREEAELEADVRKPAEAEKQAAEAEAEa 327
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1207141724 1776 --EVAKKTAATQLESKQVALTARLEESLKNEQVMVIQ-LQEEAEHLKKQQAEADKAR 1829
Cdd:COG2268 328 eaEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEkLPEIAEAAAKPLEKIDKIT 384
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
2473-2617 |
4.49e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2473 AEEAARLNIEAQEAARLRQIAESDLAKQRELAEKML--EEKKQAIQEAAKLKAEAEKL-QKQKDQAQVEAQKLLEAKKEM 2549
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQERLEKEEEERLRkeELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEER 88
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1207141724 2550 QQRLDQETEGFQKSLEAERKRQLEitaEAEKLKVKVTQLsdaQSKAEEEAKKFKKQADEIKIRLQETE 2617
Cdd:pfam05672 89 EQREQEEQERLQKQKEEAEAKARE---EAERQRQEREKI---MQQEEQERLERKKRIEEIMKRTRKSD 150
|
|
| dnaK |
PRK00290 |
molecular chaperone DnaK; Provisional |
2460-2582 |
4.57e-03 |
|
molecular chaperone DnaK; Provisional
Pssm-ID: 234715 [Multi-domain] Cd Length: 627 Bit Score: 43.17 E-value: 4.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2460 KLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESdLAKQrelAEKMLEEKKQAIQEAAKLKAEA-----EKLQKQKDQ 2534
Cdd:PRK00290 499 GLSDEEIERMVKDAEANAEEDKKRKELVEARNQADS-LIYQ---TEKTLKELGDKVPADEKEKIEAaikelKEALKGEDK 574
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2535 AQVEA--QKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLK 2582
Cdd:PRK00290 575 EAIKAktEELTQASQKLGEAMYQQAQAAQGAAGAAAKDDDVVDAEFEEVK 624
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1695-1860 |
4.64e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1695 KLRNAAQEEAEKLRKQVAEETQK-----KRKAEEELKrkseaekdaakekkkaledlEKFKLQAEEAERHLKQAELEKQR 1769
Cdd:PRK12704 27 KIAEAKIKEAEEEAKRILEEAKKeaeaiKKEALLEAK--------------------EEIHKLRNEFEKELRERRNELQK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1770 Q----IQVVEEVAKKTAAtqLESKQVALTARlEESLKNEQVMVIQLQEEAEHLKKQQAE---------ADKAR----EQA 1832
Cdd:PRK12704 87 LekrlLQKEENLDRKLEL--LEKREEELEKK-EKELEQKQQELEKKEEELEELIEEQLQelerisgltAEEAKeillEKV 163
|
170 180
....*....|....*....|....*...
gi 1207141724 1833 EKELETwrQKANEALRLRLQAEEEANKK 1860
Cdd:PRK12704 164 EEEARH--EAAVLIKEIEEEAKEEADKK 189
|
|
| TPR_MLP1_2 |
pfam07926 |
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of ... |
2207-2311 |
4.91e-03 |
|
TPR/MLP1/MLP2-like protein; The sequences featured in this family are similar to a region of human TPR protein and to yeast myosin-like proteins 1 (MLP1) and 2 (MLP2). These proteins share a number of features; for example, they all have coiled-coil regions and all three are associated with nuclear pores. TPR is thought to be a component of nuclear pore complex- attached intra-nuclear filaments, and is implicated in nuclear protein import. Moreover, its N-terminal region is involved in the activation of oncogenic kinases, possibly by mediating the dimerization of kinase domains or by targeting these kinases to the nuclear pore complex. MLP1 and MLP2 are involved in the process of telomere length regulation, where they are thought to interact with proteins such as Tel1p and modulate their activity.
Pssm-ID: 462316 [Multi-domain] Cd Length: 129 Bit Score: 40.31 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2207 RQHKAAQEEVGRLMKLAEEAKKQKEIAEKEAEKQVILVQEAaqkcsaaEQKAQNVLVQQNKDSMAQDKLKEEFEKAKKLA 2286
Cdd:pfam07926 1 AELSSLQSEIKRLKEEAADAEAQLQKLQEDLEKQAEIAREA-------QQNYERELVLHAEDIKALQALREELNELKAEI 73
|
90 100
....*....|....*....|....*
gi 1207141724 2287 QEAEKAKDNAEKEAALLHKKAEEAE 2311
Cdd:pfam07926 74 AELKAEAESAKAELEESEESWEEQK 98
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1923-2310 |
4.95e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 42.96 E-value: 4.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1923 LRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMR 2002
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2003 ELAEEATKLrSVAEEAKKQRqIAEEEAARQRAEAEKILKEkltaiNEATRLKTEAEIA---LKEKEAENDRLKRKAEEEG 2079
Cdd:pfam07888 112 ELSEEKDAL-LAQRAAHEAR-IRELEEDIKTLTQRVLERE-----TELERMKERAKKAgaqRKEEEAERKQLQAKLQQTE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2080 YQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIveeTLKQRKVVEEEIHILKLNF--EKASSGKQELELELKKLK 2157
Cdd:pfam07888 185 EELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKL---TTAHRKEAENEALLEELRSlqERLNASERKVEGLGEELS 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2158 GIAdeTQKSKAKAEEEAEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQE---------EVGRLMKLAEEAKK 2228
Cdd:pfam07888 262 SMA--AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrieklsaELQRLEERLQEERM 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2229 QKEIAEKE--AEKQVILVQEAAQKCSAAEQKAQNVLVQQNKDSMAQDKlKEEFEKAKKLAQEAEKAKDNAEKEAALLHKK 2306
Cdd:pfam07888 340 EREKLEVElgREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEK-QELLEYIRQLEQRLETVADAKWSEAALTSTE 418
|
....
gi 1207141724 2307 AEEA 2310
Cdd:pfam07888 419 RPDS 422
|
|
| PLN03229 |
PLN03229 |
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional |
1762-2079 |
5.09e-03 |
|
acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha; Provisional
Pssm-ID: 178768 [Multi-domain] Cd Length: 762 Bit Score: 43.30 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1762 QAELEKQRQiQVVEevAKKTAATQLESKQVALTARLEESLKNE---QVMVIQLQEEAEHLKKQQAEADKAREQAEKELET 1838
Cdd:PLN03229 435 EGEVEKLKE-QILK--AKESSSKPSELALNEMIEKLKKEIDLEyteAVIAMGLQERLENLREEFSKANSQDQLMHPVLME 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1839 WRQKANEALRLRL-QAEEEANKKTAAQEEAEKQKEEAKREAKKRAKAEEAALKQKEAAEMELGNQR-KMA---EETAKQK 1913
Cdd:PLN03229 512 KIEKLKDEFNKRLsRAPNYLSLKYKLDMLNEFSRAKALSEKKSKAEKLKAEINKKFKEVMDRPEIKeKMEalkAEVASSG 591
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1914 LAAEQELirlradfehaeqqrtvlDDELqrlkndVNSAVKQKKELEEELIKVRKEME---ILLQQKSKAEKETMSNTEKS 1990
Cdd:PLN03229 592 ASSGDEL-----------------DDDL------KEKVEKMKKEIELELAGVLKSMGlevIGVTKKNKDTAEQTPPPNLQ 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1991 KQL--LESEAAKMRELAEEATKLRSVAEEAKKqrQIAEEEAARQRAEAEKI------LKEKLTAINEATRLKT-----EA 2057
Cdd:PLN03229 649 EKIesLNEEINKKIERVIRSSDLKSKIELLKL--EVAKASKTPDVTEKEKIealeqqIKQKIAEALNSSELKEkfeelEA 726
|
330 340
....*....|....*....|....
gi 1207141724 2058 EIALKEK--EAENDRLKRKAEEEG 2079
Cdd:PLN03229 727 ELAAAREtaAESNGSLKNDDDKEE 750
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2452-2598 |
5.28e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2452 KKDKDNTKKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESDLAKQRELAEKmLEEKKQAIQ---EAAKLKAEAEKL 2528
Cdd:COG1579 23 EHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKK-YEEQLGNVRnnkEYEALQKEIESL 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141724 2529 QKQKDQA---QVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKRQLEITAEAEKLKVKVTQLSDAQSKAEEE 2598
Cdd:COG1579 102 KRRISDLedeILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAKIPP 174
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1686-1844 |
5.43e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1686 LRAKAVDADKLRNAAQEEAEK------LRKQVAEETQK---KRKAEEELKRKSEAEKDAAKEKKKALEDLEKFKLQAEEA 1756
Cdd:pfam13904 61 LAAKQRQRQKELQAQKEEREKeeqeaeLRKRLAKEKYQewlQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEA 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1757 ERHLKQAELEKQRQIQvveevAKKtaatqleskqvaltarleeslkneqvmviqlQEEAEHLKKQQAEADKAREQAEKEL 1836
Cdd:pfam13904 141 KEVLQEWERKKLEQQQ-----RKR-------------------------------EEEQREQLKKEEEEQERKQLAEKAW 184
|
....*...
gi 1207141724 1837 ETWRQKAN 1844
Cdd:pfam13904 185 QKWMKNVK 192
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1994-2236 |
6.08e-03 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 42.98 E-value: 6.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1994 LESEAAKMRELAEEATKLRSVAEEAKKQRQIAEE-EAARQRAEAEKILKEKLTAINEATRLKTeAEIALKEKEAENDRLK 2072
Cdd:COG4913 223 TFEAADALVEHFDDLERAHEALEDAREQIELLEPiRELAERYAAARERLAELEYLRAALRLWF-AQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2073 RKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKKSSDTELDRQKKIVEETLKQRKVVEEEIHILKlnfekassgkqelele 2152
Cdd:COG4913 302 AELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLE---------------- 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2153 lkklkgiadetqkskakaeeeaEKFRKLALEEEKKRKEAEAKVKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEI 2232
Cdd:COG4913 366 ----------------------ALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
|
....
gi 1207141724 2233 AEKE 2236
Cdd:COG4913 424 LEAE 427
|
|
| PRK08476 |
PRK08476 |
F0F1 ATP synthase subunit B'; Validated |
2448-2555 |
6.53e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 181442 [Multi-domain] Cd Length: 141 Bit Score: 40.06 E-value: 6.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2448 QELMKKDKDNTKKLLEEEAEnmkkLAEEAARLNIEAQEAARlrQIAESDLAKQRELAEKMLEEKKQAIqeAAKLKAEAEK 2527
Cdd:PRK08476 40 NASIKNDLEKVKTNSSDVSE----IEHEIETILKNAREEAN--KIRQKAIAKAKEEAEKKIEAKKAEL--ESKYEAFAKQ 111
|
90 100
....*....|....*....|....*....
gi 1207141724 2528 LQKQKDQAQVEAQ-KLLEAKKEMQQRLDQ 2555
Cdd:PRK08476 112 LANQKQELKEQLLsQMPEFKEALNAKLSK 140
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1574-1834 |
6.54e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 42.63 E-value: 6.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1574 QAELEKQKQlaethAKAiAKAEQEANELKTKMKDEVSKrqdvAVDSEKQKHNIQRELQELKTLSEQEIKA-KSQQVEEAL 1652
Cdd:PRK05035 459 QARLEREKA-----ARE-ARHKKAAEARAAKDKDAVAA----ALARVKAKKAAATQPIVIKAGARPDNSAvIAAREARKA 528
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1653 LSRTRIEEEihiirlqlettmkQKNTAETELLQLRAKAVDADKLRNAAQEEAEKlrKQVAEETQKKRKAEEEL---KRKS 1729
Cdd:PRK05035 529 QARARQAEK-------------QAAAAADPKKAAVAAAIARAKAKKAAQQAANA--EAEEEVDPKKAAVAAAIaraKAKK 593
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1730 EAEKDAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVAKKTAAtqleskqVALTARLEESLKNEQVMVI 1809
Cdd:PRK05035 594 AAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAA-------VAAAIARAKARKAAQQQAN 666
|
250 260
....*....|....*....|....*
gi 1207141724 1810 QLQEEAEHLKKQQAEADKAREQAEK 1834
Cdd:PRK05035 667 AEPEEAEDPKKAAVAAAIARAKAKK 691
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
2715-2786 |
6.59e-03 |
|
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.
Pssm-ID: 466641 [Multi-domain] Cd Length: 120 Bit Score: 39.52 E-value: 6.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2715 QFEDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEEMN--GKQKEMQDLEKKRIEQEKLLAEE 2786
Cdd:pfam20492 17 QYEEETKKAQEELEESEETAEELEEERRQAEEEAERLEQKRQEAEEEKErlEESAEMEAEEKEQLEAELAEAQE 90
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1991-2105 |
6.69e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 6.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1991 KQLLESEAAKMRELA----EEATKlrsVAEEAKKQRQI-AEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKE 2065
Cdd:PRK12704 26 KKIAEAKIKEAEEEAkrilEEAKK---EAEAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKL 102
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1207141724 2066 AENDRLKRKAEEEGYQRKVLEDQAAQHKQAIEEKIGQLKK 2105
Cdd:PRK12704 103 ELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ 142
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1745-1961 |
6.85e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.44 E-value: 6.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1745 DLEKFKLQAEEAERHLKQAE-----LEKQRQIQVVEEVAKKTAATQLESKQVALTARLEESLKNEQVMVIQLQEEAEHLK 1819
Cdd:COG4942 28 ELEQLQQEIAELEKELAALKkeekaLLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1820 KQQAEADKAREQAEKELETWRQKANEALRlRLQAEEEANKKTAAQEEAEKQKEEAKREAKKRAkaeEAALKQKEAAEMEL 1899
Cdd:COG4942 108 ELLRALYRLGRQPPLALLLSPEDFLDAVR-RLQYLKYLAPARREQAEELRADLAELAALRAEL---EAERAELEALLAEL 183
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1207141724 1900 GNQRKmaeETAKQKLAAEQELIRLRADFEHAEQQRTVLDDELQRLKNDVNSAVKQKKELEEE 1961
Cdd:COG4942 184 EEERA---ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2195-2609 |
6.89e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2195 VKQIQAAEEEAARQHKAAQEEVGRLMKLAEEAKKQKEIAE-----KEAEKQVILVQEAAQKCSAAEQ---KAQNVLVQQN 2266
Cdd:COG4717 104 LEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAElperlEELEERLEELRELEEELEELEAelaELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2267 KDSMAQDklKEEFEKAKKLAQEAEKAKDNAEKEAALLHKKAEEAERqkkaAEAEAAKQAKAQEDAEKLRKEAEKEASRRA 2346
Cdd:COG4717 184 EQLSLAT--EEELQDLAEELEELQQRLAELEEELEEAQEELEELEE----ELEQLENELEAAALEERLKEARLLLLIAAA 257
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2347 EAEAAALKLKQEADSEM----------------AKYKKLAEKTLKQKSSVEEELVKVKVQLDETDKQKSVLDVELKRLKQ 2410
Cdd:COG4717 258 LLALLGLGGSLLSLILTiagvlflvlgllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPE 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2411 EVSDAIKQKAQVEDELSkvKIQMEDLLKLKLKIEKENQELMKKDKDNTKKLLEEEAENMKKLAEEAARLNiEAQEaaRLR 2490
Cdd:COG4717 338 ELLELLDRIEELQELLR--EAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELE-ELEE--QLE 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2491 QIAESDLAKQRELAEKMLEEKKQAIQEAAKLkAEAEKLQKQKDQAQVEAQ-KLLEAKKEMQQRLDQetegfQKSLEAERK 2569
Cdd:COG4717 413 ELLGELEELLEALDEEELEEELEELEEELEE-LEEELEELREELAELEAElEQLEEDGELAELLQE-----LEELKAELR 486
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1207141724 2570 RQLEitaEAEKLKVKVTQLSDAQSKAEEE-AKKFKKQADEI 2609
Cdd:COG4717 487 ELAE---EWAALKLALELLEEAREEYREErLPPVLERASEY 524
|
|
| Spectrin |
pfam00435 |
Spectrin repeat; Spectrin repeat-domains are found in several proteins involved in ... |
828-908 |
6.94e-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: 39.22 E-value: 6.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 828 WLNEKEEEEVNYDWSDRNSNMTAKKDNYSGLMRDLEQREKRVNNVQMTGDKLLKDGHPARKTIEAFTAALQTQWSWILQL 907
Cdd:pfam00435 16 WIEEKEALLSSEDYGKDLESVQALLKKHKALEAELAAHQDRVEALNELAEKLIDEGHYASEEIQERLEELNERWEQLLEL 95
|
.
gi 1207141724 908 C 908
Cdd:pfam00435 96 A 96
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4163-4197 |
7.12e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.08 E-value: 7.12e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141724 4163 LLEAQAATGYIIDPIKNLKMNVQEAVKMGVVGPEF 4197
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
2717-2799 |
7.46e-03 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 42.67 E-value: 7.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2717 EDEVKKAEALKAEQERQRKLMEEERKKLQSAMDAAIKKQKEAEEE----MNGKQKEM--QDLEK--KRIEQeklLAEEN- 2787
Cdd:pfam13779 495 QERLSEALERGASDEEIAKLMQELREALDDYMQALAEQAQQNPQDlqqpDDPNAQEMtqQDLQRmlDRIEE---LARSGr 571
|
90
....*....|...
gi 1207141724 2788 -KNLREKLQQLQS 2799
Cdd:pfam13779 572 rAEAQQMLSQLQQ 584
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1943-2060 |
7.59e-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: 7.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1943 RLKNDVNSAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESEAAKMRELAEEATKLRSVAEEAKKQR 2022
Cdd:COG0542 401 RVRMEIDSKPEELDELERRLEQLEIEKEALKKEQDEASFERLAELRDELAELEEELEALKARWEAEKELIEEIQELKEEL 480
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1207141724 2023 qiaeEEAARQRAEAEKILKEKLTAINEATRLK----TEAEIA 2060
Cdd:COG0542 481 ----EQRYGKIPELEKELAELEEELAELAPLLreevTEEDIA 518
|
|
| Casc1_N |
pfam15927 |
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally ... |
2459-2530 |
7.85e-03 |
|
Cancer susceptibility candidate 1 N-terminus; This presumed domain is functionally uncharacterized. This domain family is found in eukaryotes, and is approximately 200 amino acids in length. The family is found in association with pfam12366. There are two completely conserved residues (N and W) that may be functionally important.
Pssm-ID: 464947 [Multi-domain] Cd Length: 201 Bit Score: 40.81 E-value: 7.85e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1207141724 2459 KKLLEEEAENMKKLAEEAARLNIEAQEAARLRQIAESD--LAKQRELAEKMLEEKKQAiqeAAKLKAEAEKLQK 2530
Cdd:pfam15927 1 ARLREEEEERLRAEEEEAERLEEERREEEEEERLAAEQdrRAEELEELKHLLEERKEA---LEKLRAEAREEAE 71
|
|
| SH3_Eps8 |
cd11764 |
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar ... |
1016-1050 |
8.05e-03 |
|
Src Homology 3 domain of Epidermal growth factor receptor kinase substrate 8 and similar proteins; This group is composed of Eps8 and Eps8-like proteins including Eps8-like 1-3, among others. These proteins contain N-terminal Phosphotyrosine-binding (PTB), central SH3, and C-terminal effector domains. Eps8 binds either Abi1 (also called E3b1) or Rab5 GTPase activating protein RN-tre through its SH3 domain. With Abi1 and Sos1, it becomes part of a trimeric complex that is required to activate Rac. Together with RN-tre, it inhibits the internalization of EGFR. The SH3 domains of Eps8 and similar proteins recognize peptides containing a PxxDY motif, instead of the classical PxxP motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.
Pssm-ID: 212698 [Multi-domain] Cd Length: 54 Bit Score: 37.63 E-value: 8.05e-03
10 20 30
....*....|....*....|....*....|....*
gi 1207141724 1016 EITVHKGDECALVNNSQPYkWKVRDSSGNEAVVPS 1050
Cdd:cd11764 15 ELSVLKGEYLEVLDDSRQW-WKVRNSRGQVGYVPH 48
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
1761-2100 |
8.09e-03 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 42.76 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1761 KQAELEKQRQIQVVEEVAKKTAATQLESKQV-ALTARLEESLKNEQVMVIQLQEEAEHLKKQQAEADKAREQAEKELETW 1839
Cdd:COG5022 822 LQKTIKREKKLRETEEVEFSLKAEVLIQKFGrSLKAKKRFSLLKKETIYLQSAQRVELAERQLQELKIDVKSISSLKLVN 901
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1840 RQKANEALRLRLQAEEEANKKTAaqeeaekqkeeakreakkrakaeeaaLKQKEAAEMELGNQRKMAEETAKQKLAAEQE 1919
Cdd:COG5022 902 LELESEIIELKKSLSSDLIENLE--------------------------FKTELIARLKKLLNNIDLEEGPSIEYVKLPE 955
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1920 LIRLRadfehaeQQRTVLDDELQRLKNdvnsAVKQKKELEEELIKVRKEMEILLQQKSKAEKETMSNTEKSKQLLESE-- 1997
Cdd:COG5022 956 LNKLH-------EVESKLKETSEEYED----LLKKSTILVREGNKANSELKNFKKELAELSKQYGALQESTKQLKELPve 1024
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1998 ----AAKMRELAEEATKLRSVAEEaKKQRQIAEEEAARQRAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKR 2073
Cdd:COG5022 1025 vaelQSASKIISSESTELSILKPL-QKLKGLLLLENNQLQARYKALKLRRENSLLDDKQLYQLESTENLLKTINVKDLEV 1103
|
330 340
....*....|....*....|....*..
gi 1207141724 2074 KAEEEGYQRKVLEDQAAQHKQAIEEKI 2100
Cdd:COG5022 1104 TNRNLVKPANVLQFIVAQMIKLNLLQE 1130
|
|
| T3SSipB |
pfam16535 |
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial ... |
2500-2616 |
8.11e-03 |
|
Type III cell invasion protein SipB; T3SSipB is a family of pathogenic Gram-negative bacterial proteins that invade human intestinal cells via the type III secretion system translocators. T3SSipB represents the coiled -coil region of the proteins and is shown to be homologous in activity to the pore-forming toxins of other Gram-negative pathogens, such as colicin Ia.
Pssm-ID: 435406 [Multi-domain] Cd Length: 155 Bit Score: 40.33 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2500 QRELAEKMLEEKKQAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLDQETEGFQKSLEAERKR-QLEITAEA 2578
Cdd:pfam16535 37 QQQKGLELSDEFQTALSEAEEATDAYEKAINKLKNAKSKAKAAEKKIDQAQTRLQSLAPDSPGKAKLEAAEqQAGIKKDA 116
|
90 100 110
....*....|....*....|....*....|....*...
gi 1207141724 2579 EKLKVKVTQLSDAQSKAEEEAKKFKKQADEIKIRLQET 2616
Cdd:pfam16535 117 LQADRTLDKALDAASKLTTKAMAKEKEADDFSAKFQGT 154
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2496-2779 |
8.33e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 41.82 E-value: 8.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2496 DLAKQRELAEKMLEEKK----QAIQEAAKLKAEAEKLQKQKDQAQVEAQKLLEAKKEMQQRLdqetegfqKSLEAERKrq 2571
Cdd:COG1340 12 ELEEKIEELREEIEELKekrdELNEELKELAEKRDELNAQVKELREEAQELREKRDELNEKV--------KELKEERD-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2572 lEITAEAEKLKVKVTQL---SDAQSKAEEEAKKFKKQADEIKIRlQETEKHTSEKH-TVVEKLEV--QRLQSKQEADGLH 2645
Cdd:COG1340 82 -ELNEKLNELREELDELrkeLAELNKAGGSIDKLRKEIERLEWR-QQTEVLSPEEEkELVEKIKEleKELEKAKKALEKN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 2646 KAIADLEKEKEKLKKEAADLQKQSKEMANVQQEQLQQEKTILQQ--SFFAEKETLlkkekaieeekkklEKQFEDEVKKA 2723
Cdd:COG1340 160 EKLKELRAELKELRKEAEEIHKKIKELAEEAQELHEEMIELYKEadELRKEADEL--------------HKEIVEAQEKA 225
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1207141724 2724 EALKAEQERqrklMEEERKKLQSAMDAAIKKQKEAEEEmngKQKEMQDLEKKRIEQ 2779
Cdd:COG1340 226 DELHEEIIE----LQKELRELRKELKKLRKKQRALKRE---KEKEELEEKAEEIFE 274
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1819-1972 |
8.63e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.31 E-value: 8.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1819 KKQQAEADK---AREQAEK-ELEtwRQK-----ANEALR---LRLQAEEEANKKTAaqeeaekqkeeakrEAKKRAKAEE 1886
Cdd:PTZ00491 662 KSQEAAARHqaeLLEQEARgRLE--RQKmhdkaKAEEQRtklLELQAESAAVESSG--------------QSRAEALAEA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1887 AALKQKEAAEMELGNQRkmaeeTAKQKLAAEQELIRLRadfehaeqQRTVLDDELQRLKNDVnsAVKQKKELEE-ELIKV 1965
Cdd:PTZ00491 726 EARLIEAEAEVEQAELR-----AKALRIEAEAELEKLR--------KRQELELEYEQAQNEL--EIAKAKELADiEATKF 790
|
....*..
gi 1207141724 1966 RKEMEIL 1972
Cdd:PTZ00491 791 ERIVEAL 797
|
|
| CH_PARVB_rpt2 |
cd21338 |
second calponin homology (CH) domain found in beta-parvin; Beta-parvin, also called affixin, ... |
223-334 |
9.19e-03 |
|
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: 39.57 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 223 ADERDRVQKKTFTKWVNKHLVKAQRHITDLYEDLRDGHNLISLLEVLSGETLPREKGRMR----FHKLQNVQIALDFLKH 298
Cdd:cd21338 15 APDKLSVVKKSLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEDYFVPLHNFYLTpesfDQKVHNVSFAFELMQD 94
|
90 100 110
....*....|....*....|....*....|....*.
gi 1207141724 299 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 334
Cdd:cd21338 95 GGLKKPKARPEDVVNLDLKSTLRVLYNLFTKYKNVE 130
|
|
| Tropomyosin_1 |
pfam12718 |
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and ... |
1941-2077 |
9.23e-03 |
|
Tropomyosin like; This family is a set of eukaryotic tropomyosins. Within the yeast Tpm1 and Tpm2, biochemical and sequence analyses indicate that Tpm2p spans four actin monomers along a filament, whereas Tpm1p spans five. Despite its shorter length, Tpm2p can compete with Tpm1p for binding to F-actin. Over-expression of Tpm2p in vivo alters the axial budding of haploids to a bipolar pattern, and this can be partially suppressed by co-over-expression of Tpm1p. This suggests distinct functions for the two tropomyosins, and indicates that the ratio between them is important for correct morphogenesis. The family also contains higher eukaryote Tpm3 members.
Pssm-ID: 403808 [Multi-domain] Cd Length: 142 Bit Score: 39.60 E-value: 9.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1941 LQRLKNDVNSAVKQKKELEEELikvrKEMEillQQKSKAEKETMSNTEKSKQL------LESEAAKMRELAEEATKLRSV 2014
Cdd:pfam12718 2 MNSLKLEAENAQERAEELEEKV----KELE---QENLEKEQEIKSLTHKNQQLeeevekLEEQLKEAKEKAEESEKLKTN 74
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1207141724 2015 AEEAKKQRQIAEEEAarqrAEAEKILKEKLTAINEATRLKTEAEIALKEKEAENDRLKRKAEE 2077
Cdd:pfam12718 75 NENLTRKIQLLEEEL----EESDKRLKETTEKLRETDVKAEHLERKVQALEQERDEWEKKYEE 133
|
|
| PRK05759 |
PRK05759 |
F0F1 ATP synthase subunit B; Validated |
1819-1916 |
9.33e-03 |
|
F0F1 ATP synthase subunit B; Validated
Pssm-ID: 180240 [Multi-domain] Cd Length: 156 Bit Score: 40.14 E-value: 9.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1819 KKQQAEADKAREQAEKELETWRQKANEalrLRLQAEEEANKKtaaqeeaekqkeeakrEAKKRAKAEEAALKQKEAAEME 1898
Cdd:PRK05759 48 ERAKKELELAQAKYEAQLAEARAEAAE---IIEQAKKRAAQI----------------IEEAKAEAEAEAARIKAQAQAE 108
|
90
....*....|....*...
gi 1207141724 1899 LGNQRKMAEETAKQKLAA 1916
Cdd:PRK05759 109 IEQERKRAREELRKQVAD 126
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1699-1934 |
9.35e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 9.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1699 AAQEEAEKLRKQVaEETQKKRKAEEELKRKseaekdAAKEKKKALEDLEKFKLQAEEAERHLKQAELEKQRQIQVVEEVA 1778
Cdd:COG4942 17 AQADAAAEAEAEL-EQLQQEIAELEKELAA------LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1779 KKTAA--TQLESKQVALTARLEESLKNEQ---VMVIQLQEEAEHLKKQQAEADKAREQAEKELETWRQKANEALRLRLQA 1853
Cdd:COG4942 90 KEIAElrAELEAQKEELAELLRALYRLGRqppLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1207141724 1854 EEEANKKtaaqeeaekqkEEAKREAKKRAKAEEAALKQKEAAEMELGNQRKMAEETAKQKLAAEQELIRLRADFEHAEQQ 1933
Cdd:COG4942 170 EAERAEL-----------EALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
.
gi 1207141724 1934 R 1934
Cdd:COG4942 239 A 239
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3549-3587 |
9.78e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 36.54 E-value: 9.78e-03
10 20 30
....*....|....*....|....*....|....*....
gi 1207141724 3549 YLQGSDCIAGVFFQKTKEKLSIYQAMKQKLLTSDTGMSL 3587
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| |
