|
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 ... |
18-127 |
2.76e-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: 243.08 E-value: 2.76e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 18 DRVQKKTFTKWVNKHLIKHWRaeaqrHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQV 97
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARR-----RVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKI 75
|
90 100 110
....*....|....*....|....*....|
gi 2124423190 98 KLVNIRNDDIADGNPKLTLGLIWTIILHFQ 127
Cdd:cd21188 76 KLVNIRAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
140-245 |
6.41e-72 |
|
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: 236.46 E-value: 6.41e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 140 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 219
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 2124423190 220 PEDVDVPQPDEKSIITYVSSLYDAMP 245
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
15-138 |
3.54e-71 |
|
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: 234.92 E-value: 3.54e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 15 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 94
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIK-----AQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 75
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2124423190 95 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 138
Cdd:cd21235 76 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
7-136 |
4.28e-70 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 232.18 E-value: 4.28e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 7 EELIQLVQDERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQ 86
Cdd:cd21236 4 ENVLERYKDERDKVQKKTFTKWINQHLMK-----VRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQ 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2124423190 87 IALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 136
Cdd:cd21236 79 IALDYLKRRQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
141-245 |
6.54e-66 |
|
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: 219.19 E-value: 6.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 220
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 2124423190 221 EDVDVPQPDEKSIITYVSSLYDAMP 245
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
15-137 |
6.65e-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: 205.27 E-value: 6.65e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 15 DERDRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 94
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMK-----VRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQ 75
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2124423190 95 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 137
Cdd:cd21237 76 RQVKLVNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
141-245 |
2.47e-57 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 194.43 E-value: 2.47e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 220
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 2124423190 221 EDVDVPQPDEKSIITYVSSLYDAMP 245
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
139-245 |
1.76e-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: 177.93 E-value: 1.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 139 DMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 218
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 2124423190 219 DPEDVDVPQPDEKSIITYVSSLYDAMP 245
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
20-128 |
1.08e-48 |
|
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: 169.87 E-value: 1.08e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 20 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 99
Cdd:cd21186 2 VQKKTFTKWINSQLSK----ANKPPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKL 77
|
90 100
....*....|....*....|....*....
gi 2124423190 100 VNIRNDDIADGNPKLTLGLIWTIILHFQI 128
Cdd:cd21186 78 VNISSNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
10-124 |
1.79e-46 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 164.08 E-value: 1.79e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 10 IQLVQDERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIA 88
Cdd:cd21246 6 IKALADEREAVQKKTFTKWVNSHLARV-----GCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKA 80
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423190 89 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 124
Cdd:cd21246 81 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
141-241 |
7.28e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 161.81 E-value: 7.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 220
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 2124423190 221 EDVDVPQPDEKSIITYVSSLY 241
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
19-352 |
6.08e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 175.13 E-value: 6.08e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 19 RVQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQ 96
Cdd:COG5069 8 KVQKKTFTKWTNEKLIS----GGQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 97 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTSSWRDGRLF 175
Cdd:COG5069 84 VKLFNIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 176 NAIIHRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD---- 242
Cdd:COG5069 161 SALIHDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidi 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 243 AMPRVPDVQDGVKANElQLRwQEYRELVLLLLQWIRHHTAAFEERKFPSSFEEIEILWCQFLKFKETE--LPAKEAD-KN 319
Cdd:COG5069 241 ALHRVYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHS 318
|
330 340 350
....*....|....*....|....*....|...
gi 2124423190 320 RSKGIYQSLEgAVQAGQLKVPPGYHPLDVEKEW 352
Cdd:COG5069 319 LAGQILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
16-128 |
3.50e-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: 157.15 E-value: 3.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 16 ERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 93
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKR---KPPMKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*
gi 2124423190 94 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 128
Cdd:cd21241 78 SKKIKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
141-241 |
5.01e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 156.40 E-value: 5.01e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 220
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2124423190 221 EDVDVPQPDEKSIITYVSSLY 241
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
16-128 |
7.17e-44 |
|
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: 156.58 E-value: 7.17e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 16 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 93
Cdd:cd21190 1 EQERVQKKTFTNWINSHLAKLSQPIV---INDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 2124423190 94 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 128
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
7-124 |
1.45e-43 |
|
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409042 Cd Length: 116 Bit Score: 155.53 E-value: 1.45e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 7 EELIQLVQDERDRVQKKTFTKWVNKHLIKHwraeaQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNV 85
Cdd:cd21193 3 KGRIRALQEERINIQKKTFTKWINSFLEKA-----NLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENV 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 2124423190 86 QIALDYLrHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 124
Cdd:cd21193 78 NKALAFL-KTKVRLENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
140-245 |
3.73e-41 |
|
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: 148.62 E-value: 3.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 140 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 219
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 2124423190 220 PEDVDVPQPDEKSIITYVSSLYDAMP 245
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
128-243 |
5.70e-41 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 148.28 E-value: 5.70e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 128 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 207
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 208 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 243
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
16-128 |
3.67e-39 |
|
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: 142.66 E-value: 3.67e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 16 ERDRVQKKTFTKWVNKHLIKHWRAEAqrhISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHR 95
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSPPSV---VSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNK 77
|
90 100 110
....*....|....*....|....*....|...
gi 2124423190 96 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 128
Cdd:cd21242 78 SIKLINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
10-124 |
1.36e-38 |
|
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: 142.47 E-value: 1.36e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 10 IQLVQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIA 88
Cdd:cd21318 28 IKALADEREAVQKKTFTKWVNSHL-----ARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKA 102
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423190 89 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 124
Cdd:cd21318 103 LQFLKEQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
137-241 |
1.47e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 141.30 E-value: 1.47e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 137 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 216
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 2124423190 217 LLDPEDVDVPQPDEKSIITYVSSLY 241
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
3-124 |
1.77e-38 |
|
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: 141.73 E-value: 1.77e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 3 RYSMEELIQLVQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHK 81
Cdd:cd21317 14 RLFERSRIKALADEREAVQKKTFTKWVNSHL-----ARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHC 88
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 2124423190 82 LQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 124
Cdd:cd21317 89 LENVDKALQFLKEQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
137-241 |
5.51e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409170 Cd Length: 119 Bit Score: 139.81 E-value: 5.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 137 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 216
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 2124423190 217 LLDPEDVDVPQPDEKSIITYVSSLY 241
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
140-241 |
2.93e-37 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409098 Cd Length: 109 Bit Score: 137.30 E-value: 2.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 140 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 219
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 2124423190 220 PEDVDVPQPDEKSIITYVSSLY 241
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1321-1952 |
9.47e-37 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 153.55 E-value: 9.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLRRMEE-EERLaeqqraeerERLAAVEAalEKQRQLAEAHAQAKaQAEQeAQELQRRMQEevarreeaavdaqqqkRS 1399
Cdd:COG1196 176 EAERKLEAtEENL---------ERLEDILG--ELERQLEPLERQAE-KAER-YRELKEELKE----------------LE 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1400 IQEELQHLRQSsEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1479
Cdd:COG1196 227 AELLLLKLREL-EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1480 RLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEVE 1559
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEE 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1560 LQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1639
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1640 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEE 1716
Cdd:COG1196 464 LLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAA 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1717 ELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAk 1796
Cdd:COG1196 544 LAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTL- 622
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1797 RQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1876
Cdd:COG1196 623 LGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAE 702
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1877 LAQLRKASESELE--RQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQaELEAM 1952
Cdd:COG1196 703 EEEERELAEAEEErlEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLER-EIEAL 779
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
20-126 |
2.28e-36 |
|
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: 134.84 E-value: 2.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 20 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 97
Cdd:cd21215 4 VQKKTFTKWLNTKL-----SSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGV 78
|
90 100
....*....|....*....|....*....
gi 2124423190 98 KLVNIRNDDIADGNPKLTLGLIWTIILHF 126
Cdd:cd21215 79 KLTNIGAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
18-124 |
2.29e-36 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 134.44 E-value: 2.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 18 DRVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQ 96
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRK-----AGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKG 77
|
90 100
....*....|....*....|....*...
gi 2124423190 97 VKLVNIRNDDIADGNPKLTLGLIWTIIL 124
Cdd:cd21214 78 VKLVSIGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
15-128 |
8.34e-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: 133.12 E-value: 8.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 15 DERDRVQKKTFTKWVNKHLIKHWRaeaqRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRH 94
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGK----PPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQK 76
|
90 100 110
....*....|....*....|....*....|....
gi 2124423190 95 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 128
Cdd:cd21231 77 NNVDLVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
144-245 |
8.81e-36 |
|
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409036 Cd Length: 104 Bit Score: 132.94 E-value: 8.81e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 144 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 222
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2124423190 223 VDVPQPDEKSIITYVSSLYDAMP 245
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
125-241 |
4.62e-35 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409171 Cd Length: 130 Bit Score: 132.10 E-value: 4.62e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 125 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 204
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 205 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 241
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1423-2031 |
6.44e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.39 E-value: 6.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1423 EAAERSRLRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVR 1502
Cdd:COG1196 182 EATEENLERLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1503 VKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1582
Cdd:COG1196 261 ELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1583 VAVAQLreeaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAE 1662
Cdd:COG1196 341 ELEEEL-----------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1742
Cdd:COG1196 410 EALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEA 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1743 RAEMEVLLASKARAEEESRSTSEKSK----QRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAervlA 1818
Cdd:COG1196 490 AARLLLLLEAEADYEGFLEGVKAALLlaglRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIE----Y 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1819 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDT 1898
Cdd:COG1196 566 LKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1899 LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 1978
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1979 EEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQA 2031
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1663-2231 |
7.45e-35 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 147.39 E-value: 7.45e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1742
Cdd:COG1196 210 EKAERYRELKEELKELEAELL---LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1743 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERVLAEKLA 1822
Cdd:COG1196 287 QAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEE-ELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1823 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKgLVEDTLRQR 1902
Cdd:COG1196 366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE-EEEEEEEAL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1903 RQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 1982
Cdd:COG1196 445 EEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAG 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1983 ARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRL-----QAEEKAHAFAVQQKEQELQQTLQQEQSM 2057
Cdd:COG1196 525 AVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAgratfLPLDKIRARAALAAALARGAIGAAVDLV 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2058 LERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQA 2137
Cdd:COG1196 605 ASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2138 ALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2217
Cdd:COG1196 685 AERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEE 764
|
570
....*....|....
gi 2124423190 2218 QMEELGKLKARIEA 2231
Cdd:COG1196 765 LERELERLEREIEA 778
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1296-1883 |
4.68e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 144.69 E-value: 4.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1296 QEYVDLRTRYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQ-------LAEAHAQAKAQ 1367
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1368 AEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTE 1447
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1448 RQRGGAEGELQALRARAE------------------EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEA 1509
Cdd:COG1196 373 ELAEAEEELEELAEELLEalraaaelaaqleeleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1510 AREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLR 1589
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1590 EEAERRAQQQAEAERAREEAERELERWQ-----LKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQ 1664
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1665 AVRQRELAEQELEKQRQLAEGTAQQRLAAEQEliRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRA 1744
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAG--RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1745 EMEVLLASKARAEEESRSTSEKSKQRleaeasrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAI 1824
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1825 GEATRLKTEAEIALKEKEAENERlrrlAEDE-AFQRRRLEEQAAQHkADIEERLAQLRKA 1883
Cdd:COG1196 763 EELERELERLEREIEALGPVNLL----AIEEyEELEERYDFLSEQR-EDLEEARETLEEA 817
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1460-2034 |
8.96e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 143.92 E-value: 8.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1460 LRARAEEAEAQKRQAQEEAERL---RRQVqdETQRKRqaeaelavrVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQ 1536
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1537 AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERW 1616
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1617 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1696
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1697 LIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAS 1776
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1777 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA----AIGEATRLKTEAEIALKEKEAENERLRRLA 1852
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1853 EDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGK----AELEL 1928
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRtlvaARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1929 ELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2008
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580
....*....|....*....|....*.
gi 2124423190 2009 RAEQESARQLQLAQDAAQKRLQAEEK 2034
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEE 740
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
141-241 |
1.55e-32 |
|
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: 123.67 E-value: 1.55e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 220
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 2124423190 221 EDVDVPQPDEKSIITYVSSLY 241
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1327-2033 |
1.68e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 140.66 E-value: 1.68e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1327 EEEERLAEQQRAEERERlaaVEAALEKQRQLAEAHAQAKAQAEQEAQELqRRMQEevARREEAAVDAQQQKRSiqEELQH 1406
Cdd:PTZ00121 1094 EEAFGKAEEAKKTETGK---AEEARKAEEAKKKAEDARKAEEARKAEDA-RKAEE--ARKAEDAKRVEIARKA--EDARK 1165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1407 LRQSSEAEiqaKARQVEAAERSrlrieEEIRVVRlQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1486
Cdd:PTZ00121 1166 AEEARKAE---DAKKAEAARKA-----EEVRKAE-ELRKAEDAR-----KAEAARKAEEERKAEEARKAEDAKKAEAVKK 1231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1487 DETQRKRQAEAELAVRVKaEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVA--LETAQRSAEVELQSKR 1564
Cdd:PTZ00121 1232 AEEAKKDAEEAKKAEEER-NNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAdeAKKAEEKKKADEAKKK 1310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1565 ASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1644
Cdd:PTZ00121 1311 AEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEK 1390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1645 EKQKEEAEREARRRGKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1724
Cdd:PTZ00121 1391 KKADEAKKKAEEDKKKADE--LKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEE 1468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1725 AAAATQKRQELE----AELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEASRFRELAEEAARLRAlAEEAKRQRQ 1800
Cdd:PTZ00121 1469 AKKADEAKKKAEeakkADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAKKADE 1538
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1801 LAEEDAARQRAEAERvlAEKLAAIGEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 1880
Cdd:PTZ00121 1539 AKKAEEKKKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEA 1612
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1881 RKASESELERQKGLVEDTLRQRrqveEEILALKVSFEKAAAGKAELELELGRIRS-----NAEDTLRSKEQA--ELEAMR 1953
Cdd:PTZ00121 1613 KKAEEAKIKAEELKKAEEEKKK----VEQLKKKEAEEKKKAEELKKAEEENKIKAaeeakKAEEDKKKAEEAkkAEEDEK 1688
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1954 QRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEE----VERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRL 2029
Cdd:PTZ00121 1689 KAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEEnkikAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEK 1768
|
....
gi 2124423190 2030 QAEE 2033
Cdd:PTZ00121 1769 KAEE 1772
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
140-238 |
1.80e-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: 123.69 E-value: 1.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 140 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 219
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 2124423190 220 PEDVDVPQPDEKSIITYVS 238
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
20-128 |
9.46e-32 |
|
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the first CH domain.
Pssm-ID: 409081 Cd Length: 107 Bit Score: 121.65 E-value: 9.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 20 VQKKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 99
Cdd:cd21232 2 VQKKTFTKWINARFSK----SGKPPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVEL 77
|
90 100
....*....|....*....|....*....
gi 2124423190 100 VNIRNDDIADGNPKLTLGLIWTIILHFQI 128
Cdd:cd21232 78 VNIGGTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
19-129 |
2.01e-31 |
|
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: 121.40 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 19 RVQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ 96
Cdd:cd21311 14 RIQQNTFTRWANEHLKT-----ANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDE 88
|
90 100 110
....*....|....*....|....*....|....
gi 2124423190 97 -VKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 129
Cdd:cd21311 89 gIKIVNIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
20-128 |
2.18e-31 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 120.47 E-value: 2.18e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 20 VQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQV 97
Cdd:cd21227 4 IQKNTFTNWVNEQL-----KPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGI 78
|
90 100 110
....*....|....*....|....*....|.
gi 2124423190 98 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 128
Cdd:cd21227 79 KLVNIGNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
128-243 |
2.73e-31 |
|
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: 120.71 E-value: 2.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 128 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 207
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 208 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 243
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
144-245 |
4.56e-31 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 119.29 E-value: 4.56e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 144 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 222
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 2124423190 223 VDVPQPDEKSIITYVSSLYDAMP 245
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
876-953 |
4.73e-31 |
|
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links desmosomal cadherins to the intermediate filaments. The N-terminal region of DP contains a plakin domain common to members of the plakin family. Plakin domains contain multiple copies of spectrin repeats (SRs) pfam00435. Spectrin repeats (SRs) consist of three alpha-helices (A, B, and C) that form an antiparallel triple-helical bundle. This entry describes SR6 which has a divergent structure relative to the other SRs. SR6 shows significant deviations in helices A and B where they are significantly shorter than in other repeats. Structural comparison revealed that SR6 is more similar to other three-helix-bundle proteins, including target of Myb1 and the syntaxin Habc domain, than to other SR proteins. Due to these differences with other spectrin repeats, this region is termed spectrin-like repeat.
Pssm-ID: 465730 Cd Length: 78 Bit Score: 118.47 E-value: 4.73e-31
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 876 LAWQSLSRDVQLIRSWSLVTFRTMKPEEQRQALRSLELHYQAFLRDSQDAGGFGPEDRLQAEREYGSCSHHYQQLLQS 953
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
10-124 |
9.96e-31 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 120.53 E-value: 9.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 10 IQLVQDERDRVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIA 88
Cdd:cd21316 43 IKALADEREAVQKKTFTKWVNSHL-----ARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKA 117
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423190 89 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 124
Cdd:cd21316 118 LQFLKEQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
144-246 |
1.31e-30 |
|
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. It is involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Mutations in dystrophin lead to Duchenne muscular dystrophy (DMD). Moreover, dystrophin deficiency is associated with abnormal cerebral diffusion and perfusion, as well as in acute Trypanosoma cruzi infection. The dystrophin subfamily has been characterized by a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, dystrophin contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, approximately 24 spectrin repeats (SRs) and a WW domain. The model corresponds to the second CH domain.
Pssm-ID: 409082 Cd Length: 111 Bit Score: 118.49 E-value: 1.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 144 EKLLL-WSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 221
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 2124423190 222 DVDVPQPDEKSIITYVSSLYDAMPR 246
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
140-238 |
1.61e-30 |
|
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and similar proteins; SYNE-2, also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409093 Cd Length: 109 Bit Score: 118.01 E-value: 1.61e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 140 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 219
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 2124423190 220 PEDVDVPQPDEKSIITYVS 238
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
146-241 |
3.37e-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: 117.06 E-value: 3.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 146 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 224
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 2124423190 225 VPQPDEKSIITYVSSLY 241
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
16-130 |
4.47e-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: 116.91 E-value: 4.47e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 16 ERDRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLR 93
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEK---CNPPLEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLE 77
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 94 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 130
Cdd:cd21191 78 DSNVKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1765-2448 |
1.87e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 129.67 E-value: 1.87e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1765 EKSKQRLEAEAsrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLaaigEATRLKTEAEIALKEKEAE 1844
Cdd:COG1196 199 ERQLEPLERQA----EKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEEL----EAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1845 NERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKglvEDTLRQRRQVEEEILALKVSFEKAAAGKA 1924
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL---EELEEELAELEEELEELEEELEELEEELE 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1925 ELELELgrirSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEAR 2004
Cdd:COG1196 348 EAEEEL----EEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEEL 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2005 RLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLqqeqsmlERLRGEAEAARRAAEEAEEARERAER 2084
Cdd:COG1196 424 EELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE-------EAALLEAALAELLEELAEAAARLLLL 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2085 EAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAemekhkkfAEQTLRQKA 2164
Cdd:COG1196 497 LEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVA--------AAAIEYLKA 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2165 QVEQELTTLRLqleETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNT 2244
Cdd:COG1196 569 AKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGR 645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2245 QRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2324
Cdd:COG1196 646 LREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEA 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2325 ARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQL----EMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIgeklh 2400
Cdd:COG1196 726 LEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL----- 800
|
650 660 670 680
....*....|....*....|....*....|....*....|....*...
gi 2124423190 2401 rtelaTQEKVTLVQTLeiqrqqsdhdaERLRQAIAELEREKEKLKQEA 2448
Cdd:COG1196 801 -----SEQREDLEEAR-----------ETLEEAIEEIDRETRERFLET 832
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1206-1925 |
2.08e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 130.65 E-value: 2.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1206 QDAKRRQEQIQAmvlADSRAVREQLRQEKALLEEIERHGEKVEECQRfAKQYINAIKDYELQlvtyKAQLEPVASPAKKP 1285
Cdd:PTZ00121 1137 EDARKAEEARKA---EDAKRVEIARKAEDARKAEEARKAEDAKKAEA-ARKAEEVRKAEELR----KAEDARKAEAARKA 1208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1286 KVQSGSESViQEYVDLRTryselttltsqyikfiSETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAK 1365
Cdd:PTZ00121 1209 EEERKAEEA-RKAEDAKK----------------AEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAA 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1366 AQAEQ--EAQELQR----------RMQEEVARREEAAVDAQQQKRSIQ-----EELQHLRQSSEAEIQAKARQVEAAERS 1428
Cdd:PTZ00121 1272 IKAEEarKADELKKaeekkkadeaKKAEEKKKADEAKKKAEEAKKADEakkkaEEAKKKADAAKKKAEEAKKAAEAAKAE 1351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1429 RLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE----------AEAQKRQAQEEAERLRRQVQDETQRKRQAEAE 1498
Cdd:PTZ00121 1352 AEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkkadeakkkAEEDKKKADELKKAAAAKKKADEAKKKAEEKK 1431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1499 LAVRVKAEAEAAREKQRALQALEEFRlQAEEAERRlrqaeAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTL 1578
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKKAEEAK-KAEEAKKK-----AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1579 QEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlQAEEVAQQKSLAQAEAEKqkeeaerearrr 1658
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELK---KAEELKKAEEKKKAEEAK------------ 1570
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1659 gKAEEqavrQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1738
Cdd:PTZ00121 1571 -KAEE----DKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEE 1645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1739 LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRAlAEEAKRQRQLaeedaaRQRAEAERVLA 1818
Cdd:PTZ00121 1646 KKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKE-AEEAKKAEEL------KKKEAEEKKKA 1718
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1819 EKLAAIGEATRLKteAEIALKEKEAENERLRRLAEDEAFQRRrleeqAAQHKADIEERLAQLRKASESELErqKGLVEDT 1898
Cdd:PTZ00121 1719 EELKKAEEENKIK--AEEAKKEAEEDKKKAEEAKKDEEEKKK-----IAHLKKEEEKKAEEIRKEKEAVIE--EELDEED 1789
|
730 740
....*....|....*....|....*..
gi 2124423190 1899 LRQRRQVEEEILALKVSFEKAAAGKAE 1925
Cdd:PTZ00121 1790 EKRRMEVDKKIKDIFDNFANIIEGGKE 1816
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
126-243 |
4.81e-29 |
|
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also called non-muscle alpha-actinin 4, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. It is associated with cell motility and cancer invasion. ACTN4 is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409139 Cd Length: 125 Bit Score: 114.41 E-value: 4.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 126 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 205
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 2124423190 206 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 243
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHA 116
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
19-126 |
1.59e-28 |
|
first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409032 Cd Length: 108 Bit Score: 112.19 E-value: 1.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 19 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 95
Cdd:cd21183 3 RIQANTFTRWCNEHL-----KERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEAD 77
|
90 100 110
....*....|....*....|....*....|.
gi 2124423190 96 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 126
Cdd:cd21183 78 HIKLVNIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
144-243 |
2.42e-28 |
|
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of the molecule interacting with CasL protein (MICAL) and EH domain-binding protein (EHBP) families. MICAL is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP proteins contain a single CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409188 Cd Length: 105 Bit Score: 111.61 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 144 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 222
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 2124423190 223 VDVPQPDEKSIITYVSSLYDA 243
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
128-243 |
2.09e-27 |
|
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: 109.79 E-value: 2.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 128 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 207
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 208 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 243
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHA 113
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1467-2455 |
3.67e-27 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 122.63 E-value: 3.67e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1467 AEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAE--AEAAREKQRALQALEEFRLQAE-EAERRLRQAEAERAR 1543
Cdd:NF041483 81 AQIQADQLRADAERELRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVAWAEQLRAR 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1544 QVQVA---LETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvavaqlreeaerraqqqaeAERAREEAERELERWQLKA 1620
Cdd:NF041483 161 TESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE--------------------AESARAEAEAILRRARKDA 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1621 NEALR-LRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQrlAAEQELIR 1699
Cdd:NF041483 221 ERLLNaASTQAQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQE---AEEALREARAEAEKVVAE--AKEAAAKQ 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1700 LRAETEQGEQQRQLLEEELARLQHEAAA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSKQRLEAEA 1775
Cdd:NF041483 296 LASAESANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAKAARTAEE 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1776 SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVlAEKLAAIG----------------EATRLKTEAEIALK 1839
Cdd:NF041483 376 VLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQ-AEQLKGAAkddtkeyraktvelqeEARRLRGEAEQLRA 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1840 EKEAENERLRRLAEDEAFQR-----RRLEEQAAQHKADIE------------------ERLAQLRKASESELERQKGLVE 1896
Cdd:NF041483 455 EAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADelrstataeservrteaiERATTLRRQAEETLERTRAEAE 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1897 dtlRQRRQVEEEILALKVSFEKAA------------AGKAELELELGRIRSNAEDTLRSKEQAELEamrqrqlaaeeeqr 1964
Cdd:NF041483 535 ---RLRAEAEEQAEEVRAAAERAArelreeteraiaARQAEAAEELTRLHTEAEERLTAAEEALAD-------------- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1965 rreaeervqkslaAEEEAARQRKAALEEVERLKAKV-EEARRLRERAEQESAR-QLQLAQDAAQKRLQAEEKAhafavqq 2042
Cdd:NF041483 598 -------------ARAEAERIRREAAEETERLRTEAaERIRTLQAQAEQEAERlRTEAAADASAARAEGENVA------- 657
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2043 keqelqqtlqqeqsmlERLRGEAEaarraaeeaeeareraereaaqsrrqvEEAERLKQSAEEQAQAQAQAQAAAEKlrK 2122
Cdd:NF041483 658 ----------------VRLRSEAA---------------------------AEAERLKSEAQESADRVRAEAAAAAE--R 692
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2123 EAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTL-RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEA 2201
Cdd:NF041483 693 VGTEAAEALAAAQEEAARRRREAEETLGSARAEADQEReRAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSA 772
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2202 ARQRS------------QVEEELFSLRVQMEELGKlKARIEAENRALILR------------DKDNTQRVLQEEAEKMKH 2257
Cdd:NF041483 773 AEQTAqqvrdsvaglqeQAEEEIAGLRSAAEHAAE-RTRTEAQEEADRVRsdayaereraseDANRLRREAQEETEAAKA 851
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2258 VAEEAarLSVAAQEAARLRELAEEDLAQQRALAEKMLKekmQAVQEATRLKAEA---------ELLQQQKEL---AQEQA 2325
Cdd:NF041483 852 LAERT--VSEAIAEAERLRSDASEYAQRVRTEASDTLA---SAEQDAARTRADAredanrirsDAAAQADRLigeATSEA 926
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2326 RRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLE-----MSAEAERLKLRVAE-MSRAQARAE---EDAQRFRKQAEEIG 2396
Cdd:NF041483 927 ERLTAEARAEAERLRDEARAEAERVRADAAAQAEqliaeATGEAERLRAEAAEtVGSAQQHAErirTEAERVKAEAAAEA 1006
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 2397 EKLhRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKS 2455
Cdd:NF041483 1007 ERL-RTEAREEADRTLDEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEALRT 1064
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1660-2447 |
1.04e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 121.40 E-value: 1.04e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaETEQGEQQRQllEEELARLQHEAAAATQKRQELEAEL 1739
Cdd:PTZ00121 1084 KEDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKAE-DARKAEEARK--AEDARKAEEARKAEDAKRVEIARKA 1160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1740 AKVRAEMEVLLASKARAEEESRSTSEKSKqrleaeASRFRElAEEAARlralAEEAKRQRQLAEEDAARQRAEAERvlAE 1819
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRK------AEELRK-AEDARK----AEAARKAEEERKAEEARKAEDAKK--AE 1227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1820 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQ-HKADIEERLAQLRKASESELERQKglvedt 1898
Cdd:PTZ00121 1228 AVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEaRKADELKKAEEKKKADEAKKAEEK------ 1301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1899 lrqrRQVEEeilalkvsfekaAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 1978
Cdd:PTZ00121 1302 ----KKADE------------AKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEK 1365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1979 EEEAARQRKAALEEVERLKAKVEEARR---LRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQ 2055
Cdd:PTZ00121 1366 AEAAEKKKEEAKKKADAAKKKAEEKKKadeAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKK 1445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2056 SmlerlrgeaeaARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaQAQAQAAAEKLRKEAEQEAARRAQAE 2135
Cdd:PTZ00121 1446 A-----------DEAKKKAEEAKKAEEAKKKAEEAKKADEAKK-----------KAEEAKKADEAKKKAEEAKKKADEAK 1503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2136 QAALRQKQAADAEMEKHKKFAEQTlrQKAQVEQELTTLRLQLEETDHQKSILDEELQrlKAEVTEAARQRSQVEEELFSL 2215
Cdd:PTZ00121 1504 KAAEAKKKADEAKKAEEAKKADEA--KKAEEAKKADEAKKAEEKKKADELKKAEELK--KAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2216 RVQMEELGKL-KARIEAENRALILRDKDNTQRVLQEEAEKMKhvAEEAARlsvaAQEAARLRELAEEDLAQQRALAEKML 2294
Cdd:PTZ00121 1580 LRKAEEAKKAeEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK--AEELKK----AEEEKKKVEQLKKKEAEEKKKAEELK 1653
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2295 KEKMQAVQEATRLKAEAEllqQQKELAQEqARRLQEDKEQMAQQLEQETQgfqrtlEAERQRQLEMSAEAERLKlrVAEM 2374
Cdd:PTZ00121 1654 KAEEENKIKAAEEAKKAE---EDKKKAEE-AKKAEEDEKKAAEALKKEAE------EAKKAEELKKKEAEEKKK--AEEL 1721
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 2375 SRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAE-LEREKEKLKQE 2447
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEeLDEEDEKRRME 1795
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
128-243 |
1.45e-26 |
|
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: 107.50 E-value: 1.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 128 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 207
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 208 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 243
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1224-2013 |
3.03e-26 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 119.78 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1224 RAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDY-ELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLR 1302
Cdd:TIGR02168 182 ERTRENLDRLEDILNELERQLKSLERQAEKAERYKELKAELrELELALLVLRLE--ELREELEELQEELKEAEEELEELT 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1303 TRYSELTTLTSQYIKFISETlrrmeeEERLAEQQraEERERLAAVEAALEKQRQLaeaHAQAKAQAEQEAQELQRRMQEE 1382
Cdd:TIGR02168 260 AELQELEEKLEELRLEVSEL------EEEIEELQ--KELYALANEISRLEQQKQI---LRERLANLERQLEELEAQLEEL 328
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1383 VARREEAAVDAQQQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRA 1462
Cdd:TIGR02168 329 ESKLDELAEELAELEEKL-EELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEA 407
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1463 RAEEAEAQKRQAQEEAERLRRQVQDetQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAE-- 1540
Cdd:TIGR02168 408 RLERLEDRRERLQQEIEELLKKLEE--AELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAEREla 485
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1541 RARQVQVALETAQRSAEVELQSKRASFAEKtaqleRTLQEEHVAVAQLREEAerraqqqaeaerareeaerelERWQLKA 1620
Cdd:TIGR02168 486 QLQARLDSLERLQENLEGFSEGVKALLKNQ-----SGLSGILGVLSELISVD---------------------EGYEAAI 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1621 NEALRLRLQA----------EEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELA------------------ 1672
Cdd:TIGR02168 540 EAALGGRLQAvvvenlnaakKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLgvakdlvkfdpklrkals 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1673 ------------EQELEKQRQL-----------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1717
Cdd:TIGR02168 620 yllggvlvvddlDNALELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIAELEKA 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1718 LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEASRfRELAEEAARLRALAE 1793
Cdd:TIGR02168 700 LAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELTELEAEI-EELEERLEEAEEELA 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1794 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAeialKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 1873
Cdd:TIGR02168 779 EAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEELSEDI 854
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1874 EERLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDtLRSK------EQA 1947
Cdd:TIGR02168 855 ESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE-LREKlaqlelRLE 932
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1948 ELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRkaalEEVERLKAKVEEARRLRERAEQE 2013
Cdd:TIGR02168 933 GLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR----RRLKRLENKIKELGPVNLAAIEE 994
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
1-128 |
3.79e-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: 106.38 E-value: 3.79e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1 MDRYSMEELIQLVQDERDRVQKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRF 79
Cdd:cd21247 1 MDTEYEKGHIRKLQEQRMTMQKKTFTKWMNNVFSKN---GAKIEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRV 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2124423190 80 HKLQNVQIALDYLRHR-QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 128
Cdd:cd21247 78 HFLENNSKAITFLKTKvPVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1330-2449 |
1.65e-25 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 117.23 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1330 ERLAEQQRAEERERLAavEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ 1409
Cdd:NF041483 93 ERELRDARAQTQRILQ--EHAEHQARLQAELHTEAVQRRQQLDQELAERRQTVESHVNENVAWAEQLRARTESQARRLLD 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1410 SSEAEiqakARQVEAAERSRL-RIEEEirvvrlqlettERQRGGAEGElqalRARAeEAEAQKRQAQEEAERLRRQVQDE 1488
Cdd:NF041483 171 ESRAE----AEQALAAARAEAeRLAEE-----------ARQRLGSEAE----SARA-EAEAILRRARKDAERLLNAASTQ 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1489 TQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQaeEAERRLRQAEAERARQVQVALETAqrsaevelqSKRASFA 1568
Cdd:NF041483 231 AQEATDHAEQLRSSTAAESDQARRQAAELSRAAEQRMQ--EAEEALREARAEAEKVVAEAKEAA---------AKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1569 EKT-AQLERTLQEEhvaVAQL-REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEK 1646
Cdd:NF041483 300 ESAnEQRTRTAKEE---IARLvGEATKEAEALKAEAEQALADARAEAEKLVAEAAEKARTVAAEDTAAQLAKAARTAEEV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1647 QKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQ-RLAAEQELIRLRAETEQgeqqrqlLEEELARLQHEa 1725
Cdd:NF041483 377 LTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQlKGAAKDDTKEYRAKTVE-------LQEEARRLRGE- 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1726 aaATQKRQELEAELAKVRAEM----------------EVLLASKARAEE-ESRSTSEKSKQRLEA--EASRFRELAE--- 1783
Cdd:NF041483 449 --AEQLRAEAVAEGERIRGEArreavqqieeaartaeELLTKAKADADElRSTATAESERVRTEAieRATTLRRQAEetl 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1784 -----EAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLAEKLA-AIGEATRLKTEAE-------IALKEKEAENERLR 1849
Cdd:NF041483 527 ertraEAERLRAEAEEqAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTEAEerltaaeEALADARAEAERIR 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1850 RLAEDEAfqrRRLEEQAAqhkadieERLAQLRKASESELERQKGLVEDTLRQRRqVEEEILALKVSFEKAAagkaelelE 1929
Cdd:NF041483 607 REAAEET---ERLRTEAA-------ERIRTLQAQAEQEAERLRTEAAADASAAR-AEGENVAVRLRSEAAA--------E 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1930 LGRIRSNAEDTlRSKEQAELEAMRQRqlaaeeeqrrrEAEERVQKSLAAEEEAARQRKaalEEVERLKAKVEEARRLRER 2009
Cdd:NF041483 668 AERLKSEAQES-ADRVRAEAAAAAER-----------VGTEAAEALAAAQEEAARRRR---EAEETLGSARAEADQERER 732
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2010 AEQESARQLQlaqdAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQS 2089
Cdd:NF041483 733 AREQSEELLA----SARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQQVRDSVAGLQEQAEEEIAGLRSAAEHAAER 808
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2090 RRQ--VEEAERLKQSAEEQAQAQAQAQAaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAEQTLRQkAQVE 2167
Cdd:NF041483 809 TRTeaQEEADRVRSDAYAERERASEDAN------------------------RLRREAQEETEAAKALAERTVSE-AIAE 863
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2168 QElttlRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQ------------MEELGKLKARIEAENRA 2235
Cdd:NF041483 864 AE----RLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDaaaqadrligeaTSEAERLTAEARAEAER 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2236 LILRDKDNTQRVLQEEAEKMKHV------------AEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEkmqAVQE 2303
Cdd:NF041483 940 LRDEARAEAERVRADAAAQAEQLiaeatgeaerlrAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTE---AREE 1016
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2304 ATRLKAEA-ELLQQQKELAQEQARRLQEDKEQMAQQL--EQETQGFQRTLEAERQRQLEMSA---EAERLKLR------- 2370
Cdd:NF041483 1017 ADRTLDEArKDANKRRSEAAEQADTLITEAAAEADQLtaKAQEEALRTTTEAEAQADTMVGAarkEAERIVAEatvegns 1096
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2371 VAEMSRAQAR-----AEEDAQRFRKQAEEIG-------EKLH---RTELATQEKVT------LVQTLEIQRQQSDHDAER 2429
Cdd:NF041483 1097 LVEKARTDADellvgARRDATAIRERAEELRdritgeiEELHeraRRESAEQMKSAgercdaLVKAAEEQLAEAEAKAKE 1176
|
1210 1220 1230 1240
....*....|....*....|....*....|....*....|....*.
gi 2124423190 2430 LR--------------------------QAIAELEREKEKLKQEAK 2449
Cdd:NF041483 1177 LVsdanseaskvriaavkkaegllkeaeQKKAELVREAEKIKAEAE 1222
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
146-241 |
1.90e-25 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 103.39 E-value: 1.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 146 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 224
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 2124423190 225 VPQPDEKSIITYVSSLY 241
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
19-126 |
2.85e-25 |
|
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: 102.95 E-value: 2.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 19 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 95
Cdd:cd21228 3 KIQQNTFTRWCNEHL-----KCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERE 77
|
90 100 110
....*....|....*....|....*....|.
gi 2124423190 96 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 126
Cdd:cd21228 78 SIKLVSIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
128-243 |
3.79e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 103.23 E-value: 3.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 128 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 207
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 208 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 243
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1387-2211 |
4.21e-25 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 116.39 E-value: 4.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1387 EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE 1466
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1467 aEAQKRQAQEEAERLR-----RQVQD--ETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAE- 1538
Cdd:PTZ00121 1114 -ARKAEEAKKKAEDARkaeeaRKAEDarKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAEEVRKAEe 1192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1539 ---AERARQVQVAletaqRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELER 1615
Cdd:PTZ00121 1193 lrkAEDARKAEAA-----RKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFAR 1267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1616 WQ--LKANEALRlrlqAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQavRQRELAEQELEKQRQLAEGtaqqrlaa 1693
Cdd:PTZ00121 1268 RQaaIKAEEARK----ADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEA--KKADEAKKKAEEAKKKADA-------- 1333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1694 eqelIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEmevllASKARAEEESRStsEKSKQRLEA 1773
Cdd:PTZ00121 1334 ----AKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD-----AAKKKAEEKKKA--DEAKKKAEE 1402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1774 EASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERvlaeklaaigEATRLKTEAEIALKEKEAENERLRRLAE 1853
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAK----------KADEAKKKAEEAKKAEEAKKKAEEAKKA 1472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1854 DEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEeilaLKVSFEKAAAGKAElelelgri 1933
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADE----AKKAEEAKKADEAK-------- 1540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1934 rsNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEeaarqrkaaLEEVErlKAKVEEARRLRERAEQE 2013
Cdd:PTZ00121 1541 --KAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE---------AKKAE--EARIEEVMKLYEEEKKM 1607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2014 SARQLQLAQDAaqkRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQv 2093
Cdd:PTZ00121 1608 KAEEAKKAEEA---KIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA- 1683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2094 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTlrqKAQVEQELTTL 2173
Cdd:PTZ00121 1684 EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEA---KKDEEEKKKIA 1760
|
810 820 830
....*....|....*....|....*....|....*...
gi 2124423190 2174 RLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2211
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDK 1798
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1083-1883 |
7.25e-25 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 115.15 E-value: 7.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1083 AEEVLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRER 1162
Cdd:TIGR02168 251 AEEELEELTAELQELEE------KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQ 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1163 VAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIER 1242
Cdd:TIGR02168 325 LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIER 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1243 hgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISET 1322
Cdd:TIGR02168 405 -----------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1323 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE-EVARREEAAVDAQQQKR--- 1398
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAALGGRlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1399 -------SIQEELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAE 1465
Cdd:TIGR02168 550 vvvenlnAAKKAIAFLKQNELgrvtflPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1466 EAEAQKRQAQEEAERLRRQVQDETQRKRQAeaeLAVRVKAEAEAAREKQRalQALEEFRLQAEEAERRLRQAEAE--RAR 1543
Cdd:TIGR02168 630 DLDNALELAKKLRPGYRIVTLDGDLVRPGG---VITGGSAKTNSSILERR--REIEELEEKIEELEEKIAELEKAlaELR 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1544 QVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehvaVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1623
Cdd:TIGR02168 705 KELEELEEELEQLRKELEELSRQISALRKDLARLEAE----VEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEA 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1624 LRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAE 1703
Cdd:TIGR02168 781 EAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAE 860
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1704 TEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEAEASRFRE 1780
Cdd:TIGR02168 861 IEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELEskRSELRRElEELREKLAQLELRLEGLEVRIDN 940
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1781 LAEE-AARLRALAEEAKRQRQLAEEDAARQRAEAERvLAEKLAAIGEATRLkteaeiALKEKEAENERLRRLaedeafqr 1859
Cdd:TIGR02168 941 LQERlSEEYSLTLEEAEALENKIEDDEEEARRRLKR-LENKIKELGPVNLA------AIEEYEELKERYDFL-------- 1005
|
810 820
....*....|....*....|....
gi 2124423190 1860 rrleeqaAQHKADIEERLAQLRKA 1883
Cdd:TIGR02168 1006 -------TAQKEDLTEAKETLEEA 1022
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1320-2460 |
8.61e-25 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 114.92 E-value: 8.61e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1320 SETLRRMEEEE--RLAEQQRAEERERLAAVEAalEKQRQLAEAHAQAKAQAEQ---EAQELQRRMQEEVARREEAAVDAQ 1394
Cdd:NF041483 154 AEQLRARTESQarRLLDESRAEAEQALAAARA--EAERLAEEARQRLGSEAESaraEAEAILRRARKDAERLLNAASTQA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1395 QQKRSIQEELqhlRQSSEAEIQAKARQveAAERSRlrieeeirvvrlqleTTERQRGGAEGELQALRARAEEAEAQKRQA 1474
Cdd:NF041483 232 QEATDHAEQL---RSSTAAESDQARRQ--AAELSR---------------AAEQRMQEAEEALREARAEAEKVVAEAKEA 291
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1475 QeeAERLRRQVQDETQRKRQAEAELAVRV-KAEAEAAREKQRALQALEEFRLQAE----EAERRLRQAEAER-ARQVQVA 1548
Cdd:NF041483 292 A--AKQLASAESANEQRTRTAKEEIARLVgEATKEAEALKAEAEQALADARAEAEklvaEAAEKARTVAAEDtAAQLAKA 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1549 LETAQR-----SAEVELQSKRAS------FAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL--ER 1615
Cdd:NF041483 370 ARTAEEvltkaSEDAKATTRAAAeeaeriRREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRAKTVELQEEARRLrgEA 449
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1616 WQLKAN---EALRLRLQAEEVAQQKslaqaeaekQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA-EGTAQQRL 1691
Cdd:NF041483 450 EQLRAEavaEGERIRGEARREAVQQ---------IEEAARTAEELLTKAKADADELRSTATAESERVRTEAiERATTLRR 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1692 AAEQELIRLRAE--------TEQGEQQRQLLEEELARLQHEAAAATQKRQ-ELEAELAKVRAEMEVLLASKARAEEESRS 1762
Cdd:NF041483 521 QAEETLERTRAEaerlraeaEEQAEEVRAAAERAARELREETERAIAARQaEAAEELTRLHTEAEERLTAAEEALADARA 600
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1763 TSEKSKQRLEAEASRFRelAEEAARLRAL----AEEAKRQRQLAEEDAARQRAEAERVlaeklaaigeATRLKTEAeial 1838
Cdd:NF041483 601 EAERIRREAAEETERLR--TEAAERIRTLqaqaEQEAERLRTEAAADASAARAEGENV----------AVRLRSEA---- 664
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1839 kekEAENERLRRLAEDEAfQRRRLEEQAAQhkadieERLAQlrKASESELERQkglvEDTLRQRRQVEEEIlalkvsfek 1918
Cdd:NF041483 665 ---AAEAERLKSEAQESA-DRVRAEAAAAA------ERVGT--EAAEALAAAQ----EEAARRRREAEETL--------- 719
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1919 aAAGKAELELELGRIRSNAEDTLRSK----EQAELEAMR----QRQLAAEEEQRRREAEERVQKSLA-----AEEEAARQ 1985
Cdd:NF041483 720 -GSARAEADQERERAREQSEELLASArkrvEEAQAEAQRlveeADRRATELVSAAEQTAQQVRDSVAglqeqAEEEIAGL 798
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1986 RKAALEEVERLKAKV-EEARRLRERAEQESARQlqlAQDAAQKRLQAEEKAHAfavqqkeqelqqtlqqEQSMLERLRGE 2064
Cdd:NF041483 799 RSAAEHAAERTRTEAqEEADRVRSDAYAERERA---SEDANRLRREAQEETEA----------------AKALAERTVSE 859
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2065 AeaarraaeeaeeareraereaaqsrrqVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQA 2144
Cdd:NF041483 860 A---------------------------IAEAERLRSDASEYAQRVRTEASDTLASAEQDAARTRADAREDANRIRSDAA 912
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2145 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT-EAARQRSQVEEELFSLRVQMEELG 2223
Cdd:NF041483 913 AQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATgEAERLRAEAAETVGSAQQHAERIR 992
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2224 KLKARIEAENRAlilrDKDNTQRVLQEEAEKMKHVAEEAA--RLSVAAQEAARLRELAEEDL------AQQRALAEKMLK 2295
Cdd:NF041483 993 TEAERVKAEAAA----EAERLRTEAREEADRTLDEARKDAnkRRSEAAEQADTLITEAAAEAdqltakAQEEALRTTTEA 1068
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2296 EKMQ------AVQEATRLKAEA-----ELLQQQKELAQE---QARR----LQEDKEQMAQQLEQETQGFQRtlEAERQRQ 2357
Cdd:NF041483 1069 EAQAdtmvgaARKEAERIVAEAtvegnSLVEKARTDADEllvGARRdataIRERAEELRDRITGEIEELHE--RARRESA 1146
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2358 LEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTelATQEKVTLVQTLEIQRQQSDHDAERLR-QAIAE 2436
Cdd:NF041483 1147 EQMKSAGERCDALVKAAEEQLAEAEAKAKELVSDANSEASKVRIA--AVKKAEGLLKEAEQKKAELVREAEKIKaEAEAE 1224
|
1210 1220
....*....|....*....|....
gi 2124423190 2437 LEREKEKLKQEAKLLQLKSEEMQT 2460
Cdd:NF041483 1225 AKRTVEEGKRELDVLVRRREDINA 1248
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
140-246 |
9.02e-25 |
|
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: 101.59 E-value: 9.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 140 MTAKEKLLLWSQRMVEGY-QGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 216
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 2124423190 217 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 246
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1659-2355 |
1.56e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 114.47 E-value: 1.56e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1659 GKAEEqaVRQRELAEQELEKQRQLAEGTAQQRLAAEQ----ELIRLRAETEQGEQQRQLleeELARLQHEAAAATQKRQE 1734
Cdd:PTZ00121 1098 GKAEE--AKKTETGKAEEARKAEEAKKKAEDARKAEEarkaEDARKAEEARKAEDAKRV---EIARKAEDARKAEEARKA 1172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1735 LEAELAK-VRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRElAEEAARLRAL--AEEAKRQRQLAEEDAARQRA 1811
Cdd:PTZ00121 1173 EDAKKAEaARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARK-AEDAKKAEAVkkAEEAKKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1812 EAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAED--EAFQRRRLEEqaAQHKADIEERLAQLRKASESELE 1889
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEakKAEEKKKADE--AKKKAEEAKKADEAKKKAEEAKK 1329
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1890 RQKGLvedtlrqRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAE-----LEAMRQRQLAAEEEQR 1964
Cdd:PTZ00121 1330 KADAA-------KKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADaakkkAEEKKKADEAKKKAEE 1402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1965 RREAEERVQKSLAAEEEAARQRKAALE--EVERLKAKVEEARRLRE-RAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQ 2041
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEkkKADEAKKKAEEAKKADEaKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2042 QKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQS--RRQVEEAERLKQSAEEQAQAQAQAQAAAEK 2119
Cdd:PTZ00121 1483 KKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAeeAKKADEAKKAEEKKKADELKKAEELKKAEE 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2120 LRKEAEQEAARRAQAEQAALRQ--KQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSIlDEELQRLKAE 2197
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEE-KKKVEQLKKK 1641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2198 VTEAARQRSQVEEELFSLRVQMEELGKL--KARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARL 2275
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKKaeEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2276 RELAEEDLAQQRALAEKMLKEKMQAvQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQlEQETQGFQRTLEAERQ 2355
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKEAEEDKKKA-EEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEE-ELDEEDEKRRMEVDKK 1799
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
19-129 |
1.58e-24 |
|
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: 101.65 E-value: 1.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 19 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR 95
Cdd:cd21310 15 KIQQNTFTRWCNEHL-----KCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDRE 89
|
90 100 110
....*....|....*....|....*....|....
gi 2124423190 96 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 129
Cdd:cd21310 90 HIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1704-2586 |
1.68e-24 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 114.47 E-value: 1.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1704 TEQGEQQRQLLEEELARLQHEAAAATqkRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFREL-- 1781
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETgk 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1782 AEEAARlralAEEAKRQrqlAEEdaARQRAEAERvlAEKLAAIGEATRLKTE--AEIALKEKEAENERLRRLAEDEafqr 1859
Cdd:PTZ00121 1111 AEEARK----AEEAKKK---AED--ARKAEEARK--AEDARKAEEARKAEDAkrVEIARKAEDARKAEEARKAEDA---- 1175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1860 RRLEEQaaqHKADIEERLAQLRKASESelerqkglvedtlrqrRQVEEeilalkvsfekaaAGKAELELELGRIRsNAED 1939
Cdd:PTZ00121 1176 KKAEAA---RKAEEVRKAEELRKAEDA----------------RKAEA-------------ARKAEEERKAEEAR-KAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1940 TLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQ 2019
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR---KADELKKAEEKKKADEAKKAE 1299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2020 LAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERlrgeaeaarraaeeaeeareraereaaqsRRQVEEAERL 2099
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEE-----------------------------AKKAAEAAKA 1350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2100 KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEE 2179
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKAEE 1429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2180 TDHQksildEELQRLKAEVTEAARQRSQVEEelfslRVQMEELGKlkaRIEAENRALILRDKDNTQRVLQE---EAEKMK 2256
Cdd:PTZ00121 1430 KKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEEAK 1496
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2257 HVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDK 2332
Cdd:PTZ00121 1497 KKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2333 EQMAQQLEQETQgfqrtleAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKVtl 2412
Cdd:PTZ00121 1577 NMALRKAEEAKK-------AEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK-- 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2413 vqtleiqrqqsdHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLlqetqalqqsflsEKDTLLQRErfiE 2492
Cdd:PTZ00121 1647 ------------KKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEK-------------KAAEALKKE---A 1698
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2493 QEKAKLEQL---FQDEVAKAQKLREEQQRQQKqmeeekqqlvasmeEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLL 2569
Cdd:PTZ00121 1699 EEAKKAEELkkkEAEEKKKAEELKKAEEENKI--------------KAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKK 1764
|
890 900
....*....|....*....|
gi 2124423190 2570 AEENQRLRERLQR---LEEE 2586
Cdd:PTZ00121 1765 EEEKKAEEIRKEKeavIEEE 1784
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
23-125 |
3.19e-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: 99.70 E-value: 3.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 23 KTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKL 99
Cdd:smart00033 1 KTLLRWVNSLLAE----YDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKV 76
|
90 100
....*....|....*....|....*.
gi 2124423190 100 VNIRNDDIADGnPKLTLGLIWTIILH 125
Cdd:smart00033 77 VLFEPEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
142-241 |
3.35e-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: 99.94 E-value: 3.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 142 AKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 221
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 2124423190 222 D-VDVPQPDEKSIITYVSSLY 241
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
144-244 |
4.08e-24 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 99.46 E-value: 4.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 144 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 223
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 2124423190 224 DVPQPDEKSIITYVSSLYDAM 244
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
775-841 |
6.00e-24 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 97.72 E-value: 6.00e-24
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 775 QLKPRNpaHPVRGRVPLLAVCDYKQVEVTVHKGDECQLVGPAQPSHWKVVSSSGSEAAVPSVCFLVP 841
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
20-128 |
1.36e-23 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 98.13 E-value: 1.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 20 VQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-V 97
Cdd:pfam00307 2 ELEKELLRWINSHLAE---YGPGVRVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgV 78
|
90 100 110
....*....|....*....|....*....|.
gi 2124423190 98 KLVNIRNDDIADGNPKLTLGLIWTIILHFQI 128
Cdd:pfam00307 79 PKVLIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
141-241 |
2.88e-23 |
|
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: 97.11 E-value: 2.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 220
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 2124423190 221 EDVDVPQ-PDEKSIITYVSSLY 241
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
141-245 |
2.94e-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: 97.17 E-value: 2.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYqGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 220
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 2124423190 221 EDVDVPQPDEKSIITYVSSLYDAMP 245
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1663-2501 |
1.50e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 107.45 E-value: 1.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1742
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1743 RAEMEVLLASKARAEEESRSTSEkskqrleaeasRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1822
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELES 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1823 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrRLEEQAAQHKADIEERLAQLrKASESELERQKGLVEDtlRQR 1902
Cdd:TIGR02168 356 LEAELEELEAELEELESRLEELEEQLETLRSKVA----QLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEE--LLK 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1903 RQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAElEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 1982
Cdd:TIGR02168 429 KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAE-QALDAAERELAQLQARLDSLERLQENLEGFSEG 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1983 ARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQ-LAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLErL 2061
Cdd:TIGR02168 508 VKALLKNQSGLSGILGVLSELISVDEGYEAAIEAALGgRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTE-I 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2062 RGEAEAARRAAEEAEEARERAEREAAQSRRQVEE-------AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2134
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSA 666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2135 EQAALRQKQaaDAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEELFS 2214
Cdd:TIGR02168 667 KTNSSILER--RREIEELEEKIEELEEKIAELEKALAELRKELEE-------LEEELEQLRKELEELSRQISALRKDLAR 737
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2215 LRVQMEELGKLKARIEAEnralilrdkdntqrvLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKmL 2294
Cdd:TIGR02168 738 LEAEVEQLEERIAQLSKE---------------LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA-L 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2295 KEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLEQETQgfqrtleaerqrqlEMSAEAERLKLRVAE 2373
Cdd:TIGR02168 802 REALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE--------------ELSEDIESLAAEIEE 863
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2374 MSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQl 2453
Cdd:TIGR02168 864 LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ- 942
|
810 820 830 840
....*....|....*....|....*....|....*....|....*...
gi 2124423190 2454 kseemQTVQQEQLLQETQALQQSFLSEKDTLLQRERfIEQEKAKLEQL 2501
Cdd:TIGR02168 943 -----ERLSEEYSLTLEEAEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
998-1562 |
1.75e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 106.94 E-value: 1.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 998 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1077
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1078 RSTHGAEEVLKAHEEQLKEAQAvpATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVE 1157
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1158 RWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALL 1237
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1238 EEIERhgekveecqrfAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyik 1317
Cdd:COG1196 477 AALAE-----------LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1318 fisetlrrMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEA----HAQAKAQAEQEAQELQRRMQEEVARREEAAVDA 1393
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1394 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1473
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1474 AQEEAERLRRQvqdETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVA-LETA 1552
Cdd:COG1196 692 ELELEEALLAE---EEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEeLERE 768
|
570
....*....|
gi 2124423190 1553 QRSAEVELQS 1562
Cdd:COG1196 769 LERLEREIEA 778
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1219-2036 |
2.71e-22 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 106.83 E-value: 2.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1219 VLADSRAVREQLrqekalleeierhgekveecqrfakqyinaikdyelqlvtykaqlepVASPAKKPKVQSGSESVIQEY 1298
Cdd:NF041483 335 ALADARAEAEKL-----------------------------------------------VAEAAEKARTVAAEDTAAQLA 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1299 VDLRTryselttltsqyikfISETLRRMEEEERLAEQQRAEERERLAAvEAALEKQRQLAEAHAQakaqaeqeAQELQRR 1378
Cdd:NF041483 368 KAART---------------AEEVLTKASEDAKATTRAAAEEAERIRR-EAEAEADRLRGEAADQ--------AEQLKGA 423
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1379 MQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE---IQAKAR-----QVEAAERSRLRIEEEIRVVRLQLETT---- 1446
Cdd:NF041483 424 AKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEgerIRGEARreavqQIEEAARTAEELLTKAKADADELRSTatae 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1447 -ERQRGGAEGELQALRARAEEAEAQKRqaqEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRL 1525
Cdd:NF041483 504 sERVRTEAIERATTLRRQAEETLERTR---AEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRL 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1526 QAeEAERRLRQAEaERARQVQVALETAQRSAEVELQSKRASFAEKTaqleRTLQEEHVAVAQLREEAERRAQQQAEAERA 1605
Cdd:NF041483 581 HT-EAEERLTAAE-EALADARAEAERIRREAAEETERLRTEAAERI----RTLQAQAEQEAERLRTEAAADASAARAEGE 654
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1606 REEAERELErwqlKANEALRLRLQAEEVAQQksLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEG 1685
Cdd:NF041483 655 NVAVRLRSE----AAAEAERLKSEAQESADR--VRAEAAAAAERVGTEAAEALAAAQEEAARRRREAEETLGSARAEADQ 728
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1686 TAQQRLAAEQELI---RLRAETEQGEQQRqLLEEELARLQHEAAAATQKRQELEAELAKV--RAEMEV--LLASKARAEE 1758
Cdd:NF041483 729 ERERAREQSEELLasaRKRVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAE 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1759 ESRSTSEKSKQRLEAEASRFRELA-EEAARLRALA-EEAKRQRQLAEEDAARQRAEAERVLAEklaAIGEATRLKTEAEI 1836
Cdd:NF041483 808 RTRTEAQEEADRVRSDAYAERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASD 884
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1837 ALKEKEAENERLRRLAEDEAFQRRrlEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSF 1916
Cdd:NF041483 885 TLASAEQDAARTRADAREDANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQL 962
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1917 EKAAAGKAElelelgRIRSNAEDTLRSKEQAeleAMRQRQLAAEEEQRrreaeervqkslaAEEEAARQRKAALEEVERL 1996
Cdd:NF041483 963 IAEATGEAE------RLRAEAAETVGSAQQH---AERIRTEAERVKAE-------------AAAEAERLRTEAREEADRT 1020
|
810 820 830 840
....*....|....*....|....*....|....*....|..
gi 2124423190 1997 --KAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAH 2036
Cdd:NF041483 1021 ldEARKDANKRRSEAAEQADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
141-239 |
3.04e-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: 94.23 E-value: 3.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYqglRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 219
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 2124423190 220 PEDVDVPQPDEKSIITYVSS 239
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1523-2399 |
3.12e-21 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 103.21 E-value: 3.12e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1523 FRLQAEEAERRLRQAEAERARqVQVALETAQRSAE-VELQSKRAS-FAEKTAQLERTlqEEHVAVAQLREEAERRAQQQA 1600
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDR-LEDILNELERQLKsLERQAEKAErYKELKAELREL--ELALLVLRLEELREELEELQE 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1601 eaerareeaerelerwQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAE-----QE 1675
Cdd:TIGR02168 247 ----------------ELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYAlaneiSR 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1676 LEKQRQLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKAR 1755
Cdd:TIGR02168 300 LEQQKQILR---ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEE 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1756 AEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAE 1835
Cdd:TIGR02168 377 LEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEEL 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1836 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELE-----RQKGLVEDTLRQRRQVEEEil 1910
Cdd:TIGR02168 457 ERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllknqSGLSGILGVLSELISVDEG-- 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1911 alkvsFEKAaagkaeLELELGrirSNAEDTLRSKEQAELEAmrqrqlaaeeeqrrreaeervqksLAAEEEAARQRKAAL 1990
Cdd:TIGR02168 535 -----YEAA------IEAALG---GRLQAVVVENLNAAKKA------------------------IAFLKQNELGRVTFL 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1991 EEV---ERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQ--------AEEKAHAFAvQQKEQELQQTLQQEQSMLE 2059
Cdd:TIGR02168 577 PLDsikGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllggvlvVDDLDNALE-LAKKLRPGYRIVTLDGDLV 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2060 RLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAER-LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAarraqaeqaa 2138
Cdd:TIGR02168 656 RPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAeLEKALAELRKELEELEEELEQLRKELEELS---------- 725
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 lRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRvq 2218
Cdd:TIGR02168 726 -RQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR-- 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2219 mEELGKLKARIEAENRAL--ILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKE 2296
Cdd:TIGR02168 803 -EALDELRAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2297 KMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRtLEAERQRQLEMSAEAERLKLRVAEmsR 2376
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEEAE--A 958
|
890 900
....*....|....*....|...
gi 2124423190 2377 AQARAEEDAQRFRKQAEEIGEKL 2399
Cdd:TIGR02168 959 LENKIEDDEEEARRRLKRLENKI 981
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1823-2606 |
3.50e-21 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 103.30 E-value: 3.50e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1823 AIGEATRLKTEAEIALKEKeAENERLRRLAEDEAFQRRRLEEQaaqHKADIEERLAQLRKASESELERQKGLVEDTLR-- 1900
Cdd:PTZ00121 1092 ATEEAFGKAEEAKKTETGK-AEEARKAEEAKKKAEDARKAEEA---RKAEDARKAEEARKAEDAKRVEIARKAEDARKae 1167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1901 QRRQVEEEilalkvsfEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQrqlaaeeeqrrreaeerVQKSLAAEE 1980
Cdd:PTZ00121 1168 EARKAEDA--------KKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERK-----------------AEEARKAED 1222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1981 EaarQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAhafavQQKEQELQQTLQQEQSMLER 2060
Cdd:PTZ00121 1223 A---KKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKA-----EEARKADELKKAEEKKKADE 1294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2061 LRgeaeaarraaEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALR 2140
Cdd:PTZ00121 1295 AK----------KAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEE 1364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2141 QKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQLEEtDHQKSildEELQRLKAEVTEAARQRSQVEEelfslrvqME 2220
Cdd:PTZ00121 1365 KAEAAEKKKEEAKKKADA-AKKKAEEKKKADEAKKKAEE-DKKKA---DELKKAAAAKKKADEAKKKAEE--------KK 1431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2221 ELGKLKARIEAENRALILRDKdntqrvlQEEAEKmkhvAEEAARLSVAAQEAARLRELAEEdlaqqRALAEKMLKEKMQA 2300
Cdd:PTZ00121 1432 KADEAKKKAEEAKKADEAKKK-------AEEAKK----AEEAKKKAEEAKKADEAKKKAEE-----AKKADEAKKKAEEA 1495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2301 VQEATRLKAEAELLQQQKELAQ-EQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAErlKLRVAEMSRaqa 2379
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKaEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE--EKKKAEEAK--- 1570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2380 RAEEDAQRFRKQAEEigeklhrteLATQEKVTLVQTLEIQRQQSDHDAERLRQAiaelerEKEKLKQEakllQLKSEEmq 2459
Cdd:PTZ00121 1571 KAEEDKNMALRKAEE---------AKKAEEARIEEVMKLYEEEKKMKAEEAKKA------EEAKIKAE----ELKKAE-- 1629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2460 tvqqeqllqetqalqqsflSEKDTLLQRERFIEQEKAKLEQLFQDE----------VAKAQKLREEQQRQQKQMEEEK-- 2527
Cdd:PTZ00121 1630 -------------------EEKKKVEQLKKKEAEEKKKAEELKKAEeenkikaaeeAKKAEEDKKKAEEAKKAEEDEKka 1690
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2528 -QQLVASMEEARQ----RQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQA 2602
Cdd:PTZ00121 1691 aEALKKEAEEAKKaeelKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKA 1770
|
....
gi 2124423190 2603 TAVK 2606
Cdd:PTZ00121 1771 EEIR 1774
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1107-1907 |
1.04e-20 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 101.29 E-value: 1.04e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1107 LEATKAALKKLRAQAEAQQpMFDALRDELRGAQE--VGERLQQRHGERDvEVERWRERVAQLLERWQAVLAQTDLrqrEL 1184
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAE-RYKELKAELRELELalLVLRLEELREELE-ELQEELKEAEEELEELTAELQELEE---KL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1185 EQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDY 1264
Cdd:TIGR02168 270 EELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEEL 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1265 ELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTtltsQYIKFISETLRRMEEE-ERLAEQQRAEERER 1343
Cdd:TIGR02168 350 KEELESLEAELE--ELEAELEELESRLEELEEQLETLRSKVAQLE----LQIASLNNEIERLEARlERLEDRRERLQQEI 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1344 LAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR------QSSEAEIQA 1417
Cdd:TIGR02168 424 EELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslERLQENLEG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1418 KARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAE----GELQALRARAEEAEAQKRQAQEEAERLRR---------- 1483
Cdd:TIGR02168 504 FSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVtflpldsikg 583
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1484 QVQDETQRKRQAEAELAVRVKAEAEAAREK-QRALQALEEFRLQAEEAERRLRQAEAERARQVQVALE------------ 1550
Cdd:TIGR02168 584 TEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlvrpggvitg 663
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1551 --TAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRL 1628
Cdd:TIGR02168 664 gsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVE 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1629 QAEEVAQQKSLAQAEAEKQkeeaerearrrgkaeeqavrqRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1708
Cdd:TIGR02168 744 QLEERIAQLSKELTELEAE---------------------IEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR 802
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1709 QQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEASRFRELAEEAARL 1788
Cdd:TIGR02168 803 EALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSED-IESLAAEIEELEELIEELESELEALLNE 881
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1789 RALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAE----NERLRRLAEDEAFQRRRLEE 1864
Cdd:TIGR02168 882 RASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRidnlQERLSEEYSLTLEEAEALEN 961
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1865 QAAQHKADIEERLAQLRK----------ASESELERQKGLVEDTLRQRRQVEE 1907
Cdd:TIGR02168 962 KIEDDEEEARRRLKRLENkikelgpvnlAAIEEYEELKERYDFLTAQKEDLTE 1014
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
145-242 |
2.90e-20 |
|
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), MICAL-3, and similar proteins; Molecule interacting with CasL protein (MICAL) is a large, multidomain, cytosolic protein with a single LIM domain, a calponin homology (CH) domain and a flavoprotein monooxygenase (MO) domain. In Drosophila, MICAL is expressed in axons, interacts with the neuronal A (PlexA) receptor and is required for Semaphorin 1a (Sema-1a)-PlexA-mediated repulsive axon guidance. The LIM and CH domains mediate interactions with the cytoskeleton, cytoskeletal adaptor proteins, and other signaling proteins. The flavoprotein MO is required for semaphorin-plexin repulsive axon guidance during axonal pathfinding in the Drosophila neuromuscular system. In addition, MICAL functions to interact with Rab13 and Rab8 to coordinate the assembly of tight junctions and adherens junctions in epithelial cells. Thus, MICAL is also called junctional Rab13-binding protein (JRAB). Members of this family, which includes MICAL-2, MICAL-3, and similar proteins, contain one CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409044 [Multi-domain] Cd Length: 110 Bit Score: 88.94 E-value: 2.90e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 145 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 223
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2124423190 224 DVPQPDEKSIITYVSSLYD 242
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
141-241 |
4.10e-20 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 88.17 E-value: 4.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 220
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 2124423190 221 EDVDV--PQPDEKSIITYVSSLY 241
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
19-129 |
4.87e-20 |
|
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: 88.98 E-value: 4.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 19 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 95
Cdd:cd21309 16 KIQQNTFTRWCNEHL-----KCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRE 90
|
90 100 110
....*....|....*....|....*....|....
gi 2124423190 96 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 129
Cdd:cd21309 91 SIKLVSIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
19-129 |
6.75e-20 |
|
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: 88.60 E-value: 6.75e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 19 RVQKKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHR 95
Cdd:cd21308 19 KIQQNTFTRWCNEHL-----KCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRE 93
|
90 100 110
....*....|....*....|....*....|....
gi 2124423190 96 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 129
Cdd:cd21308 94 SIKLVSIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1420-2236 |
1.35e-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: 97.82 E-value: 1.35e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1420 RQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEG-----------ELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1488
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1489 TQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEveLQSKRASFA 1568
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE--LESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1569 EKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELErwQLKANEALRLRLQAEEVAQQKSLAQAEaekqk 1648
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLE--TLRSKVAQLELQIASLNNEIERLEARL----- 409
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1649 eeaerearrrgkaeEQAVRQRELAEQELEKQRQlaEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAA 1728
Cdd:TIGR02168 410 --------------ERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1729 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEASRFRELAEEAARLRALAEEAKRQR--QLAEE 1804
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRlqAVVVE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1805 DAARQRAEAErvlAEKLAAIGEATRLkteAEIALKEKEAENERLRRLAEDEAFQR--RRLEEQAAQHKADIEERLAQLRK 1882
Cdd:TIGR02168 554 NLNAAKKAIA---FLKQNELGRVTFL---PLDSIKGTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLGGVLV 627
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1883 ASEselerqkglVEDTLRQRRQVEEEILALKVSFEKAAAG----KAELELELGRI-RSNAEDTLRSK--EQAELEAMRQR 1955
Cdd:TIGR02168 628 VDD---------LDNALELAKKLRPGYRIVTLDGDLVRPGgvitGGSAKTNSSILeRRREIEELEEKieELEEKIAELEK 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1956 QLAAEEEQRRREAEERVQKsLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKA 2035
Cdd:TIGR02168 699 ALAELRKELEELEEELEQL-RKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2036 HAfaVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQA 2115
Cdd:TIGR02168 778 AE--AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2116 AAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLK 2195
Cdd:TIGR02168 856 SLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
810 820 830 840
....*....|....*....|....*....|....*....|.
gi 2124423190 2196 AEVteaARQRSQVEEElfsLRVQMEELGKLKARIEAENRAL 2236
Cdd:TIGR02168 936 VRI---DNLQERLSEE---YSLTLEEAEALENKIEDDEEEA 970
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
141-240 |
2.02e-19 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 86.38 E-value: 2.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 220
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 2124423190 221 ED-VDVPQPDEKSIITYVSSL 240
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2058-2672 |
2.36e-19 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 96.93 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2058 LERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaqaQAQAAAEKLRKEAEQEAARRAQAEQA 2137
Cdd:COG1196 222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAEL-------------AELEAELEELRLELEELELELEEAQA 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2138 ALRQKQAADAEMEKHKKFAEQtlrQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2217
Cdd:COG1196 289 EEYELLAELARLEQDIARLEE---RRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2218 QMEELgklkARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEK 2297
Cdd:COG1196 366 ALLEA----EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2298 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRA 2377
Cdd:COG1196 442 EALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRG 521
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2378 QARAEEDAQRFRKQAEEIGEklhrTELATQEKVTLVQTLEIQRQQSDHDAERL--RQAIAELEREKEKLKQEAKLLQLKS 2455
Cdd:COG1196 522 LAGAVAVLIGVEAAYEAALE----AALAAALQNIVVEDDEVAAAAIEYLKAAKagRATFLPLDKIRARAALAAALARGAI 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2456 EEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERfIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASME 2535
Cdd:COG1196 598 GAAVDLVASDLREADARYYVLGDTLLGRTLVAAR-LEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLE 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2536 EARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVKALPNGRDAP 2615
Cdd:COG1196 677 AEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEEL 756
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 2616 DGPATEAEPEHAFDGLRQKVpaQRLQEVGILSTEELQRLVQGRTTVAElaQREDVRR 2672
Cdd:COG1196 757 PEPPDLEELERELERLEREI--EALGPVNLLAIEEYEELEERYDFLSE--QREDLEE 809
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
137-242 |
3.21e-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: 85.77 E-value: 3.21e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 137 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 216
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 2124423190 217 LLDPEDV-DVPQPDEKSIITYVSSLYD 242
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
144-240 |
3.71e-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: 85.45 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 144 EKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 219
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 2124423190 220 PEDVDVPQPDEKSIITYVSSL 240
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1980-2511 |
1.24e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 94.62 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1980 EEAARQRKAALEEVERLKAKVEEARRLRERAEQEsARQLQLAQDAAQKRLQAEEKAHAfAVQQKEQELQQTLQQEQSMLE 2059
Cdd:COG1196 228 ELLLLKLRELEAELEELEAELEELEAELEELEAE-LAELEAELEELRLELEELELELE-EAQAEEYELLAELARLEQDIA 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2060 RLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2139
Cdd:COG1196 306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2140 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2219
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELL 465
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2220 EELGKLKARIEAENRALILRDKDNTQR--VLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEE--DLAQQRALAEKMLK 2295
Cdd:COG1196 466 AELLEEAALLEAALAELLEELAEAAARllLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLigVEAAYEAALEAALA 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2296 EKMQA--VQEATRLKAEAELLQQQKE--------LAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAE 2365
Cdd:COG1196 546 AALQNivVEDDEVAAAAIEYLKAAKAgratflplDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGR 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2366 RLKLRVAEMSRAQARAEEDAQRFRKQAEEI----GEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREK 2441
Cdd:COG1196 626 TLVAARLEAALRRAVTLAGRLREVTLEGEGgsagGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEE 705
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2442 EKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQLfQDEVAKAQK 2511
Cdd:COG1196 706 ERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEEL-ERELERLER 774
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1314-1952 |
3.23e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 92.80 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1314 QYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHA---QAKAQAEQEAQELQRRMQEEVARREEaa 1390
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEdlrETIAETEREREELAEEVRDLRERLEE-- 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1391 vdaqqqkrsIQEELQHLRQSSE---AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEa 1467
Cdd:PRK02224 291 ---------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEE- 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1468 eaqkrqAQEEAERLrrqvqdetqrkrqaEAELavrvkAEAEAAREKQRAlqALEEFRLQAEEAERRLRQAEaerarqvqV 1547
Cdd:PRK02224 361 ------LREEAAEL--------------ESEL-----EEAREAVEDRRE--EIEELEEEIEELRERFGDAP--------V 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1548 ALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVAVAQlreeaerraqqqaeaerareeaerelerwqlkaNEALRLR 1627
Cdd:PRK02224 406 DLGNAEDFLE-ELREERDELREREAELEATLRTARERVEE---------------------------------AEALLEA 451
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1628 LQAEEVAQQkslaqaeaekqkeeaEREARRRGKAEEQAVRQRELAEqELEKQRqLAEGTAQQRLAAEQELIRLRAETEQG 1707
Cdd:PRK02224 452 GKCPECGQP---------------VEGSPHVETIEEDRERVEELEA-ELEDLE-EEVEEVEERLERAEDLVEAEDRIERL 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1708 EQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLEAEASRFRELAEEAAR 1787
Cdd:PRK02224 515 EERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEE----AEEAREEVAELNSKLAELKERIES 590
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1788 LRALAEeakrqrQLAEEDAARQRAEAervLAEKLAAIGEatrLKTEAEIALKEKeaeNERLRRLAEDeaFQRRRLEE--- 1864
Cdd:PRK02224 591 LERIRT------LLAAIADAEDEIER---LREKREALAE---LNDERRERLAEK---RERKRELEAE--FDEARIEEare 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1865 ---QAAQHKADIEERLAQLRkASESELERQKGLVE------DTLRQRR-QVEEEILALKVSFEKAaagkAELELELGRIR 1934
Cdd:PRK02224 654 dkeRAEEYLEQVEEKLDELR-EERDDLQAEIGAVEneleelEELRERReALENRVEALEALYDEA----EELESMYGDLR 728
|
650
....*....|....*...
gi 2124423190 1935 SNaedtLRSKEQAELEAM 1952
Cdd:PRK02224 729 AE----LRQRNVETLERM 742
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1453-2349 |
4.26e-18 |
|
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: 92.73 E-value: 4.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1453 AEGELQALRARAEEAEAQKRQAQEE----AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAE 1528
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAEliidLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1529 EAERRLRQAEAERARQVQVAletaqrsAEVELQSKRASFAEKTAQLErtLQEEHVAVAQLREEAERRAQQQAEAERAREE 1608
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEK-------EEEKLAQVLKENKEEEKEKK--LQEEELKLLAKEEEELKSELLKLERRKVDDE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1609 AERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQ 1688
Cdd:pfam02463 314 EKLKESEKEKKKAEKELKKEKEEIEELEKEL---------KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESE 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1689 QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKvRAEMEVLLASKARAEEESRSTSEKSK 1768
Cdd:pfam02463 385 RLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEE-SIELKQGKLTEEKEELEKQELKLLKD 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1769 QRLEAEASRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEiaLKEKEAENERL 1848
Cdd:pfam02463 464 ELELKKSEDLLKETQLVKLQEQLELLLSRQKL-EERSQKESKARSGLKVLLALIKDGVGGRIISAHG--RLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1849 RRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELEL 1928
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1929 ELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRE 2008
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2009 RAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQ 2088
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEER 780
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2089 SRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQ 2168
Cdd:pfam02463 781 EKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLE 860
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2169 ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVL 2248
Cdd:pfam02463 861 EEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEEL 940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2249 QEEAEKMKHVAEEAarlsvaaqeaarLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRL 2328
Cdd:pfam02463 941 LLEEADEKEKEENN------------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLI 1008
|
890 900
....*....|....*....|.
gi 2124423190 2329 QEDKEQMAQQLEQETQGFQRT 2349
Cdd:pfam02463 1009 RAIIEETCQRLKEFLELFVSI 1029
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
21-126 |
4.50e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 82.24 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 21 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVK 98
Cdd:cd21212 1 EIEIYTDWANHYLEKG---GHKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVD 77
|
90 100
....*....|....*....|....*...
gi 2124423190 99 LVNIRNDDIADGNPKLTLGLIWTIILHF 126
Cdd:cd21212 78 VQGITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1850-2604 |
4.66e-18 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 92.81 E-value: 4.66e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1850 RLAEDEAFQRRRLEEQAA---QHKADIEERLAQLRKASESeLERQKGLVEDTLRQ----RRQVEeeiLALKVSFEKAAAG 1922
Cdd:TIGR02168 148 EIIEAKPEERRAIFEEAAgisKYKERRKETERKLERTREN-LDRLEDILNELERQlkslERQAE---KAERYKELKAELR 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1923 KAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRK---AALEEVERLKAK 1999
Cdd:TIGR02168 224 ELELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKelyALANEISRLEQQ 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2000 VEEARRLRERAEQESAR-QLQLAQDAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEA 2078
Cdd:TIGR02168 304 KQILRERLANLERQLEElEAQLEELESKLDELAEELA---ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2079 RERAEREAAQSRRQVEEA--------ERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEME 2150
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLnneierleARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2151 KHKKFAEQTLRQKaqvEQELTTLRLQLEETDHQKSIL---DEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKA 2227
Cdd:TIGR02168 461 EALEELREELEEA---EQALDAAERELAQLQARLDSLerlQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEA 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2228 RIEA---ENRALILRDKDNTQRV---LQEEAEKMKHV----------------AEEAARLSVAAQEAARLRELAE----- 2280
Cdd:TIGR02168 538 AIEAalgGRLQAVVVENLNAAKKaiaFLKQNELGRVTflpldsikgteiqgndREILKNIEGFLGVAKDLVKFDPklrka 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2281 -----------EDLAQQRALAEKMLKEKMQAVQEATRL--------------------KAEAELLQQQKELAQEQARRLQ 2329
Cdd:TIGR02168 618 lsyllggvlvvDDLDNALELAKKLRPGYRIVTLDGDLVrpggvitggsaktnssilerRREIEELEEKIEELEEKIAELE 697
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2330 ---EDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAT 2406
Cdd:TIGR02168 698 kalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2407 QEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDTLLQ 2486
Cdd:TIGR02168 778 AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER-RIAATERRLEDLEEQIEELSEDIES 856
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2487 RERFIEQEKAKLEQLfQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQE 2566
Cdd:TIGR02168 857 LAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
|
810 820 830
....*....|....*....|....*....|....*...
gi 2124423190 2567 KLLAEENQRLRERLQRLEEEhraALAHSEEIAASQATA 2604
Cdd:TIGR02168 936 VRIDNLQERLSEEYSLTLEE---AEALENKIEDDEEEA 970
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1319-2031 |
1.07e-17 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 91.67 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1319 ISETLRRMEEEERLAEQQRAEERERLAAVEAALEKqrqLAEAHAQAKAQAEQEAQELQRRMqEEVARREEAAVDAQQQKR 1398
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1399 SIQEELQHLRQSSEAEIQAKARQVEAaersrlrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1472
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdel 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1473 --------QAQEEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQA-LEEFRLQAEEAERRLRQAEAER-- 1541
Cdd:TIGR02169 388 kdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQLAADLsk 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1542 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAerelERWQLKAN 1621
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVG----ERYATAIE 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1622 EALRLRLQA-----EEVAQQK---------------SLAQAEAEKQKEEAEREARRRGKA---------EEQAVR---QR 1669
Cdd:TIGR02169 543 VAAGNRLNNvvvedDAVAKEAiellkrrkagratflPLNKMRDERRDLSILSEDGVIGFAvdlvefdpkYEPAFKyvfGD 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1670 ELAEQELEKQRQL--------------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH 1723
Cdd:TIGR02169 623 TLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEGLKRELSSLQSELRRIEN 702
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1724 EAAAATQKRQELEAELAKVRAEMEVLLASKARAEE---ESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQ 1800
Cdd:TIGR02169 703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKErleELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALN 782
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1801 LAEEDAARQRAEAERVLAEKLAAIGEATRLKT-EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQ 1879
Cdd:TIGR02169 783 DLEARLSHSRIPEIQAELSKLEEEVSRIEARLrEIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1880 LRKAsESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKE--QAELEAMRQRQL 1957
Cdd:TIGR02169 863 KEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEalEEELSEIEDPKG 941
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1958 AAEEEQRRREAEERVQKSLAAEEEAARQ----RKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQA 2031
Cdd:TIGR02169 942 EDEEIPEEELSLEDVQAELQRVEEEIRAlepvNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREV 1019
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1321-1890 |
1.23e-17 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 91.13 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLRRMEEEERLAEQQR------AEERERLAAVEAALEKQRQLAEAHAQAKAQAEQE-AQELQRRMQEEVARREEAAVDA 1393
Cdd:COG4913 235 DDLERAHEALEDAREQIellepiRELAERYAAARERLAELEYLRAALRLWFAQRRLElLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1394 QQQKRSIQEELQHLRQ-----------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERqrggaegELQALRA 1462
Cdd:COG4913 315 EARLDALREELDELEAqirgnggdrleQLEREIERLERELEERERRRARLEALLAALGLPLPASAE-------EFAALRA 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1463 RA----EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA-------------VRVKAE-AEAAREKQRALQALEEFr 1524
Cdd:COG4913 388 EAaallEALEEELEALEEALAEAEAALRDLRRELRELEAEIAslerrksniparlLALRDAlAEALGLDEAELPFVGEL- 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1525 LQAEEAERRLRQAeAERA----------------------------RQVQVALETAQRSAEVELQSKRASFAEK------ 1570
Cdd:COG4913 467 IEVRPEEERWRGA-IERVlggfaltllvppehyaaalrwvnrlhlrGRLVYERVRTGLPDPERPRLDPDSLAGKldfkph 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1571 --TAQLERTLQEE--HVAV---AQLREEA----ERRAQQQAEAERAREEAERELERWQL-KANEALRLRLQAEEVAQQKS 1638
Cdd:COG4913 546 pfRAWLEAELGRRfdYVCVdspEELRRHPraitRAGQVKGNGTRHEKDDRRRIRSRYVLgFDNRAKLAALEAELAELEEE 625
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1639 LAQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLE 1715
Cdd:COG4913 626 LAEAEERLEAL----------EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1716 EELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEA 1795
Cdd:COG4913 692 EQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENL 771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1796 KRQRQLAEEDAARQRAEAERVLAE-KLAAIGEATRLKTEAEiALKEKEAENERLR--RLAEDEAFQRRRLEEQAAQHKAD 1872
Cdd:COG4913 772 EERIDALRARLNRAEEELERAMRAfNREWPAETADLDADLE-SLPEYLALLDRLEedGLPEYEERFKELLNENSIEFVAD 850
|
650
....*....|....*...
gi 2124423190 1873 IEERLAQLRKASESELER 1890
Cdd:COG4913 851 LLSKLRRAIREIKERIDP 868
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
22-124 |
1.86e-17 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 80.46 E-value: 1.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 22 KKTFTKWVNKHLIKhwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-K 98
Cdd:cd00014 1 EEELLKWINEVLGE----ELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpE 76
|
90 100
....*....|....*....|....*..
gi 2124423190 99 LVNIRNDDI-ADGNPKLTLGLIWTIIL 124
Cdd:cd00014 77 LDLFEPEDLyEKGNLKKVLGTLWALAL 103
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1333-2002 |
2.08e-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: 90.62 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1333 AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQ-HLRQSS 1411
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTeQLEQAK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1412 EAEIQ-AKARQVEAAERSRLriEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQ 1490
Cdd:pfam01576 370 RNKANlEKAKQALESENAEL--QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1491 RKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEVELQSKRASFA 1568
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNslQEQLEEEEEAKRNVERQLSTLQAQLS 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1569 EktaqLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQlKANEALRLRLQAEEVAQQkslaqaeaekqk 1648
Cdd:pfam01576 528 D----MKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKLE-KTKNRLQQELDDLLVDLD------------ 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1649 eeaerearrrgkaeeqavRQRELAEQELEKQRQLAEGTAQQRLAAEQELI-RLRAETEQGEQQRQLLEeelarLQHEAAA 1727
Cdd:pfam01576 591 ------------------HQRQLVSNLEKKQKKFDQMLAEEKAISARYAEeRDRAEAEAREKETRALS-----LARALEE 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1728 ATQKRQELEAELAKVRAEMEVLLASKARAeEESRSTSEKSKQRLEAEASRFRELAEEA---------ARLR------ALA 1792
Cdd:pfam01576 648 ALEAKEELERTNKQLRAEMEDLVSSKDDV-GKNVHELERSKRALEQQVEEMKTQLEELedelqatedAKLRlevnmqALK 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1793 EEAKRQRQLAEEDA-------ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1865
Cdd:pfam01576 727 AQFERDLQARDEQGeekrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1866 AAQHKADIEE-RLAQ---LRKASESElERQKGLVEDTL----------RQRRQVEEEILALKVSFEKAAAGKAELELELG 1931
Cdd:pfam01576 807 MKDLQRELEEaRASRdeiLAQSKESE-KKLKNLEAELLqlqedlaaseRARRQAQQERDELADEIASGASGKSALQDEKR 885
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1932 RIR---SNAEDTLrSKEQAELEAMRQRQlaaeeeQRRREAEERVQKSLAAEEEAARQRKAALEEVER----LKAKVEE 2002
Cdd:pfam01576 886 RLEariAQLEEEL-EEEQSNTELLNDRL------RKSTLQVEQLTTELAAERSTSQKSESARQQLERqnkeLKAKLQE 956
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1323-2043 |
2.70e-17 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 90.03 E-value: 2.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1323 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVA-----RREEAAVDAQQQK 1397
Cdd:pfam02463 167 LKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYldylkLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1398 RSIQEELQHLRQSSEAE---IQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQA 1474
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEeekLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1475 QEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQr 1554
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEK- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1555 saEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1634
Cdd:pfam02463 406 --EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQ 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1635 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR 1711
Cdd:pfam02463 484 EQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGvggRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEER 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1712 QLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEaeasrfRELAEEAARLRAL 1791
Cdd:pfam02463 564 QKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKV------VEGILKDTELTKL 637
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1792 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA 1871
Cdd:pfam02463 638 KESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKL 717
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1872 DIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAED-------TLRSK 1944
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKlkveeekEEKLK 797
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1945 EQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQ---LQLA 2021
Cdd:pfam02463 798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQellLKEE 877
|
730 740
....*....|....*....|..
gi 2124423190 2022 QDAAQKRLQAEEKAHAFAVQQK 2043
Cdd:pfam02463 878 ELEEQKLKDELESKEEKEKEEK 899
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
141-240 |
4.26e-17 |
|
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: 79.90 E-value: 4.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 220
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 2124423190 221 ED-VDVPQPDEKSIITYVSSL 240
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
145-242 |
5.86e-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: 79.54 E-value: 5.86e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 145 KLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 223
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 2124423190 224 DVPQPDEKSIITYVSSLYD 242
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
143-254 |
1.52e-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: 78.49 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 143 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 222
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100 110
....*....|....*....|....*....|...
gi 2124423190 223 -VDVPQPDEKSIITYVSSLYDAMprvpdVQDGV 254
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFYRCL-----VQKGL 110
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2224-2676 |
3.68e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.53 E-value: 3.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2224 KLKARI-EAENRaliLRD-KDNTQRV--LQEEAEK-MKHVAEEAARlsvaAQEAARLRELAEEDLAQQRALAEKMLKEKM 2298
Cdd:COG1196 169 KYKERKeEAERK---LEAtEENLERLedILGELERqLEPLERQAEK----AERYRELKEELKELEAELLLLKLRELEAEL 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2299 QAVQ-EATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGF----QRTLEAERQRQLEM------SAEAERL 2367
Cdd:COG1196 242 EELEaELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEyellAELARLEQDIARLEerrrelEERLEEL 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2368 KLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQE 2447
Cdd:COG1196 322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2448 AKLLQLKSEEMQtvqqeqllqetqALQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEK 2527
Cdd:COG1196 402 LEELEEAEEALL------------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELL 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2528 QQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVKA 2607
Cdd:COG1196 470 EEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQ 549
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2608 LPNGRDAPDGPATEAEPEHAFDGLRQKVPAQRLQEVGILSTEELQRLV-QGRTTVAELAQREDVRRYLQG 2676
Cdd:COG1196 550 NIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIgAAVDLVASDLREADARYYVLG 619
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
146-241 |
4.60e-16 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 77.02 E-value: 4.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 146 LLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 224
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 2124423190 225 VPQPDEKSIITYVSSLY 241
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
948-1857 |
5.12e-16 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 85.89 E-value: 5.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 948 QQLLQSLEQGEQEESRCQRCISELKDiRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1027
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ-QLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEE 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1028 EAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTHG----AEEVLKAHEEQLKEAQ 1098
Cdd:TIGR02169 252 ELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1099 AVPATL-PELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQllerwqavlaqt 1177
Cdd:TIGR02169 322 ERLAKLeAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD------------ 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1178 dlRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAmvladsravreqlrqekalleEIERHGEKVEECQRFAKQY 1257
Cdd:TIGR02169 390 --YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1258 INAIKDYELQLVTYKAQLepvaspakkpkvqsgsESVIQEYVDLRTRYSELTtltsqyiKFISETLRRMEEEERLAEQQR 1337
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVE-------KELSKLQRELAEAEAQARASE 503
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1338 AEERERlAAVEAALEKQ--------RQLAEAHAQAKAQAEQEAQElqrRMQEEVARREEAAVDAQQQKRS---------- 1399
Cdd:TIGR02169 504 ERVRGG-RAVEEVLKASiqgvhgtvAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflp 579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1400 ---IQEELQHLRQSSEA--------------EIQAKARQ-------VEAAERSRlRIEEEIRVVRLQLETTERQ---RGG 1452
Cdd:TIGR02169 580 lnkMRDERRDLSILSEDgvigfavdlvefdpKYEPAFKYvfgdtlvVEDIEAAR-RLMGKYRMVTLEGELFEKSgamTGG 658
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1453 A-EGELQALRARAEEAEAQKRQAQEEA-ERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFrlqaeea 1530
Cdd:TIGR02169 659 SrAPRGGILFSRSEPAELQRLRERLEGlKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQE------- 731
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1531 errlRQAEAERARQVQVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERraqqqaeaerareeae 1610
Cdd:TIGR02169 732 ----EEKLKERLEELEEDLSSLEQEIE-NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH---------------- 790
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1611 relERWQLKANEalrLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQR 1690
Cdd:TIGR02169 791 ---SRIPEIQAE---LSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKE 864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1691 lAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1770
Cdd:TIGR02169 865 -ELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGED 943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1771 LE--AEASRFRELAEE----AARLRALAEEAKRQRQLAEEDAARQRAeaervLAEKLAaigeatRLKTEAEiALKEKEAE 1844
Cdd:TIGR02169 944 EEipEEELSLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDE-----LKEKRA------KLEEERK-AILERIEE 1011
|
970
....*....|...
gi 2124423190 1845 NERLRRLAEDEAF 1857
Cdd:TIGR02169 1012 YEKKKREVFMEAF 1024
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1339-1883 |
5.60e-16 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 85.74 E-value: 5.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1339 EERERLAAVEAALEKQRQLAEAHAQAkaqaeQEAQElQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRqsseaeIQAK 1418
Cdd:COG4913 219 EEPDTFEAADALVEHFDDLERAHEAL-----EDARE-QIELLEPIRELAERYAAARERLAELEYLRAALR------LWFA 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1419 ARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRA--------RAEEAEAQKRQAQEEAERLRRQVQDETQ 1490
Cdd:COG4913 287 QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAqirgnggdRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1491 RKRQAE----------AELAVRVKAEAEAAREKQRALQ-ALEEFRLQAEEAERRLRQAEAERArqvqvALETAQRSAEVE 1559
Cdd:COG4913 367 LLAALGlplpasaeefAALRAEAAALLEALEEELEALEeALAEAEAALRDLRRELRELEAEIA-----SLERRKSNIPAR 441
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1560 LQSKRASFAEKTAQLERTLQ--EEHVAVAQLReeaerraqqqaeaerareeaerelERWQLKANEAL---RLRL------ 1628
Cdd:COG4913 442 LLALRDALAEALGLDEAELPfvGELIEVRPEE------------------------ERWRGAIERVLggfALTLlvppeh 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1629 --QAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEK--QRQLAEGTAQQRLAAEQELIRL-RAE 1703
Cdd:COG4913 498 yaAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAwlEAELGRRFDYVCVDSPEELRRHpRAI 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1704 TEQG---------------------------EQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARA 1756
Cdd:COG4913 578 TRAGqvkgngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYS 657
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1757 EEESRSTS--------EKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAAR---QRAEAERVLAEKLAAIG 1825
Cdd:COG4913 658 WDEIDVASaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRlekELEQAEEELDELQDRLE 737
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1826 EATRLKTEAEIALKEkeaenERLRRLAEDEAfqRRRLEEQAAQHKADIEERLAQLRKA 1883
Cdd:COG4913 738 AAEDLARLELRALLE-----ERFAAALGDAV--ERELRENLEERIDALRARLNRAEEE 788
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1083-1573 |
6.32e-16 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 85.96 E-value: 6.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1083 AEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQ--RHGERDVEVERWR 1160
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEdkKKADELKKAAAAK 1417
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1161 ERVAQLLERWQAVLAQTDLRQRELEqlgrqlryyRESADPLGAWLQDAKRRQEQIQAmvlADSRAVREQLRQEKALLEEI 1240
Cdd:PTZ00121 1418 KKADEAKKKAEEKKKADEAKKKAEE---------AKKADEAKKKAEEAKKAEEAKKK---AEEAKKADEAKKKAEEAKKA 1485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1241 ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESViqeyvdlrtRYSELTTLTSQYIKfiS 1320
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA---------KKAEEKKKADELKK--A 1554
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQlaeahaQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1400
Cdd:PTZ00121 1555 EELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE------EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA 1628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1401 QEELQHLRQ--SSEAEIQAKARQV-EAAERSRLRIEEEIRVVRLQLETTERQRGGAEGElqalrARAEEAEAQKRQAQEE 1477
Cdd:PTZ00121 1629 EEEKKKVEQlkKKEAEEKKKAEELkKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDE-----KKAAEALKKEAEEAKK 1703
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1478 AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAER--RLRQAEAERARQVQVALETAQRS 1555
Cdd:PTZ00121 1704 AEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKiaHLKKEEEKKAEEIRKEKEAVIEE 1783
|
490
....*....|....*...
gi 2124423190 1556 AEVELQSKRASFAEKTAQ 1573
Cdd:PTZ00121 1784 ELDEEDEKRRMEVDKKIK 1801
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
143-242 |
6.66e-16 |
|
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: 76.16 E-value: 6.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 143 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 222
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 2124423190 223 VDV--PQPDEKSIITYVSSLYD 242
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
946-1580 |
7.66e-16 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 85.49 E-value: 7.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 946 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLpldkepaRECAQRIAEQQK----AQAEVEGLGK 1020
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEV-------SELEEEIEELQKelyaLANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1021 GVARLSAEAEKVLA-LPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKE--- 1096
Cdd:TIGR02168 303 QKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqle 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1097 --AQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQ-QRHGERDVEVERWRERVAQLLERWQAV 1173
Cdd:TIGR02168 383 tlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1174 LAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMV----------------LADSRAVREQLRQ--EKA 1235
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVkallknqsglsgilgvLSELISVDEGYEAaiEAA 542
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1236 L--------------------------------LEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASP-- 1281
Cdd:TIGR02168 543 LggrlqavvvenlnaakkaiaflkqnelgrvtfLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYll 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1282 -------------AKKPKVQSGSESVIQEYVDLRTRYSelttLTSQYIKFISETL---RRMEEEERLAEQQRAEERERLA 1345
Cdd:TIGR02168 623 ggvlvvddldnalELAKKLRPGYRIVTLDGDLVRPGGV----ITGGSAKTNSSILerrREIEELEEKIEELEEKIAELEK 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1346 AVEAALEKQRQLAEAHAQAKAQAEQEAQELqRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAA 1425
Cdd:TIGR02168 699 ALAELRKELEELEEELEQLRKELEELSRQI-SALRKDLARLEAEVEQLEERIAQLSKELTEL----EAEIEELEERLEEA 773
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1426 ERSRLRIEEEIrvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKA 1505
Cdd:TIGR02168 774 EEELAEAEAEI-------EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQ 846
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1506 EAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERArQVQVALETAqRSAEVELQSKRASFAEKTAQLERTLQE 1580
Cdd:TIGR02168 847 IEELSEDIESLAAEIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
143-246 |
1.08e-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: 75.86 E-value: 1.08e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 143 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 222
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 2124423190 223 VDV--PQPDEKSIITYVSSLYDAMPR 246
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1083-2012 |
3.42e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.19 E-value: 3.42e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1083 AEEVLKAHEEQLKEAQAVpatLPELEATKAALKKLRAQAEAqqpmFDALRDELRGAqEVGERLQQrhgerdveverWRER 1162
Cdd:TIGR02169 175 ALEELEEVEENIERLDLI---IDEKRQQLERLRREREKAER----YQALLKEKREY-EGYELLKE-----------KEAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1163 VAQLlerwQAVLAQTDLRQRELEQLGRQLRyyrESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIER 1242
Cdd:TIGR02169 236 ERQK----EAIERQLASLEEELEKLTEEIS---ELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1243 hgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltsqyikfiset 1322
Cdd:TIGR02169 309 ---SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRR--DKLTEEYAELKEELEDL-------------- 369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1323 LRRMEEEERLAeqqrAEERERLAAVEAALEK-QRQLaeahaqakaqaeQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ 1401
Cdd:TIGR02169 370 RAELEEVDKEF----AETRDELKDYREKLEKlKREI------------NELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1402 EELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEaERL 1481
Cdd:TIGR02169 434 AKINEL----EEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEER-VRG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1482 RRQVQDETQRKRQAE----AELaVRVKAEAEAARE---KQRALQALEEFRLQAEEAERRLRQAEAERA--------RQVQ 1546
Cdd:TIGR02169 509 GRAVEEVLKASIQGVhgtvAQL-GSVGERYATAIEvaaGNRLNNVVVEDDAVAKEAIELLKRRKAGRAtflplnkmRDER 587
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1547 VALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQqqaeaerareeaerelerwqlkaneaLRL 1626
Cdd:TIGR02169 588 RDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGK--------------------------YRM 641
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1627 RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVR------QRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1700
Cdd:TIGR02169 642 VTLEGELFEKSGAMTGGSRAPRGGILFSRSEPAELQRLRERleglkrELSSLQSELRRIENRLDELSQELSDASRKIGEI 721
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1701 RAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstSEKSKQRLeaEASRFRE 1780
Cdd:TIGR02169 722 EKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEA----LNDLEARL--SHSRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1781 LAEEaarLRALAEEAKRQR-QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRrlaedeafqR 1859
Cdd:TIGR02169 796 IQAE---LSKLEEEVSRIEaRLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGK---------K 863
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1860 RRLEEQAAQHKA---DIEERLAQLRKASEsELERQKGLVEdtlRQRRQVEEEILALKVSFEKAAAGKAELELELGRIrsn 1936
Cdd:TIGR02169 864 EELEEELEELEAalrDLESRLGDLKKERD-ELEAQLRELE---RKIEELEAQIEKKRKRLSELKAKLEALEEELSEI--- 936
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1937 aEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ 2012
Cdd:TIGR02169 937 -EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEE 1011
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4024-4062 |
3.54e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.98 E-value: 3.54e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 4024 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4062
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1395-2338 |
3.88e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 83.19 E-value: 3.88e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1395 QQKRSIQEELQHLRQSsEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEA----- 1469
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1470 QKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAR------EKQRALQALEEFRLQAEEAE-----RRLRQAE 1538
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1539 AERARQVQVALETaqrsaEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQaeaerareeaerelerwql 1618
Cdd:TIGR02169 311 AEKERELEDAEER-----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1619 kanEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQEL 1697
Cdd:TIGR02169 367 ---EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1698 IRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAE 1774
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1775 ASRFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLAEKLAAigeatrlktEAEIALKEKEAENER---LRRL 1851
Cdd:TIGR02169 524 HGTVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKM 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1852 AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELeRQKGLVEDTLRQRRQ--------VEEEIlalkvsFEKAAAgk 1923
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLmgkyrmvtLEGEL------FEKSGA-- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1924 aeleLELGRIRSNAEDTLRSKEQAELEAMRQRqlaaeeeqrrreaeervqkslaaEEEAARQRKAALEEVERLKAKVEEA 2003
Cdd:TIGR02169 655 ----MTGGSRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDEL 707
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2004 RRLRERAEQE----SARQLQLAQDAAQKRLQAEEkahafaVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEAR 2079
Cdd:TIGR02169 708 SQELSDASRKigeiEKEIEQLEQEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL 781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2080 ERAEREAAQSRRQVEEAERLKQsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQT 2159
Cdd:TIGR02169 782 NDLEARLSHSRIPEIQAELSKL----------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDL 845
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2160 LRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEElfsLRVQMEELGKLKARIEaenralILR 2239
Cdd:TIGR02169 846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQ---LRELERKIEELEAQIE------KKR 916
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2240 DKDNTQRV-LQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQK 2318
Cdd:TIGR02169 917 KRLSELKAkLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKR 995
|
970 980
....*....|....*....|
gi 2124423190 2319 ELAQEQARRLQEDKEQMAQQ 2338
Cdd:TIGR02169 996 AKLEEERKAILERIEEYEKK 1015
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3446-3484 |
3.91e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 71.59 E-value: 3.91e-15
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3446 LLEAQIATGGIIDPVHSHRVPVEVAYQRGYFDEEMNRVL 3484
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1219-1919 |
5.13e-15 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 82.71 E-value: 5.13e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1219 VLADSRAVREQLRQEKALLEEIERHgekveecQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEY 1298
Cdd:TIGR00618 234 ALQQTQQSHAYLTQKREAQEEQLKK-------QQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIE 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1299 VDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERerlaaVEAALEKQRQLAEAHAQAKAQAEQEAQELQRR 1378
Cdd:TIGR00618 307 QQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQT-----LHSQEIHIRDAHEVATSIREISCQQHTLTQHI 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1379 MQEEvarrEEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrLQLETTERQRGGAEGELQ 1458
Cdd:TIGR00618 382 HTLQ----QQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQE-----LQQRYAELCAAAITCTAQ 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1459 ALRARaeEAEAQK-RQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAE---RRL 1534
Cdd:TIGR00618 453 CEKLE--KIHLQEsAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGpltRRM 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1535 RQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERele 1614
Cdd:TIGR00618 531 QRGEQTYAQ-----LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEK--- 602
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1615 rwQLKANEALRLRLQAEEVAQQkslaqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQ---RL 1691
Cdd:TIGR00618 603 --LSEAEDMLACEQHALLRKLQ-------------------------PEQDLQDVRLHLQQCSQELALKLTALHAlqlTL 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1692 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLAS-KARAEEESRSTSEKSK-- 1768
Cdd:TIGR00618 656 TQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdREFNEIENASSSLGSDla 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1769 QRLEAEA---SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLkteaeiaLKEKEAEN 1845
Cdd:TIGR00618 736 AREDALNqslKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------LKTLEAEI 808
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 1846 ERLRRLAEDEafqRRRLEEQAAQHKADIEERLAQLRKaSESELERQKGLVEDTLRQRRQVEEEILALKVSFEKA 1919
Cdd:TIGR00618 809 GQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSA-TLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKL 878
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
931-1482 |
6.25e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 82.29 E-value: 6.25e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 931 EDRLQAEREYGSCSHHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLrlpldkeparecAQRIAEQQK 1010
Cdd:COG1196 274 LELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEEL------------EELEEELEE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1011 AQAEVEGLGKGVARLSAEAEKVLAlpepspaapTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAH 1090
Cdd:COG1196 342 LEEELEEAEEELEEAEAELAEAEE---------ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEAL 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1091 EEQLKEAQAvpatlpELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLErw 1170
Cdd:COG1196 413 LERLERLEE------ELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLE-- 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1171 qavlAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRqekalLEEIERHGEKVEEC 1250
Cdd:COG1196 485 ----ELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE-----AALAAALQNIVVED 555
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1251 QRFAKQYINAIKDYELQLVT-YKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEE 1329
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATfLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAA 635
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1330 ERLAEQQRAEERERLAAVEAALEKQRqLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ 1409
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGS-LTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1410 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ-------AQEEAERLR 1482
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEAlgpvnllAIEEYEELE 794
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1975-2669 |
8.24e-15 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 82.11 E-value: 8.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1975 SLAAEEEAARQRKAALEEVERLKAKVEEARRlRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQE 2054
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK-TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2055 QSMLERLrgeaeaarraaeeaeeareraereaaQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2134
Cdd:PTZ00121 1154 VEIARKA--------------------------EDARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2135 EQAALRQKQAADAEMEKHK---KFAEQTlRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVE-- 2209
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAeavKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKka 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2210 EElfslRVQMEELGKLKARIEAENRALILRDKDNTQRvLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRAL 2289
Cdd:PTZ00121 1287 EE----KKKADEAKKAEEKKKADEAKKKAEEAKKADE-AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEA 1361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2290 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLEQEtqgfqrtlEAERQRQLEMSAEAErlKL 2369
Cdd:PTZ00121 1362 AEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADELKKA--------AAAKKKADEAKKKAE--EK 1430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2370 RVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvqtleiQRQQSDHDAERLRQAiAELEREKEKLKQEAK 2449
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK---------KADEAKKKAEEAKKA-DEAKKKAEEAKKKAD 1500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2450 LLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQ----MEE 2525
Cdd:PTZ00121 1501 EAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEedknMAL 1580
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2526 EKQQLVASMEEAR-----------------QRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2588
Cdd:PTZ00121 1581 RKAEEAKKAEEARieevmklyeeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENK 1660
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2589 ---AALAHSEEIAASQA-TAVKALPNGRDAPDGPATEAEPEHAFDGLRQKVPAQ--------RLQEVGILSTEELQRLVQ 2656
Cdd:PTZ00121 1661 ikaAEEAKKAEEDKKKAeEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEkkkaeelkKAEEENKIKAEEAKKEAE 1740
|
730
....*....|...
gi 2124423190 2657 GRTTVAELAQRED 2669
Cdd:PTZ00121 1741 EDKKKAEEAKKDE 1753
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2787-2825 |
1.19e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.19e-14
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 2787 LLEAQIATGGVIDPVHSHRVPVEVAYQRGYFDEEMNRVL 2825
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 ... |
1124-2034 |
1.33e-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: 1.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1124 QQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQA----------VLAQTDLRQRELEQLGRQLRY 1193
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1194 YRESADPLGAWLQ-DAKRRQEQIQAM--VLADSRAVREQLRQEKALLEeierhgekveecqrfAKqyinaIKDYELQLVT 1270
Cdd:pfam01576 83 RLEEEEERSQQLQnEKKKMQQHIQDLeeQLDEEEAARQKLQLEKVTTE---------------AK-----IKKLEEDILL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1271 YKAQlepvasPAKKPKVQSGSESVIQEYVDLRTRYSE----LTTLTSQYIKFISETLRRMEEEE----RLAEQQRAEERE 1342
Cdd:pfam01576 143 LEDQ------NSKLSKERKLLEERISEFTSNLAEEEEkaksLSKLKNKHEAMISDLEERLKKEEkgrqELEKAKRKLEGE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1343 RLAAVEAALEKQRQLAEAHAQAkAQAEQEAQELQRRMQEEVARREEaavdAQQQKRSIQEELQHLRQSSEAEIQAKARqv 1422
Cdd:pfam01576 217 STDLQEQIAELQAQIAELRAQL-AKKEEELQAALARLEEETAQKNN----ALKKIRELEAQISELQEDLESERAARNK-- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1423 eaAERSRLRIEEEIRVVRLQLETTErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELav 1501
Cdd:pfam01576 290 --AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-- 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1502 rvkaeAEAAREKQRALQALEEFRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEktAQLERTLQEE 1581
Cdd:pfam01576 362 -----TEQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAE 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1582 HVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAQAEAEKqkeeaerearrrgka 1661
Cdd:pfam01576 434 KLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL--------------- 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1662 EEQAVRQRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEaelak 1741
Cdd:pfam01576 495 EDERNSLQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKA----- 565
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1742 vrAEMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEASRFRE-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAe 1814
Cdd:pfam01576 566 --AAYDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQKKFDQmLAEEKAISARYAEERDRAEAEAREKETRALSLA- 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1815 RVLAEKLAAIGEATR----LKTEAEIALKEKEA------ENERLRRLAEDEAFQ-RRRLEE-----QAAQH-KADIEERL 1877
Cdd:pfam01576 643 RALEEALEAKEELERtnkqLRAEMEDLVSSKDDvgknvhELERSKRALEQQVEEmKTQLEEledelQATEDaKLRLEVNM 722
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1878 AQLRKASESELERQKGLVEDT----LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAeLEAMR 1953
Cdd:pfam01576 723 QALKAQFERDLQARDEQGEEKrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEA-VKQLK 801
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1954 QRQLAAEEEQRRREAEERVQKS-LAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQDAAQKRLQA 2031
Cdd:pfam01576 802 KLQAQMKDLQRELEEARASRDEiLAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQ 881
|
...
gi 2124423190 2032 EEK 2034
Cdd:pfam01576 882 DEK 884
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3705-3743 |
1.35e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.05 E-value: 1.35e-14
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3705 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3743
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1083-1586 |
1.66e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.85 E-value: 1.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1083 AEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRaqaeaqqpmfDALRDELRGAQEVGERLQQRHGERDVEVErwRER 1162
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERER----------EELAEEVRDLRERLEELEEERDDLLAEAG--LDD 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1163 VAQllerwQAVLAQTDLRQRELEQLGRQLRYYRESAdplGAWLQDAKRRQEQIQAMvlaDSRAvrEQLRQEKALLE-EIE 1241
Cdd:PRK02224 307 ADA-----EAVEARREELEDRDEELRDRLEECRVAA---QAHNEEAESLREDADDL---EERA--EELREEAAELEsELE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1242 RHGEKVEECQrfakqyiNAIKDYELQLVTYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyikfISE 1321
Cdd:PRK02224 374 EAREAVEDRR-------EEIEELEEEIEELRERFG--DAPVDLGNAEDFLEELREERDELREREAELEAT-------LRT 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1322 TLRRMEEEERLAEQ-------QRAEERERLAAVEAALEKQRQLAEAHAQAKAQaeqeaqelqrrmQEEVARREEAAVDAQ 1394
Cdd:PRK02224 438 ARERVEEAEALLEAgkcpecgQPVEGSPHVETIEEDRERVEELEAELEDLEEE------------VEEVEERLERAEDLV 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1395 QQKRsiqeELQHLRQSSEAEIQAKARQVEAAERSRLRIEE-EIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1473
Cdd:PRK02224 506 EAED----RIERLEERREDLEELIAERRETIEEKRERAEElRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKL 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1474 AQ--EEAERLRR--QVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEA--ERRLRQAEAERAR---- 1543
Cdd:PRK02224 582 AElkERIESLERirTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfdEARIEEAREDKERaeey 661
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2124423190 1544 QVQVALETAQRSAE-VELQSKRASFAEKTAQLERtLQEEHVAVA 1586
Cdd:PRK02224 662 LEQVEEKLDELREErDDLQAEIGAVENELEELEE-LRERREALE 704
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1296-1805 |
1.77e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 80.20 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1296 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERL---AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAE--Q 1370
Cdd:COG4717 53 KEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEyaeLQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQ 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1371 EAQELQRRMQEEVARREEAavdaQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQR 1450
Cdd:COG4717 133 ELEALEAELAELPERLEEL----EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRL 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1451 GGAEGELQALRARAEEAEAQKRQAQEEAERlrrqvQDETQRKRQAEAELAVRVkaeaeaarekqrALQALEEFRLQAEEA 1530
Cdd:COG4717 209 AELEEELEEAQEELEELEEELEQLENELEA-----AALEERLKEARLLLLIAA------------ALLALLGLGGSLLSL 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1531 ERRLRQAEAERARQVQVALETAQRsaevelqsKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAE 1610
Cdd:COG4717 272 ILTIAGVLFLVLGLLALLFLLLAR--------EKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1611 RELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1690
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV-----------EDEEELRAALEQAEEYQELKEELEE--LEEQ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1691 LAAEQELIRLRAETEQGEQqrqlLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQR 1770
Cdd:COG4717 411 LEELLGELEELLEALDEEE----LEEELEELEEELEELEEELEELREELAELEAELEQL---------EEDGELAELLQE 477
|
490 500 510
....*....|....*....|....*....|....*
gi 2124423190 1771 LEAEASRFRELAEEAARLRALAEEAKRQRQLAEED 1805
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
143-244 |
1.92e-14 |
|
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: 72.42 E-value: 1.92e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 143 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 222
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 2124423190 223 -VDVPQPDEKSIITYVSSLYDAM 244
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1041-1794 |
2.75e-14 |
|
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: 80.40 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1041 AAPTLRSELELTLGKLEQVRSLSAIYLEKLKtislvirSTHGAEEVLKAHEEQLKE-AQAVPATLPELEATKAALKKLRA 1119
Cdd:TIGR00618 160 AKSKEKKELLMNLFPLDQYTQLALMEFAKKK-------SLHGKAELLTLRSQLLTLcTPCMPDTYHERKQVLEKELKHLR 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1120 QAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQlgRQLRYYRESAD 1199
Cdd:TIGR00618 233 EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI--KAVTQIEQQAQ 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1200 PLGAWLQDAKRRQEQI---QAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYElQLVTYKAQLE 1276
Cdd:TIGR00618 311 RIHTELQSKMRSRAKLlmkRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKT 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1277 pvaspAKKPKVQSGSesviqeyvdlrtrySELTTLTSQYIKFISETLRRMEEEERL--AEQQRAEERERLAAVEAALEKQ 1354
Cdd:TIGR00618 390 -----TLTQKLQSLC--------------KELDILQREQATIDTRTSAFRDLQGQLahAKKQQELQQRYAELCAAAITCT 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1355 RQ---LAEAHAQ-------AKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEA--EIQAKARQV 1422
Cdd:TIGR00618 451 AQcekLEKIHLQesaqslkEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDidNPGPLTRRM 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1423 EAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRaRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVR 1502
Cdd:TIGR00618 531 QRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQ-QSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1503 VKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1582
Cdd:TIGR00618 610 LACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHAL---QLTLTQERVREHALSIRVLPKELLASRQLALQKMQ 686
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1583 VAVAQLREEAER---RAQQQAEAERAREEAERELERWQLkANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREArrrg 1659
Cdd:TIGR00618 687 SEKEQLTYWKEMlaqCQTLLRELETHIEEYDREFNEIEN-ASSSLGSDLAAREDALNQSLKELMHQARTVLKARTE---- 761
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 kaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQR-----QLLEEELARLQHEAAAATQKRQE 1734
Cdd:TIGR00618 762 --AHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEipsdeDILNLQCETLVQEEEQFLSRLEE 839
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1735 LEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEE 1794
Cdd:TIGR00618 840 KSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKFLHE 899
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
141-241 |
2.87e-14 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 72.03 E-value: 2.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 220
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 2124423190 221 ED-VDVPQPDEKSIITYVSSLY 241
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1339-2034 |
4.23e-14 |
|
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: 79.63 E-value: 4.23e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1339 EERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR--QSSEAEIQ 1416
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLReaLQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1417 AKARQVEAAERSRLRIEEEIRVVRLQLETTERQrggaegelQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqAE 1496
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ--------EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQR-IH 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1497 AELAVRvKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALetaqrsaevelqSKRASFAEKTAQLER 1576
Cdd:TIGR00618 314 TELQSK-MRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVAT------------SIREISCQQHTLTQH 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1577 TLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAlrlRLQAEEVAQQKSLAQAEA--------EKQK 1648
Cdd:TIGR00618 381 IHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLA---HAKKQQELQQRYAELCAAaitctaqcEKLE 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1649 EEAEREARRRGKAEEQAVRQRE-LAEQELEKQ----RQLAEGTAQQRLAAEQELIRLRAET------------EQGEQQR 1711
Cdd:TIGR00618 458 KIHLQESAQSLKEREQQLQTKEqIHLQETRKKavvlARLLELQEEPCPLCGSCIHPNPARQdidnpgpltrrmQRGEQTY 537
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1712 QLLEEELARLQHEAAAATQKRQELEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEaeasrfRELAEEAARLRAL 1791
Cdd:TIGR00618 538 AQLETSEEDVYHQLTSERKQRASLKEQMQEIQQS-FSILTQCDNRSKEDIPNLQNITVRLQ------DLTEKLSEAEDML 610
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1792 AEEAKRQ-RQLAEEDAARQRAEAERVLAEKLAAigEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHK 1870
Cdd:TIGR00618 611 ACEQHALlRKLQPEQDLQDVRLHLQQCSQELAL--KLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSE 688
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1871 adiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALkvsfekaAAGKAELelelgrirsNAEDTLRSKEQAELE 1950
Cdd:TIGR00618 689 ---KEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENAS-------SSLGSDL---------AAREDALNQSLKELM 749
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1951 AMRQRQLAAEEEQRRREAEERV------QKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQE-SARQLQLAQD 2023
Cdd:TIGR00618 750 HQARTVLKARTEAHFNNNEEVTaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIPSDEDIlNLQCETLVQE 829
|
730
....*....|.
gi 2124423190 2024 AAQKRLQAEEK 2034
Cdd:TIGR00618 830 EEQFLSRLEEK 840
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1056-1524 |
5.34e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 79.19 E-value: 5.34e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1056 LEQVRSLSAIYLEKLKTISLVIRSTHGAEeVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDEL 1135
Cdd:COG4913 254 LEPIRELAERYAAARERLAELEYLRAALR-LWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQI 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1136 RGA--QEVgERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQE 1213
Cdd:COG4913 333 RGNggDRL-EQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAE 411
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1214 QiqamVLADSRAVREQLRQEKALLE---------------EIERH-GEKVEEC--------------------------Q 1251
Cdd:COG4913 412 A----ALRDLRRELRELEAEIASLErrksniparllalrdALAEAlGLDEAELpfvgelievrpeeerwrgaiervlggF 487
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1252 RF-----------AKQYINAIKDyELQLVTYKAqlEPVASPAKKPKVQSGS--------ESVIQEYVD--LRTRYS---- 1306
Cdd:COG4913 488 ALtllvppehyaaALRWVNRLHL-RGRLVYERV--RTGLPDPERPRLDPDSlagkldfkPHPFRAWLEaeLGRRFDyvcv 564
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1307 ----ELT------TLTSQyIKFiSETLRRMEEEERL---------AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQ 1367
Cdd:COG4913 565 dspeELRrhpraiTRAGQ-VKG-NGTRHEKDDRRRIrsryvlgfdNRAKLAALEAELAELEEELAEAEERLEALEAELDA 642
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1368 AEQEAQELQRRmqEEVARREEAAVDAQQQKRSIQEELQHLRQSSeAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTE 1447
Cdd:COG4913 643 LQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQLEELEAELEELEEELDELKGEIGRLE 719
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1448 RQRGGAEGELQALRARAEEAEAQKRQAQ-EEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFR 1524
Cdd:COG4913 720 KELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN 797
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
21-126 |
6.41e-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: 70.79 E-value: 6.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 21 QKKTFTKWVNKHLIKHwraEAQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRH 94
Cdd:cd21213 1 QLQAYVAWVNSQLKKR---PGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMAS 73
|
90 100 110
....*....|....*....|....*....|..
gi 2124423190 95 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 126
Cdd:cd21213 74 KRIRMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
996-1544 |
7.54e-14 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 78.80 E-value: 7.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 996 EPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISL 1075
Cdd:COG4913 255 EPIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAELARLEAELERLEARLDALREELDELEA 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1076 VIRStHGAEEVlkaheEQLKEaqavpatlpELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVE 1155
Cdd:COG4913 331 QIRG-NGGDRL-----EQLER---------EIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1156 VERWRERVAQllERWQAVLAQTDLRqRELEQLGRQLRYYRESADPLGAWLQDAkrRQEQIQAMVLADSRA--------VR 1227
Cdd:COG4913 396 LEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLAL--RDALAEALGLDEAELpfvgelieVR 470
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1228 -EQLRQEKAlleeIER--HGEK----VEEcQRFAK--QYINAIKDyELQLVTYKAQLEPVASPAKKPKVQSGSEsviqey 1298
Cdd:COG4913 471 pEEERWRGA----IERvlGGFAltllVPP-EHYAAalRWVNRLHL-RGRLVYERVRTGLPDPERPRLDPDSLAG------ 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1299 vdlrtrysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-AVEAALEK--QRQLAEAH------AQ 1363
Cdd:COG4913 539 --------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGNGTRHEKddRRRIRSRYvlgfdnRA 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1364 AKAQAEQEAQELQRRMQEEVARREEAAvDAQQQKRSIQEELQHLRQSSEAEI--QAKARQVEAAERSRLRIEE---EIRV 1438
Cdd:COG4913 611 KLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDAssdDLAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1439 VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQ 1518
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRE 769
|
570 580
....*....|....*....|....*.
gi 2124423190 1519 ALEEfRLQAEEAERRLRQAEAERARQ 1544
Cdd:COG4913 770 NLEE-RIDALRARLNRAEEELERAMR 794
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
18-122 |
8.25e-14 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 70.64 E-value: 8.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 18 DRVQKKTFTKWVNKHLIKhwRAEAQrhISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRH 94
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEK--RGIPK--ISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEE 77
|
90 100
....*....|....*....|....*....
gi 2124423190 95 R-QVKLVNIRNDDIADGNPKLTLGLIWTI 122
Cdd:cd21225 78 DlKIRVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1047-1912 |
9.46e-14 |
|
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: 78.57 E-value: 9.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1047 SELELTLGKLEQVRslsaiylEKLKTISLVIRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATK--AALKKLRAQAEAQ 1124
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1125 QPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLaQTDLR--QRELEQLGRQLRYYRESadplg 1202
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV-KEKIGelEAEIASLERSIAEKERE----- 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1203 awLQDAKRRQEQIQAmvladsravreqlrQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPA 1282
Cdd:TIGR02169 317 --LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEF 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1283 KKPKvqsgsesviQEYVDLRTRYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHA 1362
Cdd:TIGR02169 381 AETR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKA 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1363 QAKAQAEQEAQELQRRMQeevarreeaavDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERSRLRIEEEIRVVRLQ 1442
Cdd:TIGR02169 448 LEIKKQEWKLEQLAADLS-----------KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAV 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1443 LETTERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDETQRKRQAEaeLAVRVKA------EAEAAREK 1513
Cdd:TIGR02169 513 EEVLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEAIE--LLKRRKAgratflPLNKMRDE 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1514 QRALQALEE-----FRLQAEEAERRLRQAEAERARQVQV--ALETAQR--------SAEVELQSKRA-----SFAEKTAQ 1573
Cdd:TIGR02169 587 RRDLSILSEdgvigFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGI 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1574 LERTLQEEHVAVAqlreeaerraqqqaeaerareeaereleRWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEaer 1653
Cdd:TIGR02169 667 LFSRSEPAELQRL----------------------------RERLEGLKRELSSLQSELRRIENRLDELSQELSDAS--- 715
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1654 earrrgKAEEQAVRQRELAEQELEKQRQLAEG-------TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqhEAA 1726
Cdd:TIGR02169 716 ------RKIGEIEKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EAR 787
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1727 AATQKRQELEAELAKVRAEmevllaskaRAEEESRSTS-EKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEED 1805
Cdd:TIGR02169 788 LSHSRIPEIQAELSKLEEE---------VSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1806 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---ERLAQLRK 1882
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIED 938
|
890 900 910
....*....|....*....|....*....|..
gi 2124423190 1883 ASESELERQKGL--VEDTLRQRRQVEEEILAL 1912
Cdd:TIGR02169 939 PKGEDEEIPEEElsLEDVQAELQRVEEEIRAL 970
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
15-125 |
9.50e-14 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 70.39 E-value: 9.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 15 DERDrvqKKTFTKWVNKHLIKHwraeaqrHISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQN 84
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDP-------LINNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVEN 66
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423190 85 VQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 125
Cdd:cd21219 67 CNYAVDLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1698-2499 |
9.68e-14 |
|
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: 78.47 E-value: 9.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1698 IRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAE--MEVLLASKARAEEESRSTSEKSKQRLEaEA 1775
Cdd:TIGR00618 94 LRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSETEEVIHDLLKLDYKtfTRVVLLPQGEFAQFLKAKSKEKKELLM-NL 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1776 SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEdE 1855
Cdd:TIGR00618 173 FPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKRE-A 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1856 AFQRRRLEEQAAQHKADIEERLAQLRKASESELERQkglvedtlrQRRQVEEeilalkvsfeKAAAGKAELELELGRIRS 1935
Cdd:TIGR00618 252 QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERIN---------RARKAAP----------LAAHIKAVTQIEQQAQRI 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1936 NAEdtLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2015
Cdd:TIGR00618 313 HTE--LQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTT 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2016 rQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEE 2095
Cdd:TIGR00618 391 -LTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLK 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2096 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRL 2175
Cdd:TIGR00618 470 EREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYH 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2176 QLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEEL-------GKLKARIEAENRALI--LRDKDNTQR 2246
Cdd:TIGR00618 550 QLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLqdlteklSEAEDMLACEQHALLrkLQPEQDLQD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2247 VLQEEAEKMKHVAEEAARLSVAA--------QEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2318
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQltltqervREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLREL 709
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2319 ELAQEQARRLQEDKEQMAQQLEQETQGfqrTLEAERQRQLEMSAEA-ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGE 2397
Cdd:TIGR00618 710 ETHIEEYDREFNEIENASSSLGSDLAA---REDALNQSLKELMHQArTVLKARTEAHFNNNEEVTAALQTGAELSHLAAE 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2398 KLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQeakLLQLKSEEMQTVQQEQLLQETQALQQsf 2477
Cdd:TIGR00618 787 IQFFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLS---RLEEKSATLGEITHQLLKYEECSKQL-- 861
|
810 820
....*....|....*....|..
gi 2124423190 2478 lsekDTLLQRERFIEQEKAKLE 2499
Cdd:TIGR00618 862 ----AQLTQEQAKIIQLSDKLN 879
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
141-238 |
1.22e-13 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 69.72 E-value: 1.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 216
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 2124423190 217 LLDPEDVDVPQPDEKSIITYVS 238
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2157-2452 |
1.76e-13 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 77.09 E-value: 1.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2157 EQTLRQKAQVEQELTTLRLQLEETDHQKSIlDEELQRLKAEVTEAARQRSQVEEELFSL--RVQMEELGKLK-------A 2227
Cdd:pfam17380 255 EYTVRYNGQTMTENEFLNQLLHIVQHQKAV-SERQQQEKFEKMEQERLRQEKEEKAREVerRRKLEEAEKARqaemdrqA 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2228 RIEAENRALILRDKDNTQRVLQEEAEKmkhvAEEAARLSVAAQEAARLRELAEEDLAQQR-----------ALAEKMLKE 2296
Cdd:pfam17380 334 AIYAEQERMAMERERELERIRQEERKR----ELERIRQEEIAMEISRMRELERLQMERQQknervrqeleaARKVKILEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2297 KMQAVQEATRLKAEaELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQlemsAEAERLKLRVAEMSR 2376
Cdd:pfam17380 410 ERQRKIQQQKVEME-QIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQE----EERKRKKLELEKEKR 484
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 2377 AQARAEEDAqrfRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRqaIAELEREKEKLKQEAKLLQ 2452
Cdd:pfam17380 485 DRKRAEEQR---RKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRR--EAEEERRKQQEMEERRRIQ 555
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
141-241 |
2.31e-13 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 69.29 E-value: 2.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 220
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 2124423190 221 ED-VDVPQPDEKSIITYVSSLY 241
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1212-2219 |
3.34e-13 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 76.75 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1212 QEQIQAM--VLADSRAVREQLRQEKALLEEI--------ERHGEKVEECQRFAKQYINAIKDYELQL-----VTYKAQLE 1276
Cdd:pfam01576 46 QEQLQAEteLCAEAEEMRARLAARKQELEEIlhelesrlEEEEERSQQLQNEKKKMQQHIQDLEEQLdeeeaARQKLQLE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1277 PVASPAKKPKVQS-------GSESVIQEYVDLRTRYSELTT--------------LTSQYIKFISETLRRMEEEE----R 1331
Cdd:pfam01576 126 KVTTEAKIKKLEEdillledQNSKLSKERKLLEERISEFTSnlaeeeekakslskLKNKHEAMISDLEERLKKEEkgrqE 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1332 LAEQQRAEERERLAAVEAALEKQRQLAEAHAQAkAQAEQEAQELQRRMQEEVARREEAavdaQQQKRSIQEELQHLRQSS 1411
Cdd:pfam01576 206 LEKAKRKLEGESTDLQEQIAELQAQIAELRAQL-AKKEEELQAALARLEEETAQKNNA----LKKIRELEAQISELQEDL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1412 EAEIQAKARqveaAERSRLRIEEEIRVVRLQLETTErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDETQ 1490
Cdd:pfam01576 281 ESERAARNK----AEKQRRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQ 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1491 RKRQAEAELAvrvkaeaEAAREKQRALQALEEFRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEk 1570
Cdd:pfam01576 353 KHTQALEELT-------EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE- 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1571 tAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAQAEAEKqkee 1650
Cdd:pfam01576 424 -SERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLSTRLRQL---- 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1651 aerearrrgkaEEQAVRQRELAEQELEKQRQLAegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQ 1730
Cdd:pfam01576 495 -----------EDERNSLQEQLEEEEEAKRNVE----RQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQ 559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1731 KRQELEAElakvraeMEVLLASKARAEEE-SRSTSEKSKQR-----LEAEASRFRE-LAEEAARLRALAEEAKRQRQLAE 1803
Cdd:pfam01576 560 QLEEKAAA-------YDKLEKTKNRLQQElDDLLVDLDHQRqlvsnLEKKQKKFDQmLAEEKAISARYAEERDRAEAEAR 632
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1804 EDAARQRAEAeRVLAEKLAAIGEATR----LKTEAEIALKEKEA------ENERLRRLAEDEAFQ-RRRLEE-----QAA 1867
Cdd:pfam01576 633 EKETRALSLA-RALEEALEAKEELERtnkqLRAEMEDLVSSKDDvgknvhELERSKRALEQQVEEmKTQLEEledelQAT 711
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1868 QH-KADIEERLAQLRKASESELERQKGLVEDT----LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLR 1942
Cdd:pfam01576 712 EDaKLRLEVNMQALKAQFERDLQARDEQGEEKrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANK 791
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1943 SKEQAeLEAMRQRQLAAEEEQRRREAEERVQKS-LAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR-QLQL 2020
Cdd:pfam01576 792 GREEA-VKQLKKLQAQMKDLQRELEEARASRDEiLAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEI 870
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2021 AQDAAQKRLQAEEKAHAFA-VQQKEQELQQTLQQEQSMLERLRGEAEAARR---AAEEAEEARERAEREAAQSRRQVEEA 2096
Cdd:pfam01576 871 ASGASGKSALQDEKRRLEArIAQLEEELEEEQSNTELLNDRLRKSTLQVEQlttELAAERSTSQKSESARQQLERQNKEL 950
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2097 eRLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAE---------MEKHKKFAEQTLRQKAQVE 2167
Cdd:pfam01576 951 -KAKLQEMEGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEkklkevllqVEDERRHADQYKDQAEKGN 1029
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 2168 QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2219
Cdd:pfam01576 1030 SRMKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
600-778 |
4.00e-13 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 71.71 E-value: 4.00e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 600 LYSFVAAATKELMWLSEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEIQNTGDRLLREDHPARPTVESFQ 679
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 680 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKYTCDrsiTVTRLEDLLQDAQDERDQLNEY 759
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 2124423190 760 RGHLSGLARRAKAIVQLKP 778
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1104-1529 |
5.06e-13 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 75.57 E-value: 5.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1104 LPELEATKAALKKLRAQAEAqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWR--ERVAQLLERWQAVLAQTDLRQ 1181
Cdd:COG4717 70 LKELKELEEELKEAEEKEEE----YAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1182 RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQekaLLEEIERHGEKVEECQRFAKQYINAI 1261
Cdd:COG4717 146 ERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQD---LAEELEELQQRLAELEEELEEAQEEL 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1262 KDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVI-------QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EE 1330
Cdd:COG4717 223 EELEEELEQLENELEAAALEERlkEARLLLLIAAALlallglgGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAslGK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1331 RLAEQQRAEERERL--AAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKrsIQEELQHLR 1408
Cdd:COG4717 303 EAEELQALPALEELeeEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE--IAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1409 QSSEAEIQAKARQVEAAErsrlRIEEEIRVVRLQLET---------TERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1479
Cdd:COG4717 381 VEDEEELRAALEQAEEYQ----ELKEELEELEEQLEEllgeleellEALDEEELEEELEELEEELEELEEELEELREELA 456
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1480 RLRRQVQ-----DETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEE 1529
Cdd:COG4717 457 ELEAELEqleedGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYRE 511
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
40-123 |
5.75e-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: 68.00 E-value: 5.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 40 EAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGN 111
Cdd:cd21223 21 EFDFAVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGH 100
|
90
....*....|..
gi 2124423190 112 PKLTLGLIWTII 123
Cdd:cd21223 101 REKTLALLWRII 112
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3039-3077 |
6.06e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 65.43 E-value: 6.06e-13
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3039 LLEAQAGTGHIIDPATSARLTVDEAVRSGLVGPELHEKL 3077
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1341-1866 |
1.01e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 75.28 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1341 RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR 1420
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1421 QVEAAERSRLRIEEEIRVV-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDETQRKRQAEA 1497
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1498 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERT 1577
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1578 LQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARR 1657
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1658 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEA 1737
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1738 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1817
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2124423190 1818 AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1866
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1660-1876 |
1.64e-12 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 72.49 E-value: 1.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1739
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1740 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEASRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1815
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423190 1816 VLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1876
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1356-1776 |
2.04e-12 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 73.62 E-value: 2.04e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1356 QLAEAHAQAKAQAEQEAQELQRRMQEEVARreeaavdaqQQKRSIQEELQHLRQSSEAEiqaKARQVEA-------AERS 1428
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLR---------QEKEEKAREVERRRKLEEAE---KARQAEMdrqaaiyAEQE 340
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1429 RLRIEEEIRVVRLQLEttERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDETQRKRQaEAELAVRVK-AEA 1507
Cdd:pfam17380 341 RMAMERERELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEE 409
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1508 EAAREKQRALQALEEFRLQAEEA-ERRLRQAEAERARqvqvaletaqrsaevELQSKRASFAEKTAQLERTLQEEhvava 1586
Cdd:pfam17380 410 ERQRKIQQQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE----- 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1587 qlreeaerraqqqaEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAqaeaekqkeeaerearrrgkaEEQav 1666
Cdd:pfam17380 470 --------------EERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMI---------------------EEE-- 512
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1667 RQRELAEQELEkQRQLAEGTAQQRLAAEQElirlraeteqgeQQRQLLEEELARLQHEAAAATQKRQELEAelakvraeM 1746
Cdd:pfam17380 513 RKRKLLEKEME-ERQKAIYEEERRREAEEE------------RRKQQEMEERRRIQEQMRKATEERSRLEA--------M 571
|
410 420 430
....*....|....*....|....*....|
gi 2124423190 1747 EvllaskaRAEEESRSTSEKSKQRLEAEAS 1776
Cdd:pfam17380 572 E-------REREMMRQIVESEKARAEYEAT 594
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3370-3408 |
2.24e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.89 E-value: 2.24e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3370 LLEAQAATGFLVDPVRNQRLYVHEAVKAGIVGPELHEKL 3408
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1408-2042 |
2.35e-12 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 74.10 E-value: 2.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1408 RQSSEAEIQAKARQVEA--AERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1481
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1482 RRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVeLQ 1561
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1562 SKRASFAEKTAQLERTLQEEHVA-VAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1640
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1641 QAEAEKQKEEAEREARRRGKAEEQAV-RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEelA 1719
Cdd:pfam12128 448 ELKLRLNQATATPELLLQLENFDERIeRAREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDE--L 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1720 RLQHEAAAAT------QKRQELEAELAKVrAEMEVLLaskaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE 1793
Cdd:pfam12128 526 ELQLFPQAGTllhflrKEAPDWEQSIGKV-ISPELLH----RTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEE 600
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1794 EAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADI 1873
Cdd:pfam12128 601 ELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSA 680
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1874 EERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILA-LKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAM 1952
Cdd:pfam12128 681 NERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAyWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDL 760
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1953 RQRQLAAEEEQRRREAEERVQKSLaaeEEAARQRKAALE-----------EVERLKAKVEEARRLRERAEQESARQlqlA 2021
Cdd:pfam12128 761 ASLGVDPDVIAKLKREIRTLERKI---ERIAVRRQEVLRyfdwyqetwlqRRPRLATQLSNIERAISELQQQLARL---I 834
|
650 660
....*....|....*....|.
gi 2124423190 2022 QDAAQKRLQAEEKAHAFAVQQ 2042
Cdd:pfam12128 835 ADTKLRRAKLEMERKASEKQQ 855
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1106-1588 |
2.36e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 73.80 E-value: 2.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1106 ELEATKAALKKLRAQAEAQQPM------FDALRDELRGAQEVGERLQQRHGERdvEVERWRERVAQLLERWQAVLAQTDL 1179
Cdd:COG4913 236 DLERAHEALEDAREQIELLEPIrelaerYAAARERLAELEYLRAALRLWFAQR--RLELLEAELEELRAELARLEAELER 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1180 RQRELEQLGRQLRyyresadplgawlqDAKRRQEQIqamvladsravreQLRQEKALLEEIERHGEKVEECQRFAKQYIN 1259
Cdd:COG4913 314 LEARLDALREELD--------------ELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1260 AIKDYELQLVTYKAQLEPVASPAK--KPKVQSGSESVIQEYVDLRTRYSELT------------------TLTSQYIKF- 1318
Cdd:COG4913 367 LLAALGLPLPASAEEFAALRAEAAalLEALEEELEALEEALAEAEAALRDLRrelreleaeiaslerrksNIPARLLALr 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1319 --ISETLRRMEEEER-LAE--QQRAEERERLAAVEAALEKQRQ--LAEAHAQAKAQAEQEAQELQRRMQ-EEVARREEAA 1390
Cdd:COG4913 447 daLAEALGLDEAELPfVGEliEVRPEEERWRGAIERVLGGFALtlLVPPEHYAAALRWVNRLHLRGRLVyERVRTGLPDP 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1391 VDAQQQKRSIQEEL------------QHLRQS-------SEAEIQAKARQVEAA-----ERSRLRIEEEIRVVRL----- 1441
Cdd:COG4913 527 ERPRLDPDSLAGKLdfkphpfrawleAELGRRfdyvcvdSPEELRRHPRAITRAgqvkgNGTRHEKDDRRRIRSRyvlgf 606
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1442 ----QLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRR--QVQDETQRKRQAEAELAvRVKAEAEAAREKQR 1515
Cdd:COG4913 607 dnraKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRlaEYSWDEIDVASAEREIA-ELEAELERLDASSD 685
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1516 ALQALEEfrlQAEEAERRLRQAEAERArqvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1588
Cdd:COG4913 686 DLAALEE---QLEELEAELEELEEELD-----ELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRAL 750
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
143-242 |
2.40e-12 |
|
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).
Pssm-ID: 409031 [Multi-domain] Cd Length: 103 Bit Score: 65.82 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 143 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 218
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 2124423190 219 DPEDVdVPQPDEKSIITYVSSLYD 242
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
143-243 |
2.78e-12 |
|
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: 65.84 E-value: 2.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 143 KEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 222
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 2124423190 223 VdVPQPDEKSIITYVSSLYDA 243
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1660-2460 |
3.13e-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: 73.56 E-value: 3.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQELEKQRQLAEGTAQ-QRLAAEQELIR-----LRAETEQGEQQRQLLEEELARLQHEAAAATQKR- 1732
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQlASLEEELEKLTeeiseLEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKi 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1733 QELEAELAKVRAEMEVLLASKARAEEESRST-SEKSKQRLEAEASRfRELAEEAARLRALAEEAKRQRQlaEEDAARQRA 1811
Cdd:TIGR02169 297 GELEAEIASLERSIAEKERELEDAEERLAKLeAEIDKLLAEIEELE-REIEEERKRRDKLTEEYAELKE--ELEDLRAEL 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1812 EAErvlAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrRRLEEQAAQHKADI---EERLAQLRKASES-- 1886
Cdd:TIGR02169 374 EEV---DKEFAETRDELKDYREKLEKLKREINELKRELDRLQEEL---QRLSEELADLNAAIagiEAKINELEEEKEDka 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1887 -ELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRirsnAEDTLRSKEQAELEAMRQRQLAAEEEQRr 1965
Cdd:TIGR02169 448 lEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAE----AEAQARASEERVRGGRAVEEVLKASIQG- 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1966 reaeerVQKSLAAEEEAARQRKAALEEV--ERLKAKVEE----ARRLRERAEQESARQL------QLAQDAAQKRLQAEE 2033
Cdd:TIGR02169 523 ------VHGTVAQLGSVGERYATAIEVAagNRLNNVVVEddavAKEAIELLKRRKAGRAtflplnKMRDERRDLSILSED 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2034 KAHAFAV-----QQKEQELQQTLQQEQSMLER---------------LRGEAEAARRAAEEAEEARERAEREAAQSRRQV 2093
Cdd:TIGR02169 597 GVIGFAVdlvefDPKYEPAFKYVFGDTLVVEDieaarrlmgkyrmvtLEGELFEKSGAMTGGSRAPRGGILFSRSEPAEL 676
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2094 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2173
Cdd:TIGR02169 677 QRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENV 756
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2174 RLQLEETDHQKSILDEELQRLKAEVteAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEaE 2253
Cdd:TIGR02169 757 KSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE-K 833
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2254 KMKHvaEEAARLSVAAQEAARLRELaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQEDKE 2333
Cdd:TIGR02169 834 EIQE--LQEQRIDLKEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGDLKKERDELEAQLRELERKIE 906
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2334 QMAQQLEQEtqgfqrtleaeRQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQrfrkqAEEIGEKLHRTELATQEKVtlv 2413
Cdd:TIGR02169 907 ELEAQIEKK-----------RKRLSELKAKLEALEEELSEIEDPKGEDEEIPE-----EELSLEDVQAELQRVEEEI--- 967
|
810 820 830 840
....*....|....*....|....*....|....*....|....*..
gi 2124423190 2414 QTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2460
Cdd:TIGR02169 968 RALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYEK 1014
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1087-1493 |
4.51e-12 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 73.17 E-value: 4.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1087 LKAHEEQLKEAQAvpatlpELEATKAALKKLRAQaeaqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQL 1166
Cdd:TIGR02168 679 IEELEEKIEELEE------KIAELEKALAELRKE-------LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1167 LERWqavlaqtDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEK 1246
Cdd:TIGR02168 746 EERI-------AQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1247 VEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspaKKPKVQSGSESVIQEYvdlrtryselttltsqyikfiSETLRRM 1326
Cdd:TIGR02168 819 AANLRERLESLERRIAATERRLEDLEEQIE------ELSEDIESLAAEIEEL---------------------EELIEEL 871
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1327 EEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1406
Cdd:TIGR02168 872 ESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSL 951
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1407 LRQSSEAEIQAKARQVEAAERSRLRIEEEI-RVVRLQLEtterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1485
Cdd:TIGR02168 952 TLEEAEALENKIEDDEEEARRRLKRLENKIkELGPVNLA--------AIEEYEELKERYDFLTAQKEDLTEAKETLEEAI 1023
|
410
....*....|
gi 2124423190 1486 Q--DETQRKR 1493
Cdd:TIGR02168 1024 EeiDREARER 1033
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4293-4331 |
5.40e-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: 5.40e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 4293 LLEAQACTGGIIDPNTGERFPVTDAVNKGLVDKIMVDRI 4331
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
143-238 |
5.56e-12 |
|
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: 65.10 E-value: 5.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 143 KEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 221
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 2124423190 222 DVDVPQPDEKSIITYVS 238
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1387-2009 |
6.38e-12 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 72.40 E-value: 6.38e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1387 EEAAVDAQQQKRSIQEELQHLRQ--SSEAEIQakaRQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARA 1464
Cdd:PRK03918 161 ENAYKNLGEVIKEIKRRIERLEKfiKRTENIE---ELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1465 EEAEAQKRQAQEEAERLR------RQVQDETQRKRQAEAELAVRVKaEAEAAREKQRALQALEEFRLQAEEAERRLRQAE 1538
Cdd:PRK03918 238 EEIEELEKELESLEGSKRkleekiRELEERIEELKKEIEELEEKVK-ELKELKEKAEEYIKLSEFYEEYLDELREIEKRL 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1539 AERARQVQVALETAQrsaevELQSKRASFAEKTAQLERTLQEehvavaqlreeaerraqqqaeaerareeaERELERWQL 1618
Cdd:PRK03918 317 SRLEEEINGIEERIK-----ELEEKEERLEELKKKLKELEKR-----------------------------LEELEERHE 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1619 KANEALRLRLQAEEVaqqkslaqaeaekqkeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTAQQRLAAEQELI 1698
Cdd:PRK03918 363 LYEEAKAKKEELERL----------------------------------KKRLTGLTPEKLEKELEELEKAKEEIEEEIS 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1699 RLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE-----LAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEA 1773
Cdd:PRK03918 409 KITARIGELKKEIKELKKAIEELKKAKGKCPVCGRELTEEhrkelLEEYTAELKRIEKELKEIEEKERKL-RKELRELEK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1774 EASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIA---LKEKEAENERLRR 1850
Cdd:PRK03918 488 VLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLeelKKKLAELEKKLDE 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1851 LAEDEAFQRRRLEEQAAQHKADIEERLAQLRKA---------SESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAaa 1921
Cdd:PRK03918 568 LEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKELKKLEEELDKAFEELAETEKRLEEL-- 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1922 gKAELElELGRIRSnaEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVE 2001
Cdd:PRK03918 646 -RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALE 721
|
....*...
gi 2124423190 2002 EARRLRER 2009
Cdd:PRK03918 722 RVEELREK 729
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3115-3153 |
6.76e-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: 6.76e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3115 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETSKAL 3153
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3948-3986 |
9.61e-12 |
|
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: 9.61e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3948 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 3986
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1295-1793 |
9.76e-12 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 71.91 E-value: 9.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1295 IQEYVDLRTRYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEahaqakaqaeqeaqE 1374
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLV--------------E 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1375 LQRRMQEEVARREEAAVDAQQQKrsiqeelQHLRQSSEAEIQAKA--RQVEAAERSRLRIEEEIRVVRLQLEtterqrgg 1452
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAAS-------DHLNLVQTALRQQEKieRYQADLEELEERLEEQNEVVEEADE-------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1453 aegelqalraRAEEAEAQKRQAQEEAERLRRQVQD-----ETQRKRQAEAELAVRVKAEAE-----AAREKQRALQALEE 1522
Cdd:PRK04863 377 ----------QQEENEARAEAAEEEVDELKSQLADyqqalDVQQTRAIQYQQAVQALERAKqlcglPDLTADNAEDWLEE 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1523 FRLQAEEA-------ERRLRQAEAERaRQVQVALETAQR-SAEVElqskRASFAEKTAQLERTLQEEHVAVAQLreeaer 1594
Cdd:PRK04863 447 FQAKEQEAteellslEQKLSVAQAAH-SQFEQAYQLVRKiAGEVS----RSEAWDVARELLRRLREQRHLAEQL------ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1595 raqqqaeaeRAREEAERELERWQLKANEALRLRLQAEEVAQQKSLaqaeaekqkeeaerearrrgkAEEQAVRQRELAEQ 1674
Cdd:PRK04863 516 ---------QQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLD---------------------DEDELEQLQEELEA 565
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1675 ELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQHEAAAATQKRQELEAELAKvraemevlLA 1751
Cdd:PRK04863 566 RLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------LL 637
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2124423190 1752 SKARAEEESRSTSEKSKQRLEAEASRFREL-AEEAARLRALAE 1793
Cdd:PRK04863 638 ERERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1331-1793 |
9.93e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 71.91 E-value: 9.93e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1331 RLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEqEAQELQRRmQEEVARREEAAVDaqqqkrsiqeelqHLrqs 1410
Cdd:COG3096 275 RHANERRELSERALELRRELFGARRQLAEEQYRLVEMAR-ELEELSAR-ESDLEQDYQAASD-------------HL--- 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1411 seAEIQAKARQVEAAERSRLRIEEeirvVRLQLETTERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQD--- 1487
Cdd:COG3096 337 --NLVQTALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLADyqq 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1488 --ETQRKRQAEAELAVRVKAEAEAAREK-----QRALQALEEFRLQAEEAERRLRQAE------AERARQVQVALETAQR 1554
Cdd:COG3096 404 alDVQQTRAIQYQQAVQALEKARALCGLpdltpENAEDYLAAFRAKEQQATEEVLELEqklsvaDAARRQFEKAYELVCK 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1555 -SAEVElqskRASFAEKTAQLERTLQeEHVAVAQlreeaerraqqqaeaerareeaerELERWQLKANEA-LRLRLQAEE 1632
Cdd:COG3096 484 iAGEVE----RSQAWQTARELLRRYR-SQQALAQ------------------------RLQQLRAQLAELeQRLRQQQNA 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1633 VAQQKSLaqaeaekqkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1712
Cdd:COG3096 535 ERLLEEF-------------------CQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1713 LLEEElARLQHEAAAATQKRQELEAE----LAKVRAEMEVLLaSKARAEEESRSTSEKSKQRLEAEASRFRELA-EEAAR 1787
Cdd:COG3096 596 ELAAR-APAWLAAQDALERLREQSGEaladSQEVTAAMQQLL-EREREATVERDELAARKQALESQIERLSQPGgAEDPR 673
|
....*.
gi 2124423190 1788 LRALAE 1793
Cdd:COG3096 674 LLALAE 679
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3781-3819 |
9.99e-12 |
|
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: 9.99e-12
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3781 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3819
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2711-2749 |
1.05e-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: 1.05e-11
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 2711 LLEAQAASGFLLDPVQNRRLTVNEAVKEGVVGPELHHKL 2749
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1081-1578 |
1.83e-11 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.10 E-value: 1.83e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1081 HGAEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELrgAQEVGERLQQRHGERDVEVERWR 1160
Cdd:COG4913 238 ERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLE 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1161 ERVAQLLERWQAVLAQtdLRQ---RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALL 1237
Cdd:COG4913 316 ARLDALREELDELEAQ--IRGnggDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALL 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1238 EEIERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIK 1317
Cdd:COG4913 394 EALEEELEALEEALAEAEA---ALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELP 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1318 FISETLRRMEEEERLaeqQRAEER-------------ERLAAVEAALEKQR-------QLAEAHAQAKAQAEQEAQELQR 1377
Cdd:COG4913 462 FVGELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAG 538
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1378 RM-----------QEEVARREEAA-VDAQQQ----KRSIQEELQ--------------HLR------QSSEAEIQAKARQ 1421
Cdd:COG4913 539 KLdfkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRsryvlgFDNRAKLAALEAE 618
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1422 VEAAERSRLRIEEEIRVVRLQLETTERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDET 1489
Cdd:COG4913 619 LAELEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELE 698
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1490 QRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEVELQSKRASF 1567
Cdd:COG4913 699 AELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDAL 778
|
570
....*....|.
gi 2124423190 1568 AEKTAQLERTL 1578
Cdd:COG4913 779 RARLNRAEEEL 789
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1670-2550 |
2.23e-11 |
|
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: 70.59 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1670 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAeME 1747
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1748 VLLASKARAEEESRSTSEKSKQRLEAEASrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1827
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKI 266
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1828 TRLktEAEIALKEKEAENERLRRLAEDEafQRRRLEEQ---------------AAQH--KADIEERLAQLRKASESELER 1890
Cdd:pfam01576 267 REL--EAQISELQEDLESERAARNKAEK--QRRDLGEElealkteledtldttAAQQelRSKREQEVTELKKALEEETRS 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1891 QKGLVEDTLRQRRQVEEEilaLKVSFEKAAAGKAELE---LELGRIRSNAEDTLRSKEQAELEAMRQRQlaaeeeqrrrE 1967
Cdd:pfam01576 343 HEAQLQEMRQKHTQALEE---LTEQLEQAKRNKANLEkakQALESENAELQAELRTLQQAKQDSEHKRK----------K 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1968 AEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR----------QLQLAQDAAQkrlqaEEKAHA 2037
Cdd:pfam01576 410 LEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKlskdvsslesQLQDTQELLQ-----EETRQK 484
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2038 FAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAE----RLKQSAEEQAQAQAQA 2113
Cdd:pfam01576 485 LNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTLEALEegkkRLQRELEALTQQLEEK 564
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2114 QAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKF--------------AEQTLRQKAQVEQELT---TLRLQ 2176
Cdd:pfam01576 565 AAAYDKLEKTKNRLQQELDDLLVDLDHQRQLVSNLEKKQKKFdqmlaeekaisaryAEERDRAEAEAREKETralSLARA 644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2177 LEETDHQKSILDEELQRLKAE--------------VTEAARQRSQVEEELFSLRVQMEELG-------KLKARIEAENRA 2235
Cdd:pfam01576 645 LEEALEAKEELERTNKQLRAEmedlvsskddvgknVHELERSKRALEQQVEEMKTQLEELEdelqateDAKLRLEVNMQA 724
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2236 LILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELA-------EEDLAQQRALAEKMLKEKMQAVQEATRLK 2308
Cdd:pfam01576 725 LKAQFERDLQARDEQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQLKKLQ 804
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2309 AEAELLQQQKE---LAQEQARRLQEDKEQMAQQLEQETQGFQRTLEA----ERQRQLE-----------------MSAEA 2364
Cdd:pfam01576 805 AQMKDLQRELEearASRDEILAQSKESEKKLKNLEAELLQLQEDLAAseraRRQAQQErdeladeiasgasgksaLQDEK 884
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2365 ERLKLRVA----EMSRAQARAEEDAQRFRKQAEEIgEKLHrTELATQEkvTLVQTLEIQRQQSDHDAERLRQAIAELERE 2440
Cdd:pfam01576 885 RRLEARIAqleeELEEEQSNTELLNDRLRKSTLQV-EQLT-TELAAER--STSQKSESARQQLERQNKELKAKLQEMEGT 960
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2441 -KEKLKQ-----EAKLLQLksEEMQTVQQEQLLQETQALQQSFLSEKDTLLQrerfIEQEKAKLEQlFQDEVAKAQklre 2514
Cdd:pfam01576 961 vKSKFKSsiaalEAKIAQL--EEQLEQESRERQAANKLVRRTEKKLKEVLLQ----VEDERRHADQ-YKDQAEKGN---- 1029
|
970 980 990
....*....|....*....|....*....|....*.
gi 2124423190 2515 eqqrqqkqmeEEKQQLVASMEEARQRQREAEEGVRR 2550
Cdd:pfam01576 1030 ----------SRMKQLKRQLEEAEEEASRANAARRK 1055
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1660-1957 |
2.68e-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: 70.15 E-value: 2.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQ-RELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRqllEEELARLQHEAAAATQKR---QEL 1735
Cdd:pfam17380 295 KMEQERLRQeKEEKAREVERRRKLEE-AEKARQAEMDRQAAIYAEQERMAMER---ERELERIRQEERKRELERirqEEI 370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1736 EAELAKVRaEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAE---EAARLRALAEEAkRQRQLAEEDAARQRaE 1812
Cdd:pfam17380 371 AMEISRMR-ELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQqkvEMEQIRAEQEEA-RQREVRRLEEERAR-E 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1813 AERVLAEKLAAIGEATRLKteaeialkEKEAENERLRRLAEDEAFQRRRLEEQ---------AAQHKADIEERlaQLRKA 1883
Cdd:pfam17380 448 MERVRLEEQERQQQVERLR--------QQEEERKRKKLELEKEKRDRKRAEEQrrkilekelEERKQAMIEEE--RKRKL 517
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1884 SESELE-RQKGLVEDtlRQRRQVEEEilalkvsfekaaaGKAELELElGRIRSNAEDTLRSKEQAELEAM-RQRQL 1957
Cdd:pfam17380 518 LEKEMEeRQKAIYEE--ERRREAEEE-------------RRKQQEME-ERRRIQEQMRKATEERSRLEAMeREREM 577
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
23-129 |
2.70e-11 |
|
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: 63.41 E-value: 2.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 23 KTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHR 95
Cdd:cd21298 9 KTYRNWMNS-------LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKL 81
|
90 100 110
....*....|....*....|....*....|....
gi 2124423190 96 QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 129
Cdd:cd21298 82 KFSLVGIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1517-2033 |
3.55e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 70.07 E-value: 3.55e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1517 LQALEEFRLQAEEAE---RRLRQAEAERARQVQVALETAQRSAEVE-LQSKRASFAEKTAQLERTLQEEHVAVAQLREEA 1592
Cdd:PRK02224 161 LGKLEEYRERASDARlgvERVLSDQRGSLDQLKAQIEEKEEKDLHErLNGLESELAELDEEIERYEEQREQARETRDEAD 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1593 ERRAQQQAEAERAREEAEReLERWQLKANEALRLRLQ-AEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQREL 1671
Cdd:PRK02224 241 EVLEEHEERREELETLEAE-IEDLRETIAETEREREElAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREEL 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1672 AEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLA 1751
Cdd:PRK02224 320 EDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRE 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1752 SKARAEEEsRSTSEKSKQRLEAEASRFRE-LAEEAARLRALAEEAKRQRQLAEE----DAARQRAEAERV--LAEKLAAI 1824
Cdd:PRK02224 399 RFGDAPVD-LGNAEDFLEELREERDELRErEAELEATLRTARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1825 GEATRLKTEAEIALKEKEAENERLRRLAEDEAF------QRRRLEEQAAQHKADIEE---RLAQLRKAS---ESELERQK 1892
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLVEAEDRierleeRREDLEELIAERRETIEEkreRAEELRERAaelEAEAEEKR 557
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1893 glvEDTLRQRRQVEEEILALKVSFEKAAAGKAELElELGRIRS------NAEDTL-----RSKEQAELEAMRQRQLaaee 1961
Cdd:PRK02224 558 ---EAAAEAEEEAEEAREEVAELNSKLAELKERIE-SLERIRTllaaiaDAEDEIerlreKREALAELNDERRERL---- 629
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1962 eqrrreaeervqkslaaeeEAARQRKAALEEvERLKAKVEEARRLRERAEQ------ESARQLQLAQDAAQKRLQAEE 2033
Cdd:PRK02224 630 -------------------AEKRERKRELEA-EFDEARIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVE 687
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1340-1824 |
3.56e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 70.37 E-value: 3.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1340 ERERLAAVEAALEKQRQLAEAHAQAKAQaeqeaQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRqssEAEIQAKA 1419
Cdd:PRK04863 278 ANERRVHLEEALELRRELYTSRRQLAAE-----QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQ---TALRQQEK 349
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1420 --RQVEAAERSRLRIEEEIRVVRLQLEtterqrggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRkrqaea 1497
Cdd:PRK04863 350 ieRYQADLEELEERLEEQNEVVEEADE------------------QQEENEARAEAAEEEVDELKSQLADYQQA------ 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1498 elavrVKAEAEAAREKQRALQALEEFR-------LQAEEAERRLRQAEAERARQVQVALETAQRsaeVELQSKRASFAEK 1570
Cdd:PRK04863 406 -----LDVQQTRAIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAAHSQFEQ 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1571 TAQLERTLQEEHVAvaqlreeaerraqqqaeaerareeaerelERWQLKANEALR----LRLQAEEVAQQKslaqaeaek 1646
Cdd:PRK04863 478 AYQLVRKIAGEVSR-----------------------------SEAWDVARELLRrlreQRHLAEQLQQLR--------- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1647 qkeeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgeqQRQLLEEELARLQHEAA 1726
Cdd:PRK04863 520 --------------MRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEA---RLESLSESVSEARERRM 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1727 AATQKRQELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAK 1796
Cdd:PRK04863 583 ALRQQLEQLQARIQRLAARAPAWLAAQDALArlreqsgeefEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIE 662
|
490 500
....*....|....*....|....*...
gi 2124423190 1797 RQRQLAEEDAARQRAEAERVLAEKLAAI 1824
Cdd:PRK04863 663 RLSQPGGSEDPRLNALAERFGGVLLSEI 690
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1455-2033 |
4.21e-11 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 69.68 E-value: 4.21e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1455 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRqaEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEA--ER 1532
Cdd:PRK02224 162 GKLEEYRERASDARLGVERVLSDQRGSLDQLKAQIEEKE--EKDLHERLNGLESELAELDEEIERYEEQREQARETrdEA 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1533 RLRQAEAERARQVQVALETA---QRSAEVELQSKRASFAEKTAQLERTLQEehvavaqlreeaerraqqqAEAERAREEA 1609
Cdd:PRK02224 240 DEVLEEHEERREELETLEAEiedLRETIAETEREREELAEEVRDLRERLEE-------------------LEEERDDLLA 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1610 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE--REARRRGKAEEQAVRQRELA---EQELEKQRQLAE 1684
Cdd:PRK02224 301 EAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEaeSLREDADDLEERAEELREEAaelESELEEAREAVE 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1685 GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVR---AEMEVLLA---------- 1751
Cdd:PRK02224 381 DRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARervEEAEALLEagkcpecgqp 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1752 ----SKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAE--EDAARQRAEAERVLAEKLAAIG 1825
Cdd:PRK02224 461 vegsPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAEDRIERLEErrEDLEELIAERRETIEEKRERAE 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1826 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE---------ERLAQLRKASESELERQKGLVE 1896
Cdd:PRK02224 541 ELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIEslerirtllAAIADAEDEIERLREKREALAE 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1897 ------DTLRQRRqveEEILALKVSFEKAAAGKAELElelgriRSNAEDTLRSKEQaELEAMRQRQlaaeeeqrrreaeE 1970
Cdd:PRK02224 621 lnderrERLAEKR---ERKRELEAEFDEARIEEARED------KERAEEYLEQVEE-KLDELREER-------------D 677
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1971 RVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2033
Cdd:PRK02224 678 DLQAEIGAVENELEELEELRERREALENRVEALEALYDEAEELESMYGDLRAELRQRNVETLE 740
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
999-1584 |
5.56e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.60 E-value: 5.56e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 999 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKL-EQVRSLSAIYLEklktislv 1076
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLsESVSEARERRMA-------- 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1077 irsthgaeevLKAHEEQLK-EAQAVPATLPELEATKAALKKLRAQAEaqqpmfdalrDELRGAQEVGERLQQrHGERDVE 1155
Cdd:PRK04863 584 ----------LRQQLEQLQaRIQRLAARAPAWLAAQDALARLREQSG----------EEFEDSQDVTEYMQQ-LLERERE 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1156 VERWRERVAqllERWQAVLAQTD-LRQRELEQLGRQLRYyresADPLGAWL----------QDA----KRRQEQIQAMVL 1220
Cdd:PRK04863 643 LTVERDELA---ARKQALDEEIErLSQPGGSEDPRLNAL----AERFGGVLlseiyddvslEDApyfsALYGPARHAIVV 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1221 ADSRAVREQLRQEKALLEEI-------ERHGEKVEECQRFAKQYINAIKDYELQLVTYKAqlEPVASPAKKPK----VQS 1289
Cdd:PRK04863 716 PDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqLRA 793
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1290 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETL----------------RRMEEEERLAEQQRAEERERLAAVEAALEK 1353
Cdd:PRK04863 794 EREELAERYATLSFDVQKLQRLHQAFSRFIGSHLavafeadpeaelrqlnRRRVELERALADHESQEQQQRSQLEQAKEG 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1354 QRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ--EELQHLRQSSEAEIQAKARQVEAAE----- 1426
Cdd:PRK04863 874 LSALNRLLPRLNLLADETLADRVEEIREQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqrd 953
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1427 -RSRLRIEEEIRVVRLQLETTERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDETQRKRQAEAELavrv 1503
Cdd:PRK04863 954 aKQQAFALTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL---- 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1504 KAEAEAAREK-QRALQALEEFRLQA-EEAERRLRQAEAE------RARQVQVALETAQRSAEVELQS--KRASFAEKTAQ 1573
Cdd:PRK04863 1026 KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDYH 1105
|
650
....*....|.
gi 2124423190 1574 LERTLQEEHVA 1584
Cdd:PRK04863 1106 EMREQVVNAKA 1116
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1764-2601 |
5.58e-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: 69.33 E-value: 5.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1764 SEKSKQRLEAEASRFRElaeeaARLRALAEEAKRQRQLAEEDaaRQRAEAERVLAEKLAAIgEATRLKTEAEIALKEK-- 1841
Cdd:TIGR02169 170 RKKEKALEELEEVEENI-----ERLDLIIDEKRQQLERLRRE--REKAERYQALLKEKREY-EGYELLKEKEALERQKea 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1842 -EAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAA 1920
Cdd:TIGR02169 242 iERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAE 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1921 AGKAELELELGRIRSNAEDtlrSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQR---KAALEEVERLK 1997
Cdd:TIGR02169 322 ERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRdelKDYREKLEKLK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1998 AKVEE----ARRLRERAEQESARQLQLAQDAA-----QKRLQAEEKAHAFAVQQKEQElqqtlqqeqsmLERLRGEAEAA 2068
Cdd:TIGR02169 399 REINElkreLDRLQEELQRLSEELADLNAAIAgieakINELEEEKEDKALEIKKQEWK-----------LEQLAADLSKY 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2069 RRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAqaqaqaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAE 2148
Cdd:TIGR02169 468 EQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERV--------------------------------RGGRAVEEV 515
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2149 MEKHKKFAEQTLRQKAQVEQELTTL-------RLQL----EETDHQKSIldEELQRLKA-EVTEAARQRSQVEEELFSLR 2216
Cdd:TIGR02169 516 LKASIQGVHGTVAQLGSVGERYATAievaagnRLNNvvveDDAVAKEAI--ELLKRRKAgRATFLPLNKMRDERRDLSIL 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2217 VQMEELGKLKARIEAENR-----------ALILRDKDNTQRV------------LQEEAEKMKHVAEEAARL-SVAAQEA 2272
Cdd:TIGR02169 594 SEDGVIGFAVDLVEFDPKyepafkyvfgdTLVVEDIEAARRLmgkyrmvtlegeLFEKSGAMTGGSRAPRGGiLFSRSEP 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2273 ARLRELAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQET 2343
Cdd:TIGR02169 674 AELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2344 QGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQS 2423
Cdd:TIGR02169 754 ENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYL 831
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2424 DHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQalqqsfLSEKDTLLQRERF-IEQEKAKLEQLF 2502
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD------LESRLGDLKKERDeLEAQLRELERKI 905
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2503 QDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEgvrrkqeelqlleqqrQQQEKLLAEENQRLRERLQR 2582
Cdd:TIGR02169 906 EELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEE----------------ELSLEDVQAELQRVEEEIRA 969
|
890
....*....|....*....
gi 2124423190 2583 LEEEHRAALAHSEEIAASQ 2601
Cdd:TIGR02169 970 LEPVNMLAIQEYEEVLKRL 988
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1338-1824 |
7.10e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 69.21 E-value: 7.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1338 AEERERLaaVEAALEKQRQLAEAHAQaKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKrsiqeelQHLrqsseAEIQA 1417
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQ-LAEEQYRLVEMARELEELSARESDLEQDYQAAS-------DHL-----NLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1418 KARQVEAAERSRLRIEEeirvVRLQLETTERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDetqrKRQAEA 1497
Cdd:COG3096 342 ALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQALD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1498 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVElqskrasfaEKTAQLERT 1577
Cdd:COG3096 407 VQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD---------AARRQFEKA 477
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1578 LQeehvAVAQLREEAERRaqqqaeaerareeaerelERWQlKANEALR----LRLQAEEVAQQKSlaqaeaekqkeeaer 1653
Cdd:COG3096 478 YE----LVCKIAGEVERS------------------QAWQ-TARELLRryrsQQALAQRLQQLRA--------------- 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1654 earRRGKAEEQAVRQRELAEQelekQRQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQ 1733
Cdd:COG3096 520 ---QLAELEQRLRQQQNAERL----LEEFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQQLE 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1734 ELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAE 1803
Cdd:COG3096 589 QLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGG 668
|
490 500
....*....|....*....|.
gi 2124423190 1804 EDAARQRAEAERVLAEKLAAI 1824
Cdd:COG3096 669 AEDPRLLALAERLGGVLLSEI 689
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1497-2033 |
7.52e-11 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 69.12 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1497 AELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAE-RARQVQVALETAQRSAEVELQSKRAS--------- 1566
Cdd:COG3899 712 ARRALARGAYAEALRYLERALELLPPDPEEEYRLALLLELAEALyLAGRFEEAEALLERALAARALAALAAlrhgnppas 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1567 -FAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAE 1645
Cdd:COG3899 792 aRAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1646 KQKEEAEREARRrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEA 1725
Cdd:COG3899 872 ALAAAAAAAAAA---AALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAA 948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1726 AAATQKRQELEAELAKVRAEMEVLLASKARAeeesrstsekskqRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEED 1805
Cdd:COG3899 949 AAAAALAAALALAAAAAAAAAAALAAAAAAA-------------AAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAAL 1015
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1806 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASE 1885
Cdd:COG3899 1016 AAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAA 1095
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1886 SELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRR 1965
Cdd:COG3899 1096 ALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAAL 1175
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1966 REAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2033
Cdd:COG3899 1176 AALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
2157-2643 |
7.54e-11 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 69.40 E-value: 7.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2157 EQTLRQKAQVEQE--LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEElfslRVQMEELGKlkaRIEAENR 2234
Cdd:PTZ00121 1057 EGKAEAKAHVGQDegLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE----ARKAEEAKK---KAEDARK 1129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2235 ALILRDKDNTQRVlqEEAEKmkhvAEEAARLSVA--AQEAARLRELAEEDLAQQRALAEKMLK-EKMQAVQEATRLKAEA 2311
Cdd:PTZ00121 1130 AEEARKAEDARKA--EEARK----AEDAKRVEIArkAEDARKAEEARKAEDAKKAEAARKAEEvRKAEELRKAEDARKAE 1203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2312 ELLQQQKELAQEQARRLQEDKE-QMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfRK 2390
Cdd:PTZ00121 1204 AARKAEEERKAEEARKAEDAKKaEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-----AR 1278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2391 QAEEIG---EKLHRTELATQEKVTLVQTLEIQrqqsdhdAERLRQAiAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLL 2467
Cdd:PTZ00121 1279 KADELKkaeEKKKADEAKKAEEKKKADEAKKK-------AEEAKKA-DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKA 1350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2468 QETQALQQSFLSEKDTLLQRERfIEQEKAKLEQLFQ--DEVAKAQKLREEQQRQQKQMEEEKQQlVASMEEARQRQREAE 2545
Cdd:PTZ00121 1351 EAEAAADEAEAAEEKAEAAEKK-KEEAKKKADAAKKkaEEKKKADEAKKKAEEDKKKADELKKA-AAAKKKADEAKKKAE 1428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2546 EGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRA--ALAHSEEIAASQATAVKALPNGRDAPDGPATEAE 2623
Cdd:PTZ00121 1429 EKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKAdeAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEA 1508
|
490 500
....*....|....*....|
gi 2124423190 2624 PEHAfDGLRQKVPAQRLQEV 2643
Cdd:PTZ00121 1509 KKKA-DEAKKAEEAKKADEA 1527
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1136-1501 |
8.47e-11 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.83 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1136 RGAQEvgERLQQRHGERDVEVERWR---------ERVAQLLERW-------------QAVLAQTDLRQRELEqlgRQLRY 1193
Cdd:COG3096 780 RAARE--KRLEELRAERDELAEQYAkasfdvqklQRLHQAFSQFvgghlavafapdpEAELAALRQRRSELE---RELAQ 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1194 YRESADPLGAWLQDAKRRQEQI-----QAMVLADsravrEQLRQekaLLEEIERHGEKVEECQRFAKQYINAIkdyelql 1268
Cdd:COG3096 855 HRAQEQQLRQQLDQLKEQLQLLnkllpQANLLAD-----ETLAD---RLEELREELDAAQEAQAFIQQHGKAL------- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1269 vtykAQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltSQYIKFISETLRRM------EEEERLAEQQRAEE-- 1340
Cdd:COG3096 920 ----AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRL----KQQIFALSEVVQRRphfsyeDAVGLLGENSDLNEkl 989
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1341 RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEevarreeaavdAQQQKRSIQEELQHLrqsseaEIQAKAR 1420
Cdd:COG3096 990 RARLEQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL------GVQADAE 1052
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1421 QVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDETQRKR 1493
Cdd:COG3096 1053 AEERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERR 1132
|
....*...
gi 2124423190 1494 QAEAELAV 1501
Cdd:COG3096 1133 LHRRELAY 1140
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1314-2025 |
9.68e-11 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 68.61 E-value: 9.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1314 QYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDA 1393
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1394 QQQKRSIQEELQHLRQ---SSEAEIQA-KARQVEAAERSRLRIEEEIRVVRLQLetteRQRGGA--------EGELQALR 1461
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHF----RSLGSAiskilrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1462 AR----AEEAEAQKRQAQEEAERLRRQVQDetqRKRQAEAELAVRVKA---EAEAAREKQRALQAleefrlQAEEAERRL 1534
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQHQD---RIEQLISEHEVEITGlteKASSARSQANSIQS------QLEIIQEQA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1535 RQAEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQeehVAVAQLREEAERRAQQQAEAERAREEAERELE 1614
Cdd:pfam15921 309 RNQNSMYMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLV---LANSELTEARTERDQFSQESGNLDDQLQKLLA 384
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1615 RWQLKANEalrLRLQAEevaQQKSLaqaeaekqkeeaerEARRRGKAEEQAVRQRELAEQELEKQRQLA---------EG 1685
Cdd:pfam15921 385 DLHKREKE---LSLEKE---QNKRL--------------WDRDTGNSITIDHLRRELDDRNMEVQRLEAllkamksecQG 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1686 TAQQRLAAEQ----ELIRLRAETEQGEQQRQLLEEELARLqheaaaaTQKRQELEAELAKVrAEMEVLLASKARAEEESR 1761
Cdd:pfam15921 445 QMERQMAAIQgkneSLEKVSSLTAQLESTKEMLRKVVEEL-------TAKKMTLESSERTV-SDLTASLQEKERAIEATN 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1762 STSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQR-QLAEEDAA----RQRAEAERVLAEKLAAIGEATRL-KTEAE 1835
Cdd:pfam15921 517 AEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKlQMAEKDKVieilRQQIENMTQLVGQHGRTAGAMQVeKAQLE 596
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1836 IALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQLRKASESELERQKGL--VEDTLRQRRQVEEEI 1909
Cdd:pfam15921 597 KEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEkvklVNAGSERLRAVKDIKQERDQLLneVKTSRNELNSLSEDY 676
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1910 LALKVSF----EKAAAGKAELELELGRIRSNAE---DTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 1982
Cdd:pfam15921 677 EVLKRNFrnksEEMETTTNKLKMQLKSAQSELEqtrNTLKSMEGSDGHAMKVAMGMQKQITAKRGQIDALQSKIQFLEEA 756
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1983 ---ARQRKAALEE-------------VERLKAKVE-EARRLRERAEQESARQLQLAQDAA 2025
Cdd:pfam15921 757 mtnANKEKHFLKEeknklsqelstvaTEKNKMAGElEVLRSQERRLKEKVANMEVALDKA 816
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1107-1814 |
1.09e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 68.44 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1107 LEATKAALKKLRAQAEaqqpmFDALRDELRGAQEVGERLQQRHGERDVEVERWRERV----AQLLERWQAVLAQT----D 1178
Cdd:COG3096 340 QTALRQQEKIERYQED-----LEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVdslkSQLADYQQALDVQQtraiQ 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1179 LRQ--RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMV------LADSRAVREQLRQEKALLEEIERHGEKVEEC 1250
Cdd:COG3096 415 YQQavQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVleleqkLSVADAARRQFEKAYELVCKIAGEVERSQAW 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1251 QRfAKQYINAIKDYELQLvtykAQLEPVAspakkpkvqsgsesviQEYVDLRTRYS---ELTTLTSQYIKFISETLRRME 1327
Cdd:COG3096 495 QT-ARELLRRYRSQQALA----QRLQQLR----------------AQLAELEQRLRqqqNAERLLEEFCQRIGQQLDAAE 553
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1328 EEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQ---------EAQELQRRMQEEVArreEAAVDAQQQKR 1398
Cdd:COG3096 554 ELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKElaarapawlAAQDALERLREQSG---EALADSQEVTA 630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1399 SIQEELQHLRQSSEAEIQAKARqveaaersRLRIEEEIRvvRLQletterQRGGAE-GELQALRAR-------------- 1463
Cdd:COG3096 631 AMQQLLEREREATVERDELAAR--------KQALESQIE--RLS------QPGGAEdPRLLALAERlggvllseiyddvt 694
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1464 ---AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DETQRKRQaEAELAVRVKAE---------- 1506
Cdd:COG3096 695 ledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVFDAE-ELEDAVVVKLSdrqwrysrfp 773
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1507 -----AEAAREKQralqaLEEFRLQAEE-----AERRLRQAEAER---------ARQVQVALETaqrSAEVELQSKRASF 1567
Cdd:COG3096 774 evplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvGGHLAVAFAP---DPEAELAALRQRR 845
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1568 AEKTAQLERTLQEEHVAVAQLREEAERRA-------QQQAEAERAREEAERELERWQLKANEALR-LRLQAEEVAQ-QKS 1638
Cdd:COG3096 846 SELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELREELDAAQEAQAfIQQHGKALAQlEPL 925
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1639 LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLAAEQELI-RLRAETEQGEQQRQLLEE 1716
Cdd:COG3096 926 VAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLGENSDLNeKLRARLEQAEEARREARE 1005
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1717 ELARLQHEAAAATQKR--------------QELEAELakvrAEMEVLLAskARAEEESRSTSEKSKQRLEAEASRFRELA 1782
Cdd:COG3096 1006 QLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQEL----EELGVQAD--AEAEERARIRRDELHEELSQNRSRRSQLE 1079
|
810 820 830
....*....|....*....|....*....|..
gi 2124423190 1783 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1814
Cdd:COG3096 1080 KQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2140-2342 |
1.52e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.33 E-value: 1.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2140 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2219
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2220 EEL----------GKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRAL 2289
Cdd:COG4942 107 AELlralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 2290 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQE 2342
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1325-2448 |
1.90e-10 |
|
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: 67.51 E-value: 1.90e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1325 RMEEEERLAEQQRAEERERLAAVEAAL----EKQRQLAEAHA--QAKAQAEQE---------------AQELQRRMQEEV 1383
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNalQEQLQAETElcaeaeemrarlaarKQELEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1384 AR---REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR-QVE--AAERSRLRIEEEIRVVrlqlettERQRGGAEGEL 1457
Cdd:pfam01576 82 SRleeEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKlQLEkvTTEAKIKKLEEDILLL-------EDQNSKLSKER 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1458 QALRARAEEAEAQKRQAQEEAERLrrqvqdeTQRKRQAEA---ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRL 1534
Cdd:pfam01576 155 KLLEERISEFTSNLAEEEEKAKSL-------SKLKNKHEAmisDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAEL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1535 RQAEAERARQVQvaletaqrSAEVELQSKRASFAEKTAQ---LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAER 1611
Cdd:pfam01576 228 QAQIAELRAQLA--------KKEEELQAALARLEEETAQknnALKKIRELEAQISELQEDLESERAARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1612 ELerwqlkanEALRLRLQ--AEEVAQQKSLAQAEAEKQKEEAerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ 1689
Cdd:pfam01576 300 EL--------EALKTELEdtLDTTAAQQELRSKREQEVTELK--------KALEEETRSHEAQLQEMRQKHTQALEELTE 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1690 RLaaeQELIRLRAETEQGeqqRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLAskaraeeesrSTSEKSKQ 1769
Cdd:pfam01576 364 QL---EQAKRNKANLEKA---KQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQA----------RLSESERQ 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1770 RLEAeASRFRELAEEAARLRALAEEAKRQRQLAEEDAarqrAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLR 1849
Cdd:pfam01576 428 RAEL-AEKLSKLQSELESVSSLLNEAEGKNIKLSKDV----SSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQ 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1850 RLAEDEAFQRRRLEEQAAQHKAdieeRLAQLRKASESELERQKGLVEDtlrqRRQVEEEILALKVSFEKAAAGKAELELE 1929
Cdd:pfam01576 503 EQLEEEEEAKRNVERQLSTLQA----QLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAAYDKLEKT 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1930 LGRIRSNAEDTLrskeqaeLEAMRQRQLAAEEEQRRREAEErvqksLAAEEEAARQRKAALEEVERLKAKVEEARRLRER 2009
Cdd:pfam01576 575 KNRLQQELDDLL-------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAEAEAREKETRALSLA 642
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2010 AEQESARQLQLAQDAAQKRLQAEekahafavqqkeqelqqtlqqeqsmLERLRGEAEAARRAAEEAEEARERAEREAAQS 2089
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEM 697
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2090 RRQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalRQKQAADAEMEKHKKfaeQTLRQKAQVEQE 2169
Cdd:pfam01576 698 KTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR---QLVKQVRELEAE 757
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2170 LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQ 2249
Cdd:pfam01576 758 LEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEILAQSKESEKKLKN 837
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2250 EEAEKMKHVAEEAARLSVAAQEAARLRELAEEdLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQ 2329
Cdd:pfam01576 838 LEAELLQLQEDLAASERARRQAQQERDELADE-IASGASGKSALQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKST 916
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2330 EDKEQMAQQLEQETQGFQRTLEA----ERQRQ------LEMSAEAE-RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEK 2398
Cdd:pfam01576 917 LQVEQLTTELAAERSTSQKSESArqqlERQNKelkaklQEMEGTVKsKFKSSIAALEAKIAQLEEQLEQESRERQAANKL 996
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2399 LHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEA 2448
Cdd:pfam01576 997 VRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
932-1581 |
2.19e-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: 67.40 E-value: 2.19e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 932 DRLQAEREYgscSHHYQQLLQSLEQGEQEESrcqrcISELKDIRLQLEACEtrtvhrlrlpldkepaRECAQRIAEQQKA 1011
Cdd:TIGR02169 201 ERLRREREK---AERYQALLKEKREYEGYEL-----LKEKEALERQKEAIE----------------RQLASLEEELEKL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1012 QAEVEGLGKGVA----RLSAEAEKVLALPEPSPAAptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVL 1087
Cdd:TIGR02169 257 TEEISELEKRLEeieqLLEELNKKIKDLGEEEQLR--VKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKL 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1088 KAHEEQLKEAQA-----VPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQE------------------VGER 1144
Cdd:TIGR02169 335 LAEIEELEREIEeerkrRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREkleklkreinelkreldrLQEE 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1145 LQQRHGER---DVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQ---AM 1218
Cdd:TIGR02169 415 LQRLSEELadlNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQrelAE 494
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1219 VLADSRAVREQLRQEKALLEEIERHGEKV-------------------------------------EECQRFAKQY---- 1257
Cdd:TIGR02169 495 AEAQARASEERVRGGRAVEEVLKASIQGVhgtvaqlgsvgeryataievaagnrlnnvvveddavaKEAIELLKRRkagr 574
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1258 -----INAIK---------------DYELQLVTYKAQLEPVASPAKKpkvqsgsESVIQEYVDLRTRY------------ 1305
Cdd:TIGR02169 575 atflpLNKMRderrdlsilsedgviGFAVDLVEFDPKYEPAFKYVFG-------DTLVVEDIEAARRLmgkyrmvtlege 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1306 ----SELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAEERErLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRmQ 1380
Cdd:TIGR02169 648 lfekSGAMTGGSRAPRGgILFSRSEPAELQRLRERLEGLKRE-LSSLQSELRRIENRLDELSQELSDASRKIGEIEKE-I 725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1381 EEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEE------------IRVVRLQLETTER 1448
Cdd:TIGR02169 726 EQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlearlshsrIPEIQAELSKLEE 805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1449 QRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK---RQAEAELAVRVKAEAEAAREKQRALQALEEfRL 1525
Cdd:TIGR02169 806 EVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIksiEKEIENLNGKKEELEEELEELEAALRDLES-RL 884
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1526 QAEEAERRLRQAEAERARQVQVALETAQRSAEV---ELQSKRASFAEKTAQLERTLQEE 1581
Cdd:TIGR02169 885 GDLKKERDELEAQLRELERKIEELEAQIEKKRKrlsELKAKLEALEEELSEIEDPKGED 943
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
22-123 |
3.54e-10 |
|
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409066 [Multi-domain] Cd Length: 114 Bit Score: 60.28 E-value: 3.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 22 KKTFTKWVNKHL-----IKHWRAEAQRHiSDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDY 91
Cdd:cd21217 3 KEAFVEHINSLLaddpdLKHLLPIDPDG-DDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNA 81
|
90 100 110
....*....|....*....|....*....|..
gi 2124423190 92 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 123
Cdd:cd21217 82 AKKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1389-1588 |
3.99e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 65.17 E-value: 3.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1389 AAVDAQQQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAE 1468
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1469 AQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF---------RLQAEEAERRLRQAEA 1539
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLaparreqaeELRADLAELAALRAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124423190 1540 ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1588
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAEL 218
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1699-2231 |
5.41e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.22 E-value: 5.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1699 RLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEASRF 1778
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1779 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKE---AENERLRRLA 1852
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1853 EDEAFQRRRLEEQA---AQHKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEILALK-------VSFEKA 1919
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRerfgdapVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1920 AAGKAELELELGRIRSNA---EDTLRSKEQAELEAMRQRQ----------LAAEEEQRRREAEERVQKSLAAEEEAARQR 1986
Cdd:PRK02224 411 EDFLEELREERDELREREaelEATLRTARERVEEAEALLEagkcpecgqpVEGSPHVETIEEDRERVEELEAELEDLEEE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1987 KAALEE-VERLKAKVEEARRLRERAEQESArqlqLAQDAAQKRLQAEEKAHAfavqqkeqelqqtlqqeqsmLERLRgea 2065
Cdd:PRK02224 491 VEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEKRER--------------------AEELR--- 543
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2066 eaarRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAA 2145
Cdd:PRK02224 544 ----ERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREALA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2146 DAEMEKHKKFAEQTLRqKAQVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRSQVEEELFSLRVQME 2220
Cdd:PRK02224 620 ELNDERRERLAEKRER-KRELEAEFDEARIEEAREDKERAEeyleqVEEKLDELREERDDLQAEIGAVENELEELEELRE 698
|
570
....*....|.
gi 2124423190 2221 ELGKLKARIEA 2231
Cdd:PRK02224 699 RREALENRVEA 709
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
16-120 |
7.16e-10 |
|
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: 59.36 E-value: 7.16e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 16 ERDRvQKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQI 87
Cdd:cd21300 4 EGER-EARVFTLWLNS-------LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNY 75
|
90 100 110
....*....|....*....|....*....|...
gi 2124423190 88 ALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIW 120
Cdd:cd21300 76 AVELGKQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
999-1584 |
8.55e-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: 65.74 E-value: 8.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 999 RECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTLGKL-EQVRSLSAIYLEklktislvi 1077
Cdd:COG3096 522 AELEQRLRQQQNAERLLEEFCQRIGQQLDAAEEL----------EELLAELEAQLEELeEQAAEAVEQRSE--------- 582
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1078 rsthgaeevLKAHEEQLKE-AQAVPATLPELEATKAALKKLRAQAEAQqpmfdalrdeLRGAQEVGERLQQRHgERDVEV 1156
Cdd:COG3096 583 ---------LRQQLEQLRArIKELAARAPAWLAAQDALERLREQSGEA----------LADSQEVTAAMQQLL-EREREA 642
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1157 ERWRERVAQllerwqavlaqtdlRQRELEQLGRQLRYYRESADP--------LGAWL----------QDA----KRRQEQ 1214
Cdd:COG3096 643 TVERDELAA--------------RKQALESQIERLSQPGGAEDPrllalaerLGGVLlseiyddvtlEDApyfsALYGPA 708
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1215 IQAMVLADSRAVREQLRQEKALLEE---IERHGEKVEECQRFAKQYINAI--KDYELQLVTYKAQLEPV----ASPAKKP 1285
Cdd:COG3096 709 RHAIVVPDLSAVKEQLAGLEDCPEDlylIEGDPDSFDDSVFDAEELEDAVvvKLSDRQWRYSRFPEVPLfgraAREKRLE 788
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1286 KVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAAVEAALEKQRQlAEAHAQAK 1365
Cdd:COG3096 789 ELRAERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQ 865
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1366 AQAEQEAQELQRRMQEEV---------ARREEAAVD---AQQQKRSIQEELQHLRQSSE--AEIQAKARQVEAAERSRLR 1431
Cdd:COG3096 866 LDQLKEQLQLLNKLLPQAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQ 945
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1432 IEEEIRVVRLQL----ETTER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDETQrkRQAE 1496
Cdd:COG3096 946 AKEQQRRLKQQIfalsEVVQRrphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ--VLAS 1023
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1497 AELAVRVKAE--AEAARE-KQRALQALEEFRLQAEEAERRLRQA-EAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1572
Cdd:COG3096 1024 LKSSRDAKQQtlQELEQElEELGVQADAEAEERARIRRDELHEElSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDY 1103
|
650
....*....|..
gi 2124423190 1573 QLERTLQEEHVA 1584
Cdd:COG3096 1104 KQEREQVVQAKA 1115
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1663-2314 |
8.77e-10 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 65.32 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1742
Cdd:COG4913 245 EDAREQIELLEPIRELAERYAAARER---LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDAL 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1743 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1822
Cdd:COG4913 322 REELDELEAQIRGNGGDRLEQLEREIERLEREL---EERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1823 AIGEATRLKTEAEIALKEKEAENERLRRlaedeafQRRRLEeqaaQHKADIEERLAQLRKA-------SESEL------- 1888
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEA-------EIASLE----RRKSNIPARLLALRDAlaealglDEAELpfvgeli 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1889 ------ERQKGLVEDTLRQRRQ---VEEEILA------------LKVSFEKAAAGKAE---------------------- 1925
Cdd:COG4913 468 evrpeeERWRGAIERVLGGFALtllVPPEHYAaalrwvnrlhlrGRLVYERVRTGLPDperprldpdslagkldfkphpf 547
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1926 ---LELELGR----IRSNAEDTLRSKEQAeleAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKA 1998
Cdd:COG4913 548 rawLEAELGRrfdyVCVDSPEELRRHPRA---ITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALEAELAELEE 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1999 KVEEArrlreraeQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLqqeqsmLERLRGEAEAARRAAEEAEEA 2078
Cdd:COG4913 625 ELAEA--------EERLEALEAELDALQERREALQRLAEYSWDEIDVASAERE------IAELEAELERLDASSDDLAAL 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2079 RERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFAEQ 2158
Cdd:COG4913 691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELREN 770
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2159 TLRQKAQVEQELTTLRLQLEET-------------DHQKSILD-----EELQRLKAEVTEAARQR------SQVEEELFS 2214
Cdd:COG4913 771 LEERIDALRARLNRAEEELERAmrafnrewpaetaDLDADLESlpeylALLDRLEEDGLPEYEERfkellnENSIEFVAD 850
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2215 LRVQM-EELGKLKARIEAENRalILRDKD-NTQRVLQEEAEKMKHvaEEAARLSVAAQEAARLRELAEEDLAQQRALAEK 2292
Cdd:COG4913 851 LLSKLrRAIREIKERIDPLND--SLKRIPfGPGRYLRLEARPRPD--PEVREFRQELRAVTSGASLFDEELSEARFAALK 926
|
730 740
....*....|....*....|..
gi 2124423190 2293 MLKEKMQAVQEATRLKAEAELL 2314
Cdd:COG4913 927 RLIERLRSEEEESDRRWRARVL 948
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1352-1573 |
9.24e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 64.06 E-value: 9.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1352 EKQRQLAEAHAQAKAQAEQEAQELQRRM---QEEVARREEAAVDAQQQKRSIQEELQhlrQSSEAEIQAKARQVEAAERS 1428
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQaaeQERLKQLEKERLAAQEQKKQAEEAAK---QAALKQKQAEEAAAKAAAAA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1429 RLRieeeirvvrlqletterqrggAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDETQRKRQAEAELAVRVKAEA 1507
Cdd:PRK09510 146 KAK---------------------AEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAAAEA 199
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1508 EAAREKQRALQAleefrlqAEEAErrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1573
Cdd:PRK09510 200 KKKAEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1360-1819 |
1.03e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 65.04 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1360 AHAQAKAQAEQEAQELQRRMQEEVARReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVV 1439
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLAL---AERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1440 RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQA 1519
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1520 LEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQ 1599
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1600 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1679
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1680 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1759
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1760 SRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1819
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1715-2447 |
1.20e-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: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1715 EEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLR---AL 1791
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIErqlAS 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1792 AEEAKRQRQLAEEDAARQRAEAERVLAEKLAAI-----GEATRLKTEaeiaLKEKEAENERLRRLAEDEAFQRRRLEEQA 1866
Cdd:TIGR02169 249 LEEELEKLTEEISELEKRLEEIEQLLEELNKKIkdlgeEEQLRVKEK----IGELEAEIASLERSIAEKERELEDAEERL 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1867 AQHKADIEERLAQLRKaSESELERQKglvedtlRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 1946
Cdd:TIGR02169 325 AKLEAEIDKLLAEIEE-LEREIEEER-------KRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEK 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1947 AELEaMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALE-EVERLKAKVEEARRLRER------AEQESARQLQ 2019
Cdd:TIGR02169 397 LKRE-INELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEeEKEDKALEIKKQEWKLEQlaadlsKYEQELYDLK 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2020 LAQDAAQKRLQA--EEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQ--VEE 2095
Cdd:TIGR02169 476 EEYDRVEKELSKlqRELAEAEAQARASEERVRGGRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGNRLNnvVVE 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2096 AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAL---------------------------RQKQAADAE 2148
Cdd:TIGR02169 556 DDAVAKEAIELLKRRKAGRATFLPLNKMRDERRDLSILSEDGVIgfavdlvefdpkyepafkyvfgdtlvvEDIEAARRL 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2149 MEK--------------------HKKFAEQTLRQKAQVEqELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV 2208
Cdd:TIGR02169 636 MGKyrmvtlegelfeksgamtggSRAPRGGILFSRSEPA-ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDA 714
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2209 EEELFSLRVQMEELGKlKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARL-----SVAAQEAARLRELAEEDL 2283
Cdd:TIGR02169 715 SRKIGEIEKEIEQLEQ-EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELeedlhKLEEALNDLEARLSHSRI 793
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2284 AQQRALAEKMlkEKMQAVQEATRLKAEAELlqQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAE 2363
Cdd:TIGR02169 794 PEIQAELSKL--EEEVSRIEARLREIEQKL--NRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEE 869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2364 AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQsdhdaerLRQAIAELEREKEK 2443
Cdd:TIGR02169 870 LEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEA-------LEEELSEIEDPKGE 942
|
....
gi 2124423190 2444 LKQE 2447
Cdd:TIGR02169 943 DEEI 946
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1511-1863 |
1.22e-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: 64.76 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1511 REKQRALQALEEFRLQaEEAERRLRqaEAERARQvqvaLETAQRSAEVELQSKRASFAEKtaqlERTLQEEHvavaqlre 1590
Cdd:pfam17380 287 RQQQEKFEKMEQERLR-QEKEEKAR--EVERRRK----LEEAEKARQAEMDRQAAIYAEQ----ERMAMERE-------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1591 eaerraqqqaeaerareeaeRELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRrgKAEEQAVRQRE 1670
Cdd:pfam17380 348 --------------------RELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERV--RQELEAARKVK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1671 LaeQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQ-QRQLLEEELARLQHEAAAATQKRQ-------ELEAELAKV 1742
Cdd:pfam17380 406 I--LEEERQRKIQQ--------QKVEMEQIRAEQEEARQrEVRRLEEERAREMERVRLEEQERQqqverlrQQEEERKRK 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1743 RAEMEVLLASKARAEEESRSTSEKskqrlEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLAE 1819
Cdd:pfam17380 476 KLELEKEKRDRKRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEME 549
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2124423190 1820 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1863
Cdd:pfam17380 550 ERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1702-2263 |
1.36e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 64.70 E-value: 1.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1702 AETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEASRFR 1779
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1780 E-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIA-----LKEKEAENERLRRLAE 1853
Cdd:PRK03918 266 ErIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINgieerIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1854 DEAFQRRRLEEQAAQHKA--DIEERLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEILALKvsfekaaAGKAELE 1927
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEISKIT-------ARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1928 LELGRIRSNAEDTLRSK-----------EQAELEAMRQRQLAAEEeqrrreaeerVQKSLAAEEEAARQRKAALEEVERL 1996
Cdd:PRK03918 419 KEIKELKKAIEELKKAKgkcpvcgreltEEHRKELLEEYTAELKR----------IEKELKEIEEKERKLRKELRELEKV 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1997 KAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAfaVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAE 2076
Cdd:PRK03918 489 LKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEK--LKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLD 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2077 EAREraereaaqsrrqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKKFA 2156
Cdd:PRK03918 567 ELEE-------------ELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2157 EQTLRQKA--QVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARI 2229
Cdd:PRK03918 634 ELAETEKRleELRKELEELEKKYSEEEYEELReeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
570 580 590
....*....|....*....|....*....|....
gi 2124423190 2230 EAENRALilrdkDNTQRvLQEEAEKMKHVAEEAA 2263
Cdd:PRK03918 714 EKLEKAL-----ERVEE-LREKVKKYKALLKERA 741
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1323-1539 |
1.57e-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: 1.57e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1323 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1402
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1403 ---ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEae 1479
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE-- 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 1480 rlRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF--RLQAEEAERRLRQAEA 1539
Cdd:COG4942 187 --RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAA 246
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1084-1274 |
1.73e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 60.92 E-value: 1.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1084 EEVLKAHEEQLKEAQaVPATLPELEATKAALKKLRAQAEAQQPMFDALrdelrgaQEVGERLQQRHGERDVEVerwRERV 1163
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1164 AQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADpLGAWLQDAKRRQEQIQamVLADSRAVREQLRQEKALLEEIERH 1243
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|.
gi 2124423190 1244 GEKVEECQRFAKQYINAIKDYELQLVTYKAQ 1274
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1671-1902 |
2.43e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 62.56 E-value: 2.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1671 LAEQELEKQRQLAEGTAQqrlAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAelakvraemevll 1750
Cdd:TIGR02794 47 AVAQQANRIQQQKKPAAK---KEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQA------------- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1751 askARAEEESRSTSEKSKQRLEAEASRfrelAEEAARLRALAEEAKRQrqlAEEDAARQRAEAervlAEKLAaigEATRL 1830
Cdd:TIGR02794 111 ---AKQAEEKQKQAEEAKAKQAAEAKA----KAEAEAERKAKEEAAKQ---AEEEAKAKAAAE----AKKKA---EEAKK 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1831 KTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIE----ERLAQLRKASESELERQKGLVEDTLRQR 1902
Cdd:TIGR02794 174 KAEAE-AKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEaaaaAAAEAERKADEAELGDIFGLASGSNAEK 248
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
141-243 |
3.05e-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: 57.77 E-value: 3.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 141 TAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 219
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 2124423190 220 PEDVDVPQPDEKSIITYVSSLYDA 243
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4369-4407 |
3.07e-09 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 55.03 E-value: 3.07e-09
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 4369 FLEVQYLTGGLIEPDVPGRVPLDEALQRGTVDARTAQKL 4407
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1660-2037 |
3.31e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 63.25 E-value: 3.31e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE--QQRQLLEEELARLQHEAAAATQKRQELEA 1737
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPlyQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1738 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAE------EDAARQRA 1811
Cdd:COG4717 161 LEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEeeleqlENELEAAA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1812 EAERVLAEKLAAIGEATRLKTEAEIAL------------------------------KEKEAENERLRRLAEDEAFQRRR 1861
Cdd:COG4717 241 LEERLKEARLLLLIAAALLALLGLGGSllsliltiagvlflvlgllallflllarekASLGKEAEELQALPALEELEEEE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1862 LEEQAAQHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEILALKVSFEKAAAGKAElelelgRIRSNAEDT 1940
Cdd:COG4717 321 LEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQA 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1941 LRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAE-EEAARQRKAALEEVERLKAKVEEAR-RLRERAEQESARQL 2018
Cdd:COG4717 395 EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEaELEQLEEDGELAEL 474
|
410
....*....|....*....
gi 2124423190 2019 QLAQDAAQKRLQAEEKAHA 2037
Cdd:COG4717 475 LQELEELKAELRELAEEWA 493
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1659-1902 |
3.80e-09 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 61.79 E-value: 3.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1659 GKAEEQAVRQRelAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARlQHEAAAATQKRQELEAE 1738
Cdd:TIGR02794 46 GAVAQQANRIQ--QQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAK-QAEQAAKQAEEKQKQAE 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1739 LAKVRAEMEVLLASKARAEeesRSTSEKSKQRLEAEAsrfreLAEEAARLRALAEEAKRQRqlaeEDAARQRAEAER-VL 1817
Cdd:TIGR02794 123 EAKAKQAAEAKAKAEAEAE---RKAKEEAAKQAEEEA-----KAKAAAEAKKKAEEAKKKA----EAEAKAKAEAEAkAK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1818 AEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVED 1897
Cdd:TIGR02794 191 AEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQ 270
|
....*
gi 2124423190 1898 TLRQR 1902
Cdd:TIGR02794 271 AIQQN 275
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1307-1522 |
5.08e-09 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 62.20 E-value: 5.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1307 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAAVEAAlEKQRQLAEAHAQAKAQ------AEQEAqEL 1375
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAIA-QANREAEEAELEQEREietariAEAEA-EL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1376 QRRMQEEVARREEAAVDAQQQKRsIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqLETTERQRggAEG 1455
Cdd:COG2268 247 AKKKAEERREAETARAEAEAAYE-IAEANAEREVQRQLEIAEREREIELQEKEAEREEAE-------LEADVRKP--AEA 316
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1456 ELQALRARAEeAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEE 1522
Cdd:COG2268 317 EKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDK 382
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1333-1531 |
5.66e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 61.75 E-value: 5.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1333 AEQQRAEE-RERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREeaavdAQQQKrsiQEELQHLRQSS 1411
Cdd:PRK09510 72 KSAKRAEEqRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQA-----ALKQK---QAEEAAAKAAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1412 EAEIQAKARQVEAAERSRlRIEEEIRvVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrrqVQDETQR 1491
Cdd:PRK09510 144 AAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK----AAAEAKK 217
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2124423190 1492 KRQAEAELAV-RVKAEAEAAREKQRALQALEEFRLQAEEAE 1531
Cdd:PRK09510 218 KAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4291-4328 |
5.85e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 54.03 E-value: 5.85e-09
10 20 30
....*....|....*....|....*....|....*...
gi 2124423190 4291 QRLLEAQACTGGIIDPNTGERFPVTDAVNKGLVDKIMV 4328
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1416-1637 |
6.06e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 61.32 E-value: 6.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1416 QAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQA 1495
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1496 EAELAVRVKAEAEAAREKQR-ALQALEEFRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1573
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1574 LERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQK 1637
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAE 241
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1078-1814 |
6.16e-09 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 62.67 E-value: 6.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1078 RSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpmfdaLRDELRGAQEvGERLQQRHGERDVEVE 1157
Cdd:PRK04863 287 EALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQA-------ASDHLNLVQT-ALRQQEKIERYQADLE 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1158 RWRERvaqlLERWQAVLAQTDLRQRELEqlgRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVReQLRQEKALL 1237
Cdd:PRK04863 359 ELEER----LEEQNEVVEEADEQQEENE---ARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAVQ-ALERAKQLC 430
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1238 E----EIERHGEKVEECQRFAKQYINAIKDYELQLVTYKA---QLEPVASPAKK-------PKVQSGSESVIQEYVDLRT 1303
Cdd:PRK04863 431 GlpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahsQFEQAYQLVRKiagevsrSEAWDVARELLRRLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1304 RYSELTTLTSQYikfisETLRRMEEEERLAEQQRAEERERL-------AAVEAALEKQRQLAEAHAQAKAQA-------E 1369
Cdd:PRK04863 511 LAEQLQQLRMRL-----SELEQRLRQQQRAERLLAEFCKRLgknlddeDELEQLQEELEARLESLSESVSEArerrmalR 585
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1370 QEAQELQRRMQEEVARREE--AAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTE 1447
Cdd:PRK04863 586 QQLEQLQARIQRLAARAPAwlAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLS 665
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1448 rQRGGAEGE-LQALRAR-----------------AEEAEA---QKRQA--QEEAERLRRQVQDET-------------QR 1491
Cdd:PRK04863 666 -QPGGSEDPrLNALAERfggvllseiyddvsledAPYFSAlygPARHAivVPDLSDAAEQLAGLEdcpedlyliegdpDS 744
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1492 KRQA-----EAELAVRVK-AEAE--------------AAREKQralqaLEEFRLQAEEAERRLRQAEAERaRQVQVALET 1551
Cdd:PRK04863 745 FDDSvfsveELEKAVVVKiADRQwrysrfpevplfgrAAREKR-----IEQLRAEREELAERYATLSFDV-QKLQRLHQA 818
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1552 AQR------------SAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlK 1619
Cdd:PRK04863 819 FSRfigshlavafeaDPEAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLPRLNLLADETLA----D 894
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1620 ANEALRLRLQAEEVAQQkSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQ--------------LAE 1684
Cdd:PRK04863 895 RVEEIREQLDEAEEAKR-FVQQHGNALAQLEPIVSVLQSDPEQFEQLKQDyQQAQQTQRDAKQqafaltevvqrrahFSY 973
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1685 GTAQQRLAAEQEL-IRLRAETEQGEQQRQLLEEEL--------------ARLQHEAAAATQKRQELEAELAK--VRAEme 1747
Cdd:PRK04863 974 EDAAEMLAKNSDLnEKLRQRLEQAEQERTRAREQLrqaqaqlaqynqvlASLKSSYDAKRQMLQELKQELQDlgVPAD-- 1051
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1748 vllaskARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1814
Cdd:PRK04863 1052 ------SGAEERARARRDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVV 1112
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
136-238 |
6.40e-09 |
|
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: 56.71 E-value: 6.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 136 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 214
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 2124423190 215 TRLLDPEDVDVPQPDEKSIITYVS 238
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1458-1983 |
7.09e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 62.57 E-value: 7.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1458 QALRARA-EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREkqRALQALEEFRLQAEEAERR--- 1533
Cdd:COG3899 714 RALARGAyAEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLE--RALAARALAALAALRHGNPpas 791
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1534 ----------LRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAE 1603
Cdd:COG3899 792 arayanlgllLLGDYEEAYEFGELALALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALL 871
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1604 RAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1683
Cdd:COG3899 872 ALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAA 951
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1684 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSt 1763
Cdd:COG3899 952 AALAAALALAAAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAA- 1030
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1764 sekskqRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA 1843
Cdd:COG3899 1031 ------AAAAALLAAAAALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAA 1104
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1844 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGK 1923
Cdd:COG3899 1105 LALAAALAALALAAALAALALAAAARAAAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLA 1184
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1924 AELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAA 1983
Cdd:COG3899 1185 AAAAAAAAAALLAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
504-693 |
7.34e-09 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 59.00 E-value: 7.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 504 LRYLQDLLAWVEENQRRVDGAEWGVDLPSVEAQLGSHRGLHHSIEEFRAKIERARTDEGQLSPATRGAY---RDCLGRLD 580
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 581 LQYAKLLNSSKGRLRSLE---SLYSFVAAATKELMWLSEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEI 657
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 2124423190 658 QNTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 693
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1665-2433 |
7.68e-09 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 62.66 E-value: 7.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1665 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQhEAAAATQK----RQ 1733
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEKieryQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1734 ELEAELAKVRAEMEVLLASkaraeEESRSTSEKSKQRLEAEASRFR-ELAE-----EAARLRALA--------EEAKRQR 1799
Cdd:COG3096 355 DLEELTERLEEQEEVVEEA-----AEQLAEAEARLEAAEEEVDSLKsQLADyqqalDVQQTRAIQyqqavqalEKARALC 429
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1800 QL-------AEEDAARQRAEAERVLAEKLAAigeATRLkTEAEIALKEKEAENERLRRLAED----EAFQR-RRLEEQAA 1867
Cdd:COG3096 430 GLpdltpenAEDYLAAFRAKEQQATEEVLEL---EQKL-SVADAARRQFEKAYELVCKIAGEversQAWQTaRELLRRYR 505
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1868 QHKAdIEERLAQLRkASESELERQkglvedtLRQRRQVEEEILALKVSFEKAAAGKAELELelgrirsnaedtlrskEQA 1947
Cdd:COG3096 506 SQQA-LAQRLQQLR-AQLAELEQR-------LRQQQNAERLLEEFCQRIGQQLDAAEELEE----------------LLA 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1948 ELEAMRQRqlaaeeeqrrreaeervqksLAAEEEAARQRKAALE-EVERLKAKVEEarrLRERAEQESARQLQLAQDAAQ 2026
Cdd:COG3096 561 ELEAQLEE--------------------LEEQAAEAVEQRSELRqQLEQLRARIKE---LAARAPAWLAAQDALERLREQ 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2027 krlQAEEKAHAFAVQQkeqelqqtlqQEQSMLERLRGeaeaarraaeeaeeaRERAEREAAQSRRQVE-EAERLKQSAEE 2105
Cdd:COG3096 618 ---SGEALADSQEVTA----------AMQQLLERERE---------------ATVERDELAARKQALEsQIERLSQPGGA 669
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2106 QAQAQAQAQAAAE------------------------KLRKEAEQEAARRAQAEQAAL-----------RQKQAADA--- 2147
Cdd:COG3096 670 EDPRLLALAERLGgvllseiyddvtledapyfsalygPARHAIVVPDLSAVKEQLAGLedcpedlylieGDPDSFDDsvf 749
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2148 ---EMEK------------HKKFAEQTLRQKAQVEQELTTLRLQLEETD---HQKSILDEELQRL--------------- 2194
Cdd:COG3096 750 daeELEDavvvklsdrqwrYSRFPEVPLFGRAAREKRLEELRAERDELAeqyAKASFDVQKLQRLhqafsqfvgghlava 829
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2195 -----KAEVTEAARQRSQVEEELFSLRVQM----EELGKLKARIEAENRAL----ILRDKDNTQRVlqEEAEKMKHVAEE 2261
Cdd:COG3096 830 fapdpEAELAALRQRRSELERELAQHRAQEqqlrQQLDQLKEQLQLLNKLLpqanLLADETLADRL--EELREELDAAQE 907
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2262 AAR-----------------------LSVAAQEAARLRELAEEDLAQQRALAekmLKEKMQ-----AVQEATRLKAEA-- 2311
Cdd:COG3096 908 AQAfiqqhgkalaqleplvavlqsdpEQFEQLQADYLQAKEQQRRLKQQIFA---LSEVVQrrphfSYEDAVGLLGENsd 984
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2312 --ELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQrTLEAERQRQLEMSAEAERlklRVAEMS-RAQARAEEDAQRF 2388
Cdd:COG3096 985 lnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLA-SLKSSRDAKQQTLQELEQ---ELEELGvQADAEAEERARIR 1060
|
890 900 910 920
....*....|....*....|....*....|....*....|....*
gi 2124423190 2389 RKqaeEIGEKLHRTElatQEKVTLVQTLEIQRQQSDHDAERLRQA 2433
Cdd:COG3096 1061 RD---ELHEELSQNR---SRRSQLEKQLTRCEAEMDSLQKRLRKA 1099
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1695-2544 |
9.68e-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: 62.01 E-value: 9.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1695 QELIRLRAETEQGEQQRQLLEE-----------ELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1763
Cdd:TIGR02169 198 QQLERLRREREKAERYQALLKEkreyegyellkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEEL 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1764 SEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAaigEATRLKTEAEIALKEKEA 1843
Cdd:TIGR02169 278 NKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEERKRRDK 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1844 ENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE---SELERQKGLVEDTLRQRRQVEEEILALKVSFEKAA 1920
Cdd:TIGR02169 355 LTEEYAELKEELEDLRAELEEVDKEFAETRDE-LKDYREKLEklkREINELKRELDRLQEELQRLSEELADLNAAIAGIE 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1921 AGKAELELEL-----------GRIRSNAEDtlRSKEQAELEAMRQRQlaaeeeqrrrEAEERVQKSLAAEEEAARQRKAA 1989
Cdd:TIGR02169 434 AKINELEEEKedkaleikkqeWKLEQLAAD--LSKYEQELYDLKEEY----------DRVEKELSKLQRELAEAEAQARA 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1990 LEEVERLKAKVEEARRLRERAEQESARQL-------QLA-QDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLErL 2061
Cdd:TIGR02169 502 SEERVRGGRAVEEVLKASIQGVHGTVAQLgsvgeryATAiEVAAGNRLNNVVVEDDAVAKEAIELLKRRKAGRATFLP-L 580
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2062 RGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRkeaeqeaarRAQAEQAALRQ 2141
Cdd:TIGR02169 581 NKMRDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDIEAARRLMGKYR---------MVTLEGELFEK 651
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2142 KQAADAEMEKHKKFAEQTLRQKAQVEQelttLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEE 2221
Cdd:TIGR02169 652 SGAMTGGSRAPRGGILFSRSEPAELQR----LRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQ 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2222 LGKlKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLsvaaqeaarlrelaEEDLAQ-QRALAEKMLKEKMQA 2300
Cdd:TIGR02169 728 LEQ-EEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEEL--------------EEDLHKlEEALNDLEARLSHSR 792
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2301 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2380
Cdd:TIGR02169 793 IPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEE 872
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2381 AEEDAQRFRKQAEEIGEKlhRTELATQEKVtlvqtLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2460
Cdd:TIGR02169 873 LEAALRDLESRLGDLKKE--RDELEAQLRE-----LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2461 VQQEQllqetqalqqsfLSEKDTLLQRERfIEQEKAKLEQ---LFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEA 2537
Cdd:TIGR02169 946 IPEEE------------LSLEDVQAELQR-VEEEIRALEPvnmLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEY 1012
|
....*..
gi 2124423190 2538 RQRQREA 2544
Cdd:TIGR02169 1013 EKKKREV 1019
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1635-1830 |
1.07e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.59 E-value: 1.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1635 QQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1714
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1715 EEELARLQHEAAAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEE 1794
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 2124423190 1795 AKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1830
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
145-240 |
1.08e-08 |
|
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated protein (ASPM) and similar proteins; ASPM, also called abnormal spindle protein homolog, or Asp homolog, is involved in mitotic spindle regulation and coordination of mitotic processes. It may also have a preferential role in regulating neurogenesis. Members of this family contain two copies of CH domain in the middle region. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409073 [Multi-domain] Cd Length: 138 Bit Score: 56.54 E-value: 1.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 145 KLLL-WSQrMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 200
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 201 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 240
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1472-1992 |
1.09e-08 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 61.85 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1472 RQAQEEAERLRRQVQ-----DETQRKRQAEAELAVRVKAEAEAAR--EKQRALQALEEfRLQAEEAERRLRQAEAERARQ 1544
Cdd:COG4913 238 ERAHEALEDAREQIEllepiRELAERYAAARERLAELEYLRAALRlwFAQRRLELLEA-ELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1545 VQVALETAQRSAEVELQSkrasfaEKTAQLERtLQEEhvavaqlreeaerraqqqaeaerareeaereLERWQLKANEAL 1624
Cdd:COG4913 317 RLDALREELDELEAQIRG------NGGDRLEQ-LERE-------------------------------IERLERELEERE 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1625 RLRLQAEEVAQQKSLAQAEAEKQKEeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1704
Cdd:COG4913 359 RRRARLEALLAALGLPLPASAEEFA----------ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEI 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1705 EQGEQQRQLLEEELARLQHEAAAATQ-KRQELE--AELAKVRAE-------MEVLLASKAR------------------- 1755
Cdd:COG4913 429 ASLERRKSNIPARLLALRDALAEALGlDEAELPfvGELIEVRPEeerwrgaIERVLGGFALtllvppehyaaalrwvnrl 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1756 ---------------AEEESRSTSEKS-KQRLEAEASRFR-----ELAEEAARLRALAEEA------------------- 1795
Cdd:COG4913 509 hlrgrlvyervrtglPDPERPRLDPDSlAGKLDFKPHPFRawleaELGRRFDYVCVDSPEElrrhpraitragqvkgngt 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1796 ----KRQRQLAEE-----DAARQRAEAERVLAEKLAAIGEATRLKTEAEialKEKEAENERLRRLAEDEAFQRRRLEEQA 1866
Cdd:COG4913 589 rhekDDRRRIRSRyvlgfDNRAKLAALEAELAELEEELAEAEERLEALE---AELDALQERREALQRLAEYSWDEIDVAS 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1867 AQHK-ADIEERLAQLRKAS------ESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAED 1939
Cdd:COG4913 666 AEREiAELEAELERLDASSddlaalEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARL 745
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1940 TLRskeqAELEAMRQRQLaaeeeqrRREAEERVQKSLAAEEEAARQRKAALEE 1992
Cdd:COG4913 746 ELR----ALLEERFAAAL-------GDAVERELRENLEERIDALRARLNRAEE 787
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1691-2544 |
1.09e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 61.73 E-value: 1.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1691 LAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEkskQR 1770
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELE---SR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1771 LEAEASRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLAEklaaigeATRLKTEAEIALKEKeaenerlrr 1850
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTE-------AKIKKLEEDILLLED--------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1851 laedeafQRRRLEEQAAQhkadIEERLAQLRKASESELERQKGLVEDTLRQrrqvEEEILALKVSFEKAAagKAELELEL 1930
Cdd:pfam01576 146 -------QNSKLSKERKL----LEERISEFTSNLAEEEEKAKSLSKLKNKH----EAMISDLEERLKKEE--KGRQELEK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1931 GRIRSNAEDTLRSKEQAELeamrqRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEarrLRERA 2010
Cdd:pfam01576 209 AKRKLEGESTDLQEQIAEL-----QAQIAELRAQLAKKEEELQAALARLEEETAQKNNALKKIRELEAQISE---LQEDL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2011 EQESArqlQLAQDAAQKRLQAEEkahafavqqkeqelqqtlqqeqsmLERLRGEAEAARRAAEEAEEARERAEREAAQSR 2090
Cdd:pfam01576 281 ESERA---ARNKAEKQRRDLGEE------------------------LEALKTELEDTLDTTAAQQELRSKREQEVTELK 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2091 RQVEEAERLKQSAEEqaqaqaqaqaaaeKLRKEAEQEAARRAQAeqaaLRQKQAADAEMEKHKKFAEQtlrQKAQVEQEL 2170
Cdd:pfam01576 334 KALEEETRSHEAQLQ-------------EMRQKHTQALEELTEQ----LEQAKRNKANLEKAKQALES---ENAELQAEL 393
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2171 TTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALilrDKD-------- 2242
Cdd:pfam01576 394 RTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKL---SKDvsslesql 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2243 -NTQRVLQEEAEKMKHVAeeaARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLqqqkELA 2321
Cdd:pfam01576 471 qDTQELLQEETRQKLNLS---TRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKKLEEDAGTL----EAL 543
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2322 QEQARRLQEDKEQMAQQLEQETQGFQR---------------TLEAERQRQL------------EMSAEAERLKLRVA-E 2373
Cdd:pfam01576 544 EEGKKRLQRELEALTQQLEEKAAAYDKlektknrlqqelddlLVDLDHQRQLvsnlekkqkkfdQMLAEEKAISARYAeE 623
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2374 MSRAQARAEEDAQRFRKQAEEIGEKL-HRTELATQEKVTL----------------VQTLEIQRQQSDHDAERLRQAIAE 2436
Cdd:pfam01576 624 RDRAEAEAREKETRALSLARALEEALeAKEELERTNKQLRaemedlvsskddvgknVHELERSKRALEQQVEEMKTQLEE 703
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2437 LEREKE-----KLKQEAKLLQLKSE---EMQTVQQEQLLQETQALQQsfLSEKDTLLQRER----FIEQEKAKLEQLFQD 2504
Cdd:pfam01576 704 LEDELQatedaKLRLEVNMQALKAQferDLQARDEQGEEKRRQLVKQ--VRELEAELEDERkqraQAVAAKKKLELDLKE 781
|
890 900 910 920
....*....|....*....|....*....|....*....|...
gi 2124423190 2505 ---EVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREA 2544
Cdd:pfam01576 782 leaQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEI 824
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1321-1543 |
1.13e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 60.24 E-value: 1.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLRRMEEEERLAEQQRAEERERLAAVE--AALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQqkr 1398
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKA--- 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1399 siQEELQHlrqssEAEIQAKARQVEAAERSRlrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRQAQEE- 1477
Cdd:TIGR02794 145 --KEEAAK-----QAEEEAKAKAAAEAKKKA-----------------------EEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1478 ---AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERAR 1543
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1323-1937 |
1.26e-08 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 61.74 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1323 LRRMEEEERLAEQQRAEERERLAAVEAA-----LEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQK 1397
Cdd:PRK10246 259 ASRRQQALQQALAAEEKAQPQLAALSLAqparqLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQS 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1398 RSIQEELQHLRQSseaeiqakarqveAAERSRLRIEEEirvvrlqletterqrggaegELQALRARAEEAEAQKRQAQEE 1477
Cdd:PRK10246 339 AELQAQQQSLNTW-------------LAEHDRFRQWNN--------------------ELAGWRAQFSQQTSDREQLRQW 385
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1478 AERLrrqvqDETQRKRQAEAELAVRVKA-EAEAAREKQRALQALEE--FRLQAEEAERRLRQAEAERARQvqvALETAQR 1554
Cdd:PRK10246 386 QQQL-----THAEQKLNALPAITLTLTAdEVAAALAQHAEQRPLRQrlVALHGQIVPQQKRLAQLQVAIQ---NVTQEQT 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1555 SAEVELQSKRASFAEKTAQLE--RTLQEEHVAVAQLrEEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEE 1632
Cdd:PRK10246 458 QRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDL-EAQRAQLQAGQPCPLCGSTSHPAVEAYQALEPGVNQSRLDALE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1633 vaQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1712
Cdd:PRK10246 537 --KEVKKLGEEGAALRGQLDALTKQLQRDESEAQSLRQ-EEQALTQQWQAVCASLNITLQPQDDIQPWLDAQEEHERQLR 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1713 LLEEELArLQHEAAAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESRSTSEKSKQRLEAEASRFRELAEEAA 1786
Cdd:PRK10246 614 LLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWLATRQQEAQSWQQRQNELTALQNRIQ 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1787 RLRALAEeakrqrQLAEEDAArqRAEAERVLAEKLAAIGEATrLKTEAEIALKEKEAENERlRRLAE-----DEAFQRRR 1861
Cdd:PRK10246 693 QLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQQDVLEA-QRLQKaqaqfDTALQASV 762
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1862 LEEQAAQHKADIEE----RLAQLRKASESELERQKGLVEdtlrQRRQVEEEILALKVSFEKAAAGKAELELEL----GRI 1933
Cdd:PRK10246 763 FDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVT----QTAQALAQHQQHRPDGLDLTVTVEQIQQELaqlaQQL 838
|
....
gi 2124423190 1934 RSNA 1937
Cdd:PRK10246 839 RENT 842
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
12-126 |
1.27e-08 |
|
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: 56.06 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 12 LVQDERDRVQ--KKTFTKWVNKHLikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNV 85
Cdd:cd21222 6 LFDEAPEKLAevKELLLQFVNKHL-----AKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNV 80
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423190 86 QIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 126
Cdd:cd21222 81 KLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2146-2677 |
1.33e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.52 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2146 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKaevtEAARQRSQVEEELFSLRVQMEELGKL 2225
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2226 KARIEAENRALILRDKdntQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELA----------EEDLAQQRALAEKMLK 2295
Cdd:TIGR00618 276 EAVLEETQERINRARK---AAPLAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLlmkraahvkqQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2296 EKMQAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLEQETQgfqrtlEAERQRQLEMSAEAERLKLRVAEMS 2375
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCK------ELDILQREQATIDTRTSAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2376 RAQARAEEDAQRFRKQAEEigekLHRTELATQEKVTLVQTLEIQrQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKS 2455
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCA----AAITCTAQCEKLEKIHLQESA-QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2456 EEmQTVQQEQLLQETQALQQSFLSEKDTllQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVAsME 2535
Cdd:TIGR00618 501 EE-PCPLCGSCIHPNPARQDIDNPGPLT--RRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSI-LT 576
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2536 EARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALaHSEEIAASQATAVKALpngrdap 2615
Cdd:TIGR00618 577 QCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRL-HLQQCSQELALKLTAL------- 648
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 2616 dgpateaepehafdglrqkvpaqrlqevgilsTEELQRLVQGRTTVAELAQREDVRRYLQGR 2677
Cdd:TIGR00618 649 --------------------------------HALQLTLTQERVREHALSIRVLPKELLASR 678
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
136-243 |
1.61e-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: 55.48 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 136 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 214
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 2124423190 215 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 243
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1338-1558 |
1.64e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 60.27 E-value: 1.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1338 AEERERLAAVEAALEKQRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVARREEAAvdAQQQKRSIQEELQhlRQSSEAEIQ 1416
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEAEAERETEiAIAQANREAEEAELEQEREIETARIAE--AEAELAKKKAEER--REAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1417 AKARQVEAAERSRLRIEEEIRVVRLQLETterqrggaegelqalraRAEEAEAQKRQAQEEAErlrrqvqdetqrkrqae 1496
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQLEIAEREREI-----------------ELQEKEAEREEAELEAD----------------- 309
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 1497 aelaVRVKAEAEAAREKQRALQALEEFRLQAE-EAERRLRQAEAERA-RQVQVALETAQRSAEV 1558
Cdd:COG2268 310 ----VRKPAEAEKQAAEAEAEAEAEAIRAKGLaEAEGKRALAEAWNKlGDAAILLMLIEKLPEI 369
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1341-1810 |
1.75e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 61.19 E-value: 1.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1341 RERLAAVEAALEKQRQLAEAHAqakAQAEQEAQELQRRMQEEVARREEAAVDaqqqkrSIQEELQHLRQSSEAEIqakAR 1420
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYL---ALAERAAAELRGPDQLAWLARLDAEHD------NLRAALRWALAHGDAEL---AL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1421 QVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1500
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1501 VRvkAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1580
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1581 EHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGK 1660
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1661 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1740
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1741 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1810
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1434-1871 |
1.97e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 60.55 E-value: 1.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1434 EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DETQRKRQAEAELAvrvkaeaeaar 1511
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQllPLYQELEALEAELA----------- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1512 EKQRALQALEEFRLQAEEAERRLRQAEAErarqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREE 1591
Cdd:COG4717 143 ELPERLEELEERLEELRELEEELEELEAE--------LAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1592 AERRAQQQAEAERAREEAERELERWQLKA--NEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQR 1669
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEErlKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1670 ELAEQELEKQRQLAEGTAQQRLaAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEME-- 1747
Cdd:COG4717 295 REKASLGKEAEELQALPALEEL-EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEia 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1748 -VLLASKARAEEESRSTSEKSKQRLEAEAsrfrELAEEAARLRALAEEAKRQRQLAEEDAARQR-AEAERVLAEKLAAIG 1825
Cdd:COG4717 374 aLLAEAGVEDEEELRAALEQAEEYQELKE----ELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 2124423190 1826 EATRLKTEAEIALKEKEaENERLRRLAEDEAFQRRRLEEQAAQHKA 1871
Cdd:COG4717 450 ELREELAELEAELEQLE-EDGELAELLQELEELKAELRELAEEWAA 494
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1660-1867 |
1.99e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.78 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAel 1739
Cdd:COG4942 41 KELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGR-- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1740 akvRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLA 1818
Cdd:COG4942 119 ---QPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKA 195
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124423190 1819 EKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1867
Cdd:COG4942 196 ERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1478-1934 |
2.01e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.80 E-value: 2.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1478 AERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQAleefRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1557
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1558 VELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQK 1637
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1638 SLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1717
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1718 LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKR 1797
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1798 QRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERL 1877
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1878 AQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIR 1934
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1859-2586 |
2.21e-08 |
|
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.
Pssm-ID: 426784 [Multi-domain] Cd Length: 1161 Bit Score: 60.76 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1859 RRRLEEQAA--QHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSN 1936
Cdd:pfam02463 155 RLEIEEEAAgsRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKL 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1937 AEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2016
Cdd:pfam02463 235 NEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2017 QLQLAQD---AAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLE-RLRGEAEAARRAAEEAEEARERAEREAAQSRRQ 2092
Cdd:pfam02463 315 KLKESEKekkKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEElEKLQEKLEQLEEELLAKKKLESERLSSAAKLKE 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2093 VEEAERLKQSAEEQAQAQAQAQAAAEKLRKeaeqeaarraqaeqaalrqKQAADAEMEKHKKFAEQTLRQKAQVEQELTT 2172
Cdd:pfam02463 395 EELELKSEEEKEAQLLLELARQLEDLLKEE-------------------KKEELEILEEEEESIELKQGKLTEEKEELEK 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2173 LRLQLEETDHQKSILDEELQRLKaevtEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEA 2252
Cdd:pfam02463 456 QELKLLKDELELKKSEDLLKETQ----LVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRL 531
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2253 EKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAvqeaTRLKAEAELLQQQKELAQEQARRLQEDK 2332
Cdd:pfam02463 532 GDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARK----LRLLIPKLKLPLKSIAVLEIDPILNLAQ 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2333 EQMAQQLEQETQGFQRTLEAERQRQLEMSaeaERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTL 2412
Cdd:pfam02463 608 LDKATLEADEDDKRAKVVEGILKDTELTK---LKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2413 VQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQalQQSFLSEKDTLLQRERFIE 2492
Cdd:pfam02463 685 AESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQ--KIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2493 QEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGvrrkqEELQLLEQQRQQQEKLLAEE 2572
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELL-----EEEQLLIEQEEKIKEEELEE 837
|
730
....*....|....
gi 2124423190 2573 NQRLRERLQRLEEE 2586
Cdd:pfam02463 838 LALELKEEQKLEKL 851
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1729-1880 |
2.64e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 59.89 E-value: 2.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1729 TQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEASRFRELAEEAARLRAlaEEAKRQRQLAEEDAAR 1808
Cdd:COG2268 215 AIAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIAE--ANAEREVQRQLEIAER 288
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1809 QR------AEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 1880
Cdd:COG2268 289 EReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKL 366
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
14-125 |
2.79e-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: 54.82 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 14 QDERDrvqKKTFTKWVNKhlikhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIA 88
Cdd:cd21299 1 ETSRE---ERCFRLWINS-------LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQV 70
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 89 LDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 125
Cdd:cd21299 71 VKIGKQLKFSLVNVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1244-2033 |
2.86e-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: 60.45 E-value: 2.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1244 GEKVEECQ---RFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFis 1320
Cdd:TIGR00606 199 GQKVQEHQmelKYLKQYKEKACEIRDQITSKEAQLE---------SSREIVKSYENELDPLKNRLKEIEHNLSKIMKL-- 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 etlrrmeEEERLAEQQRAEERERLaaveaalekQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1400
Cdd:TIGR00606 268 -------DNEIKALKSRKKQMEKD---------NSELELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKL 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1401 QEELQHLRQSS---EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRgGAEGELQALRARAEEAEAQKRQAQEE 1477
Cdd:TIGR00606 332 NKERRLLNQEKtelLVEQGRLQLQADRHQEHIRARDSLIQSLATRLELDGFER-GPFSERQIKNFHTLVIERQEDEAKTA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1478 AERLRRQVQDETQRKRQAE------AELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEaERARQVQVALET 1551
Cdd:TIGR00606 411 AQLCADLQSKERLKQEQADeirdekKGLGRTIELKKEILEKKQEELKFVIKELQQLEGSSDRILELD-QELRKAERELSK 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1552 AQRSAEVELQSKRA-SFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL---- 1626
Cdd:TIGR00606 490 AEKNSLTETLKKEVkSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDKDEQIRKIKSRHSDELTSLlgyf 569
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1627 --RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRE-LAEQELEKQRQLAEGTAQQrlAAEQELIRLRAE 1703
Cdd:TIGR00606 570 pnKKQLEDWLHSKSKEINQTRDRLAKLNKELASLEQNKNHINNELEsKEEQLSSYEDKLFDVCGSQ--DEESDLERLKEE 647
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1704 TEQGEQQRQLLE----------EELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR--- 1770
Cdd:TIGR00606 648 IEKSSKQRAMLAgatavysqfiTQLTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRrde 727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1771 ----LEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA------IGEATRLKTEAEIALKE 1840
Cdd:TIGR00606 728 mlglAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAkvcltdVTIMERFQMELKDVERK 807
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1841 KEAENERLRRLAEDEAFQRRRLEEQAAQHKAD------------IEERLAQLR--KASESELERQKGLVEDTLRQRRQVE 1906
Cdd:TIGR00606 808 IAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDtvvskielnrklIQDQQEQIQhlKSKTNELKSEKLQIGTNLQRRQQFE 887
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1907 E-------EILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAE 1979
Cdd:TIGR00606 888 EqlvelstEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDG 967
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 1980 EEAARQRK--------AALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2033
Cdd:TIGR00606 968 KDDYLKQKetelntvnAQLEECEKHQEKINEDMRLMRQDIDTQKIQERWLQDNLTLRKRENE 1029
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1324-1585 |
3.37e-08 |
|
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: 59.28 E-value: 3.37e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1324 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQ 1401
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1402 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqletterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1481
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1482 RRQVQDETQR-KRQA-EAELAVRVKAEAEAARE--KQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1557
Cdd:pfam15558 168 KVQENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 2124423190 1558 VELQSKRASFAEKTAQLERTLQEEHVAV 1585
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1833-2282 |
3.80e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 59.78 E-value: 3.80e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1833 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEqAAQHKADIEERLAQLRKASEselerqkglVEDTLRQRRQVEEEILAL 1912
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEE-LEAELEELREELEKLEKLLQ---------LLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1913 KVSFEKAAAGKAELElELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEqrrreaeerVQKSLAAEEEAARQRKAALEE 1992
Cdd:COG4717 145 PERLEELEERLEELR-ELEEELEELEAELAELQEELEELLEQLSLATEEE---------LQDLAEELEELQQRLAELEEE 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1993 VERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAA 2072
Cdd:COG4717 215 LEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2073 EEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAlRQKQAADAEMEKH 2152
Cdd:COG4717 295 REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELE-EELQLEELEQEIA 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2153 KKFA------EQTLRQKAQVEQELTTLRLQLEETDHQ-KSILDEELQRLKAEVTEAARQR-SQVEEELFSLRVQMEELGK 2224
Cdd:COG4717 374 ALLAeagvedEEELRAALEQAEEYQELKEELEELEEQlEELLGELEELLEALDEEELEEElEELEEELEELEEELEELRE 453
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 2225 LKARIEAENRALILRDK-DNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEED 2282
Cdd:COG4717 454 ELAELEAELEQLEEDGElAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1672-1880 |
3.93e-08 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 59.05 E-value: 3.93e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1672 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEmevllA 1751
Cdd:PRK09510 77 AEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAE-----A 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1752 SKARAEEESRSTSEKSKQRLEAEAsrfRELAEEAARLRALAEEAKrqrQLAEEDAARQRAEAERVlAEKLAAIGEATRLK 1831
Cdd:PRK09510 152 EAKRAAAAAKKAAAEAKKKAEAEA---AKKAAAEAKKKAEAEAAA---KAAAEAKKKAEAEAKKK-AAAEAKKKAAAEAK 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 2124423190 1832 TEAEIALKEKEAEnerlrrlAEDEAFQRRRLEEQAAQHKADIEERLAQL 1880
Cdd:PRK09510 225 AAAAKAAAEAKAA-------AEKAAAAKAAEKAAAAKAAAEVDDLFGGL 266
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1143-1450 |
4.43e-08 |
|
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: 59.75 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1143 ERLQQRHGERDVEVERWRervaQLLERWQAvlaqtdlRQRELEqlgRQLRYYRESAdplgawlQDAKRRQEQIQAMVLAD 1222
Cdd:pfam17380 299 ERLRQEKEEKAREVERRR----KLEEAEKA-------RQAEMD---RQAAIYAEQE-------RMAMERERELERIRQEE 357
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1223 SRAVREQLRQEKALLE-----EIERHGEKVEECQRFAKQYINAIKDYELQLV--TYKAQLEPVASPAKKPKVQSGSESVI 1295
Cdd:pfam17380 358 RKRELERIRQEEIAMEisrmrELERLQMERQQKNERVRQELEAARKVKILEEerQRKIQQQKVEMEQIRAEQEEARQREV 437
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1296 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEaalEKQRQLAEAHAQAKAQAEQEAQEL 1375
Cdd:pfam17380 438 RRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEEERK 514
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1376 QRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVeAAERSRLRIEEEIRVVRLQLETTERQR 1450
Cdd:pfam17380 515 RKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKA-TEERSRLEAMEREREMMRQIVESEKAR 588
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1394-1938 |
4.72e-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: 59.27 E-value: 4.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1394 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEeirvVRLQLE--TTERQRGGAEGELQALRARaeeaEAQK 1471
Cdd:pfam05701 41 ELELEKVQEEIPEYKKQSEAAEAAKAQVLEELESTKRLIEE----LKLNLEraQTEEAQAKQDSELAKLRVE----EMEQ 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1472 RQAQEEAERLRRQVQDETQRKRQAEAELAVrVKAE--------AEAAREKQRALQALEEFRLQAEEAERRLRQAEAERAr 1543
Cdd:pfam05701 113 GIADEASVAAKAQLEVAKARHAAAVAELKS-VKEEleslrkeyASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1544 QVQVALETAqRSAEVELQSKRASFA----EKTAQLERTLQEEHVAVAQLREEAERRAQQQAeaerareeaerelerwQLK 1619
Cdd:pfam05701 191 ATKESLESA-HAAHLEAEEHRIGAAlareQDKLNWEKELKQAEEELQRLNQQLLSAKDLKS----------------KLE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1620 ANEALRLRLQAEEVAQQKSlaqaeaekqkeEAEREARRRGKAEEQAVRQRE---LAEQELEKQRQLAEgtaqqRLAAEQE 1696
Cdd:pfam05701 254 TASALLLDLKAELAAYMES-----------KLKEEADGEGNEKKTSTSIQAalaSAKKELEEVKANIE-----KAKDEVN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1697 LIRLRAETEQGEQQRQllEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRLEAeas 1776
Cdd:pfam05701 318 CLRVAAASLRSELEKE--KAELASLRQREGMASIAVSSLEAELNRTKSEIALV---QAKEKEAREKMVELPKQLQQA--- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1777 rfrelAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEA--ENERLRRLAED 1854
Cdd:pfam05701 390 -----AQEAEEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEKLALAAIKAlqESESSAESTNQ 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1855 EAFQR-------------RRLEEQAAQHKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEILALKVSFEKAAA 1921
Cdd:pfam05701 465 EDSPRgvtlsleeyyelsKRAHEAEELANKRVAEAVSQIEEAKESELRSLEKL-EEVNREMEERKEALKIALEKAEKAKE 543
|
570
....*....|....*..
gi 2124423190 1922 GKAELELELGRIRSNAE 1938
Cdd:pfam05701 544 GKLAAEQELRKWRAEHE 560
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2230-2457 |
6.09e-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: 6.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2230 EAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLS-----VAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEA 2304
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEylraaLRLWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2305 TRLKAEAELLQQQK-ELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE 2383
Cdd:COG4913 319 DALREELDELEAQIrGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 2384 DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAE-LEREKEKLKQEAKLLQLKSEE 2457
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1029-1522 |
6.26e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 59.31 E-value: 6.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1029 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKEaqaVPATLPELE 1108
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1109 ATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERL----QQRHG--ERDVEVERWRERVAQL------LERWQAVLAQ 1176
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLsrleEEINGieERIKELEEKEERLEELkkklkeLEKRLEELEE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1177 TDLRQRELEQLGRQLRYYR-----ESADPLGAWLQDAKRRQEQIQ---AMVLADSRAVREQLRQEKALLEEIERHGEKVE 1248
Cdd:PRK03918 360 RHELYEEAKAKKEELERLKkrltgLTPEKLEKELEELEKAKEEIEeeiSKITARIGELKKEIKELKKAIEELKKAKGKCP 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1249 ECQR---------FAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESviqEYVDLRTRYSELTTLTSQYIKFI 1319
Cdd:PRK03918 440 VCGRelteehrkeLLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKES---ELIKLKELAEQLKELEEKLKKYN 516
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1320 SETLRRMEEE-----ERLA-----------EQQRAEERE-RLAAVEAAL-EKQRQLAEAHAQAKAQAEQEAQELQRRMQ- 1380
Cdd:PRK03918 517 LEELEKKAEEyeklkEKLIklkgeikslkkELEKLEELKkKLAELEKKLdELEEELAELLKELEELGFESVEELEERLKe 596
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1381 -EEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEE------EIRVVRLQLETTERQRgga 1453
Cdd:PRK03918 597 lEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEElekkysEEEYEELREEYLELSR--- 673
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1454 egELQALRARAEEAEAQKRQAQEEAERLRRQVqdETQRKRQAEAELAVRVKAEAEAAREKQRALQALEE 1522
Cdd:PRK03918 674 --ELAGLRAELEELEKRREEIKKTLEKLKEEL--EEREKAKKELEKLEKALERVEELREKVKKYKALLK 738
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1349-1581 |
7.78e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.81 E-value: 7.78e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1349 AALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLR--QSSEAEIQAKARQVEAA 1425
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEArAAKDKDAVAAALARVKakKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1426 ERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKA 1505
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1506 EAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEE 1581
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAK-ARKAAQQQANAEPE 670
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1752-2023 |
9.07e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 58.42 E-value: 9.07e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1752 SKARAEEESRSTSEKSKQRLEAEASRF-RELAEEAARLRAlAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRL 1830
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREARHKK-AAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARP 514
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1831 KTEAEIALKEKEAENERLRRLAEDEAfqrrrleEQAAQHKADIEERL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 1908
Cdd:PRK05035 515 DNSAVIAAREARKAQARARQAEKQAA-------AAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1909 ILALKVsfEKAAAGKAELELElgrIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKA 1988
Cdd:PRK05035 586 IARAKA--KKAAQQAASAEPE---EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKA 660
|
250 260 270
....*....|....*....|....*....|....*
gi 2124423190 1989 ALEEVERLKAKVEEARRLRERAEQESARQLQLAQD 2023
Cdd:PRK05035 661 AQQQANAEPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1210-1588 |
9.86e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1210 RRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQS 1289
Cdd:COG4717 60 KPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1290 GSESVIQEYVDLRTRYSELTTLtsqyikfiSETLRRMEEEERLAEQQRAEERERL-AAVEAALEKQRQLAEAHAQAKAQA 1368
Cdd:COG4717 140 ELAELPERLEELEERLEELREL--------EEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAEL 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1369 EQEAQELQRRMQEevARREEAAVDAQQQKRSIQEELQHLRQSSEAE---------------------------------- 1414
Cdd:COG4717 212 EEELEEAQEELEE--LEEELEQLENELEAAALEERLKEARLLLLIAaallallglggsllsliltiagvlflvlgllall 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1415 --IQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRAR-AEEAEAQKRQAQEEAERLRRQVQDETQR 1491
Cdd:COG4717 290 flLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLeLLDRIEELQELLREAEELEEELQLEELE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1492 KRQAEAELAVRVKAEaEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKT 1571
Cdd:COG4717 370 QEIAALLAEAGVEDE-EELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL 448
|
410
....*....|....*..
gi 2124423190 1572 AQLERTLQEEHVAVAQL 1588
Cdd:COG4717 449 EELREELAELEAELEQL 465
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4022-4058 |
9.99e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.56 E-value: 9.99e-08
10 20 30
....*....|....*....|....*....|....*..
gi 2124423190 4022 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4058
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2298-2443 |
1.02e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 58.49 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2298 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQ-QLEQetQGFQRTLEAERQRQLEMSAEAERLK 2368
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARgRLER--QKMHDKAKAEEQRTKLLELQAESAA 710
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 2369 LRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlRQAIAELEREKEK 2443
Cdd:PTZ00491 711 VESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1809-2172 |
1.03e-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: 58.60 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1809 QRAEAERVLAEKLAAIgEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAAQHKAdiEERLAQLRkasESEL 1888
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1889 ERQKglVEDTLRQRRQVEEEILALKVSFEKaaagkaELE-LELGRIRSNaedtlrSKEQAELEAMRQRQLAAEEEQRRRE 1967
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKILEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1968 AEERVQKSLAAEEEAARQRKAALEEVERLKakveEARRLRERaEQESARQLQ-LAQDAAQKRLQAEEKAHAfAVQQKEQE 2046
Cdd:pfam17380 417 QQKVEMEQIRAEQEEARQREVRRLEEERAR----EMERVRLE-EQERQQQVErLRQQEEERKRKKLELEKE-KRDRKRAE 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2047 LQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeklRKEAEQ 2126
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEER----------------------RKQQEM 548
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 2124423190 2127 EAARRAQAEQAALRQKQAADAEMEKHKKFAEQTLR-QKAQVEQELTT 2172
Cdd:pfam17380 549 EERRRIQEQMRKATEERSRLEAMEREREMMRQIVEsEKARAEYEATT 595
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2262-2459 |
1.12e-07 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 57.47 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2262 AARLSVAAQEAARLREL------AEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2335
Cdd:COG4942 16 AAQADAAAEAEAELEQLqqeiaeLEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2336 AQQLEQetqgfQRTLEAERQRQLEMSAEAERLKL-----------RVAEMSRAQARA-EEDAQRFRKQAEEIGEKLHRTE 2403
Cdd:COG4942 96 RAELEA-----QKEELAELLRALYRLGRQPPLALllspedfldavRRLQYLKYLAPArREQAEELRADLAELAALRAELE 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 2404 LATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQ 2459
Cdd:COG4942 171 AERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELE 226
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2149-2452 |
1.25e-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: 58.11 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2149 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKAR 2228
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2229 IEAENRAL------ILRDKDNTQRVLQEEAEKMKHVAEEAarlsvaaqeaarlRELAEE--DLAQQRALaekmLKEKMQa 2300
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2301 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEaerqrqlemsaeaeRLKLRVAEMSRAQAR 2380
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE--------------ELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 2381 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQ 2452
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1508-1951 |
1.27e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1508 EAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQ 1587
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1588 LreeaerraqqqaeaERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAeaekqkeeaerearrrgKAEEQAVR 1667
Cdd:COG4717 151 L--------------EERLEELRELEEELEELEAELAELQEELEELLEQLSLATE-----------------EELQDLAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1668 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEME 1747
Cdd:COG4717 200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1748 VLLASKARAEEESRStseKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1827
Cdd:COG4717 280 FLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREA 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1828 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLE--EQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR-RQ 1904
Cdd:COG4717 357 EELEEELQLEELEQEIAALLAEAGVEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEE 436
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2124423190 1905 VEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEA 1951
Cdd:COG4717 437 LEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKA 483
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1362-1576 |
1.31e-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: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1362 AQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArqveaAERSRLRIEEEIRvvrl 1441
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQK---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1442 qletterqrggaegelQALRARAEEAEAQKRQAQEEAERlrrQVQDETQRKRQAEAelavRVKAEAEAAREKQRALQALE 1521
Cdd:TIGR02794 120 ----------------QAEEAKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1522 EFRLQAEEAERRLRQ--AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1576
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
23-122 |
1.31e-07 |
|
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: 52.72 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 23 KTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQ 96
Cdd:cd21286 3 KIYTDWANHYLAK---SGHKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARG 75
|
90 100
....*....|....*....|....*.
gi 2124423190 97 VKLVNIRNDDIADGNPKLTLGLIWTI 122
Cdd:cd21286 76 VNVQGLSAEEIRNGNLKAILGLFFSL 101
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2189-2599 |
1.40e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2189 EELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRAL-ILRDKDNTQRVLQEEAEKMKHVAEEAARLSV 2267
Cdd:COG4717 81 KEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLpLYQELEALEAELAELPERLEELEERLEELRE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2268 AAQEAARLRELAEEdlaQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQ 2347
Cdd:COG4717 161 LEEELEELEAELAE---LQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2348 RTLEAERQRQLEMSAE----------------------AERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2405
Cdd:COG4717 238 AAALEERLKEARLLLLiaaallallglggsllsliltiAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELE 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2406 TQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQtvqqeqllqETQALQQSFLSEKDTLL 2485
Cdd:COG4717 318 EEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---------IAALLAEAGVEDEEELR 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2486 QRERFIEQEKAKLEQLfqdEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVrrkqeelqlleqqrqqq 2565
Cdd:COG4717 389 AALEQAEEYQELKEEL---EELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEEL----------------- 448
|
410 420 430
....*....|....*....|....*....|....
gi 2124423190 2566 ekllaeenQRLRERLQRLEEEHRaALAHSEEIAA 2599
Cdd:COG4717 449 --------EELREELAELEAELE-QLEEDGELAE 473
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1320-2035 |
1.49e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.43 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1320 SETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKaQAEQEAQELQRRMQEEVARREEAAVDAQQQKRS 1399
Cdd:PRK04863 375 DEQQEENEARAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQQAV-QALERAKQLCGLPDLTADNAEDWLEEFQAKEQE 453
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1400 IQEELQHLRQS-SEAeiQAKARQVEAAERSRLRIEEEI------RVVRLQLETTERQRGGAEgELQALRARAEEAEaQKR 1472
Cdd:PRK04863 454 ATEELLSLEQKlSVA--QAAHSQFEQAYQLVRKIAGEVsrseawDVARELLRRLREQRHLAE-QLQQLRMRLSELE-QRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1473 QAQEEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREkqRALQALEEFRLQAEEAERRLRQAEAERARQvqvaleTA 1552
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELE-QLQEELEARLE--SLSESVSEARERRMALRQQLEQLQARIQRL------AA 600
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1553 QRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERW-QLKANEALRLRLQAE 1631
Cdd:PRK04863 601 RAPAWLAAQDALARLREQSGEEFEDSQDVTEYMQQLLERERELTVERDELAARKQALDEEIERLsQPGGSEDPRLNALAE 680
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1632 EV--------------------------AQQ----KSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1681
Cdd:PRK04863 681 RFggvllseiyddvsledapyfsalygpARHaivvPDLSDAAEQLAGLEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVV 760
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1682 LAEGTAQQRLAAEQELIRL-RAETEQGEQQRQLLEEELARLQHEAAAATQKRQEL--------------------EAELA 1740
Cdd:PRK04863 761 VKIADRQWRYSRFPEVPLFgRAAREKRIEQLRAEREELAERYATLSFDVQKLQRLhqafsrfigshlavafeadpEAELR 840
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1741 KVRA---EMEVLLASKARAEEESRSTSEKSKQR---LEAEASRFRELAEE--AARLRALAEEAKRQRQlAEEDAARQRAE 1812
Cdd:PRK04863 841 QLNRrrvELERALADHESQEQQQRSQLEQAKEGlsaLNRLLPRLNLLADEtlADRVEEIREQLDEAEE-AKRFVQQHGNA 919
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1813 AERVlaEKLAAI-----GEATRLKTEAEIALKEKEAENERLRRLAedEAFQRRR--LEEQAAQ---HKADIEERLAQLRK 1882
Cdd:PRK04863 920 LAQL--EPIVSVlqsdpEQFEQLKQDYQQAQQTQRDAKQQAFALT--EVVQRRAhfSYEDAAEmlaKNSDLNEKLRQRLE 995
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1883 ASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELG----RIRSNAEDTLRSKE---QAELEAMRQR 1955
Cdd:PRK04863 996 QAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQdlgvPADSGAEERARARRdelHARLSANRSR 1075
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1956 QlaaeeeqrrreaeERVQKSLAAEEEAARQRKAALEEVERlkaKVEEARRLRERAEQESARQLQLAQD-AAQKRLQAEEK 2034
Cdd:PRK04863 1076 R-------------NQLEKQLTFCEAEMDNLTKKLRKLER---DYHEMREQVVNAKAGWCAVLRLVKDnGVERRLHRREL 1139
|
.
gi 2124423190 2035 A 2035
Cdd:PRK04863 1140 A 1140
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1180-1561 |
1.57e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 58.04 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1180 RQRELEQLGRQLRYYRESADPLGAWLQDAkrRQEQIQAMVLADsravrEQLRQEkalLEEIERHGEKVEECQRFAKQYIN 1259
Cdd:PRK04863 849 LERALADHESQEQQQRSQLEQAKEGLSAL--NRLLPRLNLLAD-----ETLADR---VEEIREQLDEAEEAKRFVQQHGN 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1260 AIkdyelqlvtykAQLEPVAS-----PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF-ISETLRRMEEEERLA 1333
Cdd:PRK04863 919 AL-----------AQLEPIVSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsYEDAAEMLAKNSDLN 987
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1334 EQQRAeereRLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEevarreeaavdAQQQKRSIQEELQHL--RQSS 1411
Cdd:PRK04863 988 EKLRQ----RLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA-----------KRQMLQELKQELQDLgvPADS 1052
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1412 EAEIQAKARqveaaersRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQ 1484
Cdd:PRK04863 1053 GAEERARAR--------RDELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVnakagwcAVLRL 1124
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1485 VQDETQRKRQAEAELAVRVKAEAEAAREKqrALQALeefrlqaeeaerRLRQAEAERARQVQVALETAQRsAEVELQ 1561
Cdd:PRK04863 1125 VKDNGVERRLHRRELAYLSADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRLSEDPKR-PERKVQ 1186
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1130-1955 |
1.83e-07 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 58.04 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1130 ALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAV-----LAQTDLRQREleQLGRqlryYRESADPLGAW 1204
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnLVQTALRQQE--KIER----YQEDLEELTER 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1205 LQdakrrqeqIQAMVLADSRAVREQLRQEKALLE-EIERHG-------EKVEECQRFAKQYINAIKDYE-LQLVTYKAQL 1275
Cdd:COG3096 363 LE--------EQEEVVEEAAEQLAEAEARLEAAEeEVDSLKsqladyqQALDVQQTRAIQYQQAVQALEkARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1276 EPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIsETLRRMEEE-ERLAEQQRAEERER-------LAAV 1347
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEvERSQAWQTARELLRryrsqqaLAQR 513
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1348 EAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAER 1427
Cdd:COG3096 514 LQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1428 -SRLRIEEEI-RVVRLQLETTERQRGGA---EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVR 1502
Cdd:COG3096 594 iKELAARAPAwLAAQDALERLREQSGEAladSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDPR 673
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1503 VKAEAE---------------------------------------AAREKQRAL--------------QALEEFRLQAEE 1529
Cdd:COG3096 674 LLALAErlggvllseiyddvtledapyfsalygparhaivvpdlsAVKEQLAGLedcpedlyliegdpDSFDDSVFDAEE 753
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1530 AERRL------RQAEAER----------ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE---EHVAVAqlre 1590
Cdd:COG3096 754 LEDAVvvklsdRQWRYSRfpevplfgraAREKRLEELRAERDELAEQYAKASFDVQKLQRLHQAFSQfvgGHLAVA---- 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1591 eaerRAQQQAEAERAREEAERELERWQLKANEAL-RLRLQAEEVAQQKSLAQAEAEKQKEEaerearrrgkAEEQAVRQR 1669
Cdd:COG3096 830 ----FAPDPEAELAALRQRRSELERELAQHRAQEqQLRQQLDQLKEQLQLLNKLLPQANLL----------ADETLADRL 895
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1670 ELAEQELEKQRQLAEGTAQQRLAAEQ---ELIRLRAETEQGEQQRQLLEEELARLQheaaaatQKRQELEAeLAKVRAEM 1746
Cdd:COG3096 896 EELREELDAAQEAQAFIQQHGKALAQlepLVAVLQSDPEQFEQLQADYLQAKEQQR-------RLKQQIFA-LSEVVQRR 967
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1747 EVLLASKARAE-EESRSTSEKSKQRLEAeasrfrelaeeaarlralAEEAKRQRQLAEEDAARQRAEAERVLAEklaaig 1825
Cdd:COG3096 968 PHFSYEDAVGLlGENSDLNEKLRARLEQ------------------AEEARREAREQLRQAQAQYSQYNQVLAS------ 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1826 eatrLKTEAEIA---LKEKEAENERLRRLAEDEAfqrrrlEEQAAQHKADIEERLAQLRkASESELERQKGLVE---DTL 1899
Cdd:COG3096 1024 ----LKSSRDAKqqtLQELEQELEELGVQADAEA------EERARIRRDELHEELSQNR-SRRSQLEKQLTRCEaemDSL 1092
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1900 RQR-RQVEEEILALKVSFEKAAAGKAELeLELGRiRSNAEDTLRSKEQAELEAMRQR 1955
Cdd:COG3096 1093 QKRlRKAERDYKQEREQVVQAKAGWCAV-LRLAR-DNDVERRLHRRELAYLSADELR 1147
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1669-2041 |
1.90e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.47 E-value: 1.90e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1669 RELAEQELEKQR-QLAEGTAQQRLAAEQELIRLRAETEQGEQQrqllEEELARLQHEAAAATQKRQELEAELAKVRAEME 1747
Cdd:COG4717 44 RAMLLERLEKEAdELFKPQGRKPELNLKELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1748 VLlaSKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEA 1827
Cdd:COG4717 120 KL--EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDL 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1828 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAqhKADIEERLAQLRKASESELERQkGLVEDTLRQRRQVEE 1907
Cdd:COG4717 198 AEELEELQQRLAELEEELEEAQEELEELEEELEQLENELE--AAALEERLKEARLLLLIAAALL-ALLGLGGSLLSLILT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1908 EILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRK 1987
Cdd:COG4717 275 IAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLR 354
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1988 AALEEVERLKAKVEEARR--LRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQ 2041
Cdd:COG4717 355 EAEELEEELQLEELEQEIaaLLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQ 410
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1708-1899 |
2.24e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.74 E-value: 2.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1708 EQQRQLLEEELAR-LQHEAAAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEASRFR----ELA 1782
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAKAAAaakaKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1783 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE-RVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrr 1861
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA----- 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 2124423190 1862 LEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTL 1899
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1672-1887 |
2.42e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 56.38 E-value: 2.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1672 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLA 1751
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1752 SKARAEE---------ESRSTSE--KSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1820
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1821 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESE 1887
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1394-1575 |
2.67e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 56.35 E-value: 2.67e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1394 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqletterqrggaegelqalraraEEAEAQKRQ 1473
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKER---------------------------LAAQEQKKQ 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1474 AQeEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAER---ARQVQVALE 1550
Cdd:PRK09510 120 AE-EAAKQAALKQKQAEEAAAKAAAAA-KAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKkaeAEAAAKAAA 197
|
170 180
....*....|....*....|....*
gi 2124423190 1551 TAQRSAEVELQSKRASFAEKTAQLE 1575
Cdd:PRK09510 198 EAKKKAEAEAKKKAAAEAKKKAAAE 222
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1659-1901 |
3.13e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 56.50 E-value: 3.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1659 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqheaaaATQKRQEL 1735
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1736 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEaeasrfrelaEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1815
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQ----------LQAAQERARQQQEEFRRKLQELQRKKQQEEAER 446
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1816 VLAEKlaaigeatRLKTEAEIALKEkeaENERLRRLAEDEAFQ-RRRLEEQAAQHKADIEERLAQLRKASESELERQKGL 1894
Cdd:pfam15709 447 AEAEK--------QRQKELEMQLAE---EQKRLMEMAEEERLEyQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQ 515
|
....*..
gi 2124423190 1895 VEDTLRQ 1901
Cdd:pfam15709 516 AQEQARQ 522
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1321-1569 |
3.86e-07 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 55.81 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLRRMEEEERLAEQQRAEERERL--AAVEAALEKQRQ---LAEAHAQAKAQAEQEAQELQRRMqeevarrEEAAVDAQQ 1395
Cdd:pfam15558 88 QVIEKESRWREQAEDQENQRQEKLerARQEAEQRKQCQeqrLKEKEEELQALREQNSLQLQERL-------EEACHKRQL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1396 QKRSIQEELQHLRQSSEAEIQAKARQVE---AAERSRLRIEEEIRVVRLQlettERQRGGAEGELQALRARAEEAEAQKR 1472
Cdd:pfam15558 161 KEREEQKKVQENNLSELLNHQARKVLVDcqaKAEELLRRLSLEQSLQRSQ----ENYEQLVEERHRELREKAQKEEEQFQ 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1473 QAQEEAERLRRQvQDETQRKRQAEAELAVRvKAEAEAAREKQRALQALEEFRLQAEEAERRLRQ----AEAERARQVQVA 1548
Cdd:pfam15558 237 RAKWRAEEKEEE-RQEHKEALAELADRKIQ-QARQVAHKTVQDKAQRARELNLEREKNHHILKLkvekEEKCHREGIKEA 314
|
250 260
....*....|....*....|.
gi 2124423190 1549 LETAQRSAEVELQSKRASFAE 1569
Cdd:pfam15558 315 IKKKEQRSEQISREKEATLEE 335
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1321-1557 |
4.00e-07 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 55.70 E-value: 4.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1400
Cdd:pfam13868 46 DEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQ 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1401 QEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1480
Cdd:pfam13868 126 RQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1481 LRrqvqdetqRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1557
Cdd:pfam13868 206 LR--------AKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDE 274
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1770-1956 |
4.45e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 56.46 E-value: 4.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1770 RLEAEASRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN 1845
Cdd:COG4913 222 DTFEAADALVEHFDDLERAHEALEDAREQIellePIRELAERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELR 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1846 ERLRRLAEDEAF----------QRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVS 1915
Cdd:COG4913 302 AELARLEAELERlearldalreELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEE 381
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2124423190 1916 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQ 1956
Cdd:COG4913 382 FAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1327-1492 |
5.66e-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: 5.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1327 EEEERLAEQQRAEERERLAAVEAAleKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1406
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1407 LRQSSEAEIQAKARQVEA-AERSRLRIEEEI----RVVRLQLETTERQRGGAEGELQALRARAEEAEAQK------RQAQ 1475
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 2124423190 1476 EEAERLRRQVQDETQRK 1492
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2163-2588 |
5.92e-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: 5.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2163 KAQVEQELTTLRLQLEETDHQKSILDEELQRlkaEVTEAARQRSQVEEELFSLRVQMEELGKLKAriEAENRALILRDKD 2242
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2243 NTQ-RVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2317
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2318 ----KELAQEQARRLQEDKEQMaQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEmsraqaraEEDAQRFRKQAE 2393
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2394 EIGEKLHRTElatQEKVTLVQTleiqRQQSDHDAERLRQAIAELE----REKEKLKQEAKLLQLKSEEMQTVQQEQLLQE 2469
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQA----REKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2470 TQALQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEvakaqKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVR 2549
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIE-----NLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENAR 576
|
410 420 430
....*....|....*....|....*....|....*....
gi 2124423190 2550 RKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2588
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1715-2033 |
5.94e-07 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 55.64 E-value: 5.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1715 EEELARLQHEAAAATQKRQ-ELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE 1793
Cdd:pfam02029 4 EEEAARERRRRAREERRRQkEEEEPSGQVTESVEP--NEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1794 EAKRQRQLAEEDA---------ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN----ERLRRLAEDEAFQRR 1860
Cdd:pfam02029 82 ALERQKEFDPTIAdekesvaerKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQEnkwsTEVRQAEEEGEEEED 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1861 RLEEQAAQHKADIEERLAQLRKASE---------SELERQKGLVE--------DTLRQRRQVEEEILALKVSFEKAAAGK 1923
Cdd:pfam02029 162 KSEEAEEVPTENFAKEEVKDEKIKKekkvkyeskVFLDQKRGHPEvksqngeeEVTKLKVTTKRRQGGLSQSQEREEEAE 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1924 AELELE--LGRIR-SNAEdtlrsKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEaaRQRKAalEEVERLKAKV 2000
Cdd:pfam02029 242 VFLEAEqkLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKLLEEEE--QRRKQ--EEAERKLREE 312
|
330 340 350
....*....|....*....|....*....|...
gi 2124423190 2001 EEARRLRERAEQESArqlqlaqDAAQKRLQAEE 2033
Cdd:pfam02029 313 EEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1425-1550 |
7.21e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 54.67 E-value: 7.21e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1425 AERSRLRIEEEIRVVRLQLETTERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDET---QRKRQAEAELAV 1501
Cdd:COG1566 81 LQAALAQAEAQLAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAvsqQELDEARAALDA 159
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2124423190 1502 rVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERArQVQVALE 1550
Cdd:COG1566 160 -AQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALA-QAELNLA 206
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3703-3738 |
7.23e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 7.23e-07
10 20 30
....*....|....*....|....*....|....*.
gi 2124423190 3703 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3738
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2139-2602 |
7.44e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 55.69 E-value: 7.44e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRSQVEEELF 2213
Cdd:COG4913 247 AREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELD 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2214 SLRVQMEEL-GKLKARIEAENRAL--ILRDKDNTQRVLQEEAEKMKH-VAEEAARLSVAAQEAARLRELAEEDLAQQRAL 2289
Cdd:COG4913 327 ELEAQIRGNgGDRLEQLEREIERLerELEERERRRARLEALLAALGLpLPASAEEFAALRAEAAALLEALEEELEALEEA 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2290 AEKMLKEKMQAVQEATRLKAEAELLQQQK---ELAQEQARRL----------------------QEDKE-QMAqqLEQET 2343
Cdd:COG4913 407 LAEAEAALRDLRRELRELEAEIASLERRKsniPARLLALRDAlaealgldeaelpfvgelievrPEEERwRGA--IERVL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2344 QGFQRTLEAERQRQLEMSAEAERLKLR-------VAEMSRAQARAEEDAQRFrkqAEEIGEKLH------RTELATQEKV 2410
Cdd:COG4913 485 GGFALTLLVPPEHYAAALRWVNRLHLRgrlvyerVRTGLPDPERPRLDPDSL---AGKLDFKPHpfrawlEAELGRRFDY 561
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2411 TLVQTLEIQRQQS-------------------DHDA---------------ERLRQAIAELEREKEKLKQEAKLLQLKSE 2456
Cdd:COG4913 562 VCVDSPEELRRHPraitragqvkgngtrhekdDRRRirsryvlgfdnraklAALEAELAELEEELAEAEERLEALEAELD 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2457 EMQTvqqeqLLQETQALQQSFLSEKDTLLQRERfIEQEKAKLEQL--FQDEVAKAQKLREEQQRQQKQMEEEKQQLVASM 2534
Cdd:COG4913 642 ALQE-----RREALQRLAEYSWDEIDVASAERE-IAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEI 715
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 2535 EEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEEnQRLRERLQRLEEEHRAALAHSEEIAASQA 2602
Cdd:COG4913 716 GRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEERIDALRARL 782
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2141-2326 |
8.53e-07 |
|
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: 55.42 E-value: 8.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2141 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSLRVQME 2220
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2221 ELGKLKARIEaenRAL-ILRDKDNT----QRVLQEEAEKMKHVAE--EAARLSVAAqEAARLREL-AEEDLAQQRALAE- 2291
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIE-EYRALKEAkSNKEDESQRKLEEi 456
|
170 180 190
....*....|....*....|....*....|....*..
gi 2124423190 2292 KMLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2326
Cdd:pfam05667 457 KELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1981-2325 |
8.54e-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: 55.51 E-value: 8.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1981 EAARQRKAALEEVERLKAKVEEARRLRER----AEQESARQLQLAQDAA----QKRLQAEEKAHAFAVQQKEQELQqtlq 2052
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAREVERrrklEEAEKARQAEMDRQAAiyaeQERMAMERERELERIRQEERKRE---- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2053 qeqsmLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERlkqsaeeqaqaqaqaqaaAEKLRKEAEQEAARRA 2132
Cdd:pfam17380 362 -----LERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAAR------------------KVKILEEERQRKIQQQ 418
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2133 QAEQAALRQKQAADAEmekhkkfaEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEElqrlkaevtEAARQRSQVEeel 2212
Cdd:pfam17380 419 KVEMEQIRAEQEEARQ--------REVRRLEEERAREMERVRLEEQERQQQVERLRQQ---------EEERKRKKLE--- 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2213 fslrvqMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEK 2292
Cdd:pfam17380 479 ------LEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRKQQEMEERR 552
|
330 340 350
....*....|....*....|....*....|....*..
gi 2124423190 2293 MLKEKMQ-AVQEATRLKA---EAELLQQQKELAQEQA 2325
Cdd:pfam17380 553 RIQEQMRkATEERSRLEAmerEREMMRQIVESEKARA 589
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3444-3480 |
9.15e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.86 E-value: 9.15e-07
10 20 30
....*....|....*....|....*....|....*..
gi 2124423190 3444 IRLLEAQIATGGIIDPVHSHRVPVEVAYQRGYFDEEM 3480
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4125-4153 |
9.81e-07 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 48.09 E-value: 9.81e-07
10 20
....*....|....*....|....*....
gi 2124423190 4125 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4153
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1328-1512 |
1.13e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.43 E-value: 1.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1328 EEERLAEQQR--AEERERLaaveAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQ 1405
Cdd:PRK09510 93 QQKQAAEQERlkQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAEAK 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1406 HLRQSSEAEIQAKARQVEAAERSRLRIEEEirvvrlqlettERQRGGAEGELQALRARAEEAEAQKRQAQEEAerlrrqv 1485
Cdd:PRK09510 169 KKAEAEAAKKAAAEAKKKAEAEAAAKAAAE-----------AKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKA------- 230
|
170 180
....*....|....*....|....*..
gi 2124423190 1486 qdETQRKRQAEAELAVRVKAEAEAARE 1512
Cdd:PRK09510 231 --AAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1674-2074 |
1.40e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1674 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH--EAAAATQKRQELEAELAKVRAEMEvlla 1751
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1752 sKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLK 1831
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1832 TEAEIALKEKEAENERLRRL---------------AEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVE 1896
Cdd:COG4717 229 LEQLENELEAAALEERLKEArlllliaaallallgLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQ 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1897 DTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQrrreaeerVQKSL 1976
Cdd:COG4717 309 ALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAAL--------LAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1977 AAEEEAARQRKAALEEVERLKAKVEEA-RRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQ 2055
Cdd:COG4717 381 VEDEEELRAALEQAEEYQELKEELEELeEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEA 460
|
410
....*....|....*....
gi 2124423190 2056 SMLERLRGEAEAARRAAEE 2074
Cdd:COG4717 461 ELEQLEEDGELAELLQELE 479
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1674-1831 |
1.42e-06 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 54.64 E-value: 1.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1674 QELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqhEAAAATQKRQELEAELAKVRAemevllAS 1752
Cdd:PTZ00491 647 DSLQKSVQLAiEITTKSQEAAARHQAELLEQEARGRLERQKMHDKA-----KAEEQRTKLLELQAESAAVES------SG 715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1753 KARAEEESRSTSEKSKQRLEAEASRFRelaEEAARLRALAE-EAKRQRQLAEEDAARQRAEAERVLAEKLAAIgEATRLK 1831
Cdd:PTZ00491 716 QSRAEALAEAEARLIEAEAEVEQAELR---AKALRIEAEAElEKLRKRQELELEYEQAQNELEIAKAKELADI-EATKFE 791
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1613-2013 |
1.45e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.77 E-value: 1.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1613 LERWQLKANEA------LRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGT 1686
Cdd:COG4717 104 LEELEAELEELreelekLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1687 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE---------------LAKVRAEMEVLLA 1751
Cdd:COG4717 184 EQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENEleaaaleerlkearlLLLIAAALLALLG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1752 SKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLK 1831
Cdd:COG4717 264 LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELL 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1832 TEAEIALKEKEAENERLRRLAEDEAFQRRR--LEEQAAQHKADIEERLAQLRKAseSELERQKGLVEDTLRQRRQVEEEI 1909
Cdd:COG4717 344 DRIEELQELLREAEELEEELQLEELEQEIAalLAEAGVEDEEELRAALEQAEEY--QELKEELEELEEQLEELLGELEEL 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1910 LalkvsfekAAAGKAELELELGRIRSNAEDTlrskeQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAA 1989
Cdd:COG4717 422 L--------EALDEEELEEELEELEEELEEL-----EEELEELREELAELEAELEQLEEDGELAELLQELEELKAELREL 488
|
410 420
....*....|....*....|....
gi 2124423190 1990 LEEVERLKAKVEEARRLRERAEQE 2013
Cdd:COG4717 489 AEEWAALKLALELLEEAREEYREE 512
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1698-2003 |
1.57e-06 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 54.57 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1698 IRLRA-ETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1770
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1771 LEAEASRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlaeklaaigeatrlkteAEIALKEKEAENERLRR 1850
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1851 LAEDEAFQRRrleeqaaqhkadieerlAQLRKASESELERQKGLVEDTLRQRRQVEEEILAlkvsfeKAAAGKAELELEL 1930
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA------RAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 1931 grIRSNAEDTLRSKEQAELEAMRQRQLAAeeeqrrreaeervQKSLAAEEEAARQRKAALE-EVERLKAKVEEA 2003
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKAAQ-------------QQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1345-1566 |
1.57e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 53.70 E-value: 1.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1345 AAVEAALEKQRQ----LAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAR 1420
Cdd:TIGR02794 46 GAVAQQANRIQQqkkpAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1421 QVEAAERSRlriEEEIRVVRLQLETTERQrggAEGElqalrARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1500
Cdd:TIGR02794 126 AKQAAEAKA---KAEAEAERKAKEEAAKQ---AEEE-----AKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEA 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1501 vrvKAEAEAAREKQRAlqaleEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRAS 1566
Cdd:TIGR02794 195 ---KAKAEAAKAKAAA-----EAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGA 252
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1334-1513 |
1.58e-06 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 52.62 E-value: 1.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1334 EQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRrmqeEVARREEAAVDAQQQKRSIQEELQHLRqsSEA 1413
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1414 EIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAqkrQAQEEAERLRRQVQDETQRKR 1493
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKA---ELDEELAELEAELEELEAERE 166
|
170 180
....*....|....*....|
gi 2124423190 1494 QAEAELAVRVKAEAEAAREK 1513
Cdd:COG1579 167 ELAAKIPPELLALYERIRKR 186
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1663-2062 |
1.74e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 1.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1740
Cdd:COG4717 105 EELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1741 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEED--------------- 1805
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARlllliaaallallgl 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1806 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASE 1885
Cdd:COG4717 265 GGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1886 SELERQKGLVE-DTLRQRRQVEEEILALKVSFEKAAAGKAElelelgRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQR 1964
Cdd:COG4717 345 RIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE------ELRAALEQAEEYQELKEELEELEEQLEELLGEL 418
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1965 RREAEERVQKSLAAEEEAARQRKAALEEveRLKAKVEEARRLRERAEQesarqLQLAQDAAQKRLQAEEKahafavqqke 2044
Cdd:COG4717 419 EELLEALDEEELEEELEELEEELEELEE--ELEELREELAELEAELEQ-----LEEDGELAELLQELEEL---------- 481
|
410
....*....|....*...
gi 2124423190 2045 qelqqtlqqeqsmLERLR 2062
Cdd:COG4717 482 -------------KAELR 486
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2161-2446 |
1.76e-06 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 54.58 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2161 RQKAQVEQELTTLRLQLeeTDHQKSiLDEE-------------LQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKlkA 2227
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQQA-LDVQqtraiqyqqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATE--E 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2228 RIEAENRaliLRDKDNTQRVLQEEAEKMKHVAEEAARlSVAAQEAarlRELaEEDLAQQRALAEKM---------LKEKM 2298
Cdd:PRK04863 458 LLSLEQK---LSVAQAAHSQFEQAYQLVRKIAGEVSR-SEAWDVA---REL-LRRLREQRHLAEQLqqlrmrlseLEQRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2299 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQEtqgfqrtLEAERQRQLEMSAEAERLKLRVAE-MSRA 2377
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARA 602
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 2378 QA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLRQAIAELEREKEKLKQ 2446
Cdd:PRK04863 603 PAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQ 666
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3908-3945 |
1.87e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 1.87e-06
10 20 30
....*....|....*....|....*....|....*...
gi 2124423190 3908 QKFLEGTSCIAGVFVDSTKERLSVYQAMKKGIIRPGTA 3945
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1464-1580 |
1.88e-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: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1464 AEEAEAQKRQAQEEAERLRRQvqdETQRKRQAEAELAVRVKaEAEAAREKQRAlqaleefRLQAEEAerrLRQAEAERAR 1543
Cdd:COG2268 212 TEIAIAQANREAEEAELEQER---EIETARIAEAEAELAKK-KAEERREAETA-------RAEAEAA---YEIAEANAER 277
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 1544 QVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQE 1580
Cdd:COG2268 278 EVQRQLEIAEREREIELQEKEA--EREEAELEADVRK 312
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
16-128 |
2.04e-06 |
|
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: 50.00 E-value: 2.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 16 ERDRVQKKTFTKWVNKHLIkhwraeaQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIA 88
Cdd:cd21331 18 EGETREERTFRNWMNSLGV-------NPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYA 90
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423190 89 LDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 128
Cdd:cd21331 91 VELGKHPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2285-2608 |
2.10e-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: 54.36 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2285 QQRALAEKMLKEKMQavqeatrlKAEAELLQQQKE-LAQEQARRLQEDKEQMAQQLEQETQGfqrTLEAERQR-QLEMSA 2362
Cdd:pfam17380 280 HQKAVSERQQQEKFE--------KMEQERLRQEKEeKAREVERRRKLEEAEKARQAEMDRQA---AIYAEQERmAMERER 348
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2363 EAERLKLRVAEMSRAQARAEEDAQRFRKQAEeigekLHRTELATQEKVTLV-QTLEIQRQQSDHDAERLRQaIAELEREK 2441
Cdd:pfam17380 349 ELERIRQEERKRELERIRQEEIAMEISRMRE-----LERLQMERQQKNERVrQELEAARKVKILEEERQRK-IQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2442 EKLKQEAKllQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLE-QLFQDEVAKAQKLR-----EE 2515
Cdd:pfam17380 423 EQIRAEQE--EARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLElEKEKRDRKRAEEQRrkileKE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2516 QQRQQKQMEEEKQQ---LVASMEEAR------QRQREAEEgvRRKQEELQLLEQQRQQQEKLLAEENQRL------RERL 2580
Cdd:pfam17380 501 LEERKQAMIEEERKrklLEKEMEERQkaiyeeERRREAEE--ERRKQQEMEERRRIQEQMRKATEERSRLeamereREMM 578
|
330 340
....*....|....*....|....*...
gi 2124423190 2581 QRLEEEHRaalAHSEEIAASQATAVKAL 2608
Cdd:pfam17380 579 RQIVESEK---ARAEYEATTPITTIKPI 603
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2785-2821 |
2.21e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 47.09 E-value: 2.21e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2124423190 2785 IRLLEAQIATGGVIDPVHSHRVPVEVAYQRGYFDEEM 2821
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1344-1756 |
2.37e-06 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 54.09 E-value: 2.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1344 LAAVEAALEKQRQLAEAHAQAKaqaeqEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE----------- 1412
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVAR-----EDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1413 --------AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1484
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1485 VQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKR 1564
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1565 ASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEA 1644
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1645 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1724
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 2124423190 1725 AAAATQKRQELEAELAKVRAEMEVLLASKARA 1756
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1317-1544 |
2.62e-06 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 53.00 E-value: 2.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1317 KFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQ 1396
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1397 KRSIQEELQHLRQSSEAEIQAKARQVEAAE---------RSRLRIEEEIRVVRLQLETTERQRggAEGELQALRARAEEA 1467
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQdekaerdelRAKLYQEEQERKERQKEREEAEKK--ARQRQELQQAREEQI 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1468 EAQKRQAQEEAER--------------LRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERR 1533
Cdd:pfam13868 246 ELKERRLAEEAEReeeefermlrkqaeDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEA 325
|
250
....*....|.
gi 2124423190 1534 LRQAEAERARQ 1544
Cdd:pfam13868 326 ERRERIEEERQ 336
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2266-2544 |
2.63e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 54.07 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2266 SVAAQEAARLRELAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmAQQLEqETQG 2345
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK---QQQLA-AISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2346 FQRTLEAERQRQLEMSAEAERlklrvaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2425
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2426 DAE---RLRQAIAE--LEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSflsekDTLLQRErfiEQEKAKLEQ 2500
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKS-----EAGVAQG---EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 2124423190 2501 LFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQR-QREA 2544
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1692-1787 |
2.65e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 54.19 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1692 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1771
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 2124423190 1772 EAEASRFrELAEEAAR 1787
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2146-2607 |
2.68e-06 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 54.07 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2146 DAEMEKHKKFAEQTLRQKAQVEQELTT--------LRLQLEETDHQKSILDEELQRLKAEV---TEAARQRSQVEEELFS 2214
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2215 LRvqmeeLGKLKARIeaeNRALILRDKDNTQRVLQEEAEKMKHVAEEA-ARLSVAAQEAARLRELAEEDLAQQRaLAEKM 2293
Cdd:pfam12128 444 SR-----LGELKLRL---NQATATPELLLQLENFDERIERAREEQEAAnAEVERLQSELRQARKRRDQASEALR-QASRR 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2294 LKEKMQAVQEATR------------LKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLE 2359
Cdd:pfam12128 515 LEERQSALDELELqlfpqagtllhfLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2360 MSAEAERLKLRVAEMSRA-------QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLR 2431
Cdd:pfam12128 595 WAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALA 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2432 QAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLE-------QLFQD 2504
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALDAQLALLKAAIAARRsgakaelKALET 754
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2505 EVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLE 2584
Cdd:pfam12128 755 WYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARLI 834
|
490 500
....*....|....*....|....
gi 2124423190 2585 EEHRAALAHSE-EIAASQATAVKA 2607
Cdd:pfam12128 835 ADTKLRRAKLEmERKASEKQQVRL 858
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2264-2430 |
2.89e-06 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 53.63 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2264 RLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEA---TRLKAEAELLQQQKELAQEQARRLQ-----EDKEQM 2335
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEEAKKEAEAIKKEALLEAKEEihkLRNEFEKELRERRNELQKLEKRLLQkeenlDRKLEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2336 AQQLEQETQGFQRTLEAERQRQLEMSAEAERLK-------LRVAEMSRAQAR----------AEEDAQRFRKQAEEIGEk 2398
Cdd:PRK12704 105 LEKREEELEKKEKELEQKQQELEKKEEELEELIeeqlqelERISGLTAEEAKeillekveeeARHEAAVLIKEIEEEAK- 183
|
170 180 190
....*....|....*....|....*....|...
gi 2124423190 2399 lhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2430
Cdd:PRK12704 184 ----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1300-1579 |
3.16e-06 |
|
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that suppresses cell proliferation by inducing G2/M arrest.
Pssm-ID: 464723 [Multi-domain] Cd Length: 526 Bit Score: 53.30 E-value: 3.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1300 DLRTRYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAAVEAALEKQRQL-----AEAHAQ-AKAQAEQE-A 1372
Cdd:pfam15450 226 ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdAKGQLEESqA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1373 QELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVE------AAERSRLRIEEEirVVRLQLETT 1446
Cdd:pfam15450 304 GELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ--TLGLKLSEA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1447 ERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAarekqralqalEEFRL 1525
Cdd:pfam15450 382 KKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKA-----------REFEV 450
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 1526 QAeeaerrLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1579
Cdd:pfam15450 451 EA------MRQELAALLSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1787-2597 |
3.32e-06 |
|
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: 53.82 E-value: 3.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1787 RLRALAEEAKRQRQLAEEDAARQRAEAERVLAeklaaiGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRrrleeQA 1866
Cdd:TIGR00618 53 KLPRRSEVIRSLNSLYAAPSEAAFAELEFSLG------TKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGR-----IL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1867 AQHKADIEERLAQLRKASESELERQKGLvedtlrqrRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQ 1946
Cdd:TIGR00618 122 AAKKSETEEVIHDLLKLDYKTFTRVVLL--------PQGEFAQFLKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1947 AELEAMRQR-QLAAEEEQRRREAEERVQKSLAAEEEAARqrkaalEEVERLKAKVEEARRLRERAEQESARQLQLAQDAA 2025
Cdd:TIGR00618 194 GKAELLTLRsQLLTLCTPCMPDTYHERKQVLEKELKHLR------EALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2026 Q-KRLQAEEKAHAfavqqkeqelqqtlqqeqsmlerlrgeaeaarraaeeaeeARERAEREAAQSRRQVEEAERLKQSAE 2104
Cdd:TIGR00618 268 RiEELRAQEAVLE----------------------------------------ETQERINRARKAAPLAAHIKAVTQIEQ 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2105 EQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQK--QAADAEMEKHKKFAEQTLRQKAQVEQElTTLRLQLEETDH 2182
Cdd:TIGR00618 308 QAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRllQTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLQQ 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2183 QKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKdNTQRVLQEEAEKMKHVAEEA 2262
Cdd:TIGR00618 387 QKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAA-AITCTAQCEKLEKIHLQESA 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2263 ARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQedKEQMAQQLEQE 2342
Cdd:TIGR00618 466 QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQR--GEQTYAQLETS 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2343 TQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIgekLHRTELATQEKVTLVQTLEIQRQQ 2422
Cdd:TIGR00618 544 EEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHALLRK 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2423 SDHDAERLRQAIAELEREKEKLKQEAKLLQLKSE---EMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLE 2499
Cdd:TIGR00618 621 LQPEQDLQDVRLHLQQCSQELALKLTALHALQLTltqERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLA 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2500 Q---LFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVR-----------RKQEELQLLEQQRQQQ 2565
Cdd:TIGR00618 701 QcqtLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARtvlkarteahfNNNEEVTAALQTGAEL 780
|
810 820 830
....*....|....*....|....*....|....*...
gi 2124423190 2566 EKLLAEENQRLRER------LQRLEEEHRAALAHSEEI 2597
Cdd:TIGR00618 781 SHLAAEIQFFNRLReedthlLKTLEAEIGQEIPSDEDI 818
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2246-2602 |
3.64e-06 |
|
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: 53.44 E-value: 3.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2246 RVLQEEAEKMKHVAEEAARLSVAAQEaaRLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2325
Cdd:pfam02463 169 RKKKEALKKLIEETENLAELIIDLEE--LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELL 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2326 RRLQEDKEQMAQQLEQETQGFQRTLE---AERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRT 2402
Cdd:pfam02463 247 RDEQEEIESSKQEIEKEEEKLAQVLKenkEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKA 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2403 ELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQ-EAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEK 2481
Cdd:pfam02463 327 EKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQlEEELLAKKKLESERLSSAAKLKEEELELKSEEEKE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2482 DTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEgvrrkqeelqlleQQ 2561
Cdd:pfam02463 407 AQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE-------------DL 473
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2124423190 2562 RQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQA 2602
Cdd:pfam02463 474 LKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLA 514
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3113-3149 |
3.79e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.79e-06
10 20 30
....*....|....*....|....*....|....*..
gi 2124423190 3113 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKET 3149
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1402-1774 |
5.08e-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: 52.59 E-value: 5.08e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1402 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1481
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1482 RRQVQDETQRKRQAEAELAVRVKA-EAEAAREKQRALQA---LEEFRLQAEEAERRLRQAEAERaRQVQVALETAQ---R 1554
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLEReteLERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEeelR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1555 SAEVELQSKRASFAEKTAQLERtLQEEhvaVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1634
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQ-LQDT---ITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1635 QQKSlaqaeaekqkeeaerearrRGKAEEQAVRQR--ELAEQELEKQRQLAEGTAqqRLAAEQELIRLRAETEQGEQQRq 1712
Cdd:pfam07888 265 AQRD-------------------RTQAELHQARLQaaQLTLQLADASLALREGRA--RWAQERETLQQSAEADKDRIEK- 322
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1713 lLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAE 1774
Cdd:pfam07888 323 -LSAELQRLEERLQEERMEREKLEVELGREKDCNRVQLSESRRELQELKASlrvAQKEKEQLQAE 386
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1302-1435 |
5.18e-06 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 51.52 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1302 RTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQeaqelqR 1377
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEL------L 129
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1378 RMQEEVARREEAAVDAQQQKRSIQEEL----QHLRQSSEAEIQAKARQVEAA-----ERSRLRIEEE 1435
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKEERENedlnlEQLREKANEE 196
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1663-1887 |
5.96e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1739
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1740 AKVRAEMEVLLASKARAEEESrstsekskQRLEAEAsrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1819
Cdd:COG3206 250 GSGPDALPELLQSPVIQQLRA--------QLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1820 klaAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESE 1887
Cdd:COG3206 318 ---LEAELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1285-1478 |
5.96e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.71 E-value: 5.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1285 PKVQSGSESVIQEYVDLRTRYSELTTltSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQ- 1363
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQs 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1364 -AKAQAEQEAQELQRRMQEEVARREE---AAVDAQQQKRS----IQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEE 1435
Cdd:COG3206 263 pVIQQLRAQLAELEAELAELSARYTPnhpDVIALRAQIAAlraqLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2124423190 1436 IRV---VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1478
Cdd:COG3206 343 LAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1286-1500 |
6.22e-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: 52.07 E-value: 6.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1286 KVQSGSESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHA 1362
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1363 QAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQkrsiQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIrvvrlq 1442
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEERAALEALK------ 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1443 letTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELA 1500
Cdd:COG4942 195 ---AERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2148-2585 |
6.47e-06 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 52.76 E-value: 6.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2148 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA------EVTEAARQRSQVEEELFSLRVQMEE 2221
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2222 LGKLKARIEAENRALilrdkdntQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAE--EDLAQQRALAEKMLKEKmq 2299
Cdd:PRK03918 312 IEKRLSRLEEEINGI--------EERIKELEEKEERLEELKKKLKELEKRLEELEERHElyEEAKAKKEELERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2300 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEM 2374
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2375 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKL-KQEAKL 2450
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2451 LQLKSEemqtvqqeqllqetqalqqsfLSEKDTLLQRERFIEQEKAKLEQlfqdEVAKAQKLREEQQRQQKQMEEEKQQL 2530
Cdd:PRK03918 542 KSLKKE---------------------LEKLEELKKKLAELEKKLDELEE----ELAELLKELEELGFESVEELEERLKE 596
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 2531 VASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLEE 2585
Cdd:PRK03918 597 LEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEE 651
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2188-2394 |
6.48e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.75 E-value: 6.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2188 DEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALIlRDKDNTQRVLQEEAEKMKHVAEEAARLSV 2267
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2268 AAQEAARLRELAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2339
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 2340 EQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEE 2394
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
136-243 |
6.62e-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: 6.62e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 136 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTSSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 214
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 2124423190 215 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 243
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1308-1545 |
6.76e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 6.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1308 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAAVEAALEKQRQlAEAHAQAKAQAEQEAQELQRrMQEEVAR 1385
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1386 REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRggAEGELQALRAR-A 1464
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1465 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEaAREKQRALQALEEfrlQAEEAERRLRQAEAERARQ 1544
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARE---LYESLLQRLEEARLAEALT 384
|
.
gi 2124423190 1545 V 1545
Cdd:COG3206 385 V 385
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1382-1547 |
6.89e-06 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 52.45 E-value: 6.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1382 EVARR----EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRggaegel 1457
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1458 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEtqrkrqaeaelavrvKAEAEAAREKQRALQALEEfRLQAEEAERRLRQ 1536
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 2124423190 1537 AEAERARQVQV 1547
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1329-1584 |
7.87e-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: 51.82 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1329 EERLAEQQRaEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE--EVARREEAAVDAQQQKrsiQEELQH 1406
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAElkEELRQSREKHEELEEK---YKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1407 LRQSSEAEIQAKARQVEAAERSRLRIEEEIRvvrlqleTTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ 1486
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIK-------TLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1487 DETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEA--ERARQVQVALETAQRSAEvelqSKR 1564
Cdd:pfam07888 182 QTEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAllEELRSLQERLNASERKVE----GLG 257
|
250 260
....*....|....*....|
gi 2124423190 1565 ASFAEKTAQLERTLQEEHVA 1584
Cdd:pfam07888 258 EELSSMAAQRDRTQAELHQA 277
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1320-1541 |
7.90e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 52.18 E-value: 7.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1320 SETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAK----------AQAEQEAQELQRRMQEEVARREEA 1389
Cdd:pfam02029 52 PSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEFDPTIADEKesvaerkennEEEENSSWEKEEKRDSRLGRYKEE 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1390 AV----------DAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQA 1459
Cdd:pfam02029 132 ETeirekeyqenKWSTEVRQAEEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQN 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1460 ---------------------LRARAEEAEAQKrQAQEEAERLRRQVQD------ETQRKRQAEAELAVrvkAEAEAARE 1512
Cdd:pfam02029 212 geeevtklkvttkrrqgglsqSQEREEEAEVFL-EAEQKLEELRRRRQEkeseefEKLRQKQQEAELEL---EELKKKRE 287
|
250 260
....*....|....*....|....*....
gi 2124423190 1513 KQRALQALEEFRLQAEEAERRLRQAEAER 1541
Cdd:pfam02029 288 ERRKLLEEEEQRRKQEEAERKLREEEEKR 316
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1945-2461 |
8.18e-06 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 52.45 E-value: 8.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1945 EQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA------ARQRKAALEEVERLKAKVEEARRLRERAEQESARQL 2018
Cdd:pfam07111 63 QQAELISRQLQELRRLEEEVRLLRETSLQQKMRLEAQAmeldalAVAEKAGQAEAEGLRAALAGAEMVRKNLEEGSQREL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2019 QLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVE---- 2094
Cdd:pfam07111 143 EEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGEAKQLAEAQKEAELLRKQLSKTQEELEAQVTlves 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2095 --------------------EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADA-EMEKHK 2153
Cdd:pfam07111 223 lrkyvgeqvppevhsqtwelERQELLDTMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSlEPEFPK 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2154 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR-----------SQVEEELFSLR-VQMEE 2221
Cdd:pfam07111 303 KCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQVAELQEQVTSQSQEQailqralqdkaAEVEVERMSAKgLQMEL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2222 LGKLKARIEAENRA--------LILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKM 2293
Cdd:pfam07111 383 SRAQEARRRQQQQTasaeeqlkFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLR 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2294 LK-----------------EKMQAVQEATRLKAE----AELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRT--- 2349
Cdd:pfam07111 463 QEscpppppappvdadlslELEQLREERNRLDAElqlsAHLIQQEVGRAREQGEAERQQLSEVAQQLEQELQRAQESlas 542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2350 ----LEAERQRQLEMSAEAERLKLRVAEMSRA-----QARAEEDAQRFRKQAEEIGEKLHRTEL---------------A 2405
Cdd:pfam07111 543 vgqqLEVARQGQQESTEEAASLRQELTQQQEIygqalQEKVAEVETRLREQLSDTKRRLNEARReqakavvslrqiqhrA 622
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2406 TQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKE----KLKQEAKLLQLKSEEMQTV 2461
Cdd:pfam07111 623 TQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNlmlaTLQQEGLLSRYKQQRLLAV 682
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2353-2677 |
8.39e-06 |
|
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: 52.37 E-value: 8.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2353 ERQRQLEMSAEA-ERLKLRVAEMSR------AQARAEEDAQRFRKQAEEI------------GEKLHRTELATQEKVTLV 2413
Cdd:TIGR02168 176 ETERKLERTRENlDRLEDILNELERqlksleRQAEKAERYKELKAELRELelallvlrleelREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2414 QTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQtvqqeqllQETQALQQSFLSEKDTLLQRERFIEQ 2493
Cdd:TIGR02168 256 EELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLE--------QQKQILRERLANLERQLEELEAQLEE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2494 EKAKLEQLfQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRkqeeLQLLEQQRQQQEKLLAEEN 2573
Cdd:TIGR02168 328 LESKLDEL-AEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET----LRSKVAQLELQIASLNNEI 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2574 QRLRERLQRLEEEHRAALAHSEEIAASQATAVKALPNGRDApDGPATEAEPEHAFDGLRQKVPAQRLQEvgilsTEELQR 2653
Cdd:TIGR02168 403 ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE-ELEEELEELQEELERLEEALEELREEL-----EEAEQA 476
|
330 340
....*....|....*....|....
gi 2124423190 2654 LVQGRTTVAELAQREDVRRYLQGR 2677
Cdd:TIGR02168 477 LDAAERELAQLQARLDSLERLQEN 500
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2139-2603 |
8.47e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 8.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 LRQKQA-ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDhqksILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2217
Cdd:PRK02224 211 LESELAeLDEEIERYEEQREQARETRDEADEVLEEHEERREELE----TLEAEIEDLRETIAETEREREELAEEVRDLRE 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2218 QMEELGK------------------LKARIEA-ENRALILRDKDNTQRVLQEEA---------------EKMKHVAEEAA 2263
Cdd:PRK02224 287 RLEELEEerddllaeaglddadaeaVEARREElEDRDEELRDRLEECRVAAQAHneeaeslredaddleERAEELREEAA 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2264 RLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE--- 2340
Cdd:PRK02224 367 ELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEeae 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2341 ------------QETQGFQR--TLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE------DAQRFRKQAEEIGEKLH 2400
Cdd:PRK02224 447 alleagkcpecgQPVEGSPHveTIEEDRERVEELEAELEDLEEEVEEVEERLERAEDlveaedRIERLEERREDLEELIA 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2401 RTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQlksEEMQTVQQEQLLQETQALQQSFLSE 2480
Cdd:PRK02224 527 ERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELN---SKLAELKERIESLERIRTLLAAIAD 603
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2481 KDTLLQRERfieqekAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQqlvASMEEARQRQREAEEGVRRKQEELQLLEQ 2560
Cdd:PRK02224 604 AEDEIERLR------EKREALAELNDERRERLAEKRERKRELEAEFDE---ARIEEAREDKERAEEYLEQVEEKLDELRE 674
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2124423190 2561 QRQQQEKLLA------EENQRLRERLQRLEEEHRAALAHSEEIAASQAT 2603
Cdd:PRK02224 675 ERDDLQAEIGavenelEELEELRERREALENRVEALEALYDEAEELESM 723
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1346-1519 |
8.50e-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: 50.31 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1346 AVEAALEKQRQLAEAHAQAkAQAEQEAQELQRR---MQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQV 1422
Cdd:COG1579 1 AMPEDLRALLDLQELDSEL-DRLEHRLKELPAElaeLEDELAALEARLEAAKTELEDLEKEIKRL----ELEIEEVEARI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1423 EAAER--SRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELa 1500
Cdd:COG1579 76 KKYEEqlGNVRNNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL- 154
|
170
....*....|....*....
gi 2124423190 1501 vrvKAEAEAAREKQRALQA 1519
Cdd:COG1579 155 ---EAELEELEAEREELAA 170
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1394-1580 |
8.50e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 8.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1394 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAER--SRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQK 1471
Cdd:COG3206 163 EQNLELRREEARKALEFLEEQLPELRKELEEAEAalEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1472 RQAQEEAERLRRQVQD-----ETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEfrlQAEEAERRLRQAEAERARQVQ 1546
Cdd:COG3206 243 AALRAQLGSGPDALPEllqspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA---QIAALRAQLQQEAQRILASLE 319
|
170 180 190
....*....|....*....|....*....|....
gi 2124423190 1547 VALETAQRSAEvELQSKRASFAEKTAQLERTLQE 1580
Cdd:COG3206 320 AELEALQAREA-SLQAQLAQLEARLAELPELEAE 352
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2163-2546 |
9.22e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.35 E-value: 9.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2163 KAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIE--AENRALILR 2239
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIEdlRETIAETER 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2240 DKDNtqrvLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQE----ATRLKAEAELLQ 2315
Cdd:PRK02224 273 EREE----LAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLR 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2316 QQKELAQEQARRLQEDkeqmAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEI 2395
Cdd:PRK02224 349 EDADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDEL 424
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2396 GEKLH--RTELAT-QEKVTLVQTL-----------EIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTV 2461
Cdd:PRK02224 425 REREAelEATLRTaRERVEEAEALleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERAEDL 504
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2462 QQEQllqetqalqqsflSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEqqrqqkqmeeeKQQLVASMEEARQRQ 2541
Cdd:PRK02224 505 VEAE-------------DRIERLEERREDLEELIAERRETIEEKRERAEELRER-----------AAELEAEAEEKREAA 560
|
....*
gi 2124423190 2542 REAEE 2546
Cdd:PRK02224 561 AEAEE 565
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1344-1438 |
9.71e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 52.26 E-value: 9.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1344 LAAVEAALEKQRQLAEAHAQAKAQAEQEAqelqRRMQEEVARREEAAVDAQQQKRSIQEELQHLR-QSSEAEIQAKARQV 1422
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQSQALA----EAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 2124423190 1423 EAAERSRLRI---EEEIRV 1438
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2251-2410 |
9.82e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.41 E-value: 9.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2251 EAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2330
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2331 DKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2410
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
948-1487 |
1.02e-05 |
|
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: 52.28 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 948 QQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRI-AEQQKAQAEVEGLGKGVARLS 1026
Cdd:TIGR00618 341 EEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLcKELDILQREQATIDTRTSAFR 420
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1027 AEAEKVLAlpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKtisLVIRSTHGAEEVLKAHEEQLKEAQAVpaTLPE 1106
Cdd:TIGR00618 421 DLQGQLAH----------AKKQQELQQRYAELCAAAITCTAQCEK---LEKIHLQESAQSLKEREQQLQTKEQI--HLQE 485
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1107 LEATKAALKKLRAQAEAQQPMFDALR---------DELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQT 1177
Cdd:TIGR00618 486 TRKKAVVLARLLELQEEPCPLCGSCIhpnparqdiDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQM 565
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1178 DLRQRELEQLGRQLRYYRESADPLGAWLQDAKR---RQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQrfa 1254
Cdd:TIGR00618 566 QEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDlteKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELA--- 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1255 kQYINAIKDYELQLvTYKAQLEPVASPAKKPKVQsgSESVIQEYVDLRTRYSELTTLTSQyIKFISETLRRMEEEERLAE 1334
Cdd:TIGR00618 643 -LKLTALHALQLTL-TQERVREHALSIRVLPKEL--LASRQLALQKMQSEKEQLTYWKEM-LAQCQTLLRELETHIEEYD 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1335 QQRAEERERLAAVEAALEKQRQLA-----EAHAQAKAQAEQEAQELQRRMQEEVA-----RREEAAVDAQQQKRSIQEEL 1404
Cdd:TIGR00618 718 REFNEIENASSSLGSDLAAREDALnqslkELMHQARTVLKARTEAHFNNNEEVTAalqtgAELSHLAAEIQFFNRLREED 797
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1405 QHLRQSSEAEIQAKARQVEAAersRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1484
Cdd:TIGR00618 798 THLLKTLEAEIGQEIPSDEDI---LNLQCETLVQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQL 874
|
...
gi 2124423190 1485 VQD 1487
Cdd:TIGR00618 875 SDK 877
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3332-3367 |
1.14e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.78 E-value: 1.14e-05
10 20 30
....*....|....*....|....*....|....*.
gi 2124423190 3332 LLQGSGCLAGIYLEESKEKVTIYEAMRRGLLRPSTA 3367
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1457-1731 |
1.19e-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: 50.92 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1457 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAvRVKAEAEAAREKQRALQAleefrlQAEEAERRLRQ 1536
Cdd:COG4942 15 AAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLA-ALERRIAALARRIRALEQ------ELAALEAELAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1537 AEAERARqvqvaletaqrsAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERW 1616
Cdd:COG4942 88 LEKEIAE------------LRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1617 QLKANEALRLRLQAEEVAQQKSLAQaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQLAEgtaqqrlaAEQE 1696
Cdd:COG4942 156 RADLAELAALRAELEAERAELEALL--------------------AELEEERAALEALKAERQKLLAR--------LEKE 207
|
250 260 270
....*....|....*....|....*....|....*
gi 2124423190 1697 LIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1731
Cdd:COG4942 208 LAELAAELAELQQEAEELEALIARLEAEAAAAAER 242
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3910-3948 |
1.29e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.29e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3910 FLEGTSCIAGVFVDSTKERLSVYQAMKKGIIRPGTAFEL 3948
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1077-1636 |
1.30e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 51.72 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1077 IRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAAL--KKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGER-- 1152
Cdd:PRK10246 250 TRLDELQQEASRRQQALQQALAAEEKAQPQLAALSLAQpaRQLRPHWERIQEQSAALAHTRQQIEEVNTRLQSTMALRar 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1153 --------------------------------DVEVERWRERVAQL------LERWQAVLAqTDLRQRE----------- 1183
Cdd:PRK10246 330 irhhaakqsaelqaqqqslntwlaehdrfrqwNNELAGWRAQFSQQtsdreqLRQWQQQLT-HAEQKLNalpaitltlta 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1184 ------LEQLGRQlRYYRESADPLGAWLQDAKRRQEQIQAMVladSRAVREQLRQEKALLEEIERHGEKVEE-------C 1250
Cdd:PRK10246 409 devaaaLAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQVAI---QNVTQEQTQRNAALNEMRQRYKEKTQQladvktiC 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1251 QRFAKqyinaIKDyelqLVTYKAQLEPvASPAkkPKVQSGSESVIQEYVDLRtryselttltsqyikfISETLRRMEEEE 1330
Cdd:PRK10246 485 EQEAR-----IKD----LEAQRAQLQA-GQPC--PLCGSTSHPAVEAYQALE----------------PGVNQSRLDALE 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1331 RLAEQQRAEERERLAAVEaALEKQRQLAEAHAQAKAQAEQ----EAQEL------QRRMQEEVARREEAAVDAQQQKRSI 1400
Cdd:PRK10246 537 KEVKKLGEEGAALRGQLD-ALTKQLQRDESEAQSLRQEEQaltqQWQAVcaslniTLQPQDDIQPWLDAQEEHERQLRLL 615
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1401 QEelQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEEIRVVRLQLEtterqrggAEGELQA-LRARAEEAeAQKRQAQEEA 1478
Cdd:PRK10246 616 SQ--RHELQGQIAAHNQQIIQYQQQiEQRQQQLLTALAGYALTLP--------QEDEEASwLATRQQEA-QSWQQRQNEL 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1479 ERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQaEAERARQVQVALETAqrsaev 1558
Cdd:PRK10246 685 TALQNRIQQLTPLLETLPQSDDLPHSEETVALDNWRQVHEQCLSLHSQLQTLQQQDVL-EAQRLQKAQAQFDTA------ 757
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1559 eLQSKRasFAEKTAQLERTLQEEhvAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQ 1636
Cdd:PRK10246 758 -LQASV--FDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLVTQTAQALAQHQQHRPDGLDLTVTVEQIQQE 830
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1333-1776 |
1.32e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.45 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1333 AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1412
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1413 AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRK 1492
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1493 RQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1572
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1573 QLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAE 1652
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1653 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKR 1732
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2124423190 1733 QELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAS 1776
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALAS 527
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3332-3370 |
1.40e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 44.63 E-value: 1.40e-05
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3332 LLQGSGCLAGIYLEESKEKVTIYEAMRRGLLRPSTATVL 3370
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1660-1876 |
1.46e-05 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 51.76 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQ-----ELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQE 1734
Cdd:NF012221 1555 DAAQNALADKERAEAdrqrlEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQRDAILEESRAVTKELTTLAQGLDA 1631
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1735 LEAELAKV-------RAEMEVLLasKARAEEESRSTSEKSKQRLEAEASRF----RELAEEAARLRALAEEAKRQRQLAE 1803
Cdd:NF012221 1632 LDSQATYAgesgdqwRNPFAGGL--LDRVQEQLDDAKKISGKQLADAKQRHvdnqQKVKDAVAKSEAGVAQGEQNQANAE 1709
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1804 EDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEER 1876
Cdd:NF012221 1710 QDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQADAKGAKQDESDKPNR 1782
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2228-2393 |
1.46e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 51.03 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2228 RIEAENRALILRDKdntqRVLQEEAEKMKHVAE-----EAARLSVAAQEAARLRELAEEDLAQQ--RALAEKMLKEKMQA 2300
Cdd:COG2268 199 RDARIAEAEAERET----EIAIAQANREAEEAEleqerEIETARIAEAEAELAKKKAEERREAEtaRAEAEAAYEIAEAN 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2301 VQEATRLKAEAELLQQQKELAqeQARRLQEDKEQMAQQLEQetqgfqrtLEAERQRQLEmSAEAErlklrvAEMSRAQAR 2380
Cdd:COG2268 275 AEREVQRQLEIAEREREIELQ--EKEAEREEAELEADVRKP--------AEAEKQAAEA-EAEAE------AEAIRAKGL 337
|
170
....*....|...
gi 2124423190 2381 AEedAQRFRKQAE 2393
Cdd:COG2268 338 AE--AEGKRALAE 348
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2259-2710 |
1.46e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 51.51 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2259 AEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2338
Cdd:COG4995 10 LAALLAALALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2339 LEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEI 2418
Cdd:COG4995 90 LAAALALALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2419 QRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKL 2498
Cdd:COG4995 170 LALAAAALALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAA 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2499 EQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQRLRE 2578
Cdd:COG4995 250 LAAAAAALLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2579 RLQRLEEEHRAALAHSEEIAASQATAVKALPNGRDAPDGPATEAEPEHAFDGLRQKVPAQRLQEVGILSTEELQRLVQGR 2658
Cdd:COG4995 330 LALLALLLLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLL 409
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 2659 TTVAELAQREDVRRYLQGRSSIAGLLLKP--ANEKLSIYTALRRQLLSPGTALI 2710
Cdd:COG4995 410 RLLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1323-1803 |
1.49e-05 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 51.28 E-value: 1.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1323 LRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAeahaQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1402
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1403 ELQHLRQSSE------AEIQAKARQVEAAERSRLRIEEEIR--VVRLQLET-------TERQRGGAEGELQALRARAEEA 1467
Cdd:pfam05557 133 ELEELQERLDllkakaSEAEQLRQNLEKQQSSLAEAEQRIKelEFEIQSQEqdseivkNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1468 EAQKRQAQEEAERLRRQVQDETQRKRQAEaelavrvKAEAEAAR---EKQRALQALEEFRLQAEEAERRLRQAEAERARQ 1544
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLEREE-------KYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1545 VQValetaqRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL-----ERWQLK 1619
Cdd:pfam05557 286 EQL------QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkERDGYR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1620 AN-EALRLRLQAEEVAQQKSLAQAEAE----KQKEEAEREARRRGKAEEQAVRQRELA---EQELEKQRQlAEGTAQQRL 1691
Cdd:pfam05557 360 AIlESYDKELTMSNYSPQLLERIEEAEdmtqKMQAHNEEMEAQLSVAEEELGGYKQQAqtlERELQALRQ-QESLADPSY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1692 AAE------QELIRLRAETEQGEQQRQLLEEELAR--------------LQHEAAAATQKRQELEAELAKVRAEMEvlla 1751
Cdd:pfam05557 439 SKEevdslrRKLETLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIE---- 514
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1752 skaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEA-KRQRQLAE 1803
Cdd:pfam05557 515 ---RLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAeLKNQRLKE 564
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
932-1484 |
1.56e-05 |
|
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: 51.66 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 932 DRLQAEREYGSCSHHYQQLLQSLEQGEQEESrcqrcISELKDIRL-QLEACETRTVHRLRLPLDK---EPARECAQRIAE 1007
Cdd:pfam15921 364 ERDQFSQESGNLDDQLQKLLADLHKREKELS-----LEKEQNKRLwDRDTGNSITIDHLRRELDDrnmEVQRLEALLKAM 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1008 QQKAQAEVEGLGKGVARLSAEAEKVlalpepspaaPTLRSELELTLGKLEQVrslsaiyLEKLKTISLVIRSTHGAEEVL 1087
Cdd:pfam15921 439 KSECQGQMERQMAAIQGKNESLEKV----------SSLTAQLESTKEMLRKV-------VEELTAKKMTLESSERTVSDL 501
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1088 KAHEEQLKEAqavpatlpeLEATKAALKKLRAQAEAQQPMFDALRDE---LRGAQEVGERLQQRHGERDVEVERWRERVA 1164
Cdd:pfam15921 502 TASLQEKERA---------IEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTECEALKLQMAEKDKVIEILRQQIE 572
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1165 QLLE-------RWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALL 1237
Cdd:pfam15921 573 NMTQlvgqhgrTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIK 652
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1238 EEIERHGEKVEECQrfaKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyik 1317
Cdd:pfam15921 653 QERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQ------------LKSAQSELEQTRN---- 713
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1318 fiseTLRRMEEEERlaeqqraeererlAAVEAALEKQRQLAEAHAQAKAqaeqeaqelqrrMQEEVARREEAAVDAQQQK 1397
Cdd:pfam15921 714 ----TLKSMEGSDG-------------HAMKVAMGMQKQITAKRGQIDA------------LQSKIQFLEEAMTNANKEK 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1398 RSIQEELQHLRQssEAEIQAKARQVEAAERSRLRIEEEirvvRLQLETTERQRGGAEGELQAlrarAEEAEAQKRQAQEE 1477
Cdd:pfam15921 765 HFLKEEKNKLSQ--ELSTVATEKNKMAGELEVLRSQER----RLKEKVANMEVALDKASLQF----AECQDIIQRQEQES 834
|
....*..
gi 2124423190 1478 AeRLRRQ 1484
Cdd:pfam15921 835 V-RLKLQ 840
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
603-693 |
1.70e-05 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 46.55 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 603 FVAAATKELMWLSEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEIQNTGDRLLREDHPARPTVESFQAAL 682
Cdd:smart00150 3 FLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLEEL 82
|
90
....*....|.
gi 2124423190 683 QTQWSWMLQLC 693
Cdd:smart00150 83 NERWEELKELA 93
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1251-1582 |
1.78e-05 |
|
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: 51.17 E-value: 1.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1251 QRFAKQYINAIKDYelqlvtYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRY-SELTTLTSQyikfiSETLRRMEEE 1329
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1330 ERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQ----------ELQRRMQE-EVARREEAAVDAQQQKR 1398
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyktlELEIAESDvEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1399 SIQEELQHLRQSSEAEiQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEA----EAQKRQA 1474
Cdd:NF033838 201 RDEEKIKQAKAKVESK-KAEATRLEKIKTDREKAEEEAKRRADAKLKEAVEKNVATSEQDKPKRRAKRGvlgePATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1475 QEEAERLRRQVQDET-------QRKRQAEAELAV-RVKAEAEAAREKQR---ALQALEEFRLQAEEAERRLRQAEA---- 1539
Cdd:NF033838 280 ENDAKSSDSSVGEETlpspslkPEKKVAEAEKKVeEAKKKAKDQKEEDRrnyPTNTYKTLELEIAESDVKVKEAELelvk 359
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2124423190 1540 ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1582
Cdd:NF033838 360 EEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1324-1497 |
1.91e-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: 50.72 E-value: 1.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1324 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAE----QEAQELQRRMQEEVARreEAAVDAQQQKRS 1399
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEerqrQEEEERKQRLQLQAAQ--ERARQQQEEFRR 430
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1400 IQEELQHLRQSSEAEiqakarqvEAAERSRLRIEEEIRVVrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEae 1479
Cdd:pfam15709 431 KLQELQRKKQQEEAE--------RAEAEKQRQKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE-- 496
|
170
....*....|....*...
gi 2124423190 1480 rlRRQVQDETQRKRQAEA 1497
Cdd:pfam15709 497 --RRQKEEEAARLALEEA 512
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2233-2605 |
1.97e-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: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2233 NRALILRDKDNTQRvlQEEAEKMKHVAEEAARLSVAAQEAARLRElAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2307
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEELSA-RESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2308 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGF--QRTLEAERQRQLEMSAEAERLkLRVAE 2373
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2374 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQL 2453
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2454 KSEEMQtvqqeqllqetqalqqsflsekdtlLQRERFIEQEKAKLEQLFQdEVAKAQKLREEQQRQQKQMEEEKQQLVAS 2533
Cdd:COG3096 505 RSQQAL-------------------------AQRLQQLRAQLAELEQRLR-QQQNAERLLEEFCQRIGQQLDAAEELEEL 558
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 2534 MEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQR------LRERLQRLEEEHRAALAHSEEIAASQATAV 2605
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQEVTAAMQQLL 636
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2239-2394 |
1.98e-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: 50.72 E-value: 1.98e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2239 RDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2315
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 2316 QQKELAQEQARRLQEDKEqmaQQLEQETQgfqrtLEAERQRQLEMsAEAERLKLRvAEMSRAQARAEEDAQRFRKQAEE 2394
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQ---RQKELEMQ-----LAEEQKRLMEM-AEEERLEYQ-RQKQEAEEKARLEAEERRQKEEE 503
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1499-1747 |
2.14e-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: 2.14e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1499 LAVRVKAEAEAAREKQRALQALEEfRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTL 1578
Cdd:COG4942 11 LALAAAAQADAAAEAEAELEQLQQ-EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1579 QEEHVAVAQLREEAERRAQQQAEAerareeaerelerWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRR 1658
Cdd:COG4942 90 KEIAELRAELEAQKEELAELLRAL-------------YRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1659 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlaaeqeliRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1738
Cdd:COG4942 157 ADLAELAALRAELEAERAELEALLAELEEERA--------ALEALKAERQKLLARLEKELAELAAELAELQQEAEELEAL 228
|
....*....
gi 2124423190 1739 LAKVRAEME 1747
Cdd:COG4942 229 IARLEAEAA 237
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1358-1573 |
2.29e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 50.21 E-value: 2.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1358 AEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKARQVEAAERsrlRIEEEIR 1437
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEAL----QAEIDKLQAEIAEAEA---EIEERRE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1438 VVRLQLETTERQrGGAEGELQAL--------------------RARAEEAEAQKrQAQEEAERLRRQVQDETQRKRQAEA 1497
Cdd:COG3883 87 ELGERARALYRS-GGSVSYLDVLlgsesfsdfldrlsalskiaDADADLLEELK-ADKAELEAKKAELEAKLAELEALKA 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1498 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1573
Cdd:COG3883 165 ELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1751-1950 |
2.31e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.19 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1751 ASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLAEKLAAIGEATRL 1830
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1831 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIL 1910
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 2124423190 1911 ALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELE 1950
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1669-2391 |
2.61e-05 |
|
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: 50.89 E-value: 2.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1669 RELAEQELEKQRQLAEGTAQQRLAAE---QELIRLRAETEQGEQQRQLLEEELARLQHEA--AAATQKRQELEAELAKVR 1743
Cdd:pfam15921 158 KCLKEDMLEDSNTQIEQLRKMMLSHEgvlQEIRSILVDFEEASGKKIYEHDSMSTMHFRSlgSAISKILRELDTEISYLK 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1744 AEM----EVLLASKARAEEESRSTSEKSKQRLEAEASR----FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1815
Cdd:pfam15921 238 GRIfpveDQLEALKSESQNKIELLLQQHQDRIEQLISEheveITGLTEKASSARSQANSIQSQLEIIQEQARNQNSMYMR 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1816 VLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErlaQLRKASESELERQKGLV 1895
Cdd:pfam15921 318 QLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDD---QLQKLLADLHKREKELS 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1896 EDTLRQRRQVEEEIlalkvsfekaaaGKAeleLELGRIRSNAEDtlRSKEQAELEAMRQrqlaaeeeqrrrEAEERVQKS 1975
Cdd:pfam15921 395 LEKEQNKRLWDRDT------------GNS---ITIDHLRRELDD--RNMEVQRLEALLK------------AMKSECQGQ 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1976 LAAEEEAARQRKAALEEVERLKAKVEEARR-LRERAEQESARQLQLAqdaAQKRLQAEEKAhafAVQQKEQELQQTLQQE 2054
Cdd:pfam15921 446 MERQMAAIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMTLE---SSERTVSDLTA---SLQEKERAIEATNAEI 519
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2055 QSMLERLRgeaeaarraaeeaeeareraereaaqsrRQVEEAERLKQSAEEQAQAQAQAQAAAEKLrkeaeqeaaRRAQA 2134
Cdd:pfam15921 520 TKLRSRVD----------------------------LKLQELQHLKNEGDHLRNVQTECEALKLQM---------AEKDK 562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2135 EQAALRQKQAADAEM-EKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV----E 2209
Cdd:pfam15921 563 VIEILRQQIENMTQLvGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagS 642
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2210 EELFSLRVQMEELGKLKARIEAENRAL--ILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQ---EAAR--LRELAEED 2282
Cdd:pfam15921 643 ERLRAVKDIKQERDQLLNEVKTSRNELnsLSEDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQselEQTRntLKSMEGSD 722
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2283 -------LAQQRALAEK-----MLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRT 2349
Cdd:pfam15921 723 ghamkvaMGMQKQITAKrgqidALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRL 802
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 2124423190 2350 leaeRQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQ 2391
Cdd:pfam15921 803 ----KEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1444-1581 |
2.63e-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: 2.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1444 ETTERQRGGAEGELQALRARAEEAEAQKRQAQEeaerlrRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF 1523
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK------QRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEE 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1524 RLQAEEAERRlRQAEAERARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1581
Cdd:TIGR02794 124 AKAKQAAEAK-AKAEAEAERK---AKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEA 177
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1355-1482 |
2.75e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 2.75e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1355 RQLAEAHAQAKAQ-----AEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSR 1429
Cdd:COG1566 79 TDLQAALAQAEAQlaaaeAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAAL 157
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1430 LRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1482
Cdd:COG1566 158 DAAQAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1629-1805 |
2.80e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 49.80 E-value: 2.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1629 QAEEVAQQKslaQAEAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1704
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1705 EQGEQQRQLLEEELArlQHEAAAATQKRQELEA-----ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRfr 1779
Cdd:PRK09510 161 KKAAAEAKKKAEAEA--AKKAAAEAKKKAEAEAaakaaAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKA-- 236
|
170 180
....*....|....*....|....*.
gi 2124423190 1780 elAEEAARLRALAEEAKRQRQLAEED 1805
Cdd:PRK09510 237 --AAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1330-1815 |
3.00e-05 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 50.04 E-value: 3.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1330 ERLAEQQRAEERERlAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ 1409
Cdd:COG3064 2 QEALEEKAAEAAAQ-ERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1410 SSEAEIQAKARQVeAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDET 1489
Cdd:COG3064 81 EAEKAAAEAEKKA-AAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1490 QRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAE 1569
Cdd:COG3064 160 AAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1570 KTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKE 1649
Cdd:COG3064 240 TEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1650 EAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAAT 1729
Cdd:COG3064 320 AAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1730 QKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQ 1809
Cdd:COG3064 400 LLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLAD 479
|
....*.
gi 2124423190 1810 RAEAER 1815
Cdd:COG3064 480 LLLLGG 485
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1334-1557 |
3.15e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 49.98 E-value: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1334 EQQRAEERERLAAveaalEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE---ELQHLRQS 1410
Cdd:PRK07735 3 PEKDLEDLKKEAA-----RRAKEEARKRLVAKHGAEISKLEEENREKEKALPKNDDMTIEEAKRRAAAAakaKAAALAKQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1411 SEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE-----AEAQKRQAQEEAERLRRQV 1485
Cdd:PRK07735 78 KREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAaakakAAALAKQKREGTEEVTEEE 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 1486 QDETQRKRQAEAELAVRVKAeaeAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1557
Cdd:PRK07735 158 EETDKEKAKAKAAAAAKAKA---AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQG 226
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1155-1395 |
3.78e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.87 E-value: 3.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1155 EVERWRERVAQLLERWQAVLAQTDLRQREL------EQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVRE 1228
Cdd:pfam02029 60 EEEAFLDRTAKREERRQKRLQEALERQKEFdptiadEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKE 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1229 QLRQ-----EKALLEEIERHGEKVEECQRFAKQyinAIKDYELQLVTYKAQLEPVASPAK---------KPKVQSGSESV 1294
Cdd:pfam02029 140 YQENkwsteVRQAEEEGEEEEDKSEEAEEVPTE---NFAKEEVKDEKIKKEKKVKYESKVfldqkrghpEVKSQNGEEEV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1295 IQEYVDLRTRYSELTTL--TSQYIKFISETLRRMEEEERLAEQQRAEERERL------AAVEAAL-----EKQRQLAEAH 1361
Cdd:pfam02029 217 TKLKVTTKRRQGGLSQSqeREEEAEVFLEAEQKLEELRRRRQEKESEEFEKLrqkqqeAELELEElkkkrEERRKLLEEE 296
|
250 260 270
....*....|....*....|....*....|....*...
gi 2124423190 1362 AQAKAQAEQEAQ----ELQRRMQEEVARREEAAVDAQQ 1395
Cdd:pfam02029 297 EQRRKQEEAERKlreeEEKRRMKEEIERRRAEAAEKRQ 334
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2139-2441 |
3.79e-05 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 49.68 E-value: 3.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 LRQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQksildeeLQRLKAEVTEAARQRSQVEEELFSLRVQ 2218
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2219 MEELGKLKARIEAENRALILRDKDNTQRVLQEEAEkmkhvaeeaarlsVAAQEAARLRELAEEDLAQQRALAEKM-LKEK 2297
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2298 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLEQETQGFQRT---LEAERQRQLEMSAEAERLKLRVAEM 2374
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 2375 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLRqaiAELEREK 2441
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLK---EELQRER 384
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1405-1693 |
3.87e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.95 E-value: 3.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1405 QHLRQSsEAEIQAKARQVEAAERSRLRIEEeirvvrlqletteRQrggaegelqalrARAEeaeaqkRQAQEEAERLRRQ 1484
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA-------------RQ------------ARLE------REKAAREARHKKA 476
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1485 VQDETQRKRQAEAELAVRVKAeAEAAREKQRALQALEEFRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVEL--- 1560
Cdd:PRK05035 477 AEARAAKDKDAVAAALARVKA-KKAAATQPIVIKAGARPDNSAVIAAREARKAQArARQAEKQAAAAADPKKAAVAAaia 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1561 --QSKRASFAEKTAQLERTLQEEHVAVAQlREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1638
Cdd:PRK05035 556 raKAKKAAQQAANAEAEEEVDPKKAAVAA-AIARAKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQAN 634
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1639 LAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1693
Cdd:PRK05035 635 AEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1617-2035 |
4.31e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 49.52 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1617 QLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1696
Cdd:COG5278 105 QQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAA 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1697 LIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAS 1776
Cdd:COG5278 185 LLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLA 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1777 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEA 1856
Cdd:COG5278 265 AALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAAL 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1857 FQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSN 1936
Cdd:COG5278 345 ALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALEL 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1937 AEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESAR 2016
Cdd:COG5278 425 AEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAALAEAEAAAALAAAAALSLALA 504
|
410
....*....|....*....
gi 2124423190 2017 QLQLAQDAAQKRLQAEEKA 2035
Cdd:COG5278 505 LAALLLAAAEAALAAALAA 523
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1300-1580 |
4.48e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.51 E-value: 4.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1300 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLaEAHAQAKAQAEQEAQELQRRM 1379
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1380 QEEVARREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGE 1456
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1457 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEA 1530
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEA 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1531 --ERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQE 1580
Cdd:pfam07888 316 dkDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4118-4146 |
4.58e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.58e-05
10 20
....*....|....*....|....*....
gi 2124423190 4118 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4146
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1084-1800 |
4.68e-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: 49.75 E-value: 4.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1084 EEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAqqpmfdaLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1162
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1163 VAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESAdplGAWLQDAKRRQEQIQAMVladsRAVREQLRQEKALLEEIER 1242
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRKQL----SKTQEELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1243 H-GEKV------EECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELTTLTSQY 1315
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1316 IKFISETLRRMEEEE-RLAEQQRAEERERLAAVEaalEKQRQLAEAHAQAKAQAEQEAQeLQRRMQEEVARREEAAVDAq 1394
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDKAAEVEVERMSA- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1395 qqkRSIQEELQhlrQSSEAEIQAKARQVEAAERSRLrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQA 1474
Cdd:pfam07111 376 ---KGLQMELS---RAQEARRRQQQQTASAEEQLKF-VVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1475 QEEAER--LRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEF--RLQAEEAERRLRQAEAERARQVQVALE 1550
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDAELQLsaHLIQQEVGRAREQGEAERQQLSEVAQQ 528
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1551 TAQrsaevELQSKRASFAEKTAQLERTLQEEhvavaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRlqa 1630
Cdd:pfam07111 529 LEQ-----ELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR--- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1631 EEVAQQKSLAQAEAEKQKEEAEREARrrgkaEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE-----QELIRLRAETE 1705
Cdd:pfam07111 566 QELTQQQEIYGQALQEKVAEVETRLR-----EQLSDTKRRLNEARREQAKAVVSLRQIQHRATQekernQELRRLQDEAR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1706 QGEQQR-----QLLEEE----LARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRL 1771
Cdd:pfam07111 641 KEEGQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSL 720
|
730 740
....*....|....*....|....*....
gi 2124423190 1772 EAEASRFRELAEEAARLRALAEEAKRQRQ 1800
Cdd:pfam07111 721 TVLLDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2258-2460 |
4.80e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.07 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2258 VAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2337
Cdd:TIGR02794 48 VAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAK 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2338 QLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQTLE 2417
Cdd:TIGR02794 128 QAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AAKA 203
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2124423190 2418 IQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2460
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNA 246
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1388-1594 |
4.97e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 49.07 E-value: 4.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1388 EAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRieeeirvvrlqletTERQRGGAEGELQALRARAEEA 1467
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQK--------------ELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1468 EAQKRQAQEEAErlrrqvQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERrlrQAEAERArqvqv 1547
Cdd:TIGR02794 115 EEKQKQAEEAKA------KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK---KAEAEAK----- 180
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 2124423190 1548 ALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAER 1594
Cdd:TIGR02794 181 AKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2139-2668 |
5.01e-05 |
|
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: 49.97 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILdeelqRLKAEVTEAARQRSQVEEELFSLRVQ 2218
Cdd:TIGR00618 245 LTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAA-----PLAAHIKAVTQIEQQAQRIHTELQSK 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2219 MEELGKLKARIEA--ENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAA---RLRELAEE---DLAQQRALA 2290
Cdd:TIGR00618 320 MRSRAKLLMKRAAhvKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTltqHIHTLQQQkttLTQKLQSLC 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2291 EKMLKEKMQAVQEATRLKAEAELlQQQKELAQEQARRLQEDKEQMAQQLEQETQ-----------GFQRTLEAERQ---- 2355
Cdd:TIGR00618 400 KELDILQREQATIDTRTSAFRDL-QGQLAHAKKQQELQQRYAELCAAAITCTAQceklekihlqeSAQSLKEREQQlqtk 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2356 -----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERL 2430
Cdd:TIGR00618 479 eqihlQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2431 RQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQeqllqetqaLQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQ 2510
Cdd:TIGR00618 559 ASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQN---------ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2511 KLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEE-----------NQRLRER 2579
Cdd:TIGR00618 630 VRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQltywkemlaqcQTLLREL 709
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2580 LQRLEEEHR-------AALAHSEEIAASQATAVKALPNGRDAPDGPATEAEPEHAFDGLRQKVPAQRLQEVGILSTEELQ 2652
Cdd:TIGR00618 710 ETHIEEYDRefneienASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQF 789
|
570
....*....|....*.
gi 2124423190 2653 RLVQGRTTVAELAQRE 2668
Cdd:TIGR00618 790 FNRLREEDTHLLKTLE 805
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2140-2449 |
5.02e-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: 49.72 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2140 RQKQAADAEME--KHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRV 2217
Cdd:pfam05483 448 REKEIHDLEIQltAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKK 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2218 QMEELgkLKARIEAENRALILRDKDNTQR--VLQEEAE---KMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEK 2292
Cdd:pfam05483 528 QEERM--LKQIENLEEKEMNLRDELESVReeFIQKGDEvkcKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIEN 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2293 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVA 2372
Cdd:pfam05483 606 KNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIAD 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2373 EMSRAQ---------------ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAEL 2437
Cdd:pfam05483 686 EAVKLQkeidkrcqhkiaemvALMEKHKHQYDKIIEERDSELGLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIE 765
|
330
....*....|..
gi 2124423190 2438 EREKEKLKQEAK 2449
Cdd:pfam05483 766 KEEKEKLKMEAK 777
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1660-1875 |
5.30e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.56 E-value: 5.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1731
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1732 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE--EAKRQRQLAEEDAARQ 1809
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARakAKKAAQQAASAEPEEQ 606
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1810 RAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEE 1875
Cdd:PRK05035 607 VAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEA 672
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1320-1802 |
5.36e-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: 49.75 E-value: 5.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1320 SETLRRMEEEERLAEQQRAEE--RERLAAVEAALEKQRQLAEA-----HAQAKAQAEQEAQELQRR-MQEEVARREEAAV 1391
Cdd:pfam07111 180 SLETKRAGEAKQLAEAQKEAEllRKQLSKTQEELEAQVTLVESlrkyvGEQVPPEVHSQTWELERQeLLDTMQHLQEDRA 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1392 DAQQQKRSIQ---EELQHLRQSSEAEIQAKARQVEAAE-------RSRL-RIEEEIRVVRLQLETTERQRggaEGELQAL 1460
Cdd:pfam07111 260 DLQATVELLQvrvQSLTHMLALQEEELTRKIQPSDSLEpefpkkcRSLLnRWREKVFALMVQLKAQDLEH---RDSVKQL 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1461 RARAEEAEAQKRQAQEEAERLRRQVQDETqrkrqaeAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAeAE 1540
Cdd:pfam07111 337 RGQVAELQEQVTSQSQEQAILQRALQDKA-------AEVEVERMSAKGLQMELSRAQEARRRQQQQTASAEEQLKFV-VN 408
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1541 RARQVQVALETA-----QRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELER 1615
Cdd:pfam07111 409 AMSSTQIWLETTmtrveQAVARIPSLSNRLSYAVRKVHTIKGLMARKVALAQLRQESCPPPPPAPPVDADLSLELEQLRE 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1616 WQLKANEALRL-------------------RLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQEL 1676
Cdd:pfam07111 489 ERNRLDAELQLsahliqqevgrareqgeaeRQQLSEVAQQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQEL 568
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1677 EKQRQLAeGTAQQRLAAEQElIRLRAETEQGEQQRQLLEEELAR-------LQHEAAAATQKRQELEaelakvraemevl 1749
Cdd:pfam07111 569 TQQQEIY-GQALQEKVAEVE-TRLREQLSDTKRRLNEARREQAKavvslrqIQHRATQEKERNQELR------------- 633
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1750 laskaRAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLA 1802
Cdd:pfam07111 634 -----RLQDEARKEEGQRLARRVQELERDKNLMLATLQQEGLLSRYKQQRLLA 681
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1659-1781 |
5.76e-05 |
|
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: 48.28 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1659 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQRQLLEEELARLQH-----EAAAATQKR 1732
Cdd:pfam17045 127 GKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRKQCLEASQSEIQRlrsklERAQDSLCA 206
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 1733 QELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEASRFREL 1781
Cdd:pfam17045 207 QELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2260-2601 |
6.21e-05 |
|
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: 49.58 E-value: 6.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2260 EEAARLSVAAQEAARLRELAEEDLAQQRALAEKMlKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2339
Cdd:pfam02463 160 EEAAGSRLKRKKKEALKKLIEETENLAELIIDLE-ELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEER 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2340 EQETQGFQRTLEAERQ-----RQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQ 2414
Cdd:pfam02463 239 IDLLQELLRDEQEEIEsskqeIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKL-ERRKVDDEEKLK 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2415 TLEIQRQQSDHDAERLRQAIAELEREKeKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQE 2494
Cdd:pfam02463 318 ESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEE 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2495 KAKLEQLFQdEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEENQ 2574
Cdd:pfam02463 397 LELKSEEEK-EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLK 475
|
330 340
....*....|....*....|....*..
gi 2124423190 2575 RLRERLQRLEEEHRAALAHSEEIAASQ 2601
Cdd:pfam02463 476 ETQLVKLQEQLELLLSRQKLEERSQKE 502
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1333-1494 |
6.22e-05 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 49.13 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1333 AEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1412
Cdd:PRK12678 65 AAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1413 AEIQAKARQVEAAERSRLRIEEEirvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEaERLRRQVQDETQRK 1492
Cdd:PRK12678 145 AGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREERGRDGD-DRDRRDRREQGDRR 215
|
..
gi 2124423190 1493 RQ 1494
Cdd:PRK12678 216 EE 217
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1776-2022 |
6.41e-05 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 49.12 E-value: 6.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1776 SRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDE 1855
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1856 AFQRRRLEEQAAQHKADIEE------RLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELE 1929
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1930 LGRIRSnaedtlrSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEE--AARQRKAALEE-VERLKAKVEEARRL 2006
Cdd:pfam07888 194 FQELRN-------SLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEElrSLQERLNASERkVEGLGEELSSMAAQ 266
|
250
....*....|....*..
gi 2124423190 2007 RERAEQESAR-QLQLAQ 2022
Cdd:pfam07888 267 RDRTQAELHQaRLQAAQ 283
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2141-2349 |
6.59e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 48.67 E-value: 6.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2141 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAAR--QRSQVEEELFSLRVQ 2218
Cdd:COG3883 31 ELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalYRSGGSVSYLDVLLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2219 MEELGKLKARIEAENRaLILRDKD--NTQRVLQEEAEKMKHVAEEA-ARLSVAAQEAARLRELAEEDLAQQRALAEKMLK 2295
Cdd:COG3883 111 SESFSDFLDRLSALSK-IADADADllEELKADKAELEAKKAELEAKlAELEALKAELEAAKAELEAQQAEQEALLAQLSA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 2296 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRT 2349
Cdd:COG3883 190 EEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2230-2347 |
6.84e-05 |
|
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.
Pssm-ID: 293879 [Multi-domain] Cd Length: 291 Bit Score: 47.96 E-value: 6.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2230 EAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEaarlRELAEEDLAQQRALAE--KMLKEKMQavQEATRL 2307
Cdd:cd16269 180 EAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----RELEQKLEDQERSYEEhlRQLKEKME--EERENL 253
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2124423190 2308 KAEAELLQQQKElaQEQARRLQEDKEQMAQQLEQETQGFQ 2347
Cdd:cd16269 254 LKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1324-1543 |
6.89e-05 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 48.82 E-value: 6.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1324 RRMEEEERLAEQQRAEER--ERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ 1401
Cdd:PRK07735 29 KHGAEISKLEEENREKEKalPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAKAKAKAAAAAKAKAAAL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1402 EELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1481
Cdd:PRK07735 109 AKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTEEEEETDKEKAKAKAAAAAKAKAAALAKQKAAEA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1482 RRQVQDETQR-KRQAEAELAVRVKAEAeAAREKQRALQ----ALEEFRLQAEEAERRLRQAEAERAR 1543
Cdd:PRK07735 189 GEGTEEVTEEeKAKAKAKAAAAAKAKA-AALAKQKASQgngdSGDEDAKAKAIAAAKAKAAAAARAK 254
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1461-1582 |
6.95e-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: 6.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1461 RARAEEAEAQ------KRQAQEEAerlRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQralQALEEFRLQAEEAER-- 1532
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1533 -RLRQAEAERARQVQVA----LETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1582
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQ 465
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1980-2453 |
7.26e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 49.00 E-value: 7.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1980 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEekahAFAVQQKEQELQQTLQQEQSMLE 2059
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ----LLPLYQELEALEAELAELPERLE 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2060 RLRgeaeaarraaeeaeeareraereaaQSRRQVEEAERlkqsaeeqaqaqaqaqaaaeKLRKEAEQEAARRAQAEQAAL 2139
Cdd:COG4717 150 ELE-------------------------ERLEELRELEE--------------------ELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2140 RQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA-EVTEAARQRSQVEEELFSLRVQ 2218
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALeERLKEARLLLLIAAALLALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2219 MEELGKLKARI------EAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEK 2292
Cdd:COG4717 265 GGSLLSLILTIagvlflVLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2293 MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQrtlEAERQRQLEMSAEAERLKLRVA 2372
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQE---LKEELEELEEQLEELLGELEEL 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2373 EMSRAQARAEEDAQRFRKQAEEIGEKL--HRTELATQEkvtlvqtLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKL 2450
Cdd:COG4717 422 LEALDEEELEEELEELEEELEELEEELeeLREELAELE-------AELEQLEEDGELAELLQELEELKAELRELAEEWAA 494
|
...
gi 2124423190 2451 LQL 2453
Cdd:COG4717 495 LKL 497
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
18-122 |
7.45e-05 |
|
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409134 Cd Length: 121 Bit Score: 45.34 E-value: 7.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 18 DRVQKKTFTKWVNKHLIKhwrAEAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHR 95
Cdd:cd21285 8 NGFDKQIYTDWANHYLAK---SGHKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAK 84
|
90 100
....*....|....*....|....*..
gi 2124423190 96 QVKLVNIRNDDIADGNPKLTLGLIWTI 122
Cdd:cd21285 85 GINIQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1780-2015 |
7.53e-05 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 48.61 E-value: 7.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1780 ELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRlaedeafQR 1859
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEK-------EI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1860 RRLEEQAAQHKADIEERLAQLRKASESE----LERQKGlVEDTLRQRRQVEEEILALKVSFEKAAAGKAELElelgRIRS 1935
Cdd:COG4942 93 AELRAELEAQKEELAELLRALYRLGRQPplalLLSPED-FLDAVRRLQYLKYLAPARREQAEELRADLAELA----ALRA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1936 NAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESA 2015
Cdd:COG4942 168 ELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTPAAG 247
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3779-3815 |
8.34e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 8.34e-05
10 20 30
....*....|....*....|....*....|....*..
gi 2124423190 3779 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3815
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
21-133 |
8.83e-05 |
|
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: 45.80 E-value: 8.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 21 QKKTFTKWVNKHL-----IKHWRAEAQRHISdLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDY 91
Cdd:cd21323 25 EKVAFVNWINKALegdpdCKHVVPMNPTDES-LFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNS 103
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2124423190 92 LRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 133
Cdd:cd21323 104 ASAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1106-1576 |
8.94e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 48.91 E-value: 8.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1106 ELEATKAALKKLRAQAEAQQPMFDALRDELrgaqevgERLQQRHGERDVEVERWRERVAQLLERWQAVlaqtDLRQRELE 1185
Cdd:PRK03918 173 EIKRRIERLEKFIKRTENIEELIKEKEKEL-------EEVLREINEISSELPELREELEKLEKEVKEL----EELKEEIE 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1186 QLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVladsravrEQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYE 1265
Cdd:PRK03918 242 ELEKELESLEGSKRKLEEKIRELEERIEELKKEI--------EELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIE 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1266 LQLVTYKAQLEPVASPAKK-PKVQSGSESVIQEYVDLRTRYSELTTltsqYIKFISETLRRMEEEERLAEQQRAEERERL 1344
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKElEEKEERLEELKKKLKELEKRLEELEE----RHELYEEAKAKKEELERLKKRLTGLTPEKL 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1345 AAVEAALEKqrqlaeahaqAKAQAEQEAQELQRR---MQEEVARREEAAVDAQQQK-------RSIQEE--LQHLRQSSE 1412
Cdd:PRK03918 390 EKELEELEK----------AKEEIEEEISKITARigeLKKEIKELKKAIEELKKAKgkcpvcgRELTEEhrKELLEEYTA 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1413 --AEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEgELQALRAR-----AEEAEAQKRQAQEEAERLR--- 1482
Cdd:PRK03918 460 elKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAE-QLKELEEKlkkynLEELEKKAEEYEKLKEKLIklk 538
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1483 ---RQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQA-EEAERRLRQAE--------AERARQVQVALE 1550
Cdd:PRK03918 539 geiKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESvEELEERLKELEpfyneyleLKDAEKELEREE 618
|
490 500
....*....|....*....|....*.
gi 2124423190 1551 TAQRSAEVELQSKRASFAEKTAQLER 1576
Cdd:PRK03918 619 KELKKLEEELDKAFEELAETEKRLEE 644
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1385-1738 |
8.96e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.36 E-value: 8.96e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1385 RREEAAVDAQQQKRSIQEELQHLRQsseaEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARA 1464
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1465 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQ 1544
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1545 VQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1624
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1625 RLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1704
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 2124423190 1705 EQGEQQRQLLEEELARLQHEAAAATQKRQELEAE 1738
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1513-2412 |
9.46e-05 |
|
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: 48.96 E-value: 9.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1513 KQRALQALEEFRLQAEEAERRLRQAEAERARQ----------VQVALETAQ--RSAEVELQSKRASFAEKTA-QLERTLQ 1579
Cdd:pfam15921 73 KEHIERVLEEYSHQVKDLQRRLNESNELHEKQkfylrqsvidLQTKLQEMQmeRDAMADIRRRESQSQEDLRnQLQNTVH 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1580 EEHVAVAQLREEAERRAQQQAEAERAREEAERELErwqlkanEALRLRLQAEEVAQQKslaqaeAEKQKEEAEREARRRG 1659
Cdd:pfam15921 153 ELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ-------EIRSILVDFEEASGKK------IYEHDSMSTMHFRSLG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRqrelaeqELEKQRQLAEGtaqQRLAAEQELIRLRAETEQG-----EQQRQLLEEELARLQHEAAAATQKRQE 1734
Cdd:pfam15921 220 SAISKILR-------ELDTEISYLKG---RIFPVEDQLEALKSESQNKielllQQHQDRIEQLISEHEVEITGLTEKASS 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1735 LEAELAKVRAEMEVLlaskaraEEESRSTSE---KSKQRLEAEASRFRELAEEAARL-RALAEEAKRQRQLAEEDAARQR 1810
Cdd:pfam15921 290 ARSQANSIQSQLEII-------QEQARNQNSmymRQLSDLESTVSQLRSELREAKRMyEDKIEELEKQLVLANSELTEAR 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1811 AEAERVLAEKLAAIGEATRL-----KTEAEIALkEKEaENER--------------LRRLAEDEAFQRRRLEEQAAQHKA 1871
Cdd:pfam15921 363 TERDQFSQESGNLDDQLQKLladlhKREKELSL-EKE-QNKRlwdrdtgnsitidhLRRELDDRNMEVQRLEALLKAMKS 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1872 D----IEERLAQLRKASESeLERQKGL---VEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTlrsk 1944
Cdd:pfam15921 441 EcqgqMERQMAAIQGKNES-LEKVSSLtaqLESTKEMLRKVVEELTAKKMTLESSERTVSDLTASLQEKERAIEAT---- 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1945 eQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEV-ERLKAKVEEARRL-RERAEQESARQL---Q 2019
Cdd:pfam15921 516 -NAEITKLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKViEILRQQIENMTQLvGQHGRTAGAMQVekaQ 594
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2020 LAQDAAQKRLQAEEKAhafAVQQKEQELQQTLQQEQSMLE----RLRGEAEAARRAAEEAEEARERAEREAAQSRRQV-- 2093
Cdd:pfam15921 595 LEKEINDRRLELQEFK---ILKDKKDAKIRELEARVSDLElekvKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELns 671
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2094 --EEAERLKQSAEEQAQAQAQAQAAAeklrKEAEQEAARRAQAEQAALRQKQAADAE-MEKHKKFAEQTLRQKAQV---E 2167
Cdd:pfam15921 672 lsEDYEVLKRNFRNKSEEMETTTNKL----KMQLKSAQSELEQTRNTLKSMEGSDGHaMKVAMGMQKQITAKRGQIdalQ 747
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2168 QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEaenralILRDKDNTQrv 2247
Cdd:pfam15921 748 SKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGELEVLRSQERRLKEKVANME------VALDKASLQ-- 819
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2248 LQEEAEKMKHVAEEAARLSVaaQEAARLRELAEEDLAQQRALAEKMLKEkmqavQEATRLKAEAELLQQQKELAQEQARR 2327
Cdd:pfam15921 820 FAECQDIIQRQEQESVRLKL--QHTLDVKELQGPGYTSNSSMKPRLLQP-----ASFTRTHSNVPSSQSTASFLSHHSRK 892
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2328 ---LQEDKEQMAQQLEQETQ---GFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLhr 2401
Cdd:pfam15921 893 tnaLKEDPTRDLKQLLQELRsviNEEPTVQLSKAEDKGRAPSLGALDDRVRDCIIESSLRSDICHSSSNSLQTEGSKS-- 970
|
970
....*....|.
gi 2124423190 2402 TELATQEKVTL 2412
Cdd:pfam15921 971 SETCSREPVLL 981
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1667-1891 |
9.68e-05 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 47.99 E-value: 9.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1667 RQRELAEQELEKQRQLAEGTAQQRLAAEQEL---------IRLRAETEQGEqqRQLLEEELARLQHEAAAATQKRQELEA 1737
Cdd:pfam00038 47 RLYSLYEKEIEDLRRQLDTLTVERARLQLELdnlrlaaedFRQKYEDELNL--RTSAENDLVGLRKDLDEATLARVDLEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1738 elaKVRAEMEVLLASKARAEEESRSTSEKSKQR---LEAEASRFRELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEA 1813
Cdd:pfam00038 125 ---KIESLKEELAFLKKNHEEEVRELQAQVSDTqvnVEMDAARKLDLTSALAEIRAQYEEiAAKNREEAEEWYQSKLEEL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1814 ERVLAEKLAAIGEATRLKTEAEIALKEKEAENERL--------RRLAEDEAfqrrRLEEQAAQHKADIEERLAQLRKASE 1885
Cdd:pfam00038 202 QQAAARNGDALRSAKEEITELRRTIQSLEIELQSLkkqkasleRQLAETEE----RYELQLADYQELISELEAELQETRQ 277
|
....*.
gi 2124423190 1886 sELERQ 1891
Cdd:pfam00038 278 -EMARQ 282
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1183-1498 |
1.05e-04 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 48.78 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1183 ELEQLGR---QLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQL----RQEKALLEEIERHGEKV-------- 1247
Cdd:PLN03188 892 EITQLNRlvqQYKHERECNAIIGQTREDKIIRLESLMDGVLSKEDFLEEELaslmHEHKLLKEKYENHPEVLrtkielkr 971
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1248 --EECQRFAKQY--------INAIKDYELQLVTYkaqLEPVASPAKKpkvqsgSESVIQ-EYVDLRTRYSELTTLT---- 1312
Cdd:PLN03188 972 vqDELEHYRNFYdmgerevlLEEIQDLRSQLQYY---IDSSLPSARK------RNSLLKlTYSCEPSQAPPLNTIPestd 1042
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1313 -SQYIKFISETLRRMEEEER---LAEQQRAEererLAAVEAALEKQRQLAEAH---AQAKAQAEQEAQELQRRMQEEVAR 1385
Cdd:PLN03188 1043 eSPEKKLEQERLRWTEAESKwisLAEELRTE----LDASRALAEKQKHELDTEkrcAEELKEAMQMAMEGHARMLEQYAD 1118
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1386 REEAAVDAQQQKRSIQEELQHLRQsseAEIQAKARQVE-------AAERSRLRIEEEIRVVRLQLETTERQ---RGGAE- 1454
Cdd:PLN03188 1119 LEEKHIQLLARHRRIQEGIDDVKK---AAARAGVRGAEskfinalAAEISALKVEREKERRYLRDENKSLQaqlRDTAEa 1195
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1455 ----GELQALRARAEEA--EAQKR--QAQEEA-------ERLRRQVQDETQRKRQAEAE 1498
Cdd:PLN03188 1196 vqaaGELLVRLKEAEEAltVAQKRamDAEQEAaeaykqiDKLKRKHENEISTLNQLVAE 1254
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1663-1984 |
1.05e-04 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1742
Cdd:COG4372 48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1743 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1822
Cdd:COG4372 128 EQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEK 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1823 AIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQR 1902
Cdd:COG4372 208 LIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1903 RQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEA 1982
Cdd:COG4372 288 LEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGV 367
|
..
gi 2124423190 1983 AR 1984
Cdd:COG4372 368 AD 369
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1316-1556 |
1.10e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.90 E-value: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1316 IKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQ 1395
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1396 QKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALR-------AraeEAE 1468
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKaeleaakA---ELE 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1469 AQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVA 1548
Cdd:COG3883 175 AQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGA 254
|
....*...
gi 2124423190 1549 LETAQRSA 1556
Cdd:COG3883 255 AGAAAGSA 262
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1172-1431 |
1.14e-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: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1172 AVLAQTDLR---QRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVE 1248
Cdd:COG4942 14 AAAAQADAAaeaEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1249 ECQRFAKQYINAIKdyELQLVTYKAQLEPvaspakKPKVQSGSESVIQEYvdlrtRYSELTTLTSQYIKFISETLRRMEE 1328
Cdd:COG4942 94 ELRAELEAQKEELA--ELLRALYRLGRQP------PLALLLSPEDFLDAV-----RRLQYLKYLAPARREQAEELRADLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1329 EERLAEQQRAEERERLAAVEAALEKQRqlaeahaQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR 1408
Cdd:COG4942 161 ELAALRAELEAERAELEALLAELEEER-------AALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLE 233
|
250 260
....*....|....*....|...
gi 2124423190 1409 QSSEAEIQAKARQVEAAERSRLR 1431
Cdd:COG4942 234 AEAAAAAERTPAAGFAALKGKLP 256
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
21-134 |
1.15e-04 |
|
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: 45.43 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 21 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIAL 89
Cdd:cd21325 25 EKYAFVNWINKALENDPDC---RHVipmnpntDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLAL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2124423190 90 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 134
Cdd:cd21325 102 NSASAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1334-1435 |
1.19e-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: 47.57 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1334 EQQRAEERERLAAVEAALEKQRQLAEAHAQAkaqaeqEAQELQRRMQEEVARREEaaVDAQQQKRSIQEELQHLRQSSEA 1413
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKA------EAAEQERKLLEEQQRELE--QKLEDQERSYEEHLRQLKEKMEE 248
|
90 100
....*....|....*....|..
gi 2124423190 1414 EIQAKARQVEAAERSRLRIEEE 1435
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEA 270
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1663-1929 |
1.21e-04 |
|
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.
Pssm-ID: 437057 [Multi-domain] Cd Length: 401 Bit Score: 47.75 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLEEELARLQH-------EAAAATQKRQEL 1735
Cdd:pfam19220 128 AAETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLEQENRRLQAlseeqaaELAELTRRLAEL 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1736 EAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEASRFR-ELAEEAARLRALAEEAKRQRQLAEEDAARQRaeae 1814
Cdd:pfam19220 201 ETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMKLEALTARAAATEQLLAEARNQLR---- 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1815 rvlaEKLAAIGEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAAqhKADIEERLAQLRKA---SESELERQ 1891
Cdd:pfam19220 273 ----DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA--RAELEERAEMLTKAlaaKDAALERA 344
|
250 260 270
....*....|....*....|....*....|....*....
gi 2124423190 1892 KGLVEDTLRQRRQVEEEILALKVSFEKAAAG-KAELELE 1929
Cdd:pfam19220 345 EERIASLSDRIAELTKRFEVERAALEQANRRlKEELQRE 383
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1761-1909 |
1.25e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 48.24 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1761 RSTSEKSKQRLEAEASRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALK 1839
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 1840 EKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 1909
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1319-1524 |
1.32e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 46.36 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1319 ISETLRRMEEEERLAEQQRAEERERLAAVEAALekqrqlaeahAQAKAQAEQEAQELqRRMQEEVARREEAAVDAQQQKR 1398
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQAL----------AQVIANQKRLERQL-EELEAEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1399 siqeelQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1472
Cdd:COG1842 83 ------EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKvneals 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1473 -----QAQEEAERLRRQVqDETQRKRQAEAELAVR--VKAEAEAAREKQRALQALEEFR 1524
Cdd:COG1842 157 gidsdDATSALERMEEKI-EEMEARAEAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1068-1575 |
1.34e-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: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1068 EKLKTISLVIRSTHGAeevLKAHEEQLKEAQAvpatlpELEATKAALKKLRAQAEAQ-QPMFDALRDELRGAQEvgeRLQ 1146
Cdd:pfam12128 251 NTLESAELRLSHLHFG---YKSDETLIASRQE------ERQETSAELNQLLRTLDDQwKEKRDELNGELSAADA---AVA 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1147 QRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAV 1226
Cdd:pfam12128 319 KDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDK 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1227 REQLRQEKAL-LEEIERHGEKVEECQRFA-KQYINAIKDYELQLvtykaqlepvASPAKKPKVQSGSESVIQEyvdlrtr 1304
Cdd:pfam12128 399 LAKIREARDRqLAVAEDDLQALESELREQlEAGKLEFNEEEYRL----------KSRLGELKLRLNQATATPE------- 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1305 yseltTLTSQYIKfiSETLRRMEEEErlaeQQRAEERERLAAVEAALEKQRQLA-EAHAQAKAQAEQEAQELQRRMQEEV 1383
Cdd:pfam12128 462 -----LLLQLENF--DERIERAREEQ----EAANAEVERLQSELRQARKRRDQAsEALRQASRRLEERQSALDELELQLF 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1384 AR--------REEAAVDAQQQKRSIQEELQH-------------------------LRQ-------SSEAEIQAKARQVE 1423
Cdd:pfam12128 531 PQagtllhflRKEAPDWEQSIGKVISPELLHrtdldpevwdgsvggelnlygvkldLKRidvpewaASEEELRERLDKAE 610
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1424 AA---ERSRL-RIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRrqvqdeTQRKRQAEAEl 1499
Cdd:pfam12128 611 EAlqsAREKQaAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAL------AERKDSANER- 683
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1500 avRVKAEAEAAREKQRALQALEEFRLQAEEAerrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1575
Cdd:pfam12128 684 --LNSLEAQLKQLDKKHQAWLEEQKEQKREA----RTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALE 753
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2245-2545 |
1.35e-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: 47.61 E-value: 1.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2245 QRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2324
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2325 ARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAE-RLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTE 2403
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2404 LATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEReKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDT 2483
Cdd:pfam13868 194 EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEK-KARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAE 272
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 2484 LLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAE 2545
Cdd:pfam13868 273 DEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEE 334
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2252-2437 |
1.40e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 48.37 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2252 AEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELaqEQARRLQED 2331
Cdd:COG4913 609 RAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAEL--ERLDASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2332 KEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2411
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERE 766
|
170 180
....*....|....*....|....*.
gi 2124423190 2412 LVQTLEIQRQQSDHDAERLRQAIAEL 2437
Cdd:COG4913 767 LRENLEERIDALRARLNRAEEELERA 792
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3948-3982 |
1.43e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.43e-04
10 20 30
....*....|....*....|....*....|....*
gi 2124423190 3948 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 3982
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1509-1821 |
1.44e-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: 47.61 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1509 AAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEEHVAVAQL 1588
Cdd:pfam13868 29 AEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEERE-QKRQEEYEEKLQEREQMDEIV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1589 REEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQ 1668
Cdd:pfam13868 108 ERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1669 RELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAatQKRQELEAELAKVRAEMEV 1748
Cdd:pfam13868 188 RLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIE--LKERRLAEEAEREEEEFER 265
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1749 LLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKL 1821
Cdd:pfam13868 266 MLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1806-2037 |
1.46e-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: 47.45 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1806 AARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEErLAQLRKASE 1885
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1886 SELERQKGLVEDTLRQR-RQVEEEILALKVSFEKAAAGKAELEL--ELGRIRSNAEDTLRsKEQAELEAMRQRQLAAeee 1962
Cdd:COG4942 97 AELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELR-ADLAELAALRAELEAE--- 172
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1963 qrrreaeervQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHA 2037
Cdd:COG4942 173 ----------RAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAA 237
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1385-1516 |
1.51e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1385 RREEAAVD-AQQQKRSIQEELQHLRQSS--EAEIQAKARQVEAAERSRLRIEEEI-RVVRLQletteRQRGGAEGELQAL 1460
Cdd:COG1566 79 TDLQAALAqAEAQLAAAEAQLARLEAELgaEAEIAAAEAQLAAAQAQLDLAQRELeRYQALY-----KKGAVSQQELDEA 153
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1461 RARAEEAEAQKRQAQEEAERLRRQVQDETQrKRQAEAELavrvkAEAEAAREKQRA 1516
Cdd:COG1566 154 RAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQAEL 203
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2157-2414 |
1.58e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 48.37 E-value: 1.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2157 EQTLR---QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRS------QVEEELFSLRVQmeeLGKLKA 2227
Cdd:PRK11281 66 EQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETLstlslrQLESRLAQTLDQ---LQNAQN 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2228 RIEAENRALIlrdkdnTQRVLQEEAEkmkhvaeeaARLSVAAQEAARLRELAEEDLAQQRALAEKmLKEKMQAVQEATrl 2307
Cdd:PRK11281 143 DLAEYNSQLV------SLQTQPERAQ---------AALYANSQRLQQIRNLLKGGKVGGKALRPS-QRVLLQAEQALL-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2308 kaEAELLQQQKELA-----QE--QARRlqEDKEQMAQQLEQETQGFQrtlEAERQRQLEMSAEAerlklrVAEMSRAQAR 2380
Cdd:PRK11281 205 --NAQNDLQRKSLEgntqlQDllQKQR--DYLTARIQRLEHQLQLLQ---EAINSKRLTLSEKT------VQEAQSQDEA 271
|
250 260 270
....*....|....*....|....*....|....*
gi 2124423190 2381 AEEDAQRFRKQAEEIGEKLHRTEL-ATQEKVTLVQ 2414
Cdd:PRK11281 272 ARIQANPLVAQELEINLQLSQRLLkATEKLNTLTQ 306
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1354-1487 |
1.61e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1354 QRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKArQVEAAERSRLRI 1432
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQQ-ELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1433 EEEIRVVRLQLETTERQrggaegelQALRARAEEAEAQKRQAQEEAERLRRQVQD 1487
Cdd:COG1566 161 QAQLEAAQAQLAQAQAG--------LREEEELAAAQAQVAQAEAALAQAELNLAR 207
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1410-1623 |
1.64e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 47.52 E-value: 1.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1410 SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1487
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1488 -ETQRKRQAEAELAV------------RVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAErARQVQVALETAQR 1554
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKA 171
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1555 saevELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEA 1623
Cdd:COG3883 172 ----ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAA 236
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1826-2460 |
1.66e-04 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 48.28 E-value: 1.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1826 EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQV 1905
Cdd:NF041483 23 EMDRLKTEREKAVQHAEDLGYQVEVLRAKLHEARRSLASRPAYDGADIGYQAEQLLRNAQIQADQLRADAERELRDARAQ 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1906 EEEIlaLKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQ----------AELEAMRQRQLAAEEEQRRREAEERVQKS 1975
Cdd:NF041483 103 TQRI--LQEHAEHQARLQAELHTEAVQRRQQLDQELAERRQtveshvnenvAWAEQLRARTESQARRLLDESRAEAEQAL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1976 LAAEEEA------ARQRKAALEEVERLKAK--VEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQEL 2047
Cdd:NF041483 181 AAARAEAerlaeeARQRLGSEAESARAEAEaiLRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAESDQARRQAAELS 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2048 QQTLQQEQSMLERLR-----GEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRK 2122
Cdd:NF041483 261 RAAEQRMQEAEEALRearaeAEKVVAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGEATKEAEALKAEAEQALADAR 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2123 EAEQEAARRAQAEQAALRQKQAAdAEMEKHKKFAEQTLrQKAQVEQELTTlRLQLEETDHQKSILDEELQRLKAEVTEAA 2202
Cdd:NF041483 341 AEAEKLVAEAAEKARTVAAEDTA-AQLAKAARTAEEVL-TKASEDAKATT-RAAAEEAERIRREAEAEADRLRGEAADQA 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2203 RQ-RSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAAR-----LSVAAQEAARLR 2276
Cdd:NF041483 418 EQlKGAAKDDTKEYRAKTVELQEEARRLRGEAEQLRAEAVAEGERIRGEARREAVQQIEEAARtaeelLTKAKADADELR 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2277 ELAEEDLAQQRALA-EKMLKEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQ 2355
Cdd:NF041483 498 STATAESERVRTEAiERATTLRRQAEETLERTRAEAERLRAE---AEEQAEEVRAAAERAARELREETERAIAARQAEAA 574
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2356 RQLE-MSAEAERlKLRVAEMSRAQARAEedAQRFRKQAEEIGEKLhRTELAtqEKVTLVQtleiqrQQSDHDAERLR--- 2431
Cdd:NF041483 575 EELTrLHTEAEE-RLTAAEEALADARAE--AERIRREAAEETERL-RTEAA--ERIRTLQ------AQAEQEAERLRtea 642
|
650 660 670
....*....|....*....|....*....|....*.
gi 2124423190 2432 -----QAIAELEREKEKLKQEA--KLLQLKSEEMQT 2460
Cdd:NF041483 643 aadasAARAEGENVAVRLRSEAaaEAERLKSEAQES 678
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1333-1447 |
1.69e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1333 AEQQRAEERERLAAVEAALEKQRQLAEAHAQ---AKAQAEQEAQELQRRM---------QEEVARREEAAVDAQQQKRSI 1400
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlaaAQAQLDLAQRELERYQalykkgavsQQELDEARAALDAAQAQLEAA 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 2124423190 1401 QEELQHLRQSSEAEiqakaRQVEAAERSRLRIEEEIRVVRLQLETTE 1447
Cdd:COG1566 168 QAQLAQAQAGLREE-----EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1340-1561 |
1.71e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 47.06 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1340 ERERLAAVEAALEKQRQLAEAHAQAKAQAEQ---EAQELQRRMQEEVarreeaavdaqqqkRSIQEELQHLRQSSEAEIQ 1416
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQQlrtELQELEAQQQEEA--------------ESSREQLQELEEQLATERS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1417 AKarqvEAAERSRLRIEEEIRVVRLQLETTERQRggaegelqalraraeeaEAQKRQAQEEAERLRRQVQDETQRKRQaE 1496
Cdd:pfam09787 108 AR----REAEAELERLQEELRYLEEELRRSKATL-----------------QSRIKDREAEIEKLRNQLTSKSQSSSS-Q 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1497 AELAVRVKAEAEAAREKQRALQALEEFR----LQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQ 1561
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALSTEKnslvLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLR 234
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3742-3778 |
1.71e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.71e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2124423190 3742 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPAEEA 3778
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1665-2033 |
1.81e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 48.03 E-value: 1.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1665 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--HEAAAATQKRQELEA 1737
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1738 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAsRFRELAEEAARLRAlaEEAKRQRQLaeeDAARQRAEAERvl 1817
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKS--QLADYQQAL---DVQQTRAIQYQ-- 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1818 aEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKA--DIEERLAQLRKASESELERqkglv 1895
Cdd:PRK04863 418 -QAVQALERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAahSQFEQAYQLVRKIAGEVSR----- 491
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1896 EDTLRQRRQVEEEILALKVSFEKAAAGKAELElELGRirsnaedtlRSKEQAELEAMRQRqlaaeeeqrrreAEERVQKS 1975
Cdd:PRK04863 492 SEAWDVARELLRRLREQRHLAEQLQQLRMRLS-ELEQ---------RLRQQQRAERLLAE------------FCKRLGKN 549
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1976 LAAEEEAARQRKAALEEVERLKAKVEEArrlRERAEQESARQLQLAQDAAQKRLQAEE 2033
Cdd:PRK04863 550 LDDEDELEQLQEELEARLESLSESVSEA---RERRMALRQQLEQLQARIQRLAARAPA 604
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1923-2399 |
1.83e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 47.84 E-value: 1.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1923 KAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERvQKSLAAEEEAARQRKAALEEVERLKAKVEE 2002
Cdd:COG4717 55 ADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEE-LEELEAELEELREELEKLEKLLQLLPLYQE 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2003 ARRLRERAEQESARqlqlaqdaaQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERA 2082
Cdd:COG4717 134 LEALEAELAELPER---------LEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEEL 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2083 EREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKHKK-------- 2154
Cdd:COG4717 205 QQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAgvlflvlg 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2155 ----FAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAArqrsqveEELFSLRVQMEELGKLKARIE 2230
Cdd:COG4717 285 llalLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSP-------EELLELLDRIEELQELLREAE 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2231 -AENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLkekmqAVQEATRLKA 2309
Cdd:COG4717 358 eLEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELL-----EALDEEELEE 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2310 EAELLQQQKELAQEQARRLQEDKEQMAQQLEQ-ETQGFQRTLEAERQRQL----EMSAEAERLKLRVAEMSRAQARAEED 2384
Cdd:COG4717 433 ELEELEEELEELEEELEELREELAELEAELEQlEEDGELAELLQELEELKaelrELAEEWAALKLALELLEEAREEYREE 512
|
490
....*....|....*.
gi 2124423190 2385 AQ-RFRKQAEEIGEKL 2399
Cdd:COG4717 513 RLpPVLERASEYFSRL 528
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4257-4290 |
1.92e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.92e-04
10 20 30
....*....|....*....|....*....|....
gi 2124423190 4257 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4290
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
163-240 |
1.95e-04 |
|
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: 43.45 E-value: 1.95e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 163 DNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 240
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1363-1519 |
2.06e-04 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 47.03 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1363 QAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAER---------SRLRIE 1433
Cdd:pfam00529 53 PTDYQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAqlaqaqidlARRRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1434 EEIRVV-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ-VQDETQRKRQAEAELAvrvKAEAEAAR 1511
Cdd:pfam00529 133 APIGGIsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSeLSGAQLQIAEAEAELK---LAKLDLER 209
|
....*...
gi 2124423190 1512 EKQRALQA 1519
Cdd:pfam00529 210 TEIRAPVD 217
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1683-2179 |
2.18e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 47.93 E-value: 2.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1683 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV----------RAEMEVLLAS 1752
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1753 KARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKT 1832
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1833 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILAL 1912
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1913 KVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEE 1992
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1993 VERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAA 2072
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2073 EEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKH 2152
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 2124423190 2153 KKFAEQTLRQKAQVEQELTTLRLQLEE 2179
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3666-3702 |
2.18e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 2.18e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2124423190 3666 RYLYGTGCVAGVYVPGSRQTLTIYQALKKGLLSAEVA 3702
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1324-1494 |
2.22e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 47.59 E-value: 2.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1324 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQlAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1403
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARA-AAAAAAEAASAPEAAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1404 LQHLRQSSEAEIQAKARQVEAAERSRLRieeeiRVVRLQLETTERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRR 1483
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRR 230
|
170
....*....|.
gi 2124423190 1484 QVQDETQRKRQ 1494
Cdd:PRK12678 231 RRRDRRDARGD 241
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
16-129 |
2.32e-04 |
|
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: 43.82 E-value: 2.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 16 ERDRVQKKTFTKWVNKHLIKHWraeaqrhISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQ 86
Cdd:cd21329 2 EGESSEERTFRNWMNSLGVNPY-------VNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCN 72
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2124423190 87 IALDYLRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 129
Cdd:cd21329 73 YAVELGKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2166-2546 |
2.34e-04 |
|
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: 47.41 E-value: 2.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2166 VEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKL-KARIEAENRALILRDKDNT 2244
Cdd:pfam05483 361 LEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKEVELEELKKILAEDEKLlDEKKQFEKIAEELKGKEQE 440
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2245 QRVLQEEAEKMKHVAEEAARLSVAAQEAARLR------ELAEEDL--AQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2316
Cdd:pfam05483 441 LIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEvedlktELEKEKLknIELTAHCDKLLLENKELTQEASDMTLELKKHQE 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2317 -------QKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEaERQRQLEMSAE-AERLKLRVAEMSRAQARAEEDAQRF 2388
Cdd:pfam05483 521 diinckkQEERMLKQIENLEEKEMNLRDELESVREEFIQKGD-EVKCKLDKSEEnARSIEYEVLKKEKQMKILENKCNNL 599
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2389 RKQAEEIG---EKLHRTELATQEKVTL----VQTLEIQRQQSDHDAERLRQAIAEL------EREKEKLKQEAKLLQLKS 2455
Cdd:pfam05483 600 KKQIENKNkniEELHQENKALKKKGSAenkqLNAYEIKVNKLELELASAKQKFEEIidnyqkEIEDKKISEEKLLEEVEK 679
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2456 EEMQTVQQEQLLQETQALQQSFLSEKDTLL-----QRERFIEQEKAKL---EQLFQDEVAKAQKLREEQQRQQKQMEEEK 2527
Cdd:pfam05483 680 AKAIADEAVKLQKEIDKRCQHKIAEMVALMekhkhQYDKIIEERDSELglyKNKEQEQSSAKAALEIELSNIKAELLSLK 759
|
410
....*....|....*....
gi 2124423190 2528 QQLVASMEEARQRQREAEE 2546
Cdd:pfam05483 760 KQLEIEKEEKEKLKMEAKE 778
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2183-2601 |
2.35e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.64 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2183 QKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALilrdKDNTQRVLQEEA--EKMKHVAE 2260
Cdd:PRK04863 280 ERRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAA----SDHLNLVQTALRqqEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2261 EAARLSVAAQEAARLRELAEEDLAQQRALAEkmlkekmQAVQEATRLKA------EAELLQQQKELAQEQARRLQEDKEQ 2334
Cdd:PRK04863 356 DLEELEERLEEQNEVVEEADEQQEENEARAE-------AAEEEVDELKSqladyqQALDVQQTRAIQYQQAVQALERAKQ 428
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2335 MAQ--QLEQET-QGFQRTLEAERQRQLEMSAEAERlKLRVAEMSRAQAraEEDAQRFRKQAEEIGEklhrtELATQEKVT 2411
Cdd:PRK04863 429 LCGlpDLTADNaEDWLEEFQAKEQEATEELLSLEQ-KLSVAQAAHSQF--EQAYQLVRKIAGEVSR-----SEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2412 LVQTLEIQRQQSDHdAERLRQAIAELEREkekLKQEAKLLQLKSEEMQtvqqeqllqetqALQQSFLSEKDTllqrERFI 2491
Cdd:PRK04863 501 LLRRLREQRHLAEQ-LQQLRMRLSELEQR---LRQQQRAERLLAEFCK------------RLGKNLDDEDEL----EQLQ 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2492 EQEKAKLEQLfQDEVAKAQKLREEQQRQQKQMeeekQQLVASMEEARQRQREAEEGVRRKQEELQLLEqqrqqqekllaE 2571
Cdd:PRK04863 561 EELEARLESL-SESVSEARERRMALRQQLEQL----QARIQRLAARAPAWLAAQDALARLREQSGEEF-----------E 624
|
410 420 430
....*....|....*....|....*....|
gi 2124423190 2572 ENQRLRERLQRLEEEHRAALAHSEEIAASQ 2601
Cdd:PRK04863 625 DSQDVTEYMQQLLERERELTVERDELAARK 654
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1321-1510 |
2.35e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 47.25 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLRRMEEEERLAEQQRAEERERLAAVEAALekqrqlaeAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSI 1400
Cdd:PRK05035 524 EARKAQARARQAEKQAAAAADPKKAAVAAAI--------ARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1401 QEELQHLRQSSEAEIQAKARQVEAA-ERSRLRIEEEIRVVRLQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAE 1479
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE 670
|
170 180 190
....*....|....*....|....*....|.
gi 2124423190 1480 rlrrqvQDETQRKRQAEAELAvRVKAEAEAA 1510
Cdd:PRK05035 671 ------EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1467-1587 |
2.54e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 2.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1467 AEAQKRQAQEEAERLRRQVQDETQRKRQAEaELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQ 1546
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423190 1547 VALETAQRSAEVElqSKRASFAEKTAQLERTLQEEHVAVAQ 1587
Cdd:PRK09510 140 KAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKK 178
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2142-2357 |
2.70e-04 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 47.52 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2142 KQAADAEMEKH----KKFAE---QTLRQ-KAQVEQELTTLRLQLEETDH---------QKSILDEELQRLKAEVTEAARQ 2204
Cdd:NF012221 1549 KHAKQDDAAQNaladKERAEadrQRLEQeKQQQLAAISGSQSQLESTDQnaletngqaQRDAILEESRAVTKELTTLAQG 1628
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2205 RSQVEEElfslRVQMEELGKlKARIEAENRAL--ILRDKDNTQRVLQE--EAEKMKHVAEEA-ARLSVAAQEAA-----R 2274
Cdd:NF012221 1629 LDALDSQ----ATYAGESGD-QWRNPFAGGLLdrVQEQLDDAKKISGKqlADAKQRHVDNQQkVKDAVAKSEAGvaqgeQ 1703
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2275 LRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKeqmAQQLEQETQGFQRTLEAER 2354
Cdd:NF012221 1704 NQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENK---ANQAQADAKGAKQDESDKP 1780
|
...
gi 2124423190 2355 QRQ 2357
Cdd:NF012221 1781 NRQ 1783
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2145-2386 |
2.80e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 46.75 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2145 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfslRVQMEELGK 2224
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2225 LkARIEAENRALIlrdkDNTQRVLQEEaekmkHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMlkekmqavQEA 2304
Cdd:COG3883 91 R-ARALYRSGGSV----SYLDVLLGSE-----SFSDFLDRLSALSKIADADADLLEELKADKAELEAKK--------AEL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2305 TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQEtqgfQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEED 2384
Cdd:COG3883 153 EAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE----EAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAA 228
|
..
gi 2124423190 2385 AQ 2386
Cdd:COG3883 229 AA 230
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1981-2593 |
2.90e-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: 2.90e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1981 EAARQRKAALEEV----ERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEqs 2056
Cdd:COG4913 245 EDAREQIELLEPIrelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR-- 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2057 mlERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVE-EAERLKQSAEEQAQAQAQAQAAAEKLRKEAEqeaarraqae 2135
Cdd:COG4913 323 --EELDELEAQIRGNGGDRLEQLEREIERLERELEERErRRARLEALLAALGLPLPASAEEFAALRAEAA---------- 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2136 qaalRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRsqvEEEL--- 2212
Cdd:COG4913 391 ----ALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD---EAELpfv 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2213 -------------------------FSLRVQMEELGKLKARIEAENRALILRdkdnTQRVLQEEAEKMKHVAEE---AAR 2264
Cdd:COG4913 464 gelievrpeeerwrgaiervlggfaLTLLVPPEHYAAALRWVNRLHLRGRLV----YERVRTGLPDPERPRLDPdslAGK 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2265 LSVAAQEAarlRELAEEDLAQQRALA----EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE 2340
Cdd:COG4913 540 LDFKPHPF---RAWLEAELGRRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLAALE 616
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2341 QETQGFQRTLEAERQRQLEMSAEAERL--KLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtlVQTLEI 2418
Cdd:COG4913 617 AELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD----LAALEE 692
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2419 QRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFlsekDTLLQRERFIEQEKAKL 2498
Cdd:COG4913 693 QLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVERELR 768
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2499 EQLfQDEVAKAQKLREEQQrqqkqmeeekQQLVASMEEARQRQREAEEGVRRKQEELQLLEQQRQQQEKLLAEEN-QRLR 2577
Cdd:COG4913 769 ENL-EERIDALRARLNRAE----------EELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDGLPEYeERFK 837
|
650
....*....|....*.
gi 2124423190 2578 ERLQRLEEEHRAALAH 2593
Cdd:COG4913 838 ELLNENSIEFVADLLS 853
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1660-1819 |
2.94e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 45.59 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQHEAAAATQKRQELEA 1737
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1738 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1813
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....*.
gi 2124423190 1814 ERVLAE 1819
Cdd:COG1842 207 EDELAA 212
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1696-2009 |
2.99e-04 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 47.04 E-value: 2.99e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1696 ELIRLRAETEQGEQQ--RQLLEEELARLQHEAAAATQKRQeLEAELAKVRA---EMEVLLASKARAEEESRSTSEKSKQR 1770
Cdd:pfam05557 3 ELIESKARLSQLQNEkkQMELEHKRARIELEKKASALKRQ-LDRESDRNQElqkRIRLLEKREAEAEEALREQAELNRLK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1771 LEAEASRFRELAEEAARLRALAE----------EAKRQRQLAEEDAARQRAEAERV---LAEKLAAIGEATRLKTEAEIA 1837
Cdd:pfam05557 82 KKYLEALNKKLNEKESQLADAREvisclknelsELRRQIQRAELELQSTNSELEELqerLDLLKAKASEAEQLRQNLEKQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1838 LKEKEAENERLRRLAedeafQRRRLEEQAAQHKADIEERLAQLRKAsESELERQKGLVE---DTLRQRRQVEEEILALKV 1914
Cdd:pfam05557 162 QSSLAEAEQRIKELE-----FEIQSQEQDSEIVKNSKSELARIPEL-EKELERLREHNKhlnENIENKLLLKEEVEDLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1915 S---FEKAAAGKAELELELGRIRS----------NAEDTLRSKE--QAELEAMRQRQLAAEEE----QRRREAEERVQKS 1975
Cdd:pfam05557 236 KlerEEKYREEAATLELEKEKLEQelqswvklaqDTGLNLRSPEdlSRRIEQLQQREIVLKEEnsslTSSARQLEKARRE 315
|
330 340 350
....*....|....*....|....*....|....
gi 2124423190 1976 LaaEEEAARQRKAALEEVERLKAKVEEARRLRER 2009
Cdd:pfam05557 316 L--EQELAQYLKKIEDLNKKLKRHKALVRRLQRR 347
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2154-2608 |
3.09e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.82 E-value: 3.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2154 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAEN 2233
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2234 RALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2313
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2314 LQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAE 2393
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2394 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQAL 2473
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2474 QQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEEGVRRKQE 2553
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 2554 ELQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVKAL 2608
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALASAEL 530
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3370-3403 |
3.30e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.93 E-value: 3.30e-04
10 20 30
....*....|....*....|....*....|....
gi 2124423190 3370 LLEAQAATGFLVDPVRNQRLYVHEAVKAGIVGPE 3403
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1659-1806 |
3.53e-04 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 46.77 E-value: 3.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1659 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQHEAAAATQKRQELEA 1737
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1738 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEASRF-RELAEEAARLRALAEEAKRQRQLAEEDA 1806
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLEH 506
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1980-2513 |
3.61e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.83 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1980 EEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHA--FAVQQKEQELQQTLQQEQSM 2057
Cdd:COG4913 224 FEAADALVEHFDDLERAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALrlWFAQRRLELLEAELEELRAE 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2058 LERLRGEAEAARRAAEEAEEARERAEREAAQS-RRQVEEAER----LKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRA 2132
Cdd:COG4913 304 LARLEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEReierLERELEERERRRARLEALLAALGLPLPASAEEFA 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2133 QAEQAALRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRsqvEEEL 2212
Cdd:COG4913 384 ALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAEALGLD---EAEL 460
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2213 ----------------------------FSLRVQMEELGKLKARIEAENRALILRdkdnTQRVLQEEAEKMKHVAEE--- 2261
Cdd:COG4913 461 pfvgelievrpeeerwrgaiervlggfaLTLLVPPEHYAAALRWVNRLHLRGRLV----YERVRTGLPDPERPRLDPdsl 536
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2262 AARLSVAAQEAarlRELAEEDLAQQRALA----EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2337
Cdd:COG4913 537 AGKLDFKPHPF---RAWLEAELGRRFDYVcvdsPEELRRHPRAITRAGQVKGNGTRHEKDDRRRIRSRYVLGFDNRAKLA 613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2338 QLEQETQGFQRTLEAERQRQLEMSAEAERL--KLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtlVQT 2415
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALqeRREALQRLAEYSWDEIDVASAEREIAELEAELERLDASSDD----LAA 689
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2416 LEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQLLQETQALQQSFlsekDTLLQRERFIEQEK 2495
Cdd:COG4913 690 LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALL----EERFAAALGDAVER 765
|
570
....*....|....*...
gi 2124423190 2496 AKLEQLfQDEVAKAQKLR 2513
Cdd:COG4913 766 ELRENL-EERIDALRARL 782
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1394-1545 |
3.79e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 45.30 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1394 QQQKRSIQEELQHLRQ---SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEG--ELQALRARAEEAE 1468
Cdd:COG1579 23 EHRLKELPAELAELEDelaALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNnkEYEALQKEIESLK 102
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1469 AQKRQAQEEAERLRRQVQdetqrkrQAEAELAvrvKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQV 1545
Cdd:COG1579 103 RRISDLEDEILELMERIE-------ELEEELA---ELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELA 169
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2178-2460 |
3.98e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.98 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2178 EETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDntqrvLQEEAEKMKH 2257
Cdd:PRK03918 189 ENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGS-----KRKLEEKIRE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2258 VAEeaarlsvaaqeaaRLRELAEEdlaqqralaEKMLKEKmqaVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQ 2337
Cdd:PRK03918 264 LEE-------------RIEELKKE---------IEELEEK---VKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2338 qLEQETQGFQRTL-EAErqrqlEMSAEAERLKLRVAEMSRAQARAEEDAQRFrkqaEEIGEKLHRTElatqekvtlvqtl 2416
Cdd:PRK03918 319 -LEEEINGIEERIkELE-----EKEERLEELKKKLKELEKRLEELEERHELY----EEAKAKKEELE------------- 375
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 2124423190 2417 EIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEEMQT 2460
Cdd:PRK03918 376 RLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKK 419
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3076-3112 |
4.01e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.54 E-value: 4.01e-04
10 20 30
....*....|....*....|....*....|....*..
gi 2124423190 3076 KLLSAEKAVTGYKDPYSGKSVSLFQALKKGLIPKEQG 3112
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1347-1546 |
4.84e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 4.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1347 VEAALEKQRQL----AEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQV 1422
Cdd:PRK12678 52 IAAIKEARGGGaaaaAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1423 EAAERSRLRieeeirvvrlqleTTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAElavr 1502
Cdd:PRK12678 132 ERGEAARRG-------------AARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRRE---- 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423190 1503 vkaeaEAAREKQRALQaleefRLQAEEAERRLRQAEAERARQVQ 1546
Cdd:PRK12678 195 -----ERGRDGDDRDR-----RDRREQGDRREERGRRDGGDRRG 228
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2160-2500 |
4.88e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 4.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2160 LRQKAQVEQ---ELTTLRLQLEEtdhQKSILDEelqrLKAEVTEAARQRSQVEEELFSLRVQMEELgkLKARIEAENRAL 2236
Cdd:PRK04863 344 LRQQEKIERyqaDLEELEERLEE---QNEVVEE----ADEQQEENEARAEAAEEEVDELKSQLADY--QQALDVQQTRAI 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2237 ILRdkdNTQRVLqEEAEKMKHVAEEAARLSVAAQEAARlrelAEEDLAQQRALaekMLKEKMQAVQEATRLKAEA-ELLQ 2315
Cdd:PRK04863 415 QYQ---QAVQAL-ERAKQLCGLPDLTADNAEDWLEEFQ----AKEQEATEELL---SLEQKLSVAQAAHSQFEQAyQLVR 483
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2316 Q-----QKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEmsAEAERLKLRVAEMSRAQARAEEDAQRFRK 2390
Cdd:PRK04863 484 KiagevSRSEAWDVARELLRRLREQRHLAEQLQQLRMRLSELEQRLRQQ--QRAERLLAEFCKRLGKNLDDEDELEQLQE 561
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2391 QAEEigeklhRTELATQEKVTLVQTLEIQRQQsdhdAERLRQAIAELE-REKEKLKQEAKLLQLKSEEMQTVQQEQLLQE 2469
Cdd:PRK04863 562 ELEA------RLESLSESVSEARERRMALRQQ----LEQLQARIQRLAaRAPAWLAAQDALARLREQSGEEFEDSQDVTE 631
|
330 340 350
....*....|....*....|....*....|....*
gi 2124423190 2470 TQALQQ----SFLSEKDTLLQRERFIEQEKAKLEQ 2500
Cdd:PRK04863 632 YMQQLLererELTVERDELAARKQALDEEIERLSQ 666
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2277-2401 |
5.04e-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: 45.26 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2277 ELAEEDLAQQRALAEKML---KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAE 2353
Cdd:cd16269 170 EVLQEFLQSKEAEAEAILqadQALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQERSYEEHLRQLKEKMEEE 249
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 2124423190 2354 RQRQLEmsaEAERLklrVAEMSRAQARAEEdaQRFRKQAEEIGEKLHR 2401
Cdd:cd16269 250 RENLLK---EQERA---LESKLKEQEALLE--EGFKEQAELLQEEIRS 289
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1345-1542 |
5.07e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 45.80 E-value: 5.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1345 AAVEAALEKQRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVAR--REEAAVD-AQQQKRSIQEELQHLRQSSEAEIQAKAR 1420
Cdd:COG1538 4 ELIERALANNPDLRAARARvEAARAQLRQARAGLLPSQELDLggKRRARIEaAKAQAEAAEADLRAARLDLAAEVAQAYF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1421 QVEAAERSRLRIEEEIRVVRLQLETTERQR---GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEA 1497
Cdd:COG1538 84 DLLAAQEQLALAEENLALAEELLELARARYeagLASRLDVLQAEAQLAQARAQLAQAEAQLAQARNALALLLGLPPPAPL 163
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2124423190 1498 ELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERA 1542
Cdd:COG1538 164 DLPDPLPPLPPLPPSLPGLPSEALERRPDLRAAEAQLEAAEAEIG 208
|
|
| TolC |
COG1538 |
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis]; |
1322-1561 |
5.11e-04 |
|
Outer membrane protein TolC [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 441147 [Multi-domain] Cd Length: 367 Bit Score: 45.80 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1322 TLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQ-EAQELQRRMQEEVARRE------EAAVDAQ 1394
Cdd:COG1538 84 DLLAAQEQLALAEENLALAEELLELARARYEAGLASRLDVLQAEAQLAQaRAQLAQAEAQLAQARNAlalllgLPPPAPL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1395 QQKRSIQEELQHLRQSSEAEIQAKAR--QVEAAERSRLRIEEEIRVVRLQL----------ETTERQRGGAEGELQ---- 1458
Cdd:COG1538 164 DLPDPLPPLPPLPPSLPGLPSEALERrpDLRAAEAQLEAAEAEIGVARAAFlpslslsasyGYSSSDDLFSGGSDTwsvg 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1459 -----------ALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQ-ALEEFR-- 1524
Cdd:COG1538 244 lslslplfdggRNRARVRAAKAQLEQAEAQYEQTVLQALQEVEDALAALRAAREQLEALEEALEAAEEALElARARYRag 323
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2124423190 1525 ----LQAEEAERRLRQAEAERarqvqVALETAQRSAEVELQ 1561
Cdd:COG1538 324 laslLDVLDAQRELLQAQLNL-----IQARYDYLLALVQLY 359
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2673-2711 |
5.14e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.39 E-value: 5.14e-04
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 2673 YLQGRSSIAGLLLKPANEKLSIYTALRRQLLSPGTALIL 2711
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2999-3036 |
5.44e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.44e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2124423190 2999 RQALRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVA 3036
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1375-2008 |
5.45e-04 |
|
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: 46.25 E-value: 5.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1375 LQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAE 1454
Cdd:pfam05483 79 LYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1455 gELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELavRVKAEaeaarekqralQALEEFRLQAEEAERRL 1534
Cdd:pfam05483 159 -LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEEL--RVQAE-----------NARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1535 RQAEAERARQV-----QVALETAQrSAEVELQSKRASFaektaqlerTLQEEHVAVAQLREEAERRAQQQAEAERAREEA 1609
Cdd:pfam05483 225 QHLEEEYKKEIndkekQVSLLLIQ-ITEKENKMKDLTF---------LLEESRDKANQLEEKTKLQDENLKELIEKKDHL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1610 ERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegTAQQ 1689
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR----TEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1690 RLaaeqelirlraetEQGEQQRQLLEEELARLQHEAAAATQ----KRQELEaELAKVRAEMEVLLASKARAEEESRSTSE 1765
Cdd:pfam05483 371 RL-------------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1766 KSKQRLEAEASRFRELAEEAARLRALaeEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLkteaeialkekeaEN 1845
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL-------------EN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1846 ERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEILALKVS 1915
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1916 FEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKsLAAEEEAARQR--------- 1986
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNK-LELELASAKQKfeeiidnyq 660
|
650 660 670
....*....|....*....|....*....|..
gi 2124423190 1987 ----------KAALEEVERLKAKVEEARRLRE 2008
Cdd:pfam05483 661 keiedkkiseEKLLEEVEKAKAIADEAVKLQK 692
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1650-1813 |
5.64e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 46.02 E-value: 5.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1650 EAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQElirlrAETEQGEQQRQL-LEEELARLQHEAAAA 1728
Cdd:COG2268 229 EQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA-----YEIAEANAEREVqRQLEIAEREREIELQ 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1729 TQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEedAA 1807
Cdd:COG2268 296 EKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPE--IA 370
|
....*.
gi 2124423190 1808 RQRAEA 1813
Cdd:COG2268 371 EAAAKP 376
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2139-2500 |
5.76e-04 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 46.37 E-value: 5.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTT---LRLQLEET--DHQKSILDEELQRLKAEVTEAARQRSQVEEELF 2213
Cdd:pfam12128 451 LRLNQATATPELLLQLENFDERIERAREEQEAANaevERLQSELRqaRKRRDQASEALRQASRRLEERQSALDELELQLF 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2214 S--------LRVQM----EELGKLKARieaenrALILRDKDNTQRVLQEEAEKMK------HVAEEAARLSVAAQEAARL 2275
Cdd:pfam12128 531 PqagtllhfLRKEApdweQSIGKVISP------ELLHRTDLDPEVWDGSVGGELNlygvklDLKRIDVPEWAASEEELRE 604
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2276 R-ELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEaER 2354
Cdd:pfam12128 605 RlDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSAN-ER 683
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2355 QRQLEmsAEAERLKLRVAEMSRAQAR--AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQ 2432
Cdd:pfam12128 684 LNSLE--AQLKQLDKKHQAWLEEQKEqkREARTEKQAYWQVVEGALDAQLALLKAAIAARRSGAKAELKALETWYKRDLA 761
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 2433 AIAELEREKEKLKQEAKLLQLKSEEMQtVQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQ 2500
Cdd:pfam12128 762 SLGVDPDVIAKLKREIRTLERKIERIA-VRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQ 828
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1323-1512 |
5.80e-04 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 45.76 E-value: 5.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1323 LRRMEEEERLAEQQRAEERERLAAVEAA-LEKQRQLAEAHAqakaqaEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQ 1401
Cdd:pfam05262 203 LKERESQEDAKRAQQLKEELDKKQIDADkAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVA 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1402 EELQHLRQSSEAEIQAKARQVEAAERsrlrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRqaQEEAERL 1481
Cdd:pfam05262 277 ENQKREIEKAQIEIKKNDEEALKAKD-------------------------HKAFDLKQESKASEKEAEDK--ELEAQKK 329
|
170 180 190
....*....|....*....|....*....|..
gi 2124423190 1482 RRQVQDETQR-KRQAEAElavrVKAEAEAARE 1512
Cdd:pfam05262 330 REPVAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1348-1848 |
5.98e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 46.20 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1348 EAALEKQRQLAEAhAQAKAQAEQeAQELQRRMQEeVARREEAAVDAQQQKRSIQE---ELQHLRQSSEAEiqakarqvea 1424
Cdd:PRK10929 25 EKQITQELEQAKA-AKTPAQAEI-VEALQSALNW-LEERKGSLERAKQYQQVIDNfpkLSAELRQQLNNE---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1425 aersrlriEEEIRVVRLQLETterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRrQVQDETQRKRQAEAElAVRVK 1504
Cdd:PRK10929 92 --------RDEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAR-EISDSLSQLPQQQTE-ARRQL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1505 AEAEaarekqRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSA--EVELQSKRASFAEK-TAQLERTLQee 1581
Cdd:PRK10929 154 NEIE------RRLQTLGTPNTPLAQAQLTALQAESAALKALVDELELAQLSAnnRQELARLRSELAKKrSQQLDAYLQ-- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1582 hvavaqlreeaerraqqqaeaerareeaerelerwqlkaneALRLRLQAEevaqqkslaqaeaekqkeeaerearrrgka 1661
Cdd:PRK10929 226 -----------------------------------------ALRNQLNSQ------------------------------ 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1662 eeqavRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQHEAAAATQK-RQELEA--- 1737
Cdd:PRK10929 235 -----RQRE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlre 307
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1738 ---ELAKVRAEMEVLLASKARAEEESRStsekskQRLEAEASRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRAE 1812
Cdd:PRK10929 308 qsqWLGVSNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTAE 376
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1813 AERVLAEKLAA---------------IGEATRLK---TEAEIALKE-KEAENERL 1848
Cdd:PRK10929 377 QNRILDAQLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1769-1883 |
6.27e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.10 E-value: 6.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1769 QRLEAEASRFRELAEEAARLRALAEEAKRQRQlaeedaarqraeAERVLAEKLAAIGEATRLKTEAEIA-LKEKEAENER 1847
Cdd:PRK11448 145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQ------------QELVALEGLAAELEEKQQELEAQLEqLQEKAAETSQ 212
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2124423190 1848 LRRLaedeafQRRRLEEQAAQhKADIEERL------AQLRKA 1883
Cdd:PRK11448 213 ERKQ------KRKEITDQAAK-RLELSEEEtrilidQQLRKA 247
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2219-2386 |
6.29e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.61 E-value: 6.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2219 MEELGKLKARIEAENRALILRDKdntqRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKM 2298
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQK----KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2299 QAVQEATR-LKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRvAEMSRA 2377
Cdd:TIGR02794 125 KAKQAAEAkAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAK-AEAAKA 203
|
....*....
gi 2124423190 2378 QARAEEDAQ 2386
Cdd:TIGR02794 204 KAAAEAAAK 212
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
21-133 |
6.40e-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: 43.07 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 21 QKKTFTKWVNKHLIKHWRAeaqRHI-------SDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIAL 89
Cdd:cd21324 25 EKYAFVNWINKALENDPDC---KHVipmnpntDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLAL 101
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 2124423190 90 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 133
Cdd:cd21324 102 NSASAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1660-1853 |
6.63e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 45.29 E-value: 6.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAEL 1739
Cdd:pfam13868 149 EEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAE 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1740 AKVRAEMEVLLASKARAEEESRsTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1819
Cdd:pfam13868 229 KKARQRQELQQAREEQIELKER-RLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRA 307
|
170 180 190
....*....|....*....|....*....|....
gi 2124423190 1820 KLAAIGEATRLKTEAEIALKEKEAENERLRRLAE 1853
Cdd:pfam13868 308 AEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1394-1563 |
6.83e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.16 E-value: 6.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1394 QQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRL-------RIE-EEIRVVRLQLETTerqrgGAEGELQAlRARAE 1465
Cdd:PTZ00491 647 DSLQKSVQLAIEITTKSQEAAARHQAELLEQEARGRLerqkmhdKAKaEEQRTKLLELQAE-----SAAVESSG-QSRAE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1466 -EAEAQKRQAQEEAErlrrqVQdetQRKRQAEAElavRVKAEAEAAREKQRALQALEEFRLQAE---EAERRLRQAEAER 1541
Cdd:PTZ00491 721 aLAEAEARLIEAEAE-----VE---QAELRAKAL---RIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATK 789
|
170 180
....*....|....*....|....*.
gi 2124423190 1542 ARQVQVAL--ET--AQRSAEVELQSK 1563
Cdd:PTZ00491 790 FERIVEALgrETliAIARAGPELQAK 815
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4367-4404 |
6.89e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.77 E-value: 6.89e-04
10 20 30
....*....|....*....|....*....|....*...
gi 2124423190 4367 QRFLEVQYLTGGLIEPDVPGRVPLDEALQRGTVDARTA 4404
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
1345-1552 |
6.95e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 46.08 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1345 AAVEAALEKQRQLAEAHAQAKAQAEQEAQELQ--RRMQEEVARREEAAVDAQQQKRSIQE-----------ELQHLRQSS 1411
Cdd:PHA03247 1150 STVDAAVRAHGVLADAVAALSPAVRDPACPLAflVALADSAAGYVKATRLALDARRAIARlgalgaaaadlAVAVRRENP 1229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1412 EAE------IQAKARQVEAAERSRLRIEEEIRVVrLQLETTERQRGGAEGELQAL-------RARAEEAEAQkrqAQEEA 1478
Cdd:PHA03247 1230 QAEgdraalLEAAARAVTAAREGLAACEGEFGGL-LHAEGSAGDPSPSGRALQELgkvvgatRRRADELEAA---AADLA 1305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1479 ERLRRQVQDETQRKRQAEAELAV-RVKAEAEAAREKQRALQAL--------EEFRLQAEeaerrlrQAEAERARQVQVAL 1549
Cdd:PHA03247 1306 EKMAARRARASRERWAADVEAALdRVENRAEFDAVELRRLQALaathgynpRDFRKRAE-------QALAANAKTATLAL 1378
|
...
gi 2124423190 1550 ETA 1552
Cdd:PHA03247 1379 EAA 1381
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1465-1544 |
7.06e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 46.10 E-value: 7.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1465 EEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAEL------AVRVKAEAEAAREKQRALQA-LEEFRLQAEEAERRLRQA 1537
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAeaqqqeLVALEGLAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 2124423190 1538 EAERARQ 1544
Cdd:PRK11448 218 RKEITDQ 224
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1687-2033 |
7.30e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 45.80 E-value: 7.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1687 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAA----TQKRQELEAELAKVRAEME----VLLASKARAEE 1758
Cdd:COG3064 1 AQEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEErlaeLEAKRQAEEEAREAKAEAEqraaELAAEAAKKLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1759 ESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQR----QLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEA 1834
Cdd:COG3064 81 EAEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKaeeaKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1835 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKV 1914
Cdd:COG3064 161 AAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEAT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1915 SFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVE 1994
Cdd:COG3064 241 EEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAA 320
|
330 340 350
....*....|....*....|....*....|....*....
gi 2124423190 1995 RLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEE 2033
Cdd:COG3064 321 AAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALA 359
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1048-1264 |
7.57e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.06 E-value: 7.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1048 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAALkklraqaEAQQPM 1127
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1128 FDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLlerwqavlaqtdlrQRELEQLGRQLRYYRESADPLGAWLQD 1207
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1208 AKRRQEQIQAMVladsRAVREQLRQE-KALLEEIERHGEKVEEC-QRFAKQYINAIKDY 1264
Cdd:COG4913 753 ERFAAALGDAVE----RELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1700-1954 |
7.65e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 45.45 E-value: 7.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1700 LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAemevlLASKARAEEEsrstsekskqrLEAEasrfR 1779
Cdd:COG0497 156 LLEEYREAYRAWRALKKELEELRADEAERARELDLLRFQLEELEA-----AALQPGEEEE-----------LEEE----R 215
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1780 ELAEEAARLRALAEEAkrQRQLAEED--AARQRAEAERVLaEKLAAIGE-----ATRLkTEAEIALKEKEAEnerLRRLA 1852
Cdd:COG0497 216 RRLSNAEKLREALQEA--LEALSGGEggALDLLGQALRAL-ERLAEYDPslaelAERL-ESALIELEEAASE---LRRYL 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1853 EDEAFQRRRLEEqaaqhkadIEERLAQLRKaseselerqkglvedtLRQRRQVE-EEILALkvsfekaaagKAELELELG 1931
Cdd:COG0497 289 DSLEFDPERLEE--------VEERLALLRR----------------LARKYGVTvEELLAY----------AEELRAELA 334
|
250 260
....*....|....*....|...
gi 2124423190 1932 RIrSNAEDTLRSKEQAELEAMRQ 1954
Cdd:COG0497 335 EL-ENSDERLEELEAELAEAEAE 356
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1357-1536 |
8.30e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 45.23 E-value: 8.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1357 LAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKarqveaaersrlrieeei 1436
Cdd:COG3524 160 LAESEELVNQLSERAREDAVRFAEEEVERAEERLRDAREALLAFRNRNGILDPEATAEALLQ------------------ 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1437 rvvrlQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQR-----KRQAEAELAV---RVKAEAE 1508
Cdd:COG3524 222 -----LIATLEGQLAELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARltgasGGDSLASLLAeyeRLELERE 296
|
170 180
....*....|....*....|....*....
gi 2124423190 1509 -AAREKQRALQALEEFRLqaeEAERRLRQ 1536
Cdd:COG3524 297 fAEKAYTSALAALEQARI---EAARQQRY 322
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
2143-2362 |
9.18e-04 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 44.75 E-value: 9.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2143 QAADAEMEKHKKFAEQTLRQKAQVEQEL------------TTLRLQLEETDHQKSILDEELQRLKAEV----TEAARQRS 2206
Cdd:pfam09787 3 ESAKQELADYKQKAARILQSKEKLIASLkegsgvegldssTALTLELEELRQERDLLREEIQKLRGQIqqlrTELQELEA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2207 QVEEELFSLRvqmEELGKLKARIEAENRAliLRDKDNTQRVLQEEaekMKHVAEEAARLSVAAQEAARLRELAEEDLAQQ 2286
Cdd:pfam09787 83 QQQEEAESSR---EQLQELEEQLATERSA--RREAEAELERLQEE---LRYLEEELRRSKATLQSRIKDREAEIEKLRNQ 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 2287 raLAEKMLKEKMQAVQEAtRLKAEAELLQQQkelaQEQARRLQEDKEQMAQQLEQ-ETQGFQRTLEAERQRQLEMSA 2362
Cdd:pfam09787 155 --LTSKSQSSSSQSELEN-RLHQLTETLIQK----QTMLEALSTEKNSLVLQLERmEQQIKELQGEGSNGTSINMEG 224
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1352-1483 |
9.24e-04 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 42.72 E-value: 9.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1352 EKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL--RQSSEAEIQAKARQVEAAERSR 1429
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 1430 LRIEEEIRVVRLQLETTERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1483
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| FPP |
pfam05911 |
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ... |
1660-1895 |
9.96e-04 |
|
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: 45.44 E-value: 9.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQ-RQLLEEELARLqHEAAAATQKRQEleae 1738
Cdd:pfam05911 10 KVAEEAVSGWEKAEAEALALKQQLESVTLQKLTAEERAAHLDGALKECMQQlRNVKEEQEQKI-HDVVLKKTKEWE---- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1739 laKVRAEMEVLLAskaraeeesrstsEKSKQRLEAEasrfrelAEEAARLRALAEEAKRQRQLAEEdaaRQRAEAE-RVL 1817
Cdd:pfam05911 85 --KIKAELEAKLV-------------ETEQELLRAA-------AENDALSRSLQERENLLMKLSEE---KSQAEAEiEAL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1818 AEKL-AAIGEATRLKTEAEIALKEKEAENErlrrlaEDEaFQRRRLEEQAAQHKADIeERLAQLrkasESELERQKGLV 1895
Cdd:pfam05911 140 KSRLeSCEKEINSLKYELHVLSKELEIRNE------EKN-MSRRSADAAHKQHLESV-KKIAKL----EAECQRLRGLV 206
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2156-2409 |
9.97e-04 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 45.66 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2156 AEQTLRQKAQVEQELTTLRLQLEETDHQK----------SILDEELQRLKAEVT-EAARQRSQVEEELFSLRVQMEELGK 2224
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLiRGATEGLCVHSLSKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2225 LKARIEAENRALI-LRDKDNTQRVLQEEAEKMK-HVAEEAARLSVAAQEAARLRELAEED-------------------- 2282
Cdd:PLN02939 238 LKDDIQFLKAELIeVAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPLQYDCwwekvenlqdlldratnqve 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2283 -----LAQQRALAEK--MLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTL----E 2351
Cdd:PLN02939 318 kaalvLDQNQDLRDKvdKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQLYQESIKEFQDTLsklkE 397
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 2352 AERQRQLEMSAEA------ERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2409
Cdd:PLN02939 398 ESKKRSLEHPADDmpsefwSRILLLIDGWLLEKKISNNDAKLLREMVWKRDGRIREAYLSCKGK 461
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1334-1441 |
9.97e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1334 EQQRAEERERLAAVEAALE-----------KQRQLAEAHAQAKAQAEQEAQELQRRMQEEVA------RREEAAVDAQQQ 1396
Cdd:PRK00409 526 EELERELEQKAEEAEALLKeaeklkeeleeKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADeiikelRQLQKGGYASVK 605
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 2124423190 1397 KRSIQEELQHLRQSSEAEIQAKARQVEAAErsRLRIEEEIRVVRL 1441
Cdd:PRK00409 606 AHELIEARKRLNKANEKKEKKKKKQKEKQE--ELKVGDEVKYLSL 648
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1327-1588 |
1.04e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1327 EEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEE-------VARREEAAVDAQQQKRS 1399
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafldrTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1400 IQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEI--RVVRLQLETTE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1476
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1477 EAERLRRQV-QDETQRKRQAEAELAVRVKAEAEAAREK---QRALQALEEFRLQAEEAERRLRQaeAERARQVQVALETA 1552
Cdd:pfam02029 165 EAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRghpEVKSQNGEEEVTKLKVTTKRRQG--GLSQSQEREEEAEV 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 2124423190 1553 QRSAEVELQSKRASFAEKTAQ-LERTLQEEHVAVAQL 1588
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKESEeFEKLRQKQQEAELEL 279
|
|
| PRK00106 |
PRK00106 |
ribonuclease Y; |
2254-2429 |
1.09e-03 |
|
ribonuclease Y;
Pssm-ID: 178867 [Multi-domain] Cd Length: 535 Bit Score: 45.24 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2254 KMKHvAEEAARLSV--AAQEAARLRELAEEDLAQQRALAEKMLKEK-----MQAVQEAT--RLKAEAELLQQQKELAQEQ 2324
Cdd:PRK00106 25 KMKS-AKEAAELTLlnAEQEAVNLRGKAERDAEHIKKTAKRESKALkkellLEAKEEARkyREEIEQEFKSERQELKQIE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2325 ARRLQE------------DKEQMAQQLEQETQGFQRTLEaERQRQLEMSAEAERLKL-RVAEMSRAQARAEEDAQRFRKQ 2391
Cdd:PRK00106 104 SRLTERatsldrkdenlsSKEKTLESKEQSLTDKSKHID-EREEQVEKLEEQKKAELeRVAALSQAEAREIILAETENKL 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423190 2392 AEEIGEKLHRTELATQEKVT------LVQTLeiQRQQSDHDAER 2429
Cdd:PRK00106 183 THEIATRIREAEREVKDRSDkmakdlLAQAM--QRLAGEYVTEQ 224
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1085-1729 |
1.12e-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: 45.10 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1085 EVLKAHEEQLKEAQAVPATLPE-LEATKAALKKLRAQAE-AQQPMFDALRDELRGAQEVGERLQQRHGERDVEV------ 1156
Cdd:pfam05483 169 EKTKKYEYEREETRQVYMDLNNnIEKMILAFEELRVQAEnARLEMHFKLKEDHEKIQHLEEEYKKEINDKEKQVsllliq 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1157 ---------------ERWRERVAQLLERwqavlaqTDLRQRELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLA 1221
Cdd:pfam05483 249 itekenkmkdltfllEESRDKANQLEEK-------TKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQI 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1222 DSRAVREQLRQEKALLEEIERHGE--------------KVEECQRFAKQYINAIKDyELQLVTYKAQlepvaspakkpKV 1287
Cdd:pfam05483 322 ATKTICQLTEEKEAQMEELNKAKAahsfvvtefeattcSLEELLRTEQQRLEKNED-QLKIITMELQ-----------KK 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1288 QSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETlrrmEEEERLAEQQRAEERErLAAVEAALEKQRQLAEAHAQAKAQ 1367
Cdd:pfam05483 390 SSELEEMTKFKNNKEVELEELKKILAEDEKLLDEK----KQFEKIAEELKGKEQE-LIFLLQAREKEIHDLEIQLTAIKT 464
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1368 AEQ----EAQELQRRMQEEVARREEaaVDAQQQKRSIqEELQHLRQSSEAEIQAKARQVEAAERSRlrieEEIRVVRlQL 1443
Cdd:pfam05483 465 SEEhylkEVEDLKTELEKEKLKNIE--LTAHCDKLLL-ENKELTQEASDMTLELKKHQEDIINCKK----QEERMLK-QI 536
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1444 ETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEef 1523
Cdd:pfam05483 537 ENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELH-- 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1524 rlQAEEAERRLRQAEAERARqvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLreeaerraqqqaeae 1603
Cdd:pfam05483 615 --QENKALKKKGSAENKQLN----AYEIKVNKLELELASAKQKFEEIIDNYQKEIEDKKISEEKL--------------- 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1604 rareeaERELERWQLKANEALRLRLQAEEVAQQKslaqaeaekqkEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA 1683
Cdd:pfam05483 674 ------LEEVEKAKAIADEAVKLQKEIDKRCQHK-----------IAEMVALMEKHKHQYDKIIEERDSELGLYKNKEQE 736
|
650 660 670 680
....*....|....*....|....*....|....*....|....*.
gi 2124423190 1684 EGTAqqRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAAT 1729
Cdd:pfam05483 737 QSSA--KAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2139-2546 |
1.13e-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: 45.10 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 LRQKQAadaEMEKHKKFAEQTLR--QKAQVEQELTTLRLQLE------------ETDHQKSILDEELQRLKAEVTEAARQ 2204
Cdd:pfam05483 101 LKQKEN---KLQENRKIIEAQRKaiQELQFENEKVSLKLEEEiqenkdlikennATRHLCNLLKETCARSAEKTKKYEYE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2205 RSQVEEELFSLRVQMEE--LGKLKARIEAENRALILRDKdntqrvLQEEAEKMKHVAEEAARlsvaaqeaarlrelAEED 2282
Cdd:pfam05483 178 REETRQVYMDLNNNIEKmiLAFEELRVQAENARLEMHFK------LKEDHEKIQHLEEEYKK--------------EIND 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2283 LAQQRALAEKMLKEKMQAVQEATRLkaeaellqqqkelaqeqarrLQEDKEQmAQQLEQETQGFQRTLEAERQRQLEMSA 2362
Cdd:pfam05483 238 KEKQVSLLLIQITEKENKMKDLTFL--------------------LEESRDK-ANQLEEKTKLQDENLKELIEKKDHLTK 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2363 EAERLKLRVAEMSRAQARAEEDAQRFRK-----------QAEEIGEKLHRTELATQEKVTLVQTLE----IQRQQSDHDA 2427
Cdd:pfam05483 297 ELEDIKMSLQRSMSTQKALEEDLQIATKticqlteekeaQMEELNKAKAAHSFVVTEFEATTCSLEellrTEQQRLEKNE 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2428 ERLRQAIAELEREKEKLKQEAKLLQLKSEEMQTVqqeqllqetqalqQSFLSEKDTLLqrerfieQEKAKLEQLFQDEVA 2507
Cdd:pfam05483 377 DQLKIITMELQKKSSELEEMTKFKNNKEVELEEL-------------KKILAEDEKLL-------DEKKQFEKIAEELKG 436
|
410 420 430
....*....|....*....|....*....|....*....
gi 2124423190 2508 KAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEE 2546
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAIKTSEEHYLKEVED 475
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3667-3705 |
1.13e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 39.23 E-value: 1.13e-03
10 20 30
....*....|....*....|....*....|....*....
gi 2124423190 3667 YLYGTGCVAGVYVPGSRQTLTIYQALKKGLLSAEVARLL 3705
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2174-2404 |
1.14e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.80 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2174 RLQLEETDHQKSildEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRAlilrdkdntqrvlQEEAE 2253
Cdd:PRK09510 66 RQQQQQKSAKRA---EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAA-------------KQAAL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2254 KMKHVAEEAARLSVAAQEAARLRELAEEDLAQQrALAEKMLKEKMQAVQeatrlKAEAEllqQQKELAQEQARRLQEDKE 2333
Cdd:PRK09510 130 KQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKK-AAAEAKKKAEAEAAK-----KAAAE---AKKKAEAEAAAKAAAEAK 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423190 2334 QMAQQleqetqgfqrtlEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2404
Cdd:PRK09510 201 KKAEA------------EAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
361-1310 |
1.20e-03 |
|
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: 45.43 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 361 EREKQLRSEFERLERLQRIVSKLqmeaglcEEQLNqadallqsdvRLLAAGKAPQRAGEVERDLDKADsmIRLLFNDVQT 440
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNEL-------ERQLK----------SLERQAEKAERYKELKAELRELE--LALLVLRLEE 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 441 LKDGRhpqgeqmyrrvyrlhERLVAIRTEYNLRLKAGVAAPVTQVTQVTlQSTQRRPELEDSTLRYLQDLLAWVEENQRr 520
Cdd:TIGR02168 237 LREEL---------------EELQEELKEAEEELEELTAELQELEEKLE-ELRLEVSELEEEIEELQKELYALANEISR- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 521 vdgaewgvdlpsveaqlgshrgLHHSIEEFRAKIERARTDEGQLSpatrgAYRDCLGRLDLQYAKLLNSSKGRLRSLESL 600
Cdd:TIGR02168 300 ----------------------LEQQKQILRERLANLERQLEELE-----AQLEELESKLDELAEELAELEEKLEELKEE 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 601 YSFVAAATKELMWL---SEKEEEEVGFDWSERNTNMAAKKESYSALMRELELKEKKVKEIQNTGDRLLREDHPARPTVES 677
Cdd:TIGR02168 353 LESLEAELEELEAEleeLESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 678 FQ-AALQTQwswmlqlcccIEAHLKENTAYFQFFSDVREAEEQLRKLQETLRRKytcdrsitVTRLEDLLQDAQDERDQL 756
Cdd:TIGR02168 433 AElKELQAE----------LEELEEELEELQEELERLEEALEELREELEEAEQA--------LDAAERELAQLQARLDSL 494
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 757 NEYRGHLSGLARRAKAIvqLKPRNPAHPVRGRVPLLAVCD--YKQVEVTVHKGDECQLVGPAQPSHWKVVSSSgSEAAVP 834
Cdd:TIGR02168 495 ERLQENLEGFSEGVKAL--LKNQSGLSGILGVLSELISVDegYEAAIEAALGGRLQAVVVENLNAAKKAIAFL-KQNELG 571
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 835 SVCFLVPPPNQEAQEAITRLEA-QHQALVTLWHQLHVDMKSllawqSLSRDVQLIRSWSLVTfrtmkpEEQRQALRSLEL 913
Cdd:TIGR02168 572 RVTFLPLDSIKGTEIQGNDREIlKNIEGFLGVAKDLVKFDP-----KLRKALSYLLGGVLVV------DDLDNALELAKK 640
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 914 HYQAFLRDSQD----------AGGFGPED--RLQAEREYGSCSHHYQQLLQSLEQGEQeesrcqrcisELKDIRLQLEAC 981
Cdd:TIGR02168 641 LRPGYRIVTLDgdlvrpggviTGGSAKTNssILERRREIEELEEKIEELEEKIAELEK----------ALAELRKELEEL 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 982 ETRTVHRLRLPLDKEpaRECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRS 1061
Cdd:TIGR02168 711 EEELEQLRKELEELS--RQISALRKDLARLEAEVEQLEERIAQLSKELTE-------------LEAEIEELEERLEEAEE 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1062 LSAIYLEKLKTISLVIRsthGAEEVLKAHEEQLKEAQAVPATLPELEATKA-ALKKLRAQAEAQQPMFDALRDELRGAQE 1140
Cdd:TIGR02168 776 ELAEAEAEIEELEAQIE---QLKEELKALREALDELRAELTLLNEEAANLReRLESLERRIAATERRLEDLEEQIEELSE 852
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1141 VGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYRESADPLgawLQDAKRRQEQIQAMVL 1220
Cdd:TIGR02168 853 DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSEL---RRELEELREKLAQLEL 929
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1221 ADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVaspakkpkvqsgSESVIQEYVD 1300
Cdd:TIGR02168 930 RLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPV------------NLAAIEEYEE 997
|
970
....*....|
gi 2124423190 1301 LRTRYSELTT 1310
Cdd:TIGR02168 998 LKERYDFLTA 1007
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2094-2441 |
1.24e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 44.52 E-value: 1.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2094 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAEMEKhkkfAEQTLRQKAQVEQELTTL 2173
Cdd:pfam13868 3 ENSDELRELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEE----EEKEEERKEERKRYRQEL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2174 RLQLEETDHQKSILDEELQRLKAEVTEAARQrsqveeelfslrVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEAE 2253
Cdd:pfam13868 79 EEQIEEREQKRQEEYEEKLQEREQMDEIVER------------IQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2254 KMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRAlAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2333
Cdd:pfam13868 147 KEEEREEDERILEYLKEKAEREEEREAEREEIEEE-KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKERE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2334 QMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEE----DAQRFRKQAEEIGEKLHRTELATQEK 2409
Cdd:pfam13868 226 EAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEieqeEAEKRRMKRLEHRRELEKQIEEREEQ 305
|
330 340 350
....*....|....*....|....*....|..
gi 2124423190 2410 VTLVQTLEIQRQQSDHDAERLRQAIAELEREK 2441
Cdd:pfam13868 306 RAAEREEELEEGERLREEEAERRERIEEERQK 337
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2245-2423 |
1.26e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.04 E-value: 1.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2245 QRVLQEEAEKMkhvaeEAARLsvAAQEAARLRELAEE--DLAQQRALAEKMLKE---KMQAVQEATRLKAEAELLQQQKE 2319
Cdd:PRK10929 109 QEILQVSSQLL-----EKSRQ--AQQEQDRAREISDSlsQLPQQQTEARRQLNEierRLQTLGTPNTPLAQAQLTALQAE 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2320 LA-------------------QEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAE-AERLKLRVAEMSRAQA 2379
Cdd:PRK10929 182 SAalkalvdelelaqlsannrQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIV 261
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2124423190 2380 RA----EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQS 2423
Cdd:PRK10929 262 AQfkinRELSQALNQQAQRMDLIASQQRQAASQTLQVRQALNTLREQS 309
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1719-1846 |
1.39e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 44.01 E-value: 1.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1719 ARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKqrlEAEASRfrelaEEAARLRALAEEA-KR 1797
Cdd:PRK06991 146 AWSQAQADAARARHDARQARLRREREAAEARAAARAAASAAAAAAEASAA---AAPAAD-----DAEAKKRAIIAAAlER 217
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1798 QRQLAEEDAARQRA--EAERVLAEKLAAI--GEATRLKTEAEIALKEKEAENE 1846
Cdd:PRK06991 218 ARKKKEELAAQGAGpkNTEGVSAAVQAQIdaAEARRKRLAEQRDAPDDANADG 270
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2160-2457 |
1.42e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.89 E-value: 1.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2160 LRQKAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIeaenralil 2238
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2239 RDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2318
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2319 ELAQEQARRLQEDKEQMA--QQLEQETQGFQRTLEAERQRQLEMSAEAERLKlrvAEMSRAQARAEEDAQRFRKQAEEIG 2396
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILelEGYEMDYNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2397 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLRQAIAELEREKEKL 2444
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 2124423190 2445 KQEAKllQLKSEE 2457
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1200-1400 |
1.43e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.68 E-value: 1.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1200 PLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRfakqyinAIKDYELQLVTYKAQL-EPV 1278
Cdd:PRK11637 37 AFSAHASDNRDQLKSIQQDIAAKEKSVRQQQQQRASLLAQLKKQEEAISQASR-------KLRETQNTLNQLNKQIdELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1279 ASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLT-------SQ-------YIKFISE----------------TLRRMEE 1328
Cdd:PRK11637 110 ASIAKLEQQQAAQERLLAAQLDAAFRQGEHTGLQlilsgeeSQrgerilaYFGYLNQarqetiaelkqtreelAAQKAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1329 EERLAEQQ----------------RAEERERLAAVEAALEK-QRQLAE--------------AHAQAKAQAEQEAQELQR 1377
Cdd:PRK11637 190 EEKQSQQKtllyeqqaqqqkleqaRNERKKTLTGLESSLQKdQQQLSElranesrlrdsiarAEREAKARAEREAREAAR 269
|
250 260
....*....|....*....|....
gi 2124423190 1378 -RMQEEVARREEAAVDAQQQKRSI 1400
Cdd:PRK11637 270 vRDKQKQAKRKGSTYKPTESERSL 293
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
958-1588 |
1.44e-03 |
|
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: 44.96 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 958 EQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLALPE 1037
Cdd:pfam02463 320 EKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELEL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1038 PSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTHGAEEVLKAHEEQLKEAQAVPATLPELEATKAALKKL 1117
Cdd:pfam02463 400 KSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQL 479
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1118 RAQAEAQQPMFDALRDELRGAQE-------VGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLGRQ 1190
Cdd:pfam02463 480 VKLQEQLELLLSRQKLEERSQKEskarsglKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADE 559
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1191 LRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQR---FAKQYINAIKDYELQ 1267
Cdd:pfam02463 560 VEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRakvVEGILKDTELTKLKE 639
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1268 LVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERlaEQQRAEERERLAAV 1347
Cdd:pfam02463 640 SAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKK--KEQREKEELKKLKL 717
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1348 EAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEA------AVDAQQQKRSIQEELQHLRQSSEAEIQAKARQ 1421
Cdd:pfam02463 718 EAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKeekeeeKSELSLKEKELAEEREKTEKLKVEEEKEEKLK 797
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1422 VEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ--AQEEAERLRRQVQDETQRKRQAEAEL 1499
Cdd:pfam02463 798 AQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklAEEELERLEEEITKEELLQELLLKEE 877
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1500 AVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1579
Cdd:pfam02463 878 ELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEE 957
|
....*....
gi 2124423190 1580 EEHVAVAQL 1588
Cdd:pfam02463 958 EEERNKRLL 966
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1660-1827 |
1.46e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.01 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLEEELARLQHEAAAATQKRQELEAE 1738
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLLELQAESAAVESSGQSRAEALAEAE 726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1739 LAKVRAEMEVLLAS-KARAEE-ESRSTSEKSKQRLEAEASRFRELAEEaarlralaeEAKRQRQLAEEDAARQRAEAERV 1816
Cdd:PTZ00491 727 ARLIEAEAEVEQAElRAKALRiEAEAELEKLRKRQELELEYEQAQNEL---------EIAKAKELADIEATKFERIVEAL 797
|
170
....*....|.
gi 2124423190 1817 LAEKLAAIGEA 1827
Cdd:PTZ00491 798 GRETLIAIARA 808
|
|
| AAA_13 |
pfam13166 |
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA ... |
2159-2513 |
1.46e-03 |
|
AAA domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily. Many of the proteins in this family are conjugative transfer proteins. This family includes the PrrC protein that is thought to be the active component of the anticodon nuclease.
Pssm-ID: 463796 [Multi-domain] Cd Length: 712 Bit Score: 44.67 E-value: 1.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2159 TLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT-EAARQRSQVEEELFSlrvqmEELGKLKARIEAENRAL- 2236
Cdd:pfam13166 94 IQEKIAKLKKEIKDHEEKLDAAEANLQKLDKEKEKLEADFLdECWKKIKRKKNSALS-----EALNGFKYEANFKSRLLr 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2237 -ILRDKDNTQRVLQEEAEKmkhvAEEAARLSVAAQEAARLRE-LAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2314
Cdd:pfam13166 169 eIEKDNFNAGVLLSDEDRK----AALATVFSDNKPEIAPLTFnVIDFDALEKAEILIQKVIGKSSAIEELIKNPDLADWV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2315 QQQKELAQE--------QARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEA-ERLKLRVAEMSRAQArAEEDA 2385
Cdd:pfam13166 245 EQGLELHKAhldtcpfcGQPLPAERKAALEAHFDDEFTEFQNRLQKLIEKVESAISSLlAQLPAVSDLASLLSA-FELDV 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2386 QRFRKQAEEIGEKLHrtelatqekvTLVQTLEIQRQQSDHDAErLRQAIAELEREKEKLKQEAKLLQlKSEEMQTVQQEQ 2465
Cdd:pfam13166 324 EDIESEAEVLNSQLD----------GLRRALEAKRKDPFKSIE-LDSVDAKIESINDLVASINELIA-KHNEITDNFEEE 391
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 2466 LLQETQALQQSFLSEKDTLLQRE----RFIEQEKAKLEQLFQDEVAKAQKLR 2513
Cdd:pfam13166 392 KNKAKKKLRLHLVEEFKSEIDEYkdkyAGLEKAINSLEKEIKNLEAEIKKLR 443
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1584-2039 |
1.52e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.01 E-value: 1.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1584 AVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEE 1663
Cdd:COG3903 477 AAERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWF 556
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1664 QAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVR 1743
Cdd:COG3903 557 LRGLLRE-GRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAA 635
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1744 AEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAA 1823
Cdd:COG3903 636 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAA 715
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1824 IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRR 1903
Cdd:COG3903 716 AAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAA 795
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1904 QVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAA 1983
Cdd:COG3903 796 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAA 875
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1984 RQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFA 2039
Cdd:COG3903 876 AAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAA 931
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1663-1806 |
1.54e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 44.61 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1742
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1743 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDA 1806
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
4-123 |
1.55e-03 |
|
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: 41.88 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 4 YSMEEliqlvqderdrvqKKTFTKWVNKHLIKHwrAEAQRHI------SDLYEDLRDGHNLISLLEVLSGDSLPR----E 73
Cdd:cd21292 21 YSEEE-------------KVAFVNWINKNLGDD--PDCKHLLpmdpntDDLFEKVKDGILLCKMINLSVPDTIDErainK 85
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2124423190 74 KGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 123
Cdd:cd21292 86 KKLTVFTIHENLTLALNSASAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1131-1499 |
1.64e-03 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 44.50 E-value: 1.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1131 LRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQRELEQLgrqLRYYRESADPLGAWLQDAKR 1210
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1211 RQEQIQAMVLADSRAVREQLRQEKALLEEI----ERHGEKVEECQRF---AKQYINAIKDYELQLVTYKAQLEPVASPAK 1283
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIktltQRVLERETELERMkerAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1284 K--PKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISETLRRMEEEERLAEQQRAeERERLAAVEAALEKQRQLAEAH 1361
Cdd:pfam07888 189 SlsKEFQELRNSLAQRDTQVLQLQDTITTLTQK----LTTAHRKEAENEALLEELRS-LQERLNASERKVEGLGEELSSM 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1362 AQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEiRVVRL 1441
Cdd:pfam07888 264 AAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE-RMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1442 QLETT-ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAEL 1499
Cdd:pfam07888 343 KLEVElGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1334-1437 |
1.72e-03 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 43.63 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1334 EQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAqelqrRMQEEVARREEAAVDAQQQKRS-IQEELQHLRQSSE 1412
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARAAARAAASAAA-----AAAEASAAAAPAADDAEAKKRAiIAAALERARKKKE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 2124423190 1413 ----------------AEIQAkarQVEAAERSRLRIEEEIR 1437
Cdd:PRK06991 224 elaaqgagpkntegvsAAVQA---QIDAAEARRKRLAEQRD 261
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3039-3072 |
1.72e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 1.72e-03
10 20 30
....*....|....*....|....*....|....
gi 2124423190 3039 LLEAQAGTGHIIDPATSARLTVDEAVRSGLVGPE 3072
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2299-2394 |
1.82e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2299 QAVQEA-TRLKAEAELLQQQK---ELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEA------ERQRQL-EMSAEAERL 2367
Cdd:PRK11637 166 QARQETiAELKQTREELAAQKaelEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLTGlesslqKDQQQLsELRANESRL 245
|
90 100 110
....*....|....*....|....*....|.
gi 2124423190 2368 KLRVAEMSR-AQARAEE---DAQRFRKQAEE 2394
Cdd:PRK11637 246 RDSIARAEReAKARAERearEAARVRDKQKQ 276
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1302-1588 |
1.83e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 44.12 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1302 RTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQE 1381
Cdd:COG4372 12 RLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1382 EVARREEAavdaQQQKRSIQEELQHLRQsseaeiqakarQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALR 1461
Cdd:COG4372 92 AQAELAQA----QEELESLQEEAEELQE-----------ELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1462 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAER 1541
Cdd:COG4372 157 EQLESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALS 236
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2124423190 1542 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1588
Cdd:COG4372 237 ALLDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAAL 283
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1350-1521 |
1.85e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.62 E-value: 1.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1350 ALEKQRQLA--------EAHAQAKAQA-EQEAQ-ELQR-RMQEEVARREEAAVDAQQQKRSiqEELQHLRQS-SEAEIQA 1417
Cdd:PTZ00491 648 SLQKSVQLAieittksqEAAARHQAELlEQEARgRLERqKMHDKAKAEEQRTKLLELQAES--AAVESSGQSrAEALAEA 725
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1418 KARQVEAaersrlrieeeirvvrlqletterqrggaEGELQALRARAEeaeaqkrqaqeeAERLRRQVQDETQRKRQaEA 1497
Cdd:PTZ00491 726 EARLIEA-----------------------------EAEVEQAELRAK------------ALRIEAEAELEKLRKRQ-EL 763
|
170 180
....*....|....*....|....
gi 2124423190 1498 ELAVRvKAEAEAAREKQRALQALE 1521
Cdd:PTZ00491 764 ELEYE-QAQNELEIAKAKELADIE 786
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1454-1588 |
1.87e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.59 E-value: 1.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1454 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDetqRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERR 1533
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1534 LRQAEAERARQ-VQVALETAQRSAEVELQSK----RASFAEKTAQLERTLQEEHVAVAQL 1588
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1351-1529 |
1.89e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 44.31 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1351 LEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEvaRREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKarQVEAAERSRL 1430
Cdd:PRK12705 25 LKKRQRLAKEAERILQEAQKEAEEKLEAALLE--AKELLLRERNQQRQEARREREELQREEERLVQKE--EQLDARAEKL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1431 RIEEEirvvrlQLETTERqrggaegelqALRARAEEAEAQKRQAQEEAERLrrqvqdETQRKRQAEAELAVRVKAEAEaa 1510
Cdd:PRK12705 101 DNLEN------QLEEREK----------ALSARELELEELEKQLDNELYRV------AGLTPEQARKLLLKLLDAELE-- 156
|
170 180
....*....|....*....|
gi 2124423190 1511 REK-QRALQALEEFRLQAEE 1529
Cdd:PRK12705 157 EEKaQRVKKIEEEADLEAER 176
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1084-1907 |
1.95e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1084 EEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDE-LRGAQEVGERLQQRHGERDVEVERWRER 1162
Cdd:TIGR00606 244 ENELDPLKNRLKEIEHNLSKIMKLDNEIKALKSRKKQMEKDNSELELKMEKvFQGTDEQLNDLYHNHQRTVREKERELVD 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1163 VAQLLERWQAvlAQTDLRQRELEQLGRQLRYYREsadplgawlqdAKRRQEQIQAMvlaDSRAVREQLRQEKALLEE--- 1239
Cdd:TIGR00606 324 CQRELEKLNK--ERRLLNQEKTELLVEQGRLQLQ-----------ADRHQEHIRAR---DSLIQSLATRLELDGFERgpf 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1240 IER-----HGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPK--VQSGSESVIQEYVDLRTRYSELTTLT 1312
Cdd:TIGR00606 388 SERqiknfHTLVIERQEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKGLGrtIELKKEILEKKQEELKFVIKELQQLE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1313 --SQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREeaa 1390
Cdd:TIGR00606 468 gsSDRILELDQELRKAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDK--- 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1391 VDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRI---EEEIRVVRLQLETTERQRGGAEGELQALRARAEEA 1467
Cdd:TIGR00606 545 MDKDEQIRKIKSRHSDELTSLLGYFPNKKQLEDWLHSKSKEInqtRDRLAKLNKELASLEQNKNHINNELESKEEQLSSY 624
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1468 E-----AQKRQAQE-EAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQ-------RALQALEEFRLQAEEAERRL 1534
Cdd:TIGR00606 625 EdklfdVCGSQDEEsDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQsccpvcqRVFQTEAELQEFISDLQSKL 704
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1535 RQAEAE-RARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAEREL 1613
Cdd:TIGR00606 705 RLAPDKlKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESA 784
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1614 ERWQLKANEALRLRLQAEEVaqQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1693
Cdd:TIGR00606 785 KVCLTDVTIMERFQMELKDV--ERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQQEQIQHL 862
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1694 EQELIRLRAETEQ---GEQQRQLLEEELARLQHEA----AAATQKRQE---LEAELAKVRAEMEVLLASK----ARAEEE 1759
Cdd:TIGR00606 863 KSKTNELKSEKLQigtNLQRRQQFEEQLVELSTEVqsliREIKDAKEQdspLETFLEKDQQEKEELISSKetsnKKAQDK 942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1760 SRSTSEKSKQRLEAEASRFRELAE-----------EAARLRALAEEAKRQRQLAEEDAARQRAE------AERVLAEKLa 1822
Cdd:TIGR00606 943 VNDIKEKVKNIHGYMKDIENKIQDgkddylkqketELNTVNAQLEECEKHQEKINEDMRLMRQDidtqkiQERWLQDNL- 1021
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1823 aigeaTRLKTEAEIalkeKEAENERLRRLAedEAFQRRRLEEQAAQHKadIEERLAQLRKASESELERQKGLVEDTLRQR 1902
Cdd:TIGR00606 1022 -----TLRKRENEL----KEVEEELKQHLK--EMGQMQVLQMKQEHQK--LEENIDLIKRNHVLALGRQKGYEKEIKHFK 1088
|
....*
gi 2124423190 1903 RQVEE 1907
Cdd:TIGR00606 1089 KELRE 1093
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1699-1910 |
1.95e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.62 E-value: 1.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1699 RLRAETEQGEQQRQLLEEELARLQHEAAAAtqkrqelEAELAKVRAEmEVLLASKARAEEESRSTSEKSKQRLEAEAsrf 1778
Cdd:COG3206 165 NLELRREEARKALEFLEEQLPELRKELEEA-------EAALEEFRQK-NGLVDLSEEAKLLLQQLSELESQLAEARA--- 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1779 rELAEEAARLRALAEEAKRQRQ-LAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEA- 1856
Cdd:COG3206 234 -ELAEAEARLAALRAQLGSGPDaLPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAq 312
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 1857 ---FQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEdtLRQRRQVEEEIL 1910
Cdd:COG3206 313 rilASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRR--LEREVEVARELY 367
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1670-1891 |
2.01e-03 |
|
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.
Pssm-ID: 462900 [Multi-domain] Cd Length: 305 Bit Score: 43.59 E-value: 2.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1670 ELAEQELEKQRQLAEGTAQqrlAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEV 1748
Cdd:pfam09787 3 ESAKQELADYKQKAARILQ---SKEKLIASLKeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1749 LLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARL----RALAEEAKRQRQLAEEDAARQRAEAERVlaeklaai 1824
Cdd:pfam09787 80 LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLqeelRYLEEELRRSKATLQSRIKDREAEIEKL-------- 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1825 geATRLKTEAEIALKEKEAENeRLRRLAEDEAFQRRRLEEQAAQHKADI--EERLAQLRKASESELERQ 1891
Cdd:pfam09787 152 --RNQLTSKSQSSSSQSELEN-RLHQLTETLIQKQTMLEALSTEKNSLVlqLERMEQQIKELQGEGSNG 217
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
48-123 |
2.05e-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: 41.28 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 48 LYEDLRDGHNLISLLEvlsgDSLP-------------REKGRMRFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKL 114
Cdd:cd21294 38 LFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLNNFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHL 113
|
....*....
gi 2124423190 115 TLGLIWTII 123
Cdd:cd21294 114 ILGLIWQII 122
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1408-1880 |
2.07e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 2.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1408 RQSSEAEIQAKARQVEAAERSRLRIEEEIRVvRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1487
Cdd:COG3064 7 EKAAEAAAQERLEQAEAEKRAAAEAEQKAKE-EAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKKLAEAEKA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1488 ETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASF 1567
Cdd:COG3064 86 AAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1568 AEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAEAEKQ 1647
Cdd:COG3064 166 AAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAAL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1648 KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAA 1727
Cdd:COG3064 246 GGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1728 ATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAA 1807
Cdd:COG3064 326 ALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRL 405
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1808 RQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQL 1880
Cdd:COG3064 406 DLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLA 478
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1664-2606 |
2.12e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 44.65 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1664 QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAeLAKVR 1743
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1744 AEMEVLLAS-KARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAA-------RQRAEAER 1815
Cdd:TIGR00606 279 KQMEKDNSElELKMEKVFQGTDEQLNDLYHNHQRTVREKERELVDCQRELEKLNKERRLLNQEKTellveqgRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1816 VLAEKLAAIGEATRLKTEAEIALKEKEAENERlrRLAEDEAFQRRRLEEQA---AQHKADIEERLAQLRKASESELERQK 1892
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSER--QIKNFHTLVIERQEDEAktaAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1893 GLVEDTLRQRRQVEEEILALKVSFEK----AAAGKAELELELGRIRSNAEDTLrSKEQAELEAMRQRQLAAEEEQRRREA 1968
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKElqqlEGSSDRILELDQELRKAERELSK-AEKNSLTETLKKEVKSLQNEKADLDR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1969 EErvqKSLAAEEEAARQRKAALEEVERL-KAKVEEARRLRERAEQESARQLQLAQDAAQKRlQAEEKAHAFAVQQKEqel 2047
Cdd:TIGR00606 516 KL---RKLDQEMEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKSKEINQ--- 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2048 qqtlqqeqsMLERLRgeaeaarraaeeaeeARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAeklrkeaeqe 2127
Cdd:TIGR00606 589 ---------TRDRLA---------------KLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGS---------- 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2128 aarraqaeqaalrqkQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ 2207
Cdd:TIGR00606 635 ---------------QDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQTEAELQEFISD 699
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2208 VEEELFSLRVQMEELGKLKARIEAEnRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSvaaQEAARLRELAEEDlaqqr 2287
Cdd:TIGR00606 700 LQSKLRLAPDKLKSTESELKKKEKR-RDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVN---RDIQRLKNDIEEQ----- 770
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2288 alaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRL-QEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAER 2366
Cdd:TIGR00606 771 ---ETLLGTIMPEEESAKVCLTDVTIMERFQMELKDVERKIaQQAAKLQGSDLDRTVQQVNQEKQEKQHELDTVVSKIEL 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2367 LKLRVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLeiqrQQSDHDAERLRQAIAELEREKEKLKQ 2446
Cdd:TIGR00606 848 NRKLIQDQQEQIQHLKSKTNELKSEKLQIGTNLQRRQQFEEQLVELSTEV----QSLIREIKDAKEQDSPLETFLEKDQQ 923
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2447 EAKLLQLKSEEMQTVQQEQLLQETQALQQSFLSEKDTllqrERFIEQEKAKLEQLFQDEVAKaqklreeqqrqqkqmeee 2526
Cdd:TIGR00606 924 EKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDI----ENKIQDGKDDYLKQKETELNT------------------ 981
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2527 kqqLVASMEEARQRQREAEEGVRrkqeeLQLLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEEIAASQATAVK 2606
Cdd:TIGR00606 982 ---VNAQLEECEKHQEKINEDMR-----LMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMK 1053
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2150-2501 |
2.12e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 44.24 E-value: 2.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2150 EKHKKFAEQTLRQKAQVEQ---ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLK 2226
Cdd:TIGR04523 138 KNIDKFLTEIKKKEKELEKlnnKYNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKSLE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2227 ARI-EAENRALILRD-KDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQqralAEKMLKEKMQAVQEa 2304
Cdd:TIGR04523 218 SQIsELKKQNNQLKDnIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQ----NNKKIKELEKQLNQ- 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2305 trLKAEAELLQQQKE---------LAQEQARRLQEDKEQMAQ------QLEQETQGFQRTLEAERQRQLEMSAEAERLKL 2369
Cdd:TIGR04523 293 --LKSEISDLNNQKEqdwnkelksELKNQEKKLEEIQNQISQnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQN 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2370 RVAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAK 2449
Cdd:TIGR04523 371 EIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDS 450
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 2450 LLQLKSEEMQTvQQEQLLQETQALQQSFLSEKDTLLQRERFIEQEKAKLEQL 2501
Cdd:TIGR04523 451 VKELIIKNLDN-TRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2748-2784 |
2.18e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.18e-03
10 20 30
....*....|....*....|....*....|....*..
gi 2124423190 2748 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVRDHG 2784
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1660-2098 |
2.20e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 44.26 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgeQQRQLLEEELARLQHEAAAATQKRQELEAEL 1739
Cdd:COG3064 20 QAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQ--RAAELAAEAAKKLAEAEKAAAEAEKKAAAEK 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1740 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAE 1819
Cdd:COG3064 98 AKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAG 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1820 KLAA-IGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDT 1898
Cdd:COG3064 178 AAAAlVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1899 LRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAA 1978
Cdd:COG3064 258 GVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASL 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1979 EEEAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSML 2058
Cdd:COG3064 338 EAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASA 417
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2124423190 2059 ERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAER 2098
Cdd:COG3064 418 VELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTG 457
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1795-2016 |
2.20e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 44.00 E-value: 2.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1795 AKRQRQLAEEDAARQRAEAERvlaeklaaigEATRLKTEAEIALKEkeaENERLRRLAEDEAFQRRR-LEEQaaqhkadi 1873
Cdd:PRK12704 29 AEAKIKEAEEEAKRILEEAKK----------EAEAIKKEALLEAKE---EIHKLRNEFEKELRERRNeLQKL-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1874 EERLAQlrkaSESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAaagKAELElelgrirsnaedTLRSKEQAELEAMr 1953
Cdd:PRK12704 88 EKRLLQ----KEENLDRKLELLEKREEELEKKEKELEQKQQELEKK---EEELE------------ELIEEQLQELERI- 147
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1954 qrqlaaeeeqrrreaeervqKSLAAEEeaARQRkaALEEVERlKAKVEEARRLR---ERAEQESAR 2016
Cdd:PRK12704 148 --------------------SGLTAEE--AKEI--LLEKVEE-EARHEAAVLIKeieEEAKEEADK 188
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1457-1556 |
2.27e-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: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1457 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEtQRKRQAEAElAVRVKAEAEAAREKQRALQALEefrlqaEEAERR 1533
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 2124423190 1534 LRQAEAERARQVQVALETAQRSA 1556
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2260-2457 |
2.28e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.17 E-value: 2.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2260 EEAARLSVAAQEAARLRelAEEDLAQQRALAEkmLKEKmQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQL 2339
Cdd:PRK05035 465 EKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAATQPIVIKAGARPDNSAVIAAREARKAQARARQAEKQA 539
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2340 EQETQGFQRTLEAERQR-----------QLEMSAEAERLKLRV-AEMSRAQAR-AEEDAQRFRKQAEEIGEKLHRTELAT 2406
Cdd:PRK05035 540 AAAADPKKAAVAAAIARakakkaaqqaaNAEAEEEVDPKKAAVaAAIARAKAKkAAQQAASAEPEEQVAEVDPKKAAVAA 619
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 2124423190 2407 QEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAKLLQLKSEE 2457
Cdd:PRK05035 620 AIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE 670
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1084-1372 |
2.39e-03 |
|
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: 44.34 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1084 EEVLKAHEEQLKEAQAVPATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEvgERLQQRhgERDVEVERWRE-- 1161
Cdd:pfam17380 306 EEKAREVERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRQEERKREL--ERIRQE--EIAMEISRMREle 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1162 -----------RVAQLLERWQAVLAQTDLRQRELEQLGRQLRYYREsadplgawlQDAKRRQEQIQAMVLADSRAVREQL 1230
Cdd:pfam17380 382 rlqmerqqkneRVRQELEAARKVKILEEERQRKIQQQKVEMEQIRA---------EQEEARQREVRRLEEERAREMERVR 452
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1231 RQEKALLEEIERHGEKVEECQRFAKQYINAIKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEyvdlRTRYSELTT 1310
Cdd:pfam17380 453 LEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLE----KEMEERQKA 528
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1311 LTSQYIKFISETLRR----MEEEERLAEQQR--AEERERLAAVEAALEKQRQLAEAHaqaKAQAEQEA 1372
Cdd:pfam17380 529 IYEEERRREAEEERRkqqeMEERRRIQEQMRkaTEERSRLEAMEREREMMRQIVESE---KARAEYEA 593
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1163-1440 |
2.39e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 44.13 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1163 VAQLLERWQAVLAQTDLRQRELEQLGRQlryyresadplgawLQDAKRRQEQIQAMVLADSRAVREQLRQ--EKALLEEI 1240
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQ--------------LAQAPAKLRQAQAELEALKDDNDEETREtlSTLSLRQL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1241 ERhgeKVEECQRFAKQYINAIKDYELQLVTYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSelTTLTSQyiKFIS 1320
Cdd:PRK11281 127 ES---RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALR 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLR-RMEEEERLAEQQRAEERERLAA---VEAALEKQRQLAEAHAQakaQAEQEAQELQ------RRMQ-EEVARREEA 1389
Cdd:PRK11281 191 PSQRvLLQAEQALLNAQNDLQRKSLEGntqLQDLLQKQRDYLTARIQ---RLEHQLQLLQeainskRLTLsEKTVQEAQS 267
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1390 AVDAQQQKRS--IQEELQHLRQSSEAEIQAKAR-------------QVEAAERSRLRIEEEIRVVR 1440
Cdd:PRK11281 268 QDEAARIQANplVAQELEINLQLSQRLLKATEKlntltqqnlrvknWLDRLTQSERNIKEQISVLK 333
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
2239-2392 |
2.46e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 43.93 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2239 RDKDNTQRVLQE---EAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQ 2315
Cdd:PRK12705 30 RLAKEAERILQEaqkEAEEKLEAALLEAKELLLRERNQQRQEARREREELQREE-ERLVQKEEQLDARAEKLDNLENQLE 108
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2124423190 2316 QQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQARAEEDAQRFRKQA 2392
Cdd:PRK12705 109 EREKALSARELELEELEKQLDNELYRVAGLTPEQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQNILAQA 185
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2671-2708 |
2.57e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.57e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2124423190 2671 RRYLQGRSSIAGLLLKPANEKLSIYTALRRQLLSPGTA 2708
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1392-1579 |
2.59e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 43.37 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1392 DAQQQKRSiqeELQHLRQSSEAEIQAKARQVEAA--ERSRLRIE-----EEIRVVRLQLETTERQRGGAEGELQALRARA 1464
Cdd:pfam00038 36 ELRQKKGA---EPSRLYSLYEKEIEDLRRQLDTLtvERARLQLEldnlrLAAEDFRQKYEDELNLRTSAENDLVGLRKDL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1465 EEAEAQKRQAQEEAERL------RRQVQDETQRKRQAEAELAVRVkAEAEAAReKQRALQALEEFRLQAEE-AERRLRQA 1537
Cdd:pfam00038 113 DEATLARVDLEAKIESLkeelafLKKNHEEEVRELQAQVSDTQVN-VEMDAAR-KLDLTSALAEIRAQYEEiAAKNREEA 190
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 2124423190 1538 EAerarQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQ 1579
Cdd:pfam00038 191 EE----WYQSKLEELQQAAARNGDALRSA-KEEITELRRTIQ 227
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1324-1405 |
2.63e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.14 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1324 RRMEEEERLAEQQRAEERERLAAVEA-ALEKQRQLAEAHAQAK---AQAEQEAQELQRR-----MQEEVARREEAAVDAQ 1394
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKLAAEalaeaQAEAQASKEKARREIE 111
|
90
....*....|.
gi 2124423190 1395 QQKRSIQEELQ 1405
Cdd:PRK07353 112 QQKQAALAQLE 122
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1366-1735 |
2.65e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 43.70 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1366 AQAEQEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQl 1443
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRqkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1444 ETTERQRggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKqralqalEEF 1523
Cdd:pfam02029 81 EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWST-------EVR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1524 RLQAEEAERRLRQAEAERA-RQVQVALETAQRSAEVELQSKRASfaEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEA 1602
Cdd:pfam02029 151 QAEEEGEEEEDKSEEAEEVpTENFAKEEVKDEKIKKEKKVKYES--KVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1603 ERAREEAERELERWQLKANEALrlrlqaeevaqqkslaqaeaekqkeeaerearrrgkaEEQAVRQRELAEQELEKQRQl 1682
Cdd:pfam02029 229 GLSQSQEREEEAEVFLEAEQKL-------------------------------------EELRRRRQEKESEEFEKLRQ- 270
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1683 aegtAQQRLAAEQELI--------RLRAETEQG----EQQRQLLEEELARLQHEA-----AAATQKRQEL 1735
Cdd:pfam02029 271 ----KQQEAELELEELkkkreerrKLLEEEEQRrkqeEAERKLREEEEKRRMKEEierrrAEAAEKRQKL 336
|
|
| PRK10920 |
PRK10920 |
putative uroporphyrinogen III C-methyltransferase; Provisional |
2302-2380 |
2.67e-03 |
|
putative uroporphyrinogen III C-methyltransferase; Provisional
Pssm-ID: 236795 Cd Length: 390 Bit Score: 43.55 E-value: 2.67e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 2302 QEATRLKAEAELLQQQKELAQEQArrlQEDKEQMAQQLEQETQgfqrTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2380
Cdd:PRK10920 60 QQAQNQTATNDALANQLTALQKAQ---ESQKQELEGILKQQAK----ALDQANRQQAALAKQLDELQQKVATISGSDAK 131
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2140-2340 |
2.71e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 43.71 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2140 RQKQAADAEMEKHKKFAEQTLRQK-AQVEQELTTLRLQLEETDHQKSILDEELQRlKAEVTEAARQRS-QVEEELFSLRV 2217
Cdd:COG2268 201 ARIAEAEAERETEIAIAQANREAEeAELEQEREIETARIAEAEAELAKKKAEERR-EAETARAEAEAAyEIAEANAEREV 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2218 QME-ELGKLKARIEAEnralilrdkdnTQRVLQEEAEKMKHVAEEAArlsvAAQEAARLRELAEEDLAQQRALAEKmlke 2296
Cdd:COG2268 280 QRQlEIAEREREIELQ-----------EKEAEREEAELEADVRKPAE----AEKQAAEAEAEAEAEAIRAKGLAEA---- 340
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 2124423190 2297 kmqavqEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLE 2340
Cdd:COG2268 341 ------EGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLE 378
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
948-1373 |
2.72e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 948 QQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETRTVHRLRLPLDKEPARECAQRIAEQQKAQAEVEGLGKGVARLSA 1027
Cdd:COG4717 98 EELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQE 177
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1028 EAEKVLALPEPSpaaptLRSELELTLGKLEQVRSLSAIYLEKLKTislvirsthgAEEVLKAHEEQLKEAQAVPATLPEL 1107
Cdd:COG4717 178 ELEELLEQLSLA-----TEEELQDLAEELEELQQRLAELEEELEE----------AQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1108 EATKAALKKLRAQA-----EAQQPMFDALRDELRGAQEVGERLQQRHGERDVeveRWRERVAQLLERWQAVLAQTDLRQR 1182
Cdd:COG4717 243 ERLKEARLLLLIAAallalLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEE 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1183 ELEQLGRQLRYYRE-SADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQE-KALLEEIerHGEKVEECQRFAKQYiNA 1260
Cdd:COG4717 320 ELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAEA--GVEDEEELRAALEQA-EE 396
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1261 IKDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISET---LRRMEEEERLAE--Q 1335
Cdd:COG4717 397 YQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELeaeLEQLEEDGELAEllQ 476
|
410 420 430
....*....|....*....|....*....|....*...
gi 2124423190 1336 QRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQ 1373
Cdd:COG4717 477 ELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2711-2744 |
2.73e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.23 E-value: 2.73e-03
10 20 30
....*....|....*....|....*....|....
gi 2124423190 2711 LLEAQAASGFLLDPVQNRRLTVNEAVKEGVVGPE 2744
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2090-2447 |
3.27e-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: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2090 RRQVEEAERLKQSAEEQAQAQAQaqaaaeklrkeaeqeaarraqaeqaalRQKQAADAEMEKHKKFAeQTLRQKAQVEQE 2169
Cdd:pfam07888 79 ESRVAELKEELRQSREKHEELEE---------------------------KYKELSASSEELSEEKD-ALLAQRAAHEAR 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2170 LTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRAL--ILRDKDNTQRV 2247
Cdd:pfam07888 131 IRELEEDIKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKEFQELrnSLAQRDTQVLQ 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2248 LQEEAEKMKHVAEEAARlSVAAQEAAR--LRELAEEDLAQQRALAekMLKEKMQAVQeATRLKAEAELLQQQKELAQ--- 2322
Cdd:pfam07888 211 LQDTITTLTQKLTTAHR-KEAENEALLeeLRSLQERLNASERKVE--GLGEELSSMA-AQRDRTQAELHQARLQAAQltl 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2323 ---EQARRLQEDKEQMAqqleQETQGFQRTLEAERQRQLEMSAEAERLKLRVaemsraqarAEEDAQRfrkqaeeigEKL 2399
Cdd:pfam07888 287 qlaDASLALREGRARWA----QERETLQQSAEADKDRIEKLSAELQRLEERL---------QEERMER---------EKL 344
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2124423190 2400 hRTELATQEKVTLVQTLEIQRQQSDhdaerLRQAIAELEREKEKLKQE 2447
Cdd:pfam07888 345 -EVELGREKDCNRVQLSESRRELQE-----LKASLRVAQKEKEQLQAE 386
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1189-1401 |
3.32e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1189 RQLRYYRESADPLGAWLQDAKRRQEQiqamVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINA---IKDYE 1265
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRK----ELEEAEAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAraeLAEAE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1266 LQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSEL-TTLTSQYIKF------ISETLRRMEEEERLAEQQRA 1338
Cdd:COG3206 240 ARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsARYTPNHPDVialraqIAALRAQLQQEAQRILASLE 319
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1339 EERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEE-------VARREEAAVDAQQQKRSIQ 1401
Cdd:COG3206 320 AELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelyeslLQRLEEARLAEALTVGNVR 389
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1614-2097 |
3.32e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.58 E-value: 3.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1614 ERWQLKANEALRLRLQAEEVAQQKSLAQ--AEAEKQKEEAER---------------EARRRGKAEEQAVRQRELAEQEL 1676
Cdd:pfam05557 28 ARIELEKKASALKRQLDRESDRNQELQKriRLLEKREAEAEEalreqaelnrlkkkyLEALNKKLNEKESQLADAREVIS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1677 EKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLE----------EELARLQHEAAAATQKRQELEAELAKVRAEM 1746
Cdd:pfam05557 108 CLKNELSE-LRRQIQRAELELQSTNSELEELQERLDLLKakaseaeqlrQNLEKQQSSLAEAEQRIKELEFEIQSQEQDS 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1747 EVLLASKarAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLAEKLA- 1822
Cdd:pfam05557 187 EIVKNSK--SELARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLKRkleREEKYREEAATLELEKEKLEQELQSw 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1823 -AIGEATRLKTEAEIALKEK--EAENERLRRLAEDEAFQRRRLEEQAAQhkADIEERLAQLRKASESE---LERQKGLVE 1896
Cdd:pfam05557 265 vKLAQDTGLNLRSPEDLSRRieQLQQREIVLKEENSSLTSSARQLEKAR--RELEQELAQYLKKIEDLnkkLKRHKALVR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1897 DTLRQRRQVEEEILALKV---SFEKAAAGKAELELELGRIRSNAEdtLRSKEQAELEAMR-QRQLAAEEEQRRREAEERV 1972
Cdd:pfam05557 343 RLQRRVLLLTKERDGYRAileSYDKELTMSNYSPQLLERIEEAED--MTQKMQAHNEEMEaQLSVAEEELGGYKQQAQTL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1973 QKSLAA--EEEAARQRKAALEEVERLKAKVEEAR----RLRERAEQESAR--QLQLAQDAAQKR---LQAEEKAHAFAVQ 2041
Cdd:pfam05557 421 ERELQAlrQQESLADPSYSKEEVDSLRRKLETLElerqRLREQKNELEMEleRRCLQGDYDPKKtkvLHLSMNPAAEAYQ 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 2042 QKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAE 2097
Cdd:pfam05557 501 QRKNQLEKLQAEIERLKRLLKKLEDDLEQVLRLPETTSTMNFKEVLDLRKELESAE 556
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2156-2334 |
3.35e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 43.85 E-value: 3.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2156 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR--SQVEEELFSLRVQMEELgklKARIEAEN 2233
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQSPviQQLRAQLAELEAELAEL---SARYTPNH 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2234 RALilrdkdntQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2313
Cdd:COG3206 291 PDV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV 362
|
170 180
....*....|....*....|.
gi 2124423190 2314 LQQQKELAQEQARRLQEDKEQ 2334
Cdd:COG3206 363 ARELYESLLQRLEEARLAEAL 383
|
|
| RIB43A |
pfam05914 |
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar ... |
1324-1480 |
3.64e-03 |
|
RIB43A; This family consists of several RIB43A-like eukaryotic proteins. Ciliary and flagellar microtubules contain a specialized set of protofilaments, termed ribbons, that are composed of tubulin and several associated proteins. RIB43A was first characterized in the unicellular biflagellate, Chlamydomonas reinhardtii although highly related sequences are present in several higher eukaryotes including humans. The function of this protein is unknown although the structure of RIB43A and its association with the specialized protofilament ribbons and with basal bodies is relevant to the proposed role of ribbons in forming and stabilising doublet and triplet microtubules and in organizing their three-dimensional structure. Human RIB43A homologs could represent a structural requirement in centriole replication in dividing cells.
Pssm-ID: 461780 [Multi-domain] Cd Length: 372 Bit Score: 42.96 E-value: 3.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1324 RRMEEEERLAEQQRAE---ERERLAAVEAALEKQRQLAEAHAQA---KAQA-EQEAQELQRRMQEEVARREE-------- 1388
Cdd:pfam05914 165 KQAEEEEKHAELLYDQkrlERDRRALELAKLEEECRRAVNAATKnfnQALAaEQAERRRLEKRQEQEDNLAEiynhltsd 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1389 -------AAVDAQQQKRSIQEELQHLRQSSEAEIQaKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALR 1461
Cdd:pfam05914 245 lltenpeVAQSSLGPHRVIPDRWKGMSPEQLKEIR-KEQEQQREEKERRREEEKQRDAEWDRQRLELARAALLLEREQQR 323
|
170 180
....*....|....*....|...
gi 2124423190 1462 ARAEEAEAQ----KRQAQEEAER 1480
Cdd:pfam05914 324 LRRELRRQLdeenLQLAQEQKAR 346
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2154-2321 |
3.68e-03 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 42.92 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2154 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKSILDEElqrlkAEVTEAARQRSQVEEELFSLRVQMEELgklkARIEAEN 2233
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAAL----RSYLSPN 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2234 RALIlrdkdntqRVLQEEAEKMKH-VAEEAARLSVAAQEAARLRELAE-EDLAQQRALAEKMLKEKMQAVQEAtrlKAEA 2311
Cdd:COG3524 248 SPQV--------RQLRRRIAALEKqIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAALEQA---RIEA 316
|
170
....*....|
gi 2124423190 2312 EllQQQKELA 2321
Cdd:COG3524 317 A--RQQRYLA 324
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1102-1545 |
3.79e-03 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 43.36 E-value: 3.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1102 ATLPELEATKAALKKLRAQAEAQQPMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQLLERWQAVLAQTDLRQ 1181
Cdd:COG5278 83 EARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLA 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1182 RELEQLGRQLRYYRESADPLGAWLQDAKRRQEQIQAMVLADSRAVREQLRQEKALLEEIERHGEKVEECQRFAKQYINAI 1261
Cdd:COG5278 163 LALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALAL 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1262 KDYELQLVTYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEER 1341
Cdd:COG5278 243 ALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAA 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1342 ERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQ 1421
Cdd:COG5278 323 AALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAA 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1422 VEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAV 1501
Cdd:COG5278 403 AAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAA 482
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2124423190 1502 RVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQV 1545
Cdd:COG5278 483 ALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAALA 526
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1321-1434 |
3.80e-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: 41.18 E-value: 3.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLRRMEEEERLAEQQRA-EERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQEL-QRRMQEEVARREEAAVDAQQQKR 1398
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110
....*....|....*....|....*....|....*.
gi 2124423190 1399 SIQEELQHLRQSSEAeiqAKARQVEAAERSRLRIEE 1434
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAERQRQEREK 123
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1671-1956 |
3.84e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 43.14 E-value: 3.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1671 LAEQELEKQRQLAegTAQQRLAAEQELIRlraeteQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLL 1750
Cdd:PRK11637 38 FSAHASDNRDQLK--SIQQDIAAKEKSVR------QQQQQRASLLAQLKKQEEAISQASRKLRETQNTLNQLNKQIDELN 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1751 ASKARAEeesrsTSEKSKQRLEAE--ASRFRELAEEAARLRALAEEAKRqrqlaeedaarqraeAERVLAeKLAAIGEAt 1828
Cdd:PRK11637 110 ASIAKLE-----QQQAAQERLLAAqlDAAFRQGEHTGLQLILSGEESQR---------------GERILA-YFGYLNQA- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1829 RLKTEAEialkekeaenerLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVedtlrqrrqveee 1908
Cdd:PRK11637 168 RQETIAE------------LKQTREELAAQKAELEEKQSQQKTLLYEQQAQQQKLEQARNERKKTLT------------- 222
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 1909 ilALKVSFEKAAAGKAELELELGRIRSN-AEDTLRSKEQAELEA-----MRQRQ 1956
Cdd:PRK11637 223 --GLESSLQKDQQQLSELRANESRLRDSiARAEREAKARAEREAreaarVRDKQ 274
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2302-2449 |
4.03e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.87 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2302 QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAErlklrvaeMSRAQARA 2381
Cdd:PRK09510 78 EEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKA--------AAAAKAKA 149
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2124423190 2382 EEDAQRFR---KQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSdhdAERLRQAIAELErEKEKLKQEAK 2449
Cdd:PRK09510 150 EAEAKRAAaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAK---AAAEAKKKAEAE-AKKKAAAEAK 216
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1660-1815 |
4.06e-03 |
|
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal domain of ATPase family AAA domain-containing protein 3 (ATAD3) which is involved in dimerization and interacts with the inner surface of the outer mitochondrial membrane. This domain is found associated with the AAA ATPase domain (pfam00004). ATAD3 is essential for mitochondrial network organization, mitochondrial metabolism and cell growth at organizm and cellular level. It may also play an important role in mitochondrial protein synthesis.
Pssm-ID: 463442 [Multi-domain] Cd Length: 264 Bit Score: 42.28 E-value: 4.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQelEAEL 1739
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRR--NEEL 128
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1740 AKvRAEMEVLLASKARAEEESRSTSEKskqrlEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER 1815
Cdd:pfam12037 129 LR-KQEESVAKQEAMRIQAQRRQTEEH-----EAELRRETERAKAEAEAEARAKEERENEDLNLEQ-LREKANEER 197
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1324-1731 |
4.14e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.10 E-value: 4.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1324 RRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAK-AQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1402
Cdd:COG3064 24 EKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEqRAAELAAEAAKKLAEAEKAAAEAEKKAAAEKAKAAKE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1403 ELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR 1482
Cdd:COG3064 104 AEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAARAAAAAAAAAAAAAARAAAGAAAALV 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1483 RQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQS 1562
Cdd:COG3064 184 AAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADLAAVGVLGAA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1563 KRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQA 1642
Cdd:COG3064 264 LAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSL 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1643 EAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQ 1722
Cdd:COG3064 344 LAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEAASAVELRVL 423
|
....*....
gi 2124423190 1723 HEAAAATQK 1731
Cdd:COG3064 424 LALAGAAGA 432
|
|
| ATP-synt_Fo_b |
cd06503 |
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ... |
1333-1405 |
4.17e-03 |
|
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.
Pssm-ID: 349951 [Multi-domain] Cd Length: 132 Bit Score: 40.50 E-value: 4.17e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1333 AEQQRAEERERLAAVEAALEKQRQLAEA-HAQAKAQAEQEAQELQRRMQEEVAR-REEAAVDAQQQKRSIQEELQ 1405
Cdd:cd06503 42 AEKAKEEAEELLAEYEEKLAEARAEAQEiIEEARKEAEKIKEEILAEAKEEAERiLEQAKAEIEQEKEKALAELR 116
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3002-3039 |
4.18e-03 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 37.69 E-value: 4.18e-03
10 20 30
....*....|....*....|....*....|....*...
gi 2124423190 3002 LRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVAVAL 3039
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1351-1497 |
4.25e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 42.00 E-value: 4.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1351 LEKQRQLAEAHAQ-AKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEA----- 1424
Cdd:pfam13904 47 LKLERQPLEAYENwLAAKQRQRQKELQAQKEEREKEEQEAELRKRLAKEKYQEWLQRKARQQTKKREESHKQKAAesask 126
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1425 --AERSRLRIEEEIRVVRLQLETTERQRggaegelqalraraeeaeaQKRQAQEEAERLRRQVQDETQRKRQAEA 1497
Cdd:pfam13904 127 slAKPERKVSQEEAKEVLQEWERKKLEQ-------------------QQRKREEEQREQLKKEEEEQERKQLAEK 182
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1006-1575 |
4.43e-03 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 43.19 E-value: 4.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1006 AEQQKAQAEVEGLGKGVARLSAEAEKVLALPEPspAAPTLRSELELTLGKLeqvrslsaiyLEKLKTISLVIRSTHGAEE 1085
Cdd:pfam05557 2 AELIESKARLSQLQNEKKQMELEHKRARIELEK--KASALKRQLDRESDRN----------QELQKRIRLLEKREAEAEE 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1086 VLKAHEEQLKEAQAVPATLPELEATKAALkklraQAEAQQpMFDALRDELRGAQEVGERLQQRHGERDVEVERWRERVAQ 1165
Cdd:pfam05557 70 ALREQAELNRLKKKYLEALNKKLNEKESQ-----LADARE-VISCLKNELSELRRQIQRAELELQSTNSELEELQERLDL 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1166 LLERWQavlaqtdlrqrELEQLGRQLRYYRESADPLGAWLQDAKRR-QEQIQ-AMVLADSRAVREQLRQEKALLEEIERH 1243
Cdd:pfam05557 144 LKAKAS-----------EAEQLRQNLEKQQSSLAEAEQRIKELEFEiQSQEQdSEIVKNSKSELARIPELEKELERLREH 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1244 GEKVEECQRFAKQYINAIKDYELQLVTY-KAQLEPVASPAKKPKVQS---GSESVIQEY-VDLRTRyselTTLTSQYIKF 1318
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLEREeKYREEAATLELEKEKLEQelqSWVKLAQDTgLNLRSP----EDLSRRIEQL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1319 ISETLRRMEEEERLAEQQRAEERErlaaveaalekQRQLAEAHAQAKAQAEQEAQELQRrmQEEVARReeaavdAQQQKR 1398
Cdd:pfam05557 289 QQREIVLKEENSSLTSSARQLEKA-----------RRELEQELAQYLKKIEDLNKKLKR--HKALVRR------LQRRVL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1399 SIQEELQHLRQ---------SSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGG-------AEGELQALRA 1462
Cdd:pfam05557 350 LLTKERDGYRAilesydkelTMSNYSPQLLERIEEAEDMTQKMQAHNEEMEAQLSVAEEELGGykqqaqtLERELQALRQ 429
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1463 RAEEAEAQkrQAQEEAERLRRQVQD---ETQRKRQAEAELAVRV-----KAEAEAAREKQRALQ---ALEEFRLQAEEAE 1531
Cdd:pfam05557 430 QESLADPS--YSKEEVDSLRRKLETlelERQRLREQKNELEMELerrclQGDYDPKKTKVLHLSmnpAAEAYQQRKNQLE 507
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 2124423190 1532 RrlRQAEAERAR----QVQVALETAQRSAEVELQSKRASFAEKTAQLE 1575
Cdd:pfam05557 508 K--LQAEIERLKrllkKLEDDLEQVLRLPETTSTMNFKEVLDLRKELE 553
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
1334-1450 |
4.44e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 42.66 E-value: 4.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1334 EQQRAEERERLAAVEAALEKQRQLAEAhaQAKAQAEQEAQELQRRMQEEVARREEAavdaqqQKRSIQEELQHLRQSSEA 1413
Cdd:pfam02841 183 QSKEAVEEAILQTDQALTAKEKAIEAE--RAKAEAAEAEQELLREKQKEEEQMMEA------QERSYQEHVKQLIEKMEA 254
|
90 100 110
....*....|....*....|....*....|....*..
gi 2124423190 1414 EIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQR 1450
Cdd:pfam02841 255 EREQLLAEQERMLEHKLQEQEELLKEGFKTEAESLQK 291
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2308-2449 |
4.49e-03 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 42.91 E-value: 4.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2308 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQgfQRTLEAERQRQLEMSAEAErlklrvAEMSRAQARAEEDAQR 2387
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEK--QRAAEQARQKELEQRAAAE------KAAKQAEQAAKQAEEK 117
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 2388 fRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQEAK 2449
Cdd:TIGR02794 118 -QKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1408-1543 |
4.50e-03 |
|
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.
Pssm-ID: 425733 [Multi-domain] Cd Length: 322 Bit Score: 42.80 E-value: 4.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1408 RQSSEAEIQAKARQVEA-AERSRLRIE-EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLR--- 1482
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLARRRvla 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1483 -------RQVQDETQRKRQAEAELAVRVKAEAEAAREK-QRALQALEEFRLQAEEAERRLRQAEAERAR 1543
Cdd:pfam00529 134 piggisrESLVTAGALVAQAQANLLATVAQLDQIYVQItQSAAENQAEVRSELSGAQLQIAEAEAELKL 202
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1300-1572 |
4.61e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 4.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1300 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAE---QEAQELQ 1376
Cdd:COG4372 17 GLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNeqlQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1377 RRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSS----------EAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETT 1446
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRkqleaqiaelQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1447 ERQRggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQ 1526
Cdd:COG4372 177 SEAE--AEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEE 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2124423190 1527 AEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1572
Cdd:COG4372 255 VILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLAL 300
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1660-1912 |
4.66e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1660 KAEEQAVRQRELAEQ--ELEKQRQLA-EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELE 1736
Cdd:pfam13868 67 RKEERKRYRQELEEQieEREQKRQEEyEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1737 AE--------LAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEE--AARLRALAEEAKRQRQLAEEDA 1806
Cdd:pfam13868 147 KEeereederILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQEEQERKERQKEREE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1807 ARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAEN--ERLRRLAEDEAFQRRRLEEQAAQHKAD----IEERLAQL 1880
Cdd:pfam13868 227 AEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERmlRKQAEDEEIEQEEAEKRRMKRLEHRRElekqIEEREEQR 306
|
250 260 270
....*....|....*....|....*....|..
gi 2124423190 1881 RKASESELERQKGLVEDTLRQRRQVEEEILAL 1912
Cdd:pfam13868 307 AAEREEELEEGERLREEEAERRERIEEERQKK 338
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1696-2043 |
4.73e-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: 4.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1696 ELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAElaKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA 1775
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWE--RQRRELESRVAELKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1776 SRFRELAEEAARLRAlAEEAKRQRQLAEEDAArqRAEAERVLaeklaaigeatrlkteaeialkEKEAENERLRRLAEDE 1855
Cdd:pfam07888 108 ASSEELSEEKDALLA-QRAAHEARIRELEEDI--KTLTQRVL----------------------ERETELERMKERAKKA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1856 AFQRRRLEEQAAQHKADIEERLAQLRKASeSELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGRIRS 1935
Cdd:pfam07888 163 GAQRKEEEAERKQLQAKLQQTEEELRSLS-KEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEALLEELRS 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1936 NAE-------------------DTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALE----- 1991
Cdd:pfam07888 242 LQErlnaserkveglgeelssmAAQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADkdrie 321
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1992 ----EVERLKAKVEEARRLRERAEQESARQ--LQLAQDAAQKRLQAEEKAhAFAVQQK 2043
Cdd:pfam07888 322 klsaELQRLEERLQEERMEREKLEVELGREkdCNRVQLSESRRELQELKA-SLRVAQK 378
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1319-1420 |
4.91e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.28 E-value: 4.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1319 ISETLRR----MEEEE-RL---AEQQRAEER----ERLAAVEAAlEKQRQLAEAHAQAKAqAEQEAQELQRRMQEE--VA 1384
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLliaEQHQKVVEKeaetERKRAVIEA-EKDAEVAKIQMQQKI-MEKEAEKKISEIEDEmhLA 237
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2124423190 1385 rREEAAVDAQQQKRSIQEELQHLRQSSE----AEIQAKAR 1420
Cdd:cd03406 238 -REKARADAEYYRALREAEANKLKLTPEylelKKYQAIAN 276
|
|
| HPtr |
COG2198 |
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms]; |
1661-2440 |
4.96e-03 |
|
HPt (histidine-containing phosphotransfer) domain [Signal transduction mechanisms];
Pssm-ID: 441800 [Multi-domain] Cd Length: 871 Bit Score: 43.11 E-value: 4.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1661 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1740
Cdd:COG2198 11 LLLLLLLLLLLLLALLALLLLLLLAALALLLLLLLLLALLALLLLLVALALLLALLLLLLGVLLLLLDLLELLLLLLLLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1741 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEK 1820
Cdd:COG2198 91 LLLLLLLLLLLLALLLLLLLLLALLLLLLLLLLLLLLLLLLLALLLLLLLLLALLLLLLLLLVLAALLLLLLLALLLALL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1821 LAAIGEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLR 1900
Cdd:COG2198 171 LLVLLVLLLLLLLLLLLLLLLLLLLLLLLLALTLAALLELLAAELALEALLAELAAEAAAALAAELALAELAALLLLLLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1901 QRRQVEEEILALKVSFEKAAAGKAELELELGRIRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEE 1980
Cdd:COG2198 251 LLLLLILLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLELLLLLLLALLLLLLLLLLLLLLLLLLLLLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1981 EAARQRKAALEEVERLKAKVEEARRLRERAEQESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLER 2060
Cdd:COG2198 331 LLLLLLLLLLLLLLLLLLLALLLLALLLALLLAAAAALAAALEALLTELALILLLLLLLLLLLILLGLLLLLLLSLLLSL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2061 LRGEAEAARRAAEEAEEARERAEREAAQSRRQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALR 2140
Cdd:COG2198 411 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLGLLLLLLLLLGLLLLLLLGLLLLALLLLLLLLLLLLLLLLLLLLLLLLLL 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2141 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQME 2220
Cdd:COG2198 491 LLLLLLLLLLLLLLLLVAAALAALALLLLLALLLLLLLDLLILGLLLILLLLLLGLLALGLAALLLLLALLLGLGLLLGL 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2221 ELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKMQA 2300
Cdd:COG2198 571 LLGGLLLLLLLLLLLLLLLLLLLLLLLLLLALLLALLAAAAALLLLLLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLL 650
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2301 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEMSAEAERLKLRVAEMSRAQAR 2380
Cdd:COG2198 651 LLAVLLAAAAAAAALAALDLLLDLDDMMMMLDDMMAEAARARALAARAAAIAAAAAAAAAAAAAAAAAAAALLAALLLLL 730
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 2381 AEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQR----------------QQSDHDAERLRQAIAELERE 2440
Cdd:COG2198 731 LLLLLLLLLLLLLLLAAAAAAAASPAAPALPVLDLEALRRlggdpellrellelflEELPELLAELRQALAAGDLE 806
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1677-1950 |
4.97e-03 |
|
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular sites as centrioles, basal bodies, and along ciliary and flagellar doublet microtubules. Tektins form unique protofilaments, organized as longitudinal polymers of tektin heterodimers with axial periodicity matching tubulin. Tektin polypeptides consist of several alpha-helical regions that are predicted to form coiled coils. Indeed, tektins share considerable structural similarities with intermediate filament proteins. Possible functional roles for tektins are: stabilization of tubulin protofilaments; attachment of A and B-tubules in ciliary/flagellar microtubule doublets and C-tubules in centrioles; binding of axonemal components.
Pssm-ID: 460827 [Multi-domain] Cd Length: 383 Bit Score: 42.54 E-value: 4.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1677 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQL-----LEEELARLqheaaaaTQKRQELEAELAKVRAEMEV 1748
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQYdsnrrLGERIQDI-------TFWKSELEKELEELDEEIEL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1749 LLASKARAEEESRSTSEK---SKQRLEAEASRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAAR 1808
Cdd:pfam03148 76 LLEEKRRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAAR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1809 QRAEAErvLAEKLAAIG---EATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLE--EQAAQHKADIEERLAQLR 1881
Cdd:pfam03148 154 HKLEKD--LSDKKEALEideKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIEraEKERAASAQLRELIDSIL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2124423190 1882 KASESELERQKGLVEDTLRQRrqVEEeilalkvsFEKAaagKAELELELGRIRSNAEDTlrSKEQAELE 1950
Cdd:pfam03148 232 EQTANDLRAQADAVNFALRKR--IEE--------TEDA---KNKLEWQLKKTLQEIAEL--EKNIEALE 285
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1321-1427 |
5.23e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 5.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1321 ETLRRMEEEERLAEQQRAEERErlAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARRE---EAAVDAQQQK 1397
Cdd:PRK09510 122 EAAKQAALKQKQAEEAAAKAAA--AAKAKAEAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKaeaEAAAKAAAEA 199
|
90 100 110
....*....|....*....|....*....|
gi 2124423190 1398 RSIQEELQHLRQSSEAEIQAKARQVEAAER 1427
Cdd:PRK09510 200 KKKAEAEAKKKAAAEAKKKAAAEAKAAAAK 229
|
|
| COG4191 |
COG4191 |
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal ... |
1683-1826 |
5.34e-03 |
|
Signal transduction histidine kinase regulating C4-dicarboxylate transport system [Signal transduction mechanisms];
Pssm-ID: 443345 [Multi-domain] Cd Length: 361 Bit Score: 42.48 E-value: 5.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1683 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRS 1762
Cdd:COG4191 1 ALRLLLLLLLLLALLRALALALALLLLLLLLLLALLLLLLALLLALLALLLLLLLLLLLLLLELLLLLLALLGGLLRLLL 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 1763 TSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGE 1826
Cdd:COG4191 81 LLGLLLLLLLEALLLLLLAALDAEENAELEELERDITELERAEEELRELQEQLVQSEKLAALGE 144
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1773-2283 |
5.42e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 43.31 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1773 AEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGEATRLKTEAEIALKEKEAENERLRRLa 1852
Cdd:COG3899 752 AEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAERLGDRRLEA- 830
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1853 edeafQRRRLEEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALKVSFEKAAAGKAELELELGR 1932
Cdd:COG3899 831 -----RALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAAALA 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1933 IRSNAEDTLRSKEQAELEAMRQRQLAAEEEQRRREAEERVQKSLAAEEEAARQRKAALEEVERLKAKVEEARRLRERAEQ 2012
Cdd:COG3899 906 AAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAAAAA 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2013 ESARQLQLAQDAAQKRLQAEEKAHAFAVQQKEQELQQTLQQEQSMLERLRGEAEAARRAAEEAEEARERAEREAAQSRRQ 2092
Cdd:COG3899 986 AAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAALAAA 1065
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2093 VEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALRQKQAADAemekhkkfaeqtLRQKAQVEQELTT 2172
Cdd:COG3899 1066 AALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAAL------------AALALAAAARAAA 1133
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2173 LRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQMEELGKLKARIEAENRALILRDKDNTQRVLQEEA 2252
Cdd:COG3899 1134 ALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALA 1213
|
490 500 510
....*....|....*....|....*....|.
gi 2124423190 2253 EKMKHVAEEAARLSVAAQEAARLRELAEEDL 2283
Cdd:COG3899 1214 LLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
1401-1587 |
5.51e-03 |
|
Family with sequence similarity 184, A and B; The function of FAM184 is not known.
Pssm-ID: 464788 [Multi-domain] Cd Length: 211 Bit Score: 41.57 E-value: 5.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1401 QEELQHLRQSSEAEIQakarqveaaersrlRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1480
Cdd:pfam15665 13 EAEIQALKEAHEEEIQ--------------QILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1481 LRRQVQDetqRKRQAEAELAVRVKAEAEAAREKQRALQA-LEEFRLQAEEAERRLRQAEAERARQVQVALETAQRSaeve 1559
Cdd:pfam15665 79 YKRRVEE---RELKAEAEHRQRVVELSREVEEAKRAFEEkLESFEQLQAQFEQEKRKALEELRAKHRQEIQELLTT---- 151
|
170 180
....*....|....*....|....*...
gi 2124423190 1560 LQSKRASFAEKTAQLERTLQEEHVAVAQ 1587
Cdd:pfam15665 152 QRAQSASSLAEQEKLEELHKAELESLRK 179
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1457-1546 |
5.64e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.89 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1457 LQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELavrvKAEAEaarekQRALQALEEFRLQAEEAERRLRQ 1536
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90
....*....|
gi 2124423190 1537 AEAERARQVQ 1546
Cdd:PRK00409 596 LQKGGYASVK 605
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1400-1771 |
5.72e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.58 E-value: 5.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1400 IQEELQHLRQSSEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1479
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1480 RLRRQVQDETQRKRQAEAELAVRVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAERARQvqvalETAQRSAEVE 1559
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAER-----EEELKELEEQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1560 LQSKRASFAEKTAQLERTLQEEHVAVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1639
Cdd:COG4372 159 LESLQEELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1640 AQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1719
Cdd:COG4372 239 LDALELEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALL 318
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2124423190 1720 RLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL 1771
Cdd:COG4372 319 AALLELAKKLELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
2139-2403 |
5.75e-03 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 42.21 E-value: 5.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 LRQKQAADAEMEKHKK-----FAE-QTLRQK-AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2211
Cdd:COG1340 14 EEKIEELREEIEELKEkrdelNEElKELAEKrDELNAQVKELREEAQELREKRDELNEKVKELKEERDELNEKLNELREE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2212 LFSLRVQMEELG-------KLKARIEA-------------ENRALILRDKDntqrvLQEEAEKMKHVAEEAARLSVAAQE 2271
Cdd:COG1340 94 LDELRKELAELNkaggsidKLRKEIERlewrqqtevlspeEEKELVEKIKE-----LEKELEKAKKALEKNEKLKELRAE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2272 AARLRELAEEDLAQQRALAEKM--LKEKMQAV-QEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLeqetqgfqr 2348
Cdd:COG1340 169 LKELRKEAEEIHKKIKELAEEAqeLHEEMIELyKEADELRKEADELHKEIVEAQEKADELHEEIIELQKEL--------- 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 2349 tleaerqRQLEMSAEAERLKLRVAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTE 2403
Cdd:COG1340 240 -------RELRKELKKLRKKQRALKREKEKEELEE-------KAEEIFEKLKKGE 280
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1334-1576 |
5.81e-03 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 42.71 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1334 EQQRAEERERLaaVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEA 1413
Cdd:pfam05667 238 EEYRKRKRTKL--LKRIAEQLRSAALAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAA 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1414 EIQAKARQVEAAERsRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLrrqvQDETQRKR 1493
Cdd:pfam05667 316 TSSPPTKVETEEEL-QQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEEL----EKQYKVKK 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1494 QAEAELA------VRVKAEAEAAREKQRALQAL-EEFRLQAEEAERRLRQAEAERARQVQVALETAQ------RSAEVEL 1560
Cdd:pfam05667 391 KTLDLLPdaeeniAKLQALVDASAQRLVELAGQwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEIKelrekiKEVAEEA 470
|
250
....*....|....*.
gi 2124423190 1561 QSKRASFAEKTAQLER 1576
Cdd:pfam05667 471 KQKEELYKQLVAEYER 486
|
|
| rne |
PRK10811 |
ribonuclease E; Reviewed |
1298-1588 |
5.92e-03 |
|
ribonuclease E; Reviewed
Pssm-ID: 236766 [Multi-domain] Cd Length: 1068 Bit Score: 43.10 E-value: 5.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1298 YVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEErERLAAV-------EAALEKQRQLAEAHAQAKAQAEQ 1370
Cdd:PRK10811 484 YSVLRVRKGEETPTLSYMLPKLHEEAMALPSEEEFAERKRPEQ-PALATFampdvppAPTPAEPAAPVVAAAPKAAAATP 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1371 EAQ-----------------ELQRRMQEEVARREEAAVDAQQQKRsiqeelqhlrqsseaeiqaKARQVEAAERSRLRIE 1433
Cdd:PRK10811 563 PAQpgllsrffgalkalfsgGEETKPQEQPAPKAEAKPERQQDRR-------------------KPRQNNRRDRNERRDT 623
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1434 EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAvrvKAEAEAarek 1513
Cdd:PRK10811 624 RDNRTRREGRENREENRRNRRQAQQQTAETRESQQAEVTEKARTQDEQQQAPRRERQRRRNDEKRQA---QQEAKA---- 696
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 1514 qralQALEEFRLQAEEAERRLRQAEAERA-RQV--QVALETAQrSAEVELQSKRASFAEKTAQLERTLQEEHVAVAQL 1588
Cdd:PRK10811 697 ----LNVEEQSVQETEQEERVQQVQPRRKqRQLnqKVRIEQSV-AEEAVAPVVEETVAAEPVVQEVPAPRTELVKVPL 769
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1663-1828 |
6.45e-03 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 42.51 E-value: 6.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1663 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELAKV 1742
Cdd:COG3883 115 SDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAAA 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1743 RAEMEVLLASKARAEEESRSTSEKSKQRLEAEASRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLA 1822
Cdd:COG3883 195 EAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGA 274
|
....*.
gi 2124423190 1823 AIGEAT 1828
Cdd:COG3883 275 GAAAAS 280
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1708-1901 |
6.49e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.45 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1708 EQQRQLLEeeLARLQHEAAAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTsEKSKQRLEAEAsrfRELAEEAAR 1787
Cdd:COG1579 4 EDLRALLD--LQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDL-EKEIKRLELEI---EEVEARIKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1788 LRALAEEAKRQRQLA-----EEDAARQRAEAERVLAEklaaigeatrlkteaeiALKEKEAENERLRRLAEDEAFQRRRL 1862
Cdd:COG1579 78 YEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILE-----------------LMERIEELEEELAELEAELAELEAEL 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 2124423190 1863 EEQAAQHKADIEERLAQLRKASESELERQKGLVEDTLRQ 1901
Cdd:COG1579 141 EEKKAELDEELAELEAELEELEAEREELAAKIPPELLAL 179
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2273-2448 |
6.51e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 6.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2273 ARLRELAEEDLAQQRALAEkmLKEKmqAVQEATRLkaeAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEA 2352
Cdd:pfam05262 184 EALREDNEKGVNFRRDMTD--LKER--ESQEDAKR---AQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2353 ERQRQLEMSAEAERLKLRVA-----EMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDhDA 2427
Cdd:pfam05262 257 AKNLPKPADTSSPKEDKQVAenqkrEIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP-VA 334
|
170 180
....*....|....*....|.
gi 2124423190 2428 ERLRQAIAELEREKEKLKQEA 2448
Cdd:pfam05262 335 EDLQKTKPQVEAQPTSLNEDA 355
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
27-122 |
6.55e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 39.59 E-value: 6.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 27 KWVNKHLikhWRAEAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN- 101
Cdd:cd21218 17 RWVNYHL---KKAGPTKkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYf 91
|
90 100
....*....|....*....|.
gi 2124423190 102 IRNDDIADGNPKLTLGLIWTI 122
Cdd:cd21218 92 LTPEDIVSGNPRLNLAFVATL 112
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1219-1528 |
6.64e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 42.73 E-value: 6.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1219 VLADSRAVREQLRQEkalLEEIE-----RHGEKVEECQ-------------RFAKQYINAIKDYELQLVTYKAQLEPVAS 1280
Cdd:PRK10929 17 AYAATAPDEKQITQE---LEQAKaaktpAQAEIVEALQsalnwleerkgslERAKQYQQVIDNFPKLSAELRQQLNNERD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1281 PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfisETLRRMEEEERLAE--QQRAEERERLAAVEAALEKQRQLA 1358
Cdd:PRK10929 94 EPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ------EQDRAREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1359 EAHAQAKAQAeqeaqelqrrMQEEVARReEAAVDaqqqkrsiQEELQHLRQSSEAEIqakAR-QVEAAERSRLRIEEEIR 1437
Cdd:PRK10929 168 TPLAQAQLTA----------LQAESAAL-KALVD--------ELELAQLSANNRQEL---ARlRSELAKKRSQQLDAYLQ 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1438 VVRLQLeTTERQRggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAEL---AVRVKAEA----EAA 1510
Cdd:PRK10929 226 ALRNQL-NSQRQR------------EAERALESTELLAEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAA 292
|
330
....*....|....*...
gi 2124423190 1511 REKQRALQALEEFRLQAE 1528
Cdd:PRK10929 293 SQTLQVRQALNTLREQSQ 310
|
|
| ERM_helical |
pfam20492 |
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ... |
1668-1761 |
6.68e-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: 6.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1668 QRELAEQELEKQRQLAEGTAQQRLAAEQELIRLraeteqgEQQRQLLEEELARLQHEAAAATQKRQELEAELAKVRAEME 1747
Cdd:pfam20492 21 ETKKAQEELEESEETAEELEEERRQAEEEAERL-------EQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIA 93
|
90
....*....|....
gi 2124423190 1748 VLLASKARAEEESR 1761
Cdd:pfam20492 94 RLEEEVERKEEEAR 107
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2140-2447 |
6.78e-03 |
|
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.
Pssm-ID: 464932 [Multi-domain] Cd Length: 329 Bit Score: 42.11 E-value: 6.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2140 RQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQM 2219
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2220 EELGKLKARIEAENRAlilrdkDNTQRvlqeeaekmkhvaeeaaRLSVAAQEAARLRELAEEDLAQQRALAEKMLKeKMQ 2299
Cdd:pfam15905 132 LELTRVNELLKAKFSE------DGTQK-----------------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2300 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRqLEMSAEAERLKLRVAEMSRAQA 2379
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSETEKLLEYITELSCVSEQVEKYK-LDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2124423190 2380 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLRQAIAELEREKEKLKQE 2447
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2139-2360 |
6.89e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.21 E-value: 6.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ-VEEELFSLRV 2217
Cdd:pfam13868 119 EEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIArLRAQQEKAQD 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2218 QMEELGKLKARIEAENRALILRDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEK 2297
Cdd:pfam13868 199 EKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQ 278
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 2298 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLEQETQGFQRTLEAERQRQLEM 2360
Cdd:pfam13868 279 EEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2251-2386 |
6.96e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 42.70 E-value: 6.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2251 EAEKMK-HVAEEAAR---LSVAAQEAARlrELAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQKELAQEQAR 2326
Cdd:PTZ00491 684 ERQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAEAELEKLRKR 760
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 2327 RLQEdkeqmaqqLEQETQgfQRTLEAERQRQLeMSAEAERLKLRVAEMSR----AQARAEEDAQ 2386
Cdd:PTZ00491 761 QELE--------LEYEQA--QNELEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
1659-1819 |
7.42e-03 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 41.20 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1659 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA----EQELIR-LRAETEQGEQQRQLLEEELARLQHEAAAATQKRQ 1733
Cdd:pfam04012 42 RQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAltkgNEELAReALAEKKSLEKQAEALETQLAQQRSAVEQLRKQLA 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1734 ELEAELAKVRAEMEVLLA--SKARAEEESRSTSEKSK-QRLEAEASRFRE-LAEEAARLRALAEEAKRQRQLAE-EDAAR 1808
Cdd:pfam04012 122 ALETKIQQLKAKKNLLKArlKAAKAQEAVQTSLGSLStSSATDSFERIEEkIEEREARADAAAELASAVDLDAKlEQAGI 201
|
170
....*....|.
gi 2124423190 1809 QRAEAERVLAE 1819
Cdd:pfam04012 202 QMEVSEDVLAR 212
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2220-2337 |
7.57e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 41.88 E-value: 7.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2220 EELGKLKARIEAENRALILRDKDNTQrvLQEEaekmkhVAEEAARLSVAAQEAARLRELAEEdLAQQRALAEKMLKEKMQ 2299
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQDS------VANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2300 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ 2337
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAK 173
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1492-1726 |
7.70e-03 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 42.25 E-value: 7.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1492 KRQAEAELAVRVKAEaeaaREKQRALQAleEFRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEkt 1571
Cdd:pfam15709 327 KREQEKASRDRLRAE----RAEMRRLEV--ERKRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEE-- 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1572 aqlERTLQEEHVAVAQLREEAERraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKSLAqaeaekqkeea 1651
Cdd:pfam15709 399 ---ERQRQEEEERKQRLQLQAAQ-------------------ERARQQQEEFRRKLQELQRKKQQEEAE----------- 445
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2124423190 1652 erearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAA 1726
Cdd:pfam15709 446 --------RAEAEKQRQKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEA 512
|
|
| GBP_C |
pfam02841 |
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral ... |
2253-2347 |
7.72e-03 |
|
Guanylate-binding protein, C-terminal domain; Transcription of the anti-viral guanylate-binding protein (GBP) is induced by interferon-gamma during macrophage induction. This family contains GBP1 and GPB2, both GTPases capable of binding GTP, GDP and GMP.
Pssm-ID: 460721 [Multi-domain] Cd Length: 297 Bit Score: 41.89 E-value: 7.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2253 EKMKHVAEEAARLSVAAQEAARLRELAEEDL----AQQRALAE--KMLKEKMQAVQEatRLKAEAELLQQQKElaQEQAR 2326
Cdd:pfam02841 201 AKEKAIEAERAKAEAAEAEQELLREKQKEEEqmmeAQERSYQEhvKQLIEKMEAERE--QLLAEQERMLEHKL--QEQEE 276
|
90 100
....*....|....*....|.
gi 2124423190 2327 RLQEDKEQMAQQLEQETQGFQ 2347
Cdd:pfam02841 277 LLKEGFKTEAESLQKEIQDLK 297
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2243-2546 |
7.75e-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: 42.25 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2243 NTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRElaeEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQQK--- 2318
Cdd:COG5185 233 EALKGFQDPESELEDLAQTSDKLEKLVEQNTDLRL---EKLGENAESSKRLNENANNLIKQFENTKEKiAEYTKSIDikk 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2319 --ELAQEQARRLQEDKEQMAQQLEQETqGFQRTLEAERQRQLEMSAEAERLKLRVAEM--SRAQARAEEDAQRFRKQAEE 2394
Cdd:COG5185 310 atESLEEQLAAAEAEQELEESKRETET-GIQNLTAEIEQGQESLTENLEAIKEEIENIvgEVELSKSSEELDSFKDTIES 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2395 IGEKLH--RTELATQEKVtLVQTLEIQRQQSDHDAERLRQAIAELEREkekLKQEAKLLQLKSEEMQTVQQEQLLQETQA 2472
Cdd:COG5185 389 TKESLDeiPQNQRGYAQE-ILATLEDTLKAADRQIEELQRQIEQATSS---NEEVSKLLNELISELNKVMREADEESQSR 464
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 2473 LQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREAEE 2546
Cdd:COG5185 465 LEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKATLEKLRAKLERQLEGVRSKLDQVAESLKDFMRARGYAHI 538
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1335-1529 |
7.83e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.27 E-value: 7.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1335 QQRAEERERLAAVEAALEKQRQLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE 1414
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1415 IQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEA-ERLRRQVQDETQRKR 1493
Cdd:PRK07735 156 EEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAkQKASQGNGDSGDEDA 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 2124423190 1494 QAEAELAVRVKAEAeAAREKQRALQALEEFRLQAEE 1529
Cdd:PRK07735 236 KAKAIAAAKAKAAA-AARAKTKGAEGKKEEEPKQEE 270
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
20-126 |
7.97e-03 |
|
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: 39.32 E-value: 7.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 20 VQKKTFTKWVNKHLIKhwraeAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRHR 95
Cdd:cd21306 16 VVKKSLITFVNKHLNK-----LNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQDA 90
|
90 100 110
....*....|....*....|....*....|.
gi 2124423190 96 QVKLVNIRNDDIADGNPKLTLGLIWTIILHF 126
Cdd:cd21306 91 GLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2160-2584 |
8.07e-03 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 42.41 E-value: 8.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2160 LRQKAQVEQELTTLRLQLEETDHQKSILDEELQR----LKAEVTEAARQRSQVEEELFSLRVQMEelgKLKARIEAENRA 2235
Cdd:pfam15921 316 MRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlvlANSELTEARTERDQFSQESGNLDDQLQ---KLLADLHKREKE 392
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2236 LILrDKDNTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELaeedLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQ 2315
Cdd:pfam15921 393 LSL-EKEQNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEAL----LKAMKSECQGQMERQMAAIQGKNESLEKVSSLT 467
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2316 QQKELAQEQARRLQED---KEQMAQQLEQETQGFQRTLEaERQRQLEMS-AEAERLKLRV-AEMSRAQARAEEDAQRFRK 2390
Cdd:pfam15921 468 AQLESTKEMLRKVVEEltaKKMTLESSERTVSDLTASLQ-EKERAIEATnAEITKLRSRVdLKLQELQHLKNEGDHLRNV 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2391 QAEEIGEKLhrtELATQEKVtlvqtLEIQRQQSDHDAERLRQ---AIAELEREKEKLKQEAKLLQLKSEEMQTvqqeqll 2467
Cdd:pfam15921 547 QTECEALKL---QMAEKDKV-----IEILRQQIENMTQLVGQhgrTAGAMQVEKAQLEKEINDRRLELQEFKI------- 611
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2468 qetqaLQQSFLSEKDTLLQRERFIEQEKAKLEQLFQDEVAKAQKLREEQQRQQKQMEEEKQQLVASMEEARQRQREaeeg 2547
Cdd:pfam15921 612 -----LKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLKRN---- 682
|
410 420 430
....*....|....*....|....*....|....*..
gi 2124423190 2548 VRRKQEELQLLEQQRQQQEKLLAEENQRLRERLQRLE 2584
Cdd:pfam15921 683 FRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSME 719
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1370-1509 |
8.09e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.38 E-value: 8.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1370 QEAQELQRRMqEEVARREEAAVDAQQQkrSIQEELQHLRQSsEAEIQAKARQVEAAERSRLRIEEEIRVVRLQLETTERQ 1449
Cdd:COG0542 411 EELDELERRL-EQLEIEKEALKKEQDE--ASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGK 486
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2124423190 1450 RGGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDETQRKRQAEAELAVRVKAEAEA 1509
Cdd:COG0542 487 IPELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1661-1761 |
8.11e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.63 E-value: 8.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1661 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQKRQELEAELA 1740
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 2124423190 1741 KvRAEMEVLLaskarAEEESR 1761
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1510-1564 |
8.34e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.34e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 2124423190 1510 AREKQRALQaleefRLQAEEAERRlRQAEAERARQVQVALETAQRS-AEVELQSKR 1564
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1313-1865 |
8.62e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 42.34 E-value: 8.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1313 SQYIKFISETLRRMEEEERLAEQQRAEERERLAAVEAALEKqrqLAEAHAQAKAQAEQEAQELQRRMQEEVARREEAAVD 1392
Cdd:TIGR00606 583 SKEINQTRDRLAKLNKELASLEQNKNHINNELESKEEQLSS---YEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLA 659
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1393 AQQQ-KRSIQEELQHLRQS----------SEAEIQAKARQVEAAERSrlrIEEEIRVVRLQLETTERQRGGAEGELQALR 1461
Cdd:TIGR00606 660 GATAvYSQFITQLTDENQSccpvcqrvfqTEAELQEFISDLQSKLRL---APDKLKSTESELKKKEKRRDEMLGLAPGRQ 736
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1462 ARAEEAEAQKRQAQEEAERLRRQVQDETQRKRQAEAELAVrVKAEAEAAREKQRALQALEEFRLQAEEAERRLRQAEAEr 1541
Cdd:TIGR00606 737 SIIDLKEKEIPELRNKLQKVNRDIQRLKNDIEEQETLLGT-IMPEEESAKVCLTDVTIMERFQMELKDVERKIAQQAAK- 814
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1542 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHvavaqlreeaerraqqqaeaerareeaERELERWQLKAN 1621
Cdd:TIGR00606 815 LQGSDLDRTVQQVNQEKQEKQHELDTVVSKIELNRKLIQDQ---------------------------QEQIQHLKSKTN 867
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1622 EALRLRLQAEEVAQQKSLAQAEAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLR 1701
Cdd:TIGR00606 868 ELKSEKLQIGTNLQRRQQFEEQLVELSTEVQSLIREIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIK 947
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1702 AETEQGEQQRQLLEEELarlqhEAAAATQKRQElEAELAKVRAEMEVLLASKARAEEESRST-----SEKSKQRLEAEAS 1776
Cdd:TIGR00606 948 EKVKNIHGYMKDIENKI-----QDGKDDYLKQK-ETELNTVNAQLEECEKHQEKINEDMRLMrqdidTQKIQERWLQDNL 1021
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1777 RFRELAEEaarLRALAEEAKRQRQLAEEDAARQRAEAERVLAEKLAAIGeatrlKTEAEIALKEKEAENERLRRLAEDEA 1856
Cdd:TIGR00606 1022 TLRKRENE---LKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDLIK-----RNHVLALGRQKGYEKEIKHFKKELRE 1093
|
....*....
gi 2124423190 1857 FQRRRLEEQ 1865
Cdd:TIGR00606 1094 PQFRDAEEK 1102
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2139-2303 |
8.66e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 8.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2139 LRQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSLRVQ 2218
Cdd:COG1579 9 LLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 2219 mEELGKLKARIEAENRALILRDKDnTQRVLQEEAEKMKHVAEEAARLSVAAQEAARLRELAEEDLAQQRALAEKMLKEKM 2298
Cdd:COG1579 89 -KEYEALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAERE 166
|
....*
gi 2124423190 2299 QAVQE 2303
Cdd:COG1579 167 ELAAK 171
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1766-1914 |
8.84e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 8.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1766 KSKQRLEAEASRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LAEKLAAigEATRLKTE 1833
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1834 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEILALK 1913
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
.
gi 2124423190 1914 V 1914
Cdd:PRK12705 181 I 181
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1661-1909 |
8.88e-03 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 41.95 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1661 AEEQAVRQRELAEQELEKQRQLAEGTAQ---------QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAAAATQK 1731
Cdd:pfam15558 90 IEKESRWREQAEDQENQRQEKLERARQEaeqrkqcqeQRLKEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKV 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1732 RQELEAELAKVRAeMEVLLASKARAEEESRSTS-EKSKQRLEAEASRFRELAEEAARLRALAEEAKRQR-QLAEEDAARQ 1809
Cdd:pfam15558 170 QENNLSELLNHQA-RKVLVDCQAKAEELLRRLSlEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRaKWRAEEKEEE 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1810 RAEAERVLAEKLAAIGEATRLKTEAEIALK---------EKEAENERLRRLAEDEAFQRRRLEEQAAQHKadiEERLAQL 1880
Cdd:pfam15558 249 RQEHKEALAELADRKIQQARQVAHKTVQDKaqrarelnlEREKNHHILKLKVEKEEKCHREGIKEAIKKK---EQRSEQI 325
|
250 260
....*....|....*....|....*....
gi 2124423190 1881 RKASESELERQKGLVEDTLRQRRQVEEEI 1909
Cdd:pfam15558 326 SREKEATLEEARKTARASFHMREKVREET 354
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4263-4293 |
9.55e-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: 9.55e-03
10 20 30
....*....|....*....|....*....|.
gi 2124423190 4263 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4293
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1391-1537 |
9.68e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 9.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2124423190 1391 VDAQQQKRSIQEELQHLRQSSEAEIQAKARQVEAAERsrlrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQ 1470
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2124423190 1471 KRQAQEEAERLRRQVQdetqrkrQAEAElavrvkaeaEAAREKQRALQALEEFRLqaEEAERR------LRQA 1537
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| |
