|
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 ... |
9-113 |
7.48e-76 |
|
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: 247.31 E-value: 7.48e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 9 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNI 88
Cdd:cd21188 1 DAVQKKTFTKWVNKHLIKARRRVVDLFEDLRDGHNLISLLEVLSGESLPRERGRMRFHRLQNVQTALDFLKYRKIKLVNI 80
|
90 100
....*....|....*....|....*
gi 254675251 89 RNDDIADGNPKLTLGLIWTIILHFQ 113
Cdd:cd21188 81 RAEDIVDGNPKLTLGLIWTIILHFQ 105
|
|
| CH_PLEC_rpt1 |
cd21235 |
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
6-124 |
2.89e-73 |
|
first calponin homology (CH) domain found in plectin and similar proteins; Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It can also bind muscle proteins such as actin to membrane complexes in muscle. Plectin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409084 Cd Length: 119 Bit Score: 240.70 E-value: 2.89e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 6 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 85
Cdd:cd21235 1 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 254675251 86 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 124
Cdd:cd21235 81 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQSE 119
|
|
| CH_PLEC_rpt2 |
cd21238 |
second calponin homology (CH) domain found in plectin and similar proteins; Plectin, also ... |
126-231 |
9.05e-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: 236.07 E-value: 9.05e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 126 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 205
Cdd:cd21238 1 MTAKEKLLLWSQRMVEGYQGLRCDNFTSSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 80
|
90 100
....*....|....*....|....*.
gi 254675251 206 PEDVDVPQPDEKSIITYVSSLYDAMP 231
Cdd:cd21238 81 PEDVDVPQPDEKSIITYVSSLYDAMP 106
|
|
| CH_DYST_rpt1 |
cd21236 |
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
6-122 |
2.75e-71 |
|
first calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409085 Cd Length: 128 Bit Score: 235.26 E-value: 2.75e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 6 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 85
Cdd:cd21236 12 DERDKVQKKTFTKWINQHLMKVRKHVNDLYEDLRDGHNLISLLEVLSGDTLPREKGRMRFHRLQNVQIALDYLKRRQVKL 91
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675251 86 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQ 122
Cdd:cd21236 92 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIHVTGE 128
|
|
| CH_PLEC-like_rpt2 |
cd21189 |
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ... |
127-231 |
1.07e-65 |
|
second calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409038 Cd Length: 105 Bit Score: 218.41 E-value: 1.07e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 206
Cdd:cd21189 1 SAKEALLLWARRTTEGYPGVRVTNFTSSWRDGLAFNAIIHRNRPDLIDFRSVRNQSNRENLENAFNVAEKEFGVTRLLDP 80
|
90 100
....*....|....*....|....*
gi 254675251 207 EDVDVPQPDEKSIITYVSSLYDAMP 231
Cdd:cd21189 81 EDVDVPEPDEKSIITYVSSLYDVFP 105
|
|
| CH_MACF1_rpt1 |
cd21237 |
first calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
6-123 |
7.52e-63 |
|
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: 211.04 E-value: 7.52e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 6 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKL 85
Cdd:cd21237 1 DERDRVQKKTFTKWVNKHLMKVRKHINDLYEDLRDGHNLISLLEVLSGVKLPREKGRMRFHRLQNVQIALDFLKQRQVKL 80
|
90 100 110
....*....|....*....|....*....|....*...
gi 254675251 86 VNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVSGQS 123
Cdd:cd21237 81 VNIRNDDITDGNPKLTLGLIWTIILHFQISDIYISGES 118
|
|
| CH_DYST_rpt2 |
cd21239 |
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also ... |
127-231 |
9.49e-58 |
|
second calponin homology (CH) domain found in dystonin and similar proteins; Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. Dystonin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409088 Cd Length: 104 Bit Score: 195.59 E-value: 9.49e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 206
Cdd:cd21239 1 SAKERLLLWSQQMTEGYTGIRCENFTTCWRDGRLFNAIIHKYRPDLIDMNTVAVQSNLANLEHAFYVAEK-LGVTRLLDP 79
|
90 100
....*....|....*....|....*
gi 254675251 207 EDVDVPQPDEKSIITYVSSLYDAMP 231
Cdd:cd21239 80 EDVDVSSPDEKSVITYVSSLYDVFP 104
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
125-231 |
5.10e-51 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 176.77 E-value: 5.10e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 125 DMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLL 204
Cdd:cd21240 2 DMSAKEKLLLWTQKVTAGYTGIKCTNFSSCWSDGKMFNALIHRYRPDLVDMERVQIQSNRENLEQAFEVAER-LGVTRLL 80
|
90 100
....*....|....*....|....*..
gi 254675251 205 DPEDVDVPQPDEKSIITYVSSLYDAMP 231
Cdd:cd21240 81 DAEDVDVPSPDEKSVITYVSSIYDAFP 107
|
|
| CH_DMD-like_rpt1 |
cd21186 |
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
11-114 |
1.19e-50 |
|
first calponin homology (CH) domain found in the dystrophin family; The dystrophin family includes dystrophin and its paralog, utrophin. Dystrophin, encoded by the DMD gene, is a large, submembrane cytoskeletal protein that is the main component of the dystrophin-glycoprotein complex (DGC) in skeletal muscles. It links the transmembrane DGC to the actin cytoskeleton through binding strongly to the cytoplasmic tail of beta-dystroglycan, the transmembrane subunit of a highly O-glycosylated cell-surface protein. Dystrophin is also involved in maintaining the structural integrity of cells, as well as in the formation of the blood-brain barrier (BBB). Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and links the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409035 Cd Length: 107 Bit Score: 175.65 E-value: 1.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 11 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 89
Cdd:cd21186 2 VQKKTFTKWINSQLSKANKpPIKDLFEDLRDGTRLLALLEVLTGKKLKPEKGRMRVHHLNNVNRALQVLEQNNVKLVNIS 81
|
90 100
....*....|....*....|....*
gi 254675251 90 NDDIADGNPKLTLGLIWTIILHFQI 114
Cdd:cd21186 82 SNDIVDGNPKLTLGLVWSIILHWQV 106
|
|
| CH_SPTB-like_rpt1 |
cd21246 |
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
2-110 |
1.13e-47 |
|
first calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409095 Cd Length: 117 Bit Score: 167.54 E-value: 1.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2 KIVPDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRH 80
Cdd:cd21246 7 KALADEREAVQKKTFTKWVNSHLARVGCRINDLYTDLRDGRMLIKLLEVLSGERLPKpTKGKMRIHCLENVDKALQFLKE 86
|
90 100 110
....*....|....*....|....*....|
gi 254675251 81 RQVKLVNIRNDDIADGNPKLTLGLIWTIIL 110
Cdd:cd21246 87 QRVHLENMGSHDIVDGNHRLTLGLIWTIIL 116
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
127-227 |
2.45e-46 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 162.97 E-value: 2.45e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 206
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGVNIQNFTTSWRDGLAFNALIHAHRPDLIDYNRLDPNDHLGNLNNAFDVAEQELGIAKLLDA 81
|
90 100
....*....|....*....|.
gi 254675251 207 EDVDVPQPDEKSIITYVSSLY 227
Cdd:cd21194 82 EDVDVARPDEKSIMTYVASYY 102
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
10-338 |
3.58e-45 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 175.90 E-value: 3.58e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 10 RVQKKTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLV 86
Cdd:COG5069 8 KVQKKTFTKWTNEKLISGgQKEFGDLDTDLKDGVKLAQLLEALQKDNAGEynETPETRIHVMENVSGRLEFIKGKGVKLF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILHFQISDIQvsgQSEDMTAKEKLLLWSQRMVEGYQ-GLRCDNFTTSWRDGRLFNAII 165
Cdd:COG5069 88 NIGPQDIVDGNPKLILGLIWSLISRLTIATIN---EEGELTKHINLLLWCDEDTGGYKpEVDTFDFFRSWRDGLAFSALI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 166 HRHKPMLIDMNKVYRQTNLE--NLDQAFSVAERDLGVTRLLDPEDV-DVPQPDEKSIITYVS------SLYD----AMPR 232
Cdd:COG5069 165 HDSRPDTLDPNVLDLQKKNKalNNFQAFENANKVIGIARLIGVEDIvNVSIPDERSIMTYVSwyiirfGLLEkidiALHR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 233 VPGAQDGVRANElQLRwQEYRELVLLLLQWIRHHTAAFEERKFPSSFEEIEILWCQFLKFKETE--LPAKEAD-KNRSKV 309
Cdd:COG5069 245 VYRLLEADETLI-QLR-LPYEIILLRLLNLIHLKQANWKVVNFSKDVSDGENYTDLLNQLNALCsrAPLETTDlHSLAGQ 322
|
330 340
....*....|....*....|....*....
gi 254675251 310 IYQSLEgAVQAGQLKIPPGYHPLDVEKEW 338
Cdd:COG5069 323 ILQNAE-KYDCRKYLPPAGNPKLDLAFVA 350
|
|
| CH_SPTB_like_rpt2 |
cd21248 |
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I ... |
127-227 |
1.80e-44 |
|
second calponin homology (CH) domain found in the beta-I spectrin-like subfamily; The beta-I spectrin-like family includes beta-I, -II, -III and -IV spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-III spectrin, also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5), may play a crucial role as a longer actin-membrane cross-linker or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409097 Cd Length: 105 Bit Score: 157.94 E-value: 1.80e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 206
Cdd:cd21248 2 SAKDALLLWCQMKTAGYPNVNVRNFTTSWRDGLAFNALIHKHRPDLIDYDKLSKSNALYNLQNAFNVAEQKLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 254675251 207 EDVDVPQPDEKSIITYVSSLY 227
Cdd:cd21248 82 EDVNVEQPDEKSIITYVVTYY 102
|
|
| CH_SYNE1_rpt1 |
cd21241 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 1 and similar ... |
7-114 |
5.04e-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: 156.77 E-value: 5.04e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 7 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLRHRQ 82
Cdd:cd21241 1 EQERVQKKTFTNWINSYLAKRKPpmKVEDLFEDIKDGTKLLALLEVLSGEKLPCEKGRRlkRVHFLSNINTALKFLESKK 80
|
90 100 110
....*....|....*....|....*....|..
gi 254675251 83 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 114
Cdd:cd21241 81 IKLVNINPTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_beta_spectrin_rpt1 |
cd21193 |
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
6-110 |
1.61e-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: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 6 DERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLrHRQVK 84
Cdd:cd21193 11 EERINIQKKTFTKWINSFLEKANLEIGDLFTDLSDGKLLLKLLEIISGEKLGKpNRGRLRVQKIENVNKALAFL-KTKVR 89
|
90 100
....*....|....*....|....*.
gi 254675251 85 LVNIRNDDIADGNPKLTLGLIWTIIL 110
Cdd:cd21193 90 LENIGAEDIVDGNPRLILGLIWTIIL 115
|
|
| CH_SYNE-like_rpt1 |
cd21190 |
first calponin homology (CH) domain found in the synaptic nuclear envelope protein family; The ... |
7-114 |
2.20e-43 |
|
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: 155.04 E-value: 2.20e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 7 ERDRVQKKTFTKWVNKHLikaQRH-----ISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM--RFHKLQNVQIALDYLR 79
Cdd:cd21190 1 EQERVQKKTFTNWINSHL---AKLsqpivINDLFVDIKDGTALLRLLEVLSGQKLPIESGRVlqRAHKLSNIRNALDFLT 77
|
90 100 110
....*....|....*....|....*....|....*
gi 254675251 80 HRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 114
Cdd:cd21190 78 KRCIKLVNINSTDIVDGKPSIVLGLIWTIILYFQI 112
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
114-229 |
2.97e-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: 149.05 E-value: 2.97e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 114 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 193
Cdd:cd21216 1 IQDISV----EELSAKEGLLLWCQRKTAPYKNVNVQNFHTSWKDGLAFCALIHRHRPDLLDYDKLRKDDPRENLNLAFDV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675251 194 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 229
Cdd:cd21216 77 AEKHLDIPKMLDAEDiVNTPRPDERSVMTYVSCYYHA 113
|
|
| CH_SYNE1_rpt2 |
cd21243 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 1 (SYNE-1) and ... |
126-231 |
6.92e-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: 147.85 E-value: 6.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 126 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 205
Cdd:cd21243 4 GGAKKALLKWVQNAAAKRFGIEVKDFGPSWRDGVAFNAIIHSIRPDLVDMESLKRRSNRENLETAFTVAEKELGIPRLLD 83
|
90 100
....*....|....*....|....*.
gi 254675251 206 PEDVDVPQPDEKSIITYVSSLYDAMP 231
Cdd:cd21243 84 PEDVDVDKPDEKSIMTYVAQFLKKYP 109
|
|
| CH_SPTBN4_rpt1 |
cd21318 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
1-110 |
1.72e-40 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN4, also called beta-IV spectrin, or spectrin, non-erythroid beta chain 3 (SPTBN3), is a novel spectrin isolated as an interactor of the receptor tyrosine phosphatase-like protein ICA512. Its mutation associates with congenital myopathy, neuropathy, and central deafness. SPTBN4 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409167 Cd Length: 139 Bit Score: 147.86 E-value: 1.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1 MKIVPDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 79
Cdd:cd21318 28 IKALADEREAVQKKTFTKWVNSHLARVPCRINDLYTDLRDGYVLTRLLEVLSGEQLPKpTRGRMRIHSLENVDKALQFLK 107
|
90 100 110
....*....|....*....|....*....|.
gi 254675251 80 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 110
Cdd:cd21318 108 EQRVHLENVGSHDIVDGNHRLTLGLIWTIIL 138
|
|
| CH_SPTBN2_rpt1 |
cd21317 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
1-110 |
2.80e-39 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN2, also called beta-III spectrin, or spinocerebellar ataxia 5 protein (SCA5), probably plays an important role in the neuronal membrane skeleton. Mutations in SPTBN2 is associated with spinocerebellar ataxia type 5. SPTBN2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409166 Cd Length: 132 Bit Score: 144.04 E-value: 2.80e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1 MKIVPDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 79
Cdd:cd21317 21 IKALADEREAVQKKTFTKWVNSHLARVTCRIGDLYTDLRDGRMLIRLLEVLSGEQLPKpTKGRMRIHCLENVDKALQFLK 100
|
90 100 110
....*....|....*....|....*....|.
gi 254675251 80 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 110
Cdd:cd21317 101 EQKVHLENMGSHDIVDGNHRLTLGLIWTIIL 131
|
|
| CH_SPTBN2_rpt2 |
cd21321 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 2 (SPTBN2) ... |
123-227 |
1.60e-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: 141.35 E-value: 1.60e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 123 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 202
Cdd:cd21321 1 KEKKSAKDALLLWCQMKTAGYPNVNVHNFTTSWRDGLAFNAIVHKHRPDLIDFETLKKSNAHYNLQNAFNVAEKELGLTK 80
|
90 100
....*....|....*....|....*
gi 254675251 203 LLDPEDVDVPQPDEKSIITYVSSLY 227
Cdd:cd21321 81 LLDPEDVNVDQPDEKSIITYVATYY 105
|
|
| CH_SpAIN1-like_rpt1 |
cd21215 |
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
11-112 |
1.88e-38 |
|
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409064 Cd Length: 107 Bit Score: 140.61 E-value: 1.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 11 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 88
Cdd:cd21215 4 VQKKTFTKWLNTKLSSRGLSITDLVTDLSDGVRLIQLLEIIGDESLGRynKNPKMRVQKLENVNKALEFIKSRGVKLTNI 83
|
90 100
....*....|....*....|....
gi 254675251 89 RNDDIADGNPKLTLGLIWTIILHF 112
Cdd:cd21215 84 GAEDIVDGNLKLILGLLWTLILRF 107
|
|
| CH_ACTN_rpt1 |
cd21214 |
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ... |
9-110 |
2.29e-38 |
|
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409063 Cd Length: 105 Bit Score: 140.22 E-value: 2.29e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 9 DRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHRQVKLVN 87
Cdd:cd21214 3 EKQQRKTFTAWCNSHLRKAGTQIENIEEDFRDGLKLMLLLEVISGERLPKpERGKMRFHKIANVNKALDFIASKGVKLVS 82
|
90 100
....*....|....*....|...
gi 254675251 88 IRNDDIADGNPKLTLGLIWTIIL 110
Cdd:cd21214 83 IGAEEIVDGNLKMTLGMIWTIIL 105
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1316-1938 |
2.63e-38 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 158.56 E-value: 2.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1316 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQAKaQAElEAQELQRRMQEevarreeaavdaqqqkRSIQEELQHLRQSs 1394
Cdd:COG1196 177 AERKLEATEENLERLEDILgELERQLEPLERQAE-KAE-RYRELKEELKE----------------LEAELLLLKLREL- 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1395 EAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQR 1474
Cdd:COG1196 238 EAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER 317
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1475 KRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALEtaQRSAEVELQSKRASFAEKT 1554
Cdd:COG1196 318 LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAE--AEEELEELAEELLEALRAA 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1555 AQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEA 1634
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALL 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1635 EREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQG---EQQRQLLEEELARLQHEATAA 1711
Cdd:COG1196 476 EAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGveaAYEAALEAALAAALQNIVVED 555
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1712 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA-----LAEEAKRQRQLAE 1786
Cdd:COG1196 556 DEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVlgdtlLGRTLVAARLEAA 635
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1787 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKA 1866
Cdd:COG1196 636 LRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1867 SESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRsnaedtmrsKEQAELEAARQR 1938
Cdd:COG1196 716 RLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELE---------RELERLEREIEA 778
|
|
| CH_SYNE2_rpt1 |
cd21242 |
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic ... |
7-114 |
2.67e-38 |
|
first calponin homology (CH) domain found in synaptic nuclear envelope protein 2; Synaptic nuclear envelope protein 2 (SYNE-2), also called nesprin-2, KASH domain-containing protein 2 (KASH2), nuclear envelope spectrin repeat protein 2, nucleus and actin connecting element protein, or protein NUANCE, is a multi-isomeric modular protein which forms a linking network between organelles and the actin cytoskeleton to maintain subcellular spatial organization. SYNE-2 also acts as a component of the LINC (LInker of Nucleoskeleton and Cytoskeleton) complex, which is involved in the connection between the nuclear lamina and the cytoskeleton. SYNE-2 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409091 Cd Length: 111 Bit Score: 140.35 E-value: 2.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 7 ERDRVQKKTFTKWVNKHLIKAQ--RHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 84
Cdd:cd21242 1 EQEQTQKRTFTNWINSQLAKHSppSVVSDLFTDIQDGHRLLDLLEVLSGQQLPREKGHNVFQCRSNIETALSFLKNKSIK 80
|
90 100 110
....*....|....*....|....*....|
gi 254675251 85 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 114
Cdd:cd21242 81 LINIHVPDIIEGKPSIILGLIWTIILHFHI 110
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
123-227 |
2.72e-38 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 140.53 E-value: 2.72e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 123 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 202
Cdd:cd21319 1 RETRSAKDALLLWCQMKTAGYPNVNVTNFTSSWKDGLAFNALIHKHRPDLVDFGKLKKSNARHNLEHAFNVAERQLGITK 80
|
90 100
....*....|....*....|....*
gi 254675251 203 LLDPEDVDVPQPDEKSIITYVSSLY 227
Cdd:cd21319 81 LLDPEDVFTENPDEKSIITYVVAFY 105
|
|
| CH_SPTBN5_rpt2 |
cd21249 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
126-227 |
6.65e-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: 136.15 E-value: 6.65e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 126 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 205
Cdd:cd21249 3 RSAKEALLIWCQRKTAGYTNVNVQDFSRSWRDGLAFNALIHAHRPDLIDYGSLRPDRPLYNLANAFLVAEQELGISQLLD 82
|
90 100
....*....|....*....|..
gi 254675251 206 PEDVDVPQPDEKSIITYVSSLY 227
Cdd:cd21249 83 PEDVAVPHPDERSIMTYVSLYY 104
|
|
| CH_DMD_rpt1 |
cd21231 |
first calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
6-114 |
1.79e-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: 135.05 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 6 DERDRVQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVK 84
Cdd:cd21231 1 YEREDVQKKTFTKWINAQFAKFGKpPIEDLFTDLQDGRRLLELLEGLTGQKLVKEKGSTRVHALNNVNKALQVLQKNNVD 80
|
90 100 110
....*....|....*....|....*....|
gi 254675251 85 LVNIRNDDIADGNPKLTLGLIWTIILHFQI 114
Cdd:cd21231 81 LVNIGSADIVDGNHKLTLGLIWSIILHWQV 110
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1311-2016 |
2.63e-36 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 153.37 E-value: 2.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1311 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSiqEELQHL 1390
Cdd:PTZ00121 1101 EEAKKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKA--EDAKKA 1178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1391 RQSSEAEIQAKAQQVEAAERSRmRIEEEIRVVRLQlETTERQRGGAEGELQALRaRAEEAeaqkRQAQEEAERLRRQVQD 1470
Cdd:PTZ00121 1179 EAARKAEEVRKAEELRKAEDAR-KAEAARKAEEER-KAEEARKAEDAKKAEAVK-KAEEA----KKDAEEAKKAEEERNN 1251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1471 ESQRKRQAEAELALRVKAEAEAAREKQRAlqalDELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASF 1550
Cdd:PTZ00121 1252 EEIRKFEEARMAHFARRQAAIKAEEARKA----DELK-KAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEE 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1551 AEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRlqAEEVaqqkslAQADAEKQ 1630
Cdd:PTZ00121 1327 AKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKK--AEEK------KKADEAKK 1398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1631 KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATA 1710
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1711 ATQKRQeleAELAKVRAEmevllASKARAEEESRSTSEKSKqrleAEAGRFRELAEEAARLRAlAEEAKRQRQLAEEDAA 1790
Cdd:PTZ00121 1479 AEEAKK---ADEAKKKAE-----EAKKKADEAKKAAEAKKK----ADEAKKAEEAKKADEAKK-AEEAKKADEAKKAEEK 1545
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1791 RQRAEAERvlTEKLAAISEatrlKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESE 1870
Cdd:PTZ00121 1546 KKADELKK--AEELKKAEE----KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAK 1619
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1871 L--------ERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDtMRSKEQAELEAARQRQLAA 1942
Cdd:PTZ00121 1620 IkaeelkkaEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEE-AKKAEEDEKKAAEALKKEA 1698
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1943 EEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2016
Cdd:PTZ00121 1699 EEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1414-2014 |
3.49e-36 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 151.63 E-value: 3.49e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1414 RIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1493
Cdd:COG1196 190 RLEDILGELERQLEPLERQAEKAE-RYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAE 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1494 REKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLre 1573
Cdd:COG1196 269 LEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL-- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1574 eaerraqqqAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1653
Cdd:COG1196 347 ---------EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1654 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL 1733
Cdd:COG1196 418 RLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLL 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1734 ASKARAEEESRST---SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEA 1810
Cdd:COG1196 498 EAEADYEGFLEGVkaaLLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFL 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1811 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQkglVEDTLRQRRQVEE 1890
Cdd:COG1196 578 PLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVT---LAGRLREVTLEGE 654
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1891 EIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRK 1970
Cdd:COG1196 655 GGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAER 734
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 254675251 1971 VALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQA 2014
Cdd:COG1196 735 EELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEA 778
|
|
| CH_DMD-like_rpt2 |
cd21187 |
second calponin homology (CH) domain found in the dystrophin family; The dystrophin family ... |
130-231 |
4.76e-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: 133.71 E-value: 4.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 130 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 208
Cdd:cd21187 2 EKTLLaWCRQSTRGYEQVDVKNFTTSWRDGLAFNALIHRHRPDLFDFDSLVKDSPESRLEHAFTVAHEHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 254675251 209 VDVPQPDEKSIITYVSSLYDAMP 231
Cdd:cd21187 82 VNVEQPDKKSILMYVTSLFQVLP 104
|
|
| CH_SPTBN4_rpt2 |
cd21322 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 4 (SPTBN4) ... |
111-227 |
1.96e-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: 132.87 E-value: 1.96e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 111 HFQISDIQVSGQSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQA 190
Cdd:cd21322 1 QIQVIKIETEDNRETRSAKDALLLWCQMKTAGYPEVNIQNFTTSWRDGLAFNALIHRHRPDLIDFSKLTKSNATYNLQQA 80
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675251 191 FSVAERDLGVTRLLDPEDVDVPQPDEKSIITYVSSLY 227
Cdd:cd21322 81 FNTAEQHLGLTKLLDPEDVNMEAPDEKSIITYVVSFY 117
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1443-2043 |
1.09e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 146.62 E-value: 1.09e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1443 LRARAEEAEAQKRQAQEEAERL---RRQVqdESQRKRqaeaelalrVKAEAEAAREKQRALQALDELRLQAEEAERRLRQ 1519
Cdd:COG1196 170 YKERKEEAERKLEATEENLERLediLGEL--ERQLEP---------LERQAEKAERYRELKEELKELEAELLLLKLRELE 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1520 AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERW 1599
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1600 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1679
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAE----AELAEAEEALLEAEAELAEAEEELEELAEELLEALRA 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1680 LIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1759
Cdd:COG1196 395 AAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAAL 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1760 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLA----AISEATRLKTEAEIALKEKEAENERLRRLA 1835
Cdd:COG1196 475 LEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRglagAVAVLIGVEAAYEAALEAALAAALQNIVVE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1836 EDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGR 1915
Cdd:COG1196 555 DDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEA 634
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1916 IRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQ 1995
Cdd:COG1196 635 ALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEE 714
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 254675251 1996 ESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDR 2043
Cdd:COG1196 715 ERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1645-2207 |
1.90e-34 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 145.85 E-value: 1.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1645 EEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK 1724
Cdd:COG1196 220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1725 VRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKL 1804
Cdd:COG1196 300 LEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1805 AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLvEDTLRQ 1884
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEE-AELEEE 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1885 RRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEE 1964
Cdd:COG1196 458 EEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYE 537
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1965 AARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRL 2044
Cdd:COG1196 538 AALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYV 617
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2045 RSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ 2124
Cdd:COG1196 618 LGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEE 697
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2125 KQAADAEMEKHKKFAE-QTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQME 2203
Cdd:COG1196 698 ALLAEEEEERELAEAEeERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIE 777
|
....
gi 254675251 2204 ELGK 2207
Cdd:COG1196 778 ALGP 781
|
|
| CH_dFLNA-like_rpt1 |
cd21311 |
first calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
10-115 |
1.86e-33 |
|
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: 127.18 E-value: 1.86e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 10 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQ-VKLV 86
Cdd:cd21311 14 RIQQNTFTRWANEHLKTANKHIADLETDLSDGLRLIALVEVLSGKKFPKFNKRptFRSQKLENVSVALKFLEEDEgIKIV 93
|
90 100
....*....|....*....|....*....
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILHFQIS 115
Cdd:cd21311 94 NIDSSDIVDGKLKLILGLIWTLILHYSIS 122
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1279-1866 |
2.85e-33 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 142.38 E-value: 2.85e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1279 QEYVDLRTRYSEL-TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ-------LAEAHAQAKAQ 1350
Cdd:COG1196 213 ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLeleelelELEEAQAEEYE 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1351 AELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTE 1430
Cdd:COG1196 293 LLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1431 RQRGGAEGELQALRARAE------------------EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1492
Cdd:COG1196 373 ELAEAEEELEELAEELLEalraaaelaaqleeleeaEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1493 AREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLR 1572
Cdd:COG1196 453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV 532
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1573 EEAERRAQQQAEAERAREEAERELERWQ-----LKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQ 1647
Cdd:COG1196 533 EAAYEAALEAALAAALQNIVVEDDEVAAaaieyLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREAD 612
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1648 AVRQRELAEQELEKQRQLAEGTAQQRLAAEQEliRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRA 1727
Cdd:COG1196 613 ARYYVLGDTLLGRTLVAARLEAALRRAVTLAG--RLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAE 690
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1728 EMEVLLASKARAEEESRSTSEKSKQRleaeagrfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI 1807
Cdd:COG1196 691 EELELEEALLAEEEEERELAEAEEER--------LEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDL 762
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1808 SEATRLKTEAEIALKEKEAENerLRRLAEDEAFQRRR--LEEQaalhKADIEERLAQLRKA 1866
Cdd:COG1196 763 EELERELERLEREIEALGPVN--LLAIEEYEELEERYdfLSEQ----REDLEEARETLEEA 817
|
|
| CH_SPTBN1_rpt2 |
cd21320 |
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
127-227 |
5.31e-33 |
|
second calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409169 Cd Length: 108 Bit Score: 125.21 E-value: 5.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 206
Cdd:cd21320 2 SAKDALLLWCQMKTAGYPNVNIHNFTTSWRDGMAFNALIHKHRPDLIDFDKLKKSNAHYNLQNAFNLAEQHLGLTKLLDP 81
|
90 100
....*....|....*....|.
gi 254675251 207 EDVDVPQPDEKSIITYVSSLY 227
Cdd:cd21320 82 EDISVDHPDEKSIITYVVTYY 102
|
|
| CH_jitterbug-like_rpt1 |
cd21227 |
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
11-114 |
1.64e-32 |
|
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409076 Cd Length: 109 Bit Score: 123.55 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 11 VQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR--EKGRMRFHKLQNVQIALDYLRHRQVKLVNI 88
Cdd:cd21227 4 IQKNTFTNWVNEQLKPTGMSVEDLATDLEDGVKLIALVEILQGRKLGRviKKPLNQHQKLENVTLALKAMAEDGIKLVNI 83
|
90 100
....*....|....*....|....*.
gi 254675251 89 RNDDIADGNPKLTLGLIWTIILHFQI 114
Cdd:cd21227 84 GNEDIVNGNLKLILGLIWHLILRYQI 109
|
|
| CH_UTRN_rpt1 |
cd21232 |
first calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
11-114 |
1.71e-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: 123.58 E-value: 1.71e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 11 VQKKTFTKWVNKHLIKAQR-HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRFHKLQNVQIALDYLRHRQVKLVNIR 89
Cdd:cd21232 2 VQKKTFTKWINARFSKSGKpPIKDMFTDLRDGRKLLDLLEGLTGKSLPKERGSTRVHALNNVNRVLQVLHQNNVELVNIG 81
|
90 100
....*....|....*....|....*
gi 254675251 90 NDDIADGNPKLTLGLIWTIILHFQI 114
Cdd:cd21232 82 GTDIVDGNHKLTLGLLWSIILHWQV 106
|
|
| CH_SPTBN1_rpt1 |
cd21316 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) ... |
1-110 |
1.97e-32 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 1 (SPTBN1) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN1, also called beta-II spectrin, fodrin beta chain, or spectrin, non-erythroid beta chain 1, is also a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. SPTBN1 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409165 Cd Length: 154 Bit Score: 125.16 E-value: 1.97e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1 MKIVPDERDRVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLR 79
Cdd:cd21316 43 IKALADEREAVQKKTFTKWVNSHLARVSCRITDLYMDLRDGRMLIKLLEVLSGERLPKpTKGRMRIHCLENVDKALQFLK 122
|
90 100 110
....*....|....*....|....*....|.
gi 254675251 80 HRQVKLVNIRNDDIADGNPKLTLGLIWTIIL 110
Cdd:cd21316 123 EQRVHLENMGSHDIVDGNHRLTLGLIWTIIL 153
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1304-1925 |
6.13e-32 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 138.74 E-value: 6.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1304 ETLRRMEEEERLAEQQRAEERERLAEVEAALE--KQRQLAEAHAQAKAQAELEAQELQR----RMQEEVARREEAAVDAQ 1377
Cdd:PTZ00121 1161 EDARKAEEARKAEDAKKAEAARKAEEVRKAEElrKAEDARKAEAARKAEEERKAEEARKaedaKKAEAVKKAEEAKKDAE 1240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1378 QQKRSIQE-------ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRlQLETTERQRGGAEGELQALRAR-AEE 1449
Cdd:PTZ00121 1241 EAKKAEEErnneeirKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKAD-EAKKAEEKKKADEAKKKAEEAKkADE 1319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1450 AEAQKRQAQEEAERLRRQVQdESQRKRQAEAELALRVKAEAEAAREKQRALQ--------ALDELRLQAEE---AERRLR 1518
Cdd:PTZ00121 1320 AKKKAEEAKKKADAAKKKAE-EAKKAAEAAKAEAEAAADEAEAAEEKAEAAEkkkeeakkKADAAKKKAEEkkkADEAKK 1398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1519 QAEAERARQVQVALETAQRSAEVELQsKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELER 1598
Cdd:PTZ00121 1399 KAEEDKKKADELKKAAAAKKKADEAK-KKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKK 1477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1599 WQLKANEALRLRLQAEEVAQqkslaQADAEKQKEEAEREARRRGKAEEqAVRQRELAEQELEKQRQLAEGTAQQRLAAE- 1677
Cdd:PTZ00121 1478 KAEEAKKADEAKKKAEEAKK-----KADEAKKAAEAKKKADEAKKAEE-AKKADEAKKAEEAKKADEAKKAEEKKKADEl 1551
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1678 --QELIRLRAETEQGEQQRQlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRlE 1755
Cdd:PTZ00121 1552 kkAEELKKAEEKKKAEEAKK-AEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA-E 1629
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1756 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAA--RQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRR 1833
Cdd:PTZ00121 1630 EEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAeeAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKK 1709
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1834 LAEDEAFQRRRLEEQAALHKADIEE--RLAQLRKASESELERQKGlvEDTLRQRRQVEEEIMALKVSFEKAAAGKAELEL 1911
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEakKEAEEDKKKAEEAKKDEE--EKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787
|
650
....*....|....
gi 254675251 1912 ELGRIRSNAEDTMR 1925
Cdd:PTZ00121 1788 EDEKRRMEVDKKIK 1801
|
|
| CH_SYNE-like_rpt2 |
cd21192 |
second calponin homology (CH) domain found in the synaptic nuclear envelope protein (SYNE) ... |
126-224 |
6.90e-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: 121.76 E-value: 6.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 126 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 205
Cdd:cd21192 2 GSAEKALLKWVQAEIGKYYGIRVTDFDKSWRDGVAFLALIHAIRPDLVDMKTVKNRSPRDNLELAFRIAEQHLNIPRLLE 81
|
90
....*....|....*....
gi 254675251 206 PEDVDVPQPDEKSIITYVS 224
Cdd:cd21192 82 VEDVLVDKPDERSIMTYVS 100
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
114-229 |
9.25e-32 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 121.87 E-value: 9.25e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 114 ISDIQvsgqSEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 193
Cdd:cd21291 1 IADIN----EEGLTAKEGLLLWCQRKTAGYDEVDVQDFTTSWTDGLAFCALIHRHRPDLIDYDKLDKKDHRGNMQLAFDI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675251 194 AERDLGVTRLLDPEDV-DVPQPDEKSIITYVSSLYDA 229
Cdd:cd21291 77 ASKEIGIPQLLDVEDVcDVAKPDERSIMTYVAYYFHA 113
|
|
| CH_UTRN_rpt2 |
cd21234 |
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also ... |
130-231 |
9.70e-32 |
|
second calponin homology (CH) domain found in utrophin and similar proteins; Utrophin, also called dystrophin-related protein 1 (DRP-1), is an autosomal dystrophin homolog that increases dystrophic muscle function and reduces pathology. It is broadly expressed in both the mRNA and protein levels, and occurs in the cerebrovascular endothelium. Utrophin forms the utrophin-glycoprotein complex (UGC) by interacting with dystroglycans (DGs) and sarcoglycan-dystroglycans, as well as sarcoglycan and sarcospan (SG-SSPN) subcomplexes. It may act as a scaffolding protein that stabilizes lipid microdomains and clusters mechanosensitive channel subunits, and link the F-actin cytoskeleton to the cell membrane via the associated glycoprotein complex. Like dystrophin, utrophin has a compact cluster of domains comprising four EF-hand-like motifs and a ZZ-domain, followed by a looser region with two coiled-coils. These domains are believed to be involved in protein-protein interactions. In addition, it contains two syntrophin binding sites (SBSs) and a long N-terminal extension that comprises two actin-binding calponin homology (CH) domains, up to 24 spectrin repeats (SRs), and a WW domain. However, utrophin lacks the intrinsic microtubule binding activity of dystrophin SRs. This model corresponds to the second CH domain.
Pssm-ID: 409083 [Multi-domain] Cd Length: 104 Bit Score: 121.22 E-value: 9.70e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 130 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 208
Cdd:cd21234 2 EKILLsWVRQSTRPYSQVNVLNFTTSWTDGLAFNAVLHRHKPDLFSWDKVVKMSPVERLEHAFSKAKNHLGIEKLLDPED 81
|
90 100
....*....|....*....|...
gi 254675251 209 VDVPQPDEKSIITYVSSLYDAMP 231
Cdd:cd21234 82 VAVQLPDKKSIIMYLTSLFEVLP 104
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
132-227 |
1.26e-30 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 118.22 E-value: 1.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 132 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 210
Cdd:cd21253 6 LQQWCRQQTEGYRDVKVTNMTTSWRDGLAFCAIIHRFRPDLIDFDSLSKENVYENNKLAFTVAEKELGIPALLDAEDmVA 85
|
90
....*....|....*..
gi 254675251 211 VPQPDEKSIITYVSSLY 227
Cdd:cd21253 86 LKVPDKLSILTYVSQYY 102
|
|
| CH_DMD_rpt2 |
cd21233 |
second calponin homology (CH) domain found in dystrophin and similar proteins; Dystrophin, ... |
130-232 |
2.10e-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: 117.72 E-value: 2.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 130 EKLLL-WSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN-LENLDQAFSVAERDLGVTRLLDPE 207
Cdd:cd21233 2 EKILLsWVRQSTRNYPQVNVINFTSSWSDGLAFNALIHSHRPDLFDWNSVVSQQSaTERLDHAFNIARQHLGIEKLLDPE 81
|
90 100
....*....|....*....|....*
gi 254675251 208 DVDVPQPDEKSIITYVSSLYDAMPR 232
Cdd:cd21233 82 DVATAHPDKKSILMYVTSLFQVLPQ 106
|
|
| CH_SYNE2_rpt2 |
cd21244 |
second calponin homology (CH) domain found in synaptic nuclear envelope protein 2 (SYNE-2) and ... |
126-224 |
3.04e-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: 117.24 E-value: 3.04e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 126 MTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 205
Cdd:cd21244 4 MSARKALLLWAQEQCAKVGSISVTDFKSSWRNGLAFLAIIHALRPGLVDMEKLKGRSNRENLEEAFRIAEQELKIPRLLE 83
|
90
....*....|....*....
gi 254675251 206 PEDVDVPQPDEKSIITYVS 224
Cdd:cd21244 84 PEDVDVVNPDEKSIMTYVA 102
|
|
| CH_ACTN4_rpt2 |
cd21290 |
second calponin homology (CH) domain found in alpha-actinin-4; Alpha-actinin-4 (ACTN4), also ... |
112-239 |
3.78e-30 |
|
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: 117.49 E-value: 3.78e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 112 FQISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAF 191
Cdd:cd21290 2 FAIQDISV----EETSAKEGLLLWCQRKTAPYKNVNVQNFHISWKDGLAFNALIHRHRPELIEYDKLRKDDPVTNLNNAF 77
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 254675251 192 SVAERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQDG 239
Cdd:cd21290 78 EVAEKYLDIPKMLDAEDiVNTARPDEKAIMTYVSSFYHAF---SGAQKA 123
|
|
| CH_CLMN_rpt1 |
cd21191 |
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
7-116 |
4.12e-30 |
|
first calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called calponin-like transmembrane domain protein, is a protein with calponin homology (CH) and transmembrane domains expressed in maturing spermatogenic cells. It may be involved in the development and/or maintenance of neuronal functions. Calmin contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409040 Cd Length: 114 Bit Score: 117.30 E-value: 4.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 7 ERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQ 82
Cdd:cd21191 1 ERENVQKRTFTRWINLHLEKCNPplEVKDLFVDIQDGKILMALLEVLSGQNLLQEykPSSHRIFRLNNIAKALKFLEDSN 80
|
90 100 110
....*....|....*....|....*....|....
gi 254675251 83 VKLVNIRNDDIADGNPKLTLGLIWTIILHFQISD 116
Cdd:cd21191 81 VKLVSIDAAEIADGNPSLVLGLIWNIILFFQIKE 114
|
|
| CH_FLN-like_rpt1 |
cd21183 |
first calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
10-112 |
8.86e-30 |
|
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: 116.04 E-value: 8.86e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 10 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 86
Cdd:cd21183 3 RIQANTFTRWCNEHLKERGMQIHDLATDFSDGLCLIALLENLSTRPLKRsynRRPAFQQHYLENVSTALKFIEADHIKLV 82
|
90 100
....*....|....*....|....*.
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILHF 112
Cdd:cd21183 83 NIGSGDIVNGNIKLILGLIWTLILHY 108
|
|
| Spectrin_like |
pfam18373 |
Spectrin like domain; Desmoplakin (DP) is an integral part of desmosomes, where it links ... |
859-936 |
1.43e-29 |
|
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: 114.24 E-value: 1.43e-29
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 859 LAWQSLSRDIQLIRSWSLVTFRTLKPEEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLVAEREYGSCSRHYQQLLQS 936
Cdd:pfam18373 1 VSWQYLLKDIQRINSWTISMLKTMRPEEYRQVLKNLETHYQDFLRDSQESEMFGAEDRRQLEREVNSAQQHYQTLLVS 78
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1687-2534 |
3.34e-29 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 129.88 E-value: 3.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1687 TEQGEQQRQLLEEELARLQHEATAATqkRQELEAELAKVR------AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR 1760
Cdd:PTZ00121 1033 TEYGNNDDVLKEKDIIDEDIDGNHEG--KAEAKAHVGQDEglkpsyKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGK 1110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1761 FRElAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEdeaf 1840
Cdd:PTZ00121 1111 AEE-ARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEEARKAEDAKKAEAARKAE---- 1185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1841 QRRRLEEqaaLHKADIEERLAQLRKASEselerqkglvEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNA 1920
Cdd:PTZ00121 1186 EVRKAEE---LRKAEDARKAEAARKAEE----------ERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNE 1252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1921 EdtMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKValEEVERLKAKVEEARRLRERAEQesarq 2000
Cdd:PTZ00121 1253 E--IRKFEEARMAHFARRQAAIKAEEARKADELKKAEEKKKADEAKKAEEK--KKADEAKKKAEEAKKADEAKKK----- 1323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2001 lqlAQEAAQKRLQAEEKAhafvvqqreeelqqtlqqeqnmldrlrseaeaarraaeeaeeareqaereaaQSRKQVEEAE 2080
Cdd:PTZ00121 1324 ---AEEAKKKADAAKKKA----------------------------------------------------EEAKKAAEAA 1348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2081 RLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQtLRQKAQVEQELTTLRLQL 2160
Cdd:PTZ00121 1349 KAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKADE-LKKAAAAKKKADEAKKKA 1427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2161 EETDHQksildEELQRLKAEVTEAARQRSQVEEelfsvRVQMEELGKlkaRIEAENRALILRDKDNTQRFLEE---EAEK 2237
Cdd:PTZ00121 1428 EEKKKA-----DEAKKKAEEAKKADEAKKKAEE-----AKKAEEAKK---KAEEAKKADEAKKKAEEAKKADEakkKAEE 1494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2238 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK----EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQE 2313
Cdd:PTZ00121 1495 AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeaKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEE 1574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2314 DKeQMAQQLVEETQgfqrtlEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKqAEEIGEKLHRTELATQEKV 2393
Cdd:PTZ00121 1575 DK-NMALRKAEEAK------KAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKK-AEEEKKKVEQLKKKEAEEK 1646
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2394 TLVQTL-------EIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ-----EQILQETQALQKSFL 2461
Cdd:PTZ00121 1647 KKAEELkkaeeenKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEElkkkeAEEKKKAEELKKAEE 1726
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 2462 SEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRK 2534
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKK 1799
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1075-1781 |
9.31e-29 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 127.36 E-value: 9.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1075 EQLKEAQAVPATLQELEATKASLKKLRAQAEAQQpvfntLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQ 1154
Cdd:COG1196 210 EKAERYRELKEELKELEAELLLLKLRELEAELEE-----LEAELEELEAELEELEAELAELEAELEELRLELEELELELE 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1155 AVLAQTDVRQRELEQLGRQLRYYRESadplsawLQDAKRRQEQIQAvpiancqaareqlrQEKALLEEIERHGEKVEECQ 1234
Cdd:COG1196 285 EAQAEEYELLAELARLEQDIARLEER-------RRELEERLEELEE--------------ELAELEEELEELEEELEELE 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1235 kfakqyinaikdyelqlitykaqlepvaspakkpkvqsgsesviqeyvdlrtryselttltsqyikfisETLRRMEEEER 1314
Cdd:COG1196 344 ---------------------------------------------------------------------EELEEAEEELE 354
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1315 LAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRmQEEVARREEAAVDAQQQKRSIQEELQHLRQSS 1394
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ-LEELEEAEEALLERLERLEEELEELEEALAEL 433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1395 EAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEA--------EAQKRQAQEEAERLRR 1466
Cdd:COG1196 434 EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAaarlllllEAEADYEGFLEGVKAA 513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1467 QVQDESQRKRQAEAELALRVKAE--AEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQ 1544
Cdd:COG1196 514 LLLAGLRGLAGAVAVLIGVEAAYeaALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALA 593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1545 SKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQ 1624
Cdd:COG1196 594 RGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAA 673
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1625 ADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARL 1704
Cdd:COG1196 674 LLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEER--LEEELEEEALEEQLEAEREELLEELLEEEELLEEE 751
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1705 QHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrLEAEAGRFRELAEEAARLralaEEAKRQ 1781
Cdd:COG1196 752 ALEELPEPPDLEELERELERLEREIEALGPVNLLAIEE-----------YEELEERYDFLSEQREDL----EEARET 813
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1748-2431 |
1.60e-28 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 126.59 E-value: 1.60e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1748 EKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEedaaRQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1827
Cdd:COG1196 199 ERQLEPLERQA----EKAERYRELKEELKELEAELLLLK----LRELEAELEELEAELEELEAELEELEAELAELEAELE 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1828 NERLRRLAEDEAFQRRRLEEQAAlhkadiEERLAQLRKASESELERQkglvEDTLRQRRQVEEEIMALKVSFEKAAAGKA 1907
Cdd:COG1196 271 ELRLELEELELELEEAQAEEYEL------LAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELE 340
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1908 ELELELgrirSNAEDTMRSKEQAELEAARQRQlaaeeeqrrrEAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEAR 1987
Cdd:COG1196 341 ELEEEL----EEAEEELEEAEAELAEAEEALL----------EAEAELAEAEEELEELAEELLEALRAAAELAAQLEELE 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1988 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAER 2067
Cdd:COG1196 407 EAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEEL 486
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2068 EAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAE--MEKHKKFAEQTLRQ 2145
Cdd:COG1196 487 AEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNivVEDDEVAAAAIEYL 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2146 KAQVEQELTTLRLqleETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKD 2225
Cdd:COG1196 567 KAAKAGRATFLPL---DKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLA 643
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2226 NTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2305
Cdd:COG1196 644 GRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEERELAEAEEERLEEELEE 723
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2306 EQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQL----EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgek 2381
Cdd:COG1196 724 EALEEQLEAEREELLEELLEEEELLEEEALEELPEPpdleELERELERLEREIEALGPVNLLAIEEYEELEERYDFL--- 800
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 254675251 2382 lhrtelaTQEKVTLVQTLeiqrqqsdhdaERLREAIAELEREKEKLKQEA 2431
Cdd:COG1196 801 -------SEQREDLEEAR-----------ETLEEAIEEIDRETRERFLET 832
|
|
| CH_MICAL_EHBP-like |
cd22198 |
calponin homology (CH) domain found in the MICAL and EHBP families; This group is composed of ... |
130-229 |
2.74e-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: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 130 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED- 208
Cdd:cd22198 3 EELLSWCQEQTEGYRGVKVTDLTSSWRSGLALCAIIHRFRPDLIDFSSLDPENIAENNQLAFDVAEQELGIPPVMTGQEm 82
|
90 100
....*....|....*....|.
gi 254675251 209 VDVPQPDEKSIITYVSSLYDA 229
Cdd:cd22198 83 ASLAVPDKLSMVSYLSQFYEA 103
|
|
| CH_ACTN1_rpt2 |
cd21287 |
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also ... |
114-238 |
5.52e-28 |
|
second calponin homology (CH) domain found in alpha-actinin-1; Alpha-actinin-1 (ACTN1), also called alpha-actinin cytoskeletal isoform, or non-muscle alpha-actinin-1, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN1 is a bundling protein. Its mutations cause congenital macrothrombocytopenia. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409136 Cd Length: 124 Bit Score: 111.33 E-value: 5.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 114 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 193
Cdd:cd21287 1 IQDISV----EETSAKEGLLLWCQRKTAPYKNVNIQNFHISWKDGLGFCALIHRHRPELIDYGKLRKDDPLTNLNTAFDV 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 254675251 194 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDAMprvPGAQD 238
Cdd:cd21287 77 AEKYLDIPKMLDAEDiVGTARPDEKAIMTYVSSFYHAF---SGAQK 119
|
|
| CH_FLN_rpt1 |
cd21228 |
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
10-112 |
4.12e-27 |
|
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409077 Cd Length: 108 Bit Score: 108.34 E-value: 4.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 10 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 86
Cdd:cd21228 3 KIQQNTFTRWCNEHLKCVNKRIYNLETDLSDGLRLIALLEVLSQKRMYKkynKRPTFRQMKLENVSVALEFLERESIKLV 82
|
90 100
....*....|....*....|....*.
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILHF 112
Cdd:cd21228 83 SIDSSAIVDGNLKLILGLIWTLILHY 108
|
|
| CH_ACTN3_rpt2 |
cd21289 |
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also ... |
114-229 |
9.31e-27 |
|
second calponin homology (CH) domain found in alpha-actinin-3; Alpha-actinin-3 (ACTN3), also called alpha-actinin skeletal muscle isoform 3, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN3 is a bundling protein. It is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409138 Cd Length: 124 Bit Score: 107.89 E-value: 9.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 114 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 193
Cdd:cd21289 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNVQNFHTSWKDGLALCALIHRHRPDLIDYAKLRKDDPIGNLNTAFEV 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675251 194 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 229
Cdd:cd21289 77 AEKYLDIPKMLDAEDiVNTPKPDEKAIMTYVSCFYHA 113
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1208-1996 |
1.09e-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: 120.93 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1208 AAREQLRQEKALLEEIERHGEKVEECQKFAKQYI---NAIKDYELQLITYkaqlepvaspakkpkvqsgsesviqEYVDL 1284
Cdd:TIGR02168 183 RTRENLDRLEDILNELERQLKSLERQAEKAERYKelkAELRELELALLVL-------------------------RLEEL 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1285 RTRYSELTTLTSQYikfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQE 1364
Cdd:TIGR02168 238 REELEELQEELKEA----EEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1365 EVARREEAAVDAQQQKRSIQE------ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEG 1438
Cdd:TIGR02168 314 LERQLEELEAQLEELESKLDElaeelaELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1439 ELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqALDELRLQAEEAERRLR 1518
Cdd:TIGR02168 394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE--ELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1519 QAEAERarqvqvaletaqRSAEVELQSKRASFAEKTAQLERtLQEEHVTVAQLREEAERRAQQQAEAERAREEAerelER 1598
Cdd:TIGR02168 472 EAEQAL------------DAAERELAQLQARLDSLERLQEN-LEGFSEGVKALLKNQSGLSGILGVLSELISVD----EG 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1599 WQLKANEALRLRLQA---EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQE----------------- 1658
Cdd:TIGR02168 535 YEAAIEAALGGRLQAvvvENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIegflgvakdlvkfdpkl 614
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1659 --------------------LEKQRQL-----------------------AEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1695
Cdd:TIGR02168 615 rkalsyllggvlvvddldnaLELAKKLrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEELEEKIA 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1696 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEAGRfRELAEEAARL 1771
Cdd:TIGR02168 695 ELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlSKELTELEAEI-EELEERLEEA 773
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1772 RALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAeialKEKEAENERLRRLAEDEAFQRRRLEEQAAL 1851
Cdd:TIGR02168 774 EEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIEE 849
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1852 HKADIEERLAQLRKASESELERQKGLvEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQ-- 1929
Cdd:TIGR02168 850 LSEDIESLAAEIEELEELIEELESEL-EALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQle 928
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1930 ---AELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvalEEVERLKAKVEEARRLRERAEQE 1996
Cdd:TIGR02168 929 lrlEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR----RRLKRLENKIKELGPVNLAAIEE 994
|
|
| CH_FLNC_rpt1 |
cd21310 |
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C ... |
10-115 |
2.00e-26 |
|
first calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; Filamin-C (FLN-C), also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. FLN-C contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409159 Cd Length: 125 Bit Score: 107.04 E-value: 2.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 10 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHRQVKLV 86
Cdd:cd21310 15 KIQQNTFTRWCNEHLKCVQKRLNDLQKDLSDGLRLIALLEVLSQKKMYRKyhpRPNFRQMKLENVSVALEFLDREHIKLV 94
|
90 100
....*....|....*....|....*....
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILHFQIS 115
Cdd:cd21310 95 SIDSKAIVDGNLKLILGLIWTLILHYSIS 123
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1307-2351 |
2.42e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.93 E-value: 2.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1307 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLA-EAHAQAKAQAELEAQELQRRMQEEVARR-EEAAVDAQQQKRSIQ 1384
Cdd:NF041483 254 RQAAELSRAAEQRMQEAEEALREARAEAEKVVAEAkEAAAKQLASAESANEQRTRTAKEEIARLvGEATKEAEALKAEAE 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1385 EELQhlrqssEAEIQAKAQQVEAAERSRMRIEEEIRVvrlQLETTERQrggAEgelQALRARAEEAEAQKRQAQEEAERL 1464
Cdd:NF041483 334 QALA------DARAEAEKLVAEAAEKARTVAAEDTAA---QLAKAART---AE---EVLTKASEDAKATTRAAAEEAERI 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1465 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqalDELRLQaEEAeRRLRqAEAERARQVQVA----LETAQRSAE 1540
Cdd:NF041483 399 RREAEAEADRLRGEAADQAEQLKGAAKDDTKEYRA----KTVELQ-EEA-RRLR-GEAEQLRAEAVAegerIRGEARREA 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1541 VELQSKRASFAEKTAQLERTLQEEHVTVAQLREeaerraqqqaeaerareeaerelERWQLKANE-ALRLRLQAEEVAQQ 1619
Cdd:NF041483 472 VQQIEEAARTAEELLTKAKADADELRSTATAES-----------------------ERVRTEAIErATTLRRQAEETLER 528
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1620 kslAQADAEKQKeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA-AEQELIRLRAEteqGEQQRQLLE 1698
Cdd:NF041483 529 ---TRAEAERLR----------AEAEEQAEEVRAAAERAARELREETERAIAARQAeAAEELTRLHTE---AEERLTAAE 592
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1699 EELARLQHEataATQKRQELEAELAKVRAEM-EVLLASKARAEEEsrstSEKSKQRLEAEAGRFRELAEEAA-RLRA-LA 1775
Cdd:NF041483 593 EALADARAE---AERIRREAAEETERLRTEAaERIRTLQAQAEQE----AERLRTEAAADASAARAEGENVAvRLRSeAA 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1776 EEAKRQRQLAEEDAARQRAE----AERVLTEKL----AAISEATRLKTEAEIALKEKEAENERLRRLAedeafqRRRLEE 1847
Cdd:NF041483 666 AEAERLKSEAQESADRVRAEaaaaAERVGTEAAealaAAQEEAARRRREAEETLGSARAEADQERERA------REQSEE 739
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1848 QAALHKADIEERLAQLRKASESELERQKGLV---EDTLRQRR--------QVEEEIMALKVSFEKAAA-GKAELELELGR 1915
Cdd:NF041483 740 LLASARKRVEEAQAEAQRLVEEADRRATELVsaaEQTAQQVRdsvaglqeQAEEEIAGLRSAAEHAAErTRTEAQEEADR 819
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1916 IRSnaeDTMRSKEQAELEAARQRQlaaeeeqrrreaeERVQRSLAAEEEAARQRKVALEEVERLKAKVEE-ARRLRERA- 1993
Cdd:NF041483 820 VRS---DAYAERERASEDANRLRR-------------EAQEETEAAKALAERTVSEAIAEAERLRSDASEyAQRVRTEAs 883
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1994 ------EQESARQLQLAQEAAQK-RLQAEEKAHAFVVQQREEELQQTLQQEQNMlDRLRSEAEAARRAAEEAEEAREQAE 2066
Cdd:NF041483 884 dtlasaEQDAARTRADAREDANRiRSDAAAQADRLIGEATSEAERLTAEARAEA-ERLRDEARAEAERVRADAAAQAEQL 962
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2067 REAAQS---RKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQA------------ADAE 2131
Cdd:NF041483 963 IAEATGeaeRLRAEAAETVGSAQQHAERIRTEAERVKAEAAAEAERLRTEAREEADRTLDEARKdankrrseaaeqADTL 1042
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2132 MEKHKKFAEQtLRQKAQVEQELTTLRLQlEETDHQKSILDEELQRLKAEVT-----EAARQRSQVEEELFSVRVQM---- 2202
Cdd:NF041483 1043 ITEAAAEADQ-LTAKAQEEALRTTTEAE-AQADTMVGAARKEAERIVAEATvegnsLVEKARTDADELLVGARRDAtair 1120
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2203 EELGKLKARIEAENRALilrdkdnTQRFLEEEAEKMKQVAEEAARLSVAAQEaarlrQLAEEDLAQQRALAE---KMLKE 2279
Cdd:NF041483 1121 ERAEELRDRITGEIEEL-------HERARRESAEQMKSAGERCDALVKAAEE-----QLAEAEAKAKELVSDansEASKV 1188
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 2280 KMQAVQEATRLKAEAEllqQQKELAQEQARRLQEDKEQMAQQLVEETqgfQRTLEAERQRQLEMSAEAERLK 2351
Cdd:NF041483 1189 RIAAVKKAEGLLKEAE---QKKAELVREAEKIKAEAEAEAKRTVEEG---KRELDVLVRRREDINAEISRVQ 1254
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1449-2431 |
3.22e-26 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 119.55 E-value: 3.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1449 EAEAQKRQAQEEAERLR-------RQVQDESQRKRQAEAELALRVKAE--AEAAREKQRALQALDELRLQAE-EAERRLR 1518
Cdd:NF041483 73 QAEQLLRNAQIQADQLRadaerelRDARAQTQRILQEHAEHQARLQAElhTEAVQRRQQLDQELAERRQTVEsHVNENVA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1519 QAEAERARQVQVA---LETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvaqlreEAERRAQQQAEAERAREEAERE 1595
Cdd:NF041483 153 WAEQLRARTESQArrlLDESRAEAEQALAAARAEAERLAEEARQRLGSE---------AESARAEAEAILRRARKDAERL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1596 LERWQLKANEALRlrlQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQrelAEQELEKQRQLAEGTAQQRLA 1675
Cdd:NF041483 224 LNAASTQAQEATD---HAEQLRSSTAAESDQARRQAAELSRAAEQRMQEAEEALRE---ARAEAEKVVAEAKEAAAKQLA 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1676 AeqelirlrAETeQGEQQRQLLEEELARLQHEATA-ATQKRQELEAELAKVRAEMEVLLAS---KARAEEESRSTSEKSK 1751
Cdd:NF041483 298 S--------AES-ANEQRTRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEKLVAEaaeKARTVAAEDTAAQLAK 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1752 QRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAI---------------SEATRLKTE 1816
Cdd:NF041483 369 AARTAEEVLTKASEDAKATTRAAAEEAERIRREAEAEADRLRGEAADQAEQLKGAAkddtkeyraktvelqEEARRLRGE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1817 AEIALKEKEAENERLRRLAEDEAFQR-----RRLEEQAALHKADIEErlaqLRKASESELERQKG-LVEDTLRQRRQVEE 1890
Cdd:NF041483 449 AEQLRAEAVAEGERIRGEARREAVQQieeaaRTAEELLTKAKADADE----LRSTATAESERVRTeAIERATTLRRQAEE 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1891 eimALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLA------AEEE 1964
Cdd:NF041483 525 ---TLERTRAEAERLRAEAEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAeealadARAE 601
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1965 AARQRKVALEEVERLKAKV-EEARRLRERAEQESAR-QLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqNMLD 2042
Cdd:NF041483 602 AERIRREAAEETERLRTEAaERIRTLQAQAEQEAERlRTEAAADASAARAEGE-----------------------NVAV 658
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2043 RLRSEAEaarraaeeaeeareqaereaaqsrkqvEEAERLKqsaeeqaqaqAQAQAAAEKLRKEAEQEAARRAQAEQAAL 2122
Cdd:NF041483 659 RLRSEAA---------------------------AEAERLK----------SEAQESADRVRAEAAAAAERVGTEAAEAL 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2123 kqkQAADAEMEKHKKFAEQTL------------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQ 2190
Cdd:NF041483 702 ---AAAQEEAARRRREAEETLgsaraeadqereRAREQSEELLASARKRVEEAQAEAQRLVEEADRRATELVSAAEQTAQ 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2191 -VEEELFSVRVQM-EELGKLkaRIEAENRAlilrdkDNTQRFLEEEAEKMKqvAEEAARLSVAAQEAARLRQLAEEDLAQ 2268
Cdd:NF041483 779 qVRDSVAGLQEQAeEEIAGL--RSAAEHAA------ERTRTEAQEEADRVR--SDAYAERERASEDANRLRREAQEETEA 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2269 QRALAEKMLKEkmqAVQEATRLKAEAELLQQQ-------------------KELAQEQARRLQEDKEQMAQQLVEETQGF 2329
Cdd:NF041483 849 AKALAERTVSE---AIAEAERLRSDASEYAQRvrteasdtlasaeqdaartRADAREDANRIRSDAAAQADRLIGEATSE 925
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2330 QRTLEAE-----RQRQLEMSAEAERLKLRMAEMS-RAQARAEEDAQRFRKQAEEIgeklhrTELATQEKVTLVQTLEIQR 2403
Cdd:NF041483 926 AERLTAEaraeaERLRDEARAEAERVRADAAAQAeQLIAEATGEAERLRAEAAET------VGSAQQHAERIRTEAERVK 999
|
1050 1060
....*....|....*....|....*....
gi 254675251 2404 QQSDHDAERLR-EAIAELEREKEKLKQEA 2431
Cdd:NF041483 1000 AEAAAEAERLRtEAREEADRTLDEARKDA 1028
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1370-2016 |
4.27e-26 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 119.48 E-value: 4.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1370 EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEE 1449
Cdd:PTZ00121 1034 EYGNNDDVLKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEATEEAFGKAEEAKKTETGKAEE 1113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1450 aEAQKRQAQEEAERLRRqvqdeSQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQ-AEEAERRLRQAEAERARQV 1528
Cdd:PTZ00121 1114 -ARKAEEAKKKAEDARK-----AEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKAEeARKAEDAKKAEAARKAEEV 1187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1529 QVALETaqRSAEvelQSKRASFAEKtAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALR 1608
Cdd:PTZ00121 1188 RKAEEL--RKAE---DARKAEAARK-AEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEAR 1261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1609 L--------------RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEE-----QAVRQRELAEQELEKQRQLAEGT 1669
Cdd:PTZ00121 1262 MahfarrqaaikaeeARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEakkadEAKKKAEEAKKKADAAKKKAEEA 1341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1670 AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQEL-EAELAKVRAEMEVLLASKARAEEESRSTSE 1748
Cdd:PTZ00121 1342 KKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkKADEAKKKAEEDKKKADELKKAAAAKKKAD 1421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1749 KSKQRLEA-----EAGRFRELAEEAARLRALAEEAKRQRQL---AEE----DAARQRAEAERVLTEKLAAISEATRLKTE 1816
Cdd:PTZ00121 1422 EAKKKAEEkkkadEAKKKAEEAKKADEAKKKAEEAKKAEEAkkkAEEakkaDEAKKKAEEAKKADEAKKKAEEAKKKADE 1501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1817 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA---LHKADIEERLAQLRKASESELERQKGLVEDtlrQRRQVEEEIM 1893
Cdd:PTZ00121 1502 AKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKadeAKKAEEKKKADELKKAEELKKAEEKKKAEE---AKKAEEDKNM 1578
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1894 ALKVSFEKAAAGKAELELELGRIRSnaEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL 1973
Cdd:PTZ00121 1579 ALRKAEEAKKAEEARIEEVMKLYEE--EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAE 1656
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1974 EEV----ERLKAKVEEARR----LRERAEQESARQLQLAQEAAQKRlQAEE 2016
Cdd:PTZ00121 1657 EENkikaAEEAKKAEEDKKkaeeAKKAEEDEKKAAEALKKEAEEAK-KAEE 1706
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
14-111 |
2.17e-25 |
|
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of spectrin-like proteins (including dystrophin, alpha-actinin). These domains cross-link actin filaments into bundles and networks. A calponin homology domain is predicted in yeasst Cdc24p.
Pssm-ID: 214479 [Multi-domain] Cd Length: 101 Bit Score: 103.16 E-value: 2.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 14 KTFTKWVNKHLIKA-QRHISDLYEDLRDGHNLISLLEVLSGDSLPREK---GRMRFHKLQNVQIALDYLRHRQVKLVNIR 89
Cdd:smart00033 1 KTLLRWVNSLLAEYdKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKvaaSLSRFKKIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|..
gi 254675251 90 NDDIADGnPKLTLGLIWTIILH 111
Cdd:smart00033 81 PEDLVEG-PKLILGVIWTLISL 101
|
|
| CH_SPTBN5_rpt1 |
cd21247 |
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) ... |
6-114 |
2.55e-25 |
|
first calponin homology (CH) domain found in spectrin beta chain, non-erythrocytic 5 (SPTBN5) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTBN5, also called beta-V spectrin, is a mammalian ortholog of Drosophila beta H spectrin that may play a crucial role as a longer actin-membrane cross-linker or to fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. SPTBN5 contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409096 Cd Length: 125 Bit Score: 103.68 E-value: 2.55e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 6 DERDRVQKKTFTKWVNKHLIKAQR--HISDLYEDLRDGHNLISLLEVLSGDSLPR-EKGRMRFHKLQNVQIALDYLRHR- 81
Cdd:cd21247 15 EQRMTMQKKTFTKWMNNVFSKNGAkiEITDIYTELKDGIHLLRLLELISGEQLPRpSRGKMRVHFLENNSKAITFLKTKv 94
|
90 100 110
....*....|....*....|....*....|...
gi 254675251 82 QVKLVNIRNddIADGNPKLTLGLIWTIILHFQI 114
Cdd:cd21247 95 PVKLIGPEN--IVDGDRTLILGLIWIIILRFQI 125
|
|
| CH_ACTN2_rpt2 |
cd21288 |
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also ... |
114-229 |
2.56e-25 |
|
second calponin homology (CH) domain found in alpha-actinin-2; Alpha-actinin-2 (ACTN2), also called alpha-actinin skeletal muscle isoform 2, is an F-actin cross-linking protein which is thought to anchor actin to a variety of intracellular structures. ACTN2 is a bundling protein. Its mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. It contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409137 Cd Length: 124 Bit Score: 104.00 E-value: 2.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 114 ISDIQVsgqsEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSV 193
Cdd:cd21288 1 IQDISV----EETSAKEGLLLWCQRKTAPYRNVNIQNFHTSWKDGLGLCALIHRHRPDLIDYSKLNKDDPIGNINLAMEI 76
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675251 194 AERDLGVTRLLDPED-VDVPQPDEKSIITYVSSLYDA 229
Cdd:cd21288 77 AEKHLDIPKMLDAEDiVNTPKPDERAIMTYVSCFYHA 113
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
132-227 |
2.66e-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: 103.00 E-value: 2.66e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 132 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED-VD 210
Cdd:cd21197 5 LLRWCRRQCEGYPGVNITNLTSSFRDGLAFCAILHRHRPELIDFHSLKKDNWLENNRLAFRVAETSLGIPALLDAEDmVT 84
|
90
....*....|....*..
gi 254675251 211 VPQPDEKSIITYVSSLY 227
Cdd:cd21197 85 MHVPDRLSIITYVSQYY 101
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
126-232 |
8.56e-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: 8.56e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 126 MTAKEKLLLWSQRMVEGY-QGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY--RQTNLENLDQAFSVAERDLGVTR 202
Cdd:pfam00307 1 LELEKELLRWINSHLAEYgPGVRVTNFTTDLRDGLALCALLNKLAPGLVDKKKLNksEFDKLENINLALDVAEKKLGVPK 80
|
90 100 110
....*....|....*....|....*....|.
gi 254675251 203 -LLDPEDVDvpQPDEKSIITYVSSLYDAMPR 232
Cdd:pfam00307 81 vLIEPEDLV--EGDNKSVLTYLASLFRRFQA 109
|
|
| CH |
pfam00307 |
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal ... |
11-114 |
3.60e-24 |
|
Calponin homology (CH) domain; The CH domain is found in both cytoskeletal proteins and signal transduction proteins. The CH domain is involved in actin binding in some members of the family. However in calponins there is evidence that the CH domain is not involved in its actin binding activity. Most member proteins have from two to four copies of the CH domain, however some proteins such as calponin have only a single copy.
Pssm-ID: 425596 [Multi-domain] Cd Length: 109 Bit Score: 100.05 E-value: 3.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 11 VQKKTFTKWVNKHLIKAQRH--ISDLYEDLRDGHNLISLLEVLSGDSLP-REKGRMRFHKLQNVQIALDYLRHRQ-VKLV 86
Cdd:pfam00307 2 ELEKELLRWINSHLAEYGPGvrVTNFTTDLRDGLALCALLNKLAPGLVDkKKLNKSEFDKLENINLALDVAEKKLgVPKV 81
|
90 100
....*....|....*....|....*...
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILHFQI 114
Cdd:pfam00307 82 LIEPEDLVEGDNKSVLTYLASLFRRFQA 109
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
128-227 |
4.60e-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: 99.56 E-value: 4.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 128 AKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 207
Cdd:cd21252 1 ARRALQAWCRRQCEGYPGVEIRDLSSSFRDGLAFCAILHRHRPDLIDFDSLSKDNVYENNRLAFEVAERELGIPALLDPE 80
|
90 100
....*....|....*....|.
gi 254675251 208 D-VDVPQPDEKSIITYVSSLY 227
Cdd:cd21252 81 DmVSMKVPDCLSIMTYVSQYY 101
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1303-2019 |
5.21e-24 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 112.23 E-value: 5.21e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1303 SETLRRMEEEERL---AEQQRAE---ERERLaEVEAALEKQRQLAEAHAQAK---AQAELEAQELQRRMQEEVAR-REEA 1372
Cdd:NF041483 433 AKTVELQEEARRLrgeAEQLRAEavaEGERI-RGEARREAVQQIEEAARTAEellTKAKADADELRSTATAESERvRTEA 511
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1373 AVDAQQQKRSIQEELQHLRqsSEAEiQAKAQQVEAAERSRMRIEEEIRVVRLQLE-TTERQRGGAEGELQALRARAEE-- 1449
Cdd:NF041483 512 IERATTLRRQAEETLERTR--AEAE-RLRAEAEEQAEEVRAAAERAARELREETErAIAARQAEAAEELTRLHTEAEErl 588
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1450 --AEAQKRQAQEEAERLRRQVQDESQRKRqaeaelalrvkaeAEAArEKQRALQAldelrlQAEEAERRLRQAEAERARQ 1527
Cdd:NF041483 589 taAEEALADARAEAERIRREAAEETERLR-------------TEAA-ERIRTLQA------QAEQEAERLRTEAAADASA 648
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1528 VQVALEtaqrSAEVELQSKrasfaektaqlertlqeehvtvaqlreeaerraqqqaeaerareeaerelerwqlKANEAL 1607
Cdd:NF041483 649 ARAEGE----NVAVRLRSE-------------------------------------------------------AAAEAE 669
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1608 RLRLQAEEVAQQ-KSLAQADAEKqkeEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELI---RL 1683
Cdd:NF041483 670 RLKSEAQESADRvRAEAAAAAER---VGTEAAEALAAAQEEAARRRREAEETLGSARAEADQERERAREQSEELLasaRK 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1684 RAETEQGEQQRqLLEEELARLQHEATAATQKRQELEAELAKV--RAEMEV--LLASKARAEEESRSTSEKSKQRLEAEAG 1759
Cdd:NF041483 747 RVEEAQAEAQR-LVEEADRRATELVSAAEQTAQQVRDSVAGLqeQAEEEIagLRSAAEHAAERTRTEAQEEADRVRSDAY 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1760 RFRELA-EEAARLRALA-EEAKRQRQLAEEDAARQRAEAERVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAED 1837
Cdd:NF041483 826 AERERAsEDANRLRREAqEETEAAKALAERTVSEAIAEAERLRSD---ASEYAQRVRTEASDTLASAEQDAARTRADARE 902
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1838 EAFQRRrlEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAElelelgRIR 1917
Cdd:NF041483 903 DANRIR--SDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLIAEATGEAE------RLR 974
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1918 SNAEDTMRSKEQAeleAARQRQLAAEEEQRrreaeervqrslaAEEEAARQRKVALEEVERL--KAKVEEARRLRERAEQ 1995
Cdd:NF041483 975 AEAAETVGSAQQH---AERIRTEAERVKAE-------------AAAEAERLRTEAREEADRTldEARKDANKRRSEAAEQ 1038
|
730 740
....*....|....*....|....
gi 254675251 1996 ESARQLQLAQEAAQKRLQAEEKAH 2019
Cdd:NF041483 1039 ADTLITEAAAEADQLTAKAQEEAL 1062
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1646-2484 |
6.17e-24 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 112.07 E-value: 6.17e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1646 EQAVRQRELAEQELEKQRQLAegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1725
Cdd:TIGR02168 210 EKAERYKELKAELRELELALL---VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEEL 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1726 RAEMEVLLASKARAEEESRSTSEkskqrleaeagRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK-- 1803
Cdd:TIGR02168 287 QKELYALANEISRLEQQKQILRE-----------RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELes 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1804 -LAAISEATRLKTEAEIALKEKEAENERLRRLaedeafqRRRLEEQAALHKADIEERLAQLrKASESELERQKGLVEDtl 1882
Cdd:TIGR02168 356 lEAELEELEAELEELESRLEELEEQLETLRSK-------VAQLELQIASLNNEIERLEARL-ERLEDRRERLQQEIEE-- 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1883 RQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEdtmrsKEQAELEAARQRQLaaeeeqrrreaeervqrSLAAE 1962
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALE-----ELREELEEAEQALD-----------------AAERE 483
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1963 EEAARQRKVALEEV-ERLKAKVEEARRLRERAEQ------------ESARQLQLAQEAA---------QKRLQAEEKAHA 2020
Cdd:TIGR02168 484 LAQLQARLDSLERLqENLEGFSEGVKALLKNQSGlsgilgvlseliSVDEGYEAAIEAAlggrlqavvVENLNAAKKAIA 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2021 FVVQQREEELQQTLqqeqnmLDRLRSEAEAARRAAEEAEEAREQAEREAAqsrkqVEEAERLKQSAEEQAQAQAQAQAAA 2100
Cdd:TIGR02168 564 FLKQNELGRVTFLP------LDSIKGTEIQGNDREILKNIEGFLGVAKDL-----VKFDPKLRKALSYLLGGVLVVDDLD 632
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2101 EKLRKEAEQEAARRAQAEQAALKQKQAADAEmeKHKKFAEQTLRQKaqveQELTTLRLQLEETDHQKSILDEELQRLKAE 2180
Cdd:TIGR02168 633 NALELAKKLRPGYRIVTLDGDLVRPGGVITG--GSAKTNSSILERR----REIEELEEKIEELEEKIAELEKALAELRKE 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2181 VTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALiLRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQ 2260
Cdd:TIGR02168 707 LEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL-EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIE 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2261 LAEEDLAQQRALAEKmLKEKMQAVQ-EATRLKAEAellqQQKELAQEQARRLQEDKEQMAQQLVEETQgfqrtleaerqr 2339
Cdd:TIGR02168 786 ELEAQIEQLKEELKA-LREALDELRaELTLLNEEA----ANLRERLESLERRIAATERRLEDLEEQIE------------ 848
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2340 qlEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE 2419
Cdd:TIGR02168 849 --ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQ 926
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 2420 LEREKEKLKQE-AKLLQLKSEEMQTVQQEqilqetqALQKSFLSEKDSLLQRERfIEQEKAKLEQL 2484
Cdd:TIGR02168 927 LELRLEGLEVRiDNLQERLSEEYSLTLEE-------AEALENKIEDDEEEARRR-LKRLENKIKEL 984
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
127-227 |
1.13e-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: 98.27 E-value: 1.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 206
Cdd:cd21198 1 SSGQDLLEWCQEVTKGYRGVKITNLTTSWRNGLAFCAILHHFRPDLIDFSSLSPHDIKENCKLAFDAAAK-LGIPRLLDP 79
|
90 100
....*....|....*....|..
gi 254675251 207 EDVDVPQ-PDEKSIITYVSSLY 227
Cdd:cd21198 80 ADMVLLSvPDKLSVMTYLHQIR 101
|
|
| CH_CTX_rpt2 |
cd21226 |
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
130-230 |
1.37e-23 |
|
second calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409075 Cd Length: 103 Bit Score: 97.92 E-value: 1.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 130 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPEDV 209
Cdd:cd21226 3 DGLLAWCRQTTEGYDGVNITSFKSSFNDGRAFLALLHAYDPELFKQAAIEQMDAEARLNLAFDFAEKKLGIPKLLEAEDV 82
|
90 100
....*....|....*....|.
gi 254675251 210 DVPQPDEKSIITYVSSLYDAM 230
Cdd:cd21226 83 MTGNPDERSIVLYTSLFYHAF 103
|
|
| CH_CLMN_rpt2 |
cd21245 |
second calponin homology (CH) domain found in calmin and similar proteins; Calmin, also called ... |
127-231 |
7.96e-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: 96.01 E-value: 7.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYqGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 206
Cdd:cd21245 3 KAIKALLNWVQRRTRKY-GVAVQDFGSSWRSGLAFLALIKAIDPSLVDMRQALEKSPRENLEDAFRIAQESLGIPPLLEP 81
|
90 100
....*....|....*....|....*
gi 254675251 207 EDVDVPQPDEKSIITYVSSLYDAMP 231
Cdd:cd21245 82 EDVMVDSPDEQSIMTYVAQFLEHFP 106
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
981-1526 |
1.42e-22 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 107.33 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 981 ARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKvlalpepspaaptLRSELELTLGKLEQVRSLSAIYLEKLKTISLVI 1060
Cdd:COG1196 252 EAELEELEAELAELEAELEELRLELEELELELEE-------------AQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1061 RSTQGAEEVLKTHEEQLKEAQAvpATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVE 1140
Cdd:COG1196 319 EELEEELAELEEELEELEEELE--ELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAA 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1141 RWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAvpiancqAAREQLRQEKALL 1220
Cdd:COG1196 397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEE-------EEEALLELLAELL 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1221 EEIERHGEKVEEcqkfAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyik 1300
Cdd:COG1196 470 EEAALLEAALAE----LLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAA------ 539
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1301 fisetlrrMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEA----HAQAKAQAELEAQELQRRMQEEVARREEAAVDA 1376
Cdd:COG1196 540 --------LEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRAtflpLDKIRARAALAAALARGAIGAAVDLVASDLREA 611
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1377 QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1456
Cdd:COG1196 612 DARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEE 691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1457 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQA-----------------EEAERRLRQ 1519
Cdd:COG1196 692 ELELEEALLAEEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEelleeealeelpeppdlEELERELER 771
|
....*..
gi 254675251 1520 AEAERAR 1526
Cdd:COG1196 772 LEREIEA 778
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1316-2020 |
1.69e-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: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1316 AEQQRAEERERLAEVEAAL-EKQRQLAEAHAQA-KAQAELEAQELQRRMQEEV-ARREEAAVDAQQQKRSIQEELQHLRQ 1392
Cdd:TIGR02168 177 TERKLERTRENLDRLEDILnELERQLKSLERQAeKAERYKELKAELRELELALlVLRLEELREELEELQEELKEAEEELE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1393 SSEAEIQAKAQQVEAAERSRMRIEEEIRVvrlqletterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRR------ 1466
Cdd:TIGR02168 257 ELTAELQELEEKLEELRLEVSELEEEIEE--------------LQKELYALANEISRLEQQKQILRERLANLERqleele 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1467 -QVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLR--QAEAERarqvqvaletaQRSAEVEL 1543
Cdd:TIGR02168 323 aQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEelEEQLET-----------LRSKVAQL 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1544 QSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLA 1623
Cdd:TIGR02168 392 ELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELE 471
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1624 QADAEKQKEeaerearrrgKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQ---------ELIRLRAETEQG--- 1690
Cdd:TIGR02168 472 EAEQALDAA----------ERELAQLQARlDSLERLQENLEGFSEGVKALLKNQSGlsgilgvlsELISVDEGYEAAiea 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1691 --------------EQQRQ----LLEEELARL----------------QHEATAATQKRQELEAELAKVRAEMEVLLA-- 1734
Cdd:TIGR02168 542 alggrlqavvvenlNAAKKaiafLKQNELGRVtflpldsikgteiqgnDREILKNIEGFLGVAKDLVKFDPKLRKALSyl 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1735 --------SKARAEEESRSTSEK-----------------SKQRLEAEAGRF---RELAEEAARLRALAEEAKRQRQlAE 1786
Cdd:TIGR02168 622 lggvlvvdDLDNALELAKKLRPGyrivtldgdlvrpggviTGGSAKTNSSILerrREIEELEEKIEELEEKIAELEK-AL 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1787 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEErLAQLRKA 1866
Cdd:TIGR02168 701 AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE-AEEELAE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1867 SESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQlaaeeeq 1946
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSE------- 852
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1947 rrreAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLqlaQEAAQKRLQAEEKAHA 2020
Cdd:TIGR02168 853 ----DIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEEL---RELESKRSELRRELEE 919
|
|
| CH_FLN-like_rpt2 |
cd21184 |
second calponin homology (CH) domain found in the filamin family; The filamin family includes ... |
127-225 |
2.42e-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: 94.61 E-value: 2.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYqglRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVY-RQTNLENLDQAFSVAERDLGVTRLLD 205
Cdd:cd21184 1 SGKSLLLEWVNSKIPEY---KVKNFTTDWNDGKALAALVDALKPGLIPDNESLdKENPLENATKAMDIAEEELGIPKIIT 77
|
90 100
....*....|....*....|
gi 254675251 206 PEDVDVPQPDEKSIITYVSS 225
Cdd:cd21184 78 PEDMVSPNVDELSVMTYLSY 97
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1028-1866 |
5.61e-22 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 105.52 E-value: 5.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1028 LRSELELTLGKLEQVRSLSaiylEKLKTISLVIRSTQGAeeVLKTHEEQLKEAQAvpATLQELEATKASLKKLRAQAEAQ 1107
Cdd:TIGR02168 194 ILNELERQLKSLERQAEKA----ERYKELKAELRELELA--LLVLRLEELREELE--ELQEELKEAEEELEELTAELQEL 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1108 QPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAW 1187
Cdd:TIGR02168 266 EEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1188 LQDAKRRQEQIQAVPIANC----------QAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQ 1257
Cdd:TIGR02168 346 LEELKEELESLEAELEELEaeleelesrlEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1258 LEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ 1337
Cdd:TIGR02168 426 LLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE----LREELEEAEQALDAAERELAQLQARLDSLERLQENL 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1338 RQLAEAHAQAKAQAELEAQELQRRMQE-EVARREEAAVDAQQQKR----------SIQEELQHLRQSSE------AEIQA 1400
Cdd:TIGR02168 502 EGFSEGVKALLKNQSGLSGILGVLSELiSVDEGYEAAIEAALGGRlqavvvenlnAAKKAIAFLKQNELgrvtflPLDSI 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1401 KAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAea 1480
Cdd:TIGR02168 582 KGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDGDLVRPGG-- 659
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1481 eLALRVKAEAEAAREKQRalQALDELRLQAEEAERRLRQAEAE--RARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1558
Cdd:TIGR02168 660 -VITGGSAKTNSSILERR--REIEELEEKIEELEEKIAELEKAlaELRKELEELEEELEQLRKELEELSRQISALRKDLA 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1559 RtLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERwQLKANEALRLRLQAeEVAQQKSLAQADAEKQKEEAEREA 1638
Cdd:TIGR02168 737 R-LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEE-ELAEAEAEIEELEA-QIEQLKEELKALREALDELRAELT 813
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1639 RRRGKAEEQAVRQRELaEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQEL 1718
Cdd:TIGR02168 814 LLNEEAANLRERLESL-ERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALL 892
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1719 EAELAKVRAEMEVLL--ASKARAE-EESRSTSEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEDAARQRA 1794
Cdd:TIGR02168 893 RSELEELSEELRELEskRSELRRElEELREKLAQLELRLEGLEVRIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARR 972
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1795 EAERvLTEKLAAISEATRLkteaeiALKEKEAENERLRRLAEdeafqrrrleeqaalHKADIEERLAQLRKA 1866
Cdd:TIGR02168 973 RLKR-LENKIKELGPVNLA------AIEEYEELKERYDFLTA---------------QKEDLTEAKETLEEA 1022
|
|
| SH3_10 |
pfam17902 |
SH3 domain; This entry represents an SH3 domain. |
758-824 |
7.46e-22 |
|
SH3 domain; This entry represents an SH3 domain.
Pssm-ID: 407754 Cd Length: 65 Bit Score: 91.55 E-value: 7.46e-22
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 758 QLKPRNpaHPVRGHVPLIAVCDYKQVEVTVHKGDQCQLVGPAQPSHWKVLSGSSSEAAVPSVCFLVP 824
Cdd:pfam17902 1 PLKQRR--SPVTRPIPVKALCDYKQGEVTVEKGEECTLLDNSDREKWKVQTSSGVEKLVPSVCFLIP 65
|
|
| CH_FLNB_rpt1 |
cd21309 |
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B ... |
10-115 |
7.51e-22 |
|
first calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; Filamin-B (FLN-B) is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton. It may promote orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It anchors various transmembrane proteins to the actin cytoskeleton. FLN-B contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409158 Cd Length: 131 Bit Score: 94.38 E-value: 7.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 10 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 86
Cdd:cd21309 16 KIQQNTFTRWCNEHLKCVNKRIGNLQTDLSDGLRLIALLEVLSQKRMYRkyhQRPTFRQMQLENVSVALEFLDRESIKLV 95
|
90 100
....*....|....*....|....*....
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILHFQIS 115
Cdd:cd21309 96 SIDSKAIVDGNLKLILGLVWTLILHYSIS 124
|
|
| CH_FLNA_rpt1 |
cd21308 |
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A ... |
10-115 |
8.00e-22 |
|
first calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; Filamin-A (FLN-A) is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also anchors various transmembrane proteins to the actin cytoskeleton and serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-A contains two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409157 Cd Length: 129 Bit Score: 94.00 E-value: 8.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 10 RVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR---EKGRMRFHKLQNVQIALDYLRHRQVKLV 86
Cdd:cd21308 19 KIQQNTFTRWCNEHLKCVSKRIANLQTDLSDGLRLIALLEVLSQKKMHRkhnQRPTFRQMQLENVSVALEFLDRESIKLV 98
|
90 100
....*....|....*....|....*....
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILHFQIS 115
Cdd:cd21308 99 SIDSKAIVDGNLKLILGLIWTLILHYSIS 127
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1511-2385 |
3.06e-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: 3.06e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1511 EEAERRLRQAEAERARqVQVALETAQRSAE-VELQSKRAS-FAEKTAQLERTlqEEHVTVAQLREEAERRAQQQAeaera 1588
Cdd:TIGR02168 175 KETERKLERTRENLDR-LEDILNELERQLKsLERQAEKAErYKELKAELREL--ELALLVLRLEELREELEELQE----- 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1589 reeaerelerwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgKAEEQAVRQRELAE-----QELEKQR 1663
Cdd:TIGR02168 247 -----------ELKEAEEELEELTAELQELEEKLEELRLEVSE-----------LEEEIEELQKELYAlaneiSRLEQQK 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1664 QLAEgtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEvllaskaraeeES 1743
Cdd:TIGR02168 305 QILR---ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELE-----------EL 370
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1744 RSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK-LAAISEATRLKTEAEIALK 1822
Cdd:TIGR02168 371 ESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLeEAELKELQAELEELEEELE 450
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1823 EKEAENERLRRLAEdEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVED--TLRQRRQVEEEIMALKVSFE 1900
Cdd:TIGR02168 451 ELQEELERLEEALE-ELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGvkALLKNQSGLSGILGVLSELI 529
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1901 KAAAG-KAELELELGRIRSNAedTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERL 1979
Cdd:TIGR02168 530 SVDEGyEAAIEAALGGRLQAV--VVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDL 607
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1980 KAKVEEARRL----------RERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAE 2049
Cdd:TIGR02168 608 VKFDPKLRKAlsyllggvlvVDDLDNALELAKKLRPGYRIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIE 687
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2050 AARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAAD 2129
Cdd:TIGR02168 688 ELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELE 767
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2130 AEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLK 2209
Cdd:TIGR02168 768 ERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2210 ARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATR 2289
Cdd:TIGR02168 848 EELSEDIESLAAEIEE-----LEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELRE 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2290 LKAEAEL----LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQLEMS------------AEAERLKLR 2353
Cdd:TIGR02168 923 KLAQLELrlegLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR-RRLKRLENKikelgpvnlaaiEEYEELKER 1001
|
890 900 910
....*....|....*....|....*....|..
gi 254675251 2354 MAEMSRAQaraeEDAQRFRKQAEEIGEKLHRT 2385
Cdd:TIGR02168 1002 YDFLTAQK----EDLTEAKETLEEAIEEIDRE 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1841-2430 |
8.94e-21 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 101.55 E-value: 8.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1841 QRRRLEEQAA---LHKADIEERLAQLRKASE---------SELERQKGLVEdtlRQRRQVEE-------------EIMAL 1895
Cdd:COG1196 156 ERRAIIEEAAgisKYKERKEEAERKLEATEEnlerledilGELERQLEPLE---RQAEKAERyrelkeelkeleaELLLL 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1896 KVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRkvaleE 1975
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIAR-----L 307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1976 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKahafvvQQREEELQQTLQQEQNMLDRLRSEAEAARRAA 2055
Cdd:COG1196 308 EERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA------EEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2056 EEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKH 2135
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2136 KKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAE 2215
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2216 NRAL-----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRL 2290
Cdd:COG1196 542 AALAaalqnIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2291 KAEAELLQQQKELAQEQARRLQEDKE------QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARA 2364
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLRevtlegEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 2365 EEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREA--------IAELEREKEKLKQE 2430
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALeelpeppdLEELERELERLERE 775
|
|
| CH_MICAL2_3-like |
cd21195 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2 (MICAL-2), ... |
131-228 |
1.12e-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: 90.10 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 131 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 209
Cdd:cd21195 8 KLLTWCQQQTEGYQHVNVTDLTTSWRSGLALCAIIHRFRPELINFDSLNEDDAVENNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 254675251 210 DVPQPDEKSIITYVSSLYD 228
Cdd:cd21195 88 SAQEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1090-1892 |
1.36e-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: 100.90 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1090 LEATKASLKKLRAQAEAQQPvFNTLRDELRgaqevgerlqqrhgerDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQ 1169
Cdd:TIGR02168 195 LNELERQLKSLERQAEKAER-YKELKAELR----------------ELELALLVLRLEELREELEELQEELKEAEEELEE 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1170 LGRQLRYYRESADPLSAWLQDAKRRQEQIQAV------PIANC----QAAREQLRQEKALLEEIERHGEKVEECQKFAKQ 1239
Cdd:TIGR02168 258 LTAELQELEEKLEELRLEVSELEEEIEELQKElyalanEISRLeqqkQILRERLANLERQLEELEAQLEELESKLDELAE 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1240 YINAIKDYELQLITYKAQLEpvASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEE-ERLAEQ 1318
Cdd:TIGR02168 338 ELAELEEKLEELKEELESLE--AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARlERLEDR 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1319 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR------Q 1392
Cdd:TIGR02168 416 RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQarldslE 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1393 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAE----GELQALRARAEEAEAQKRQAQEEAERLRR-- 1466
Cdd:TIGR02168 496 RLQENLEGFSEGVKALLKNQSGLSGILGVLSELISVDEGYEAAIEaalgGRLQAVVVENLNAAKKAIAFLKQNELGRVtf 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1467 --------QVQDESQRKRQAEAELALRVKAEAEAAREK-QRALQALDELRLQAEEAERRLRQAEAERARQVQVALE---- 1533
Cdd:TIGR02168 576 lpldsikgTEIQGNDREILKNIEGFLGVAKDLVKFDPKlRKALSYLLGGVLVVDDLDNALELAKKLRPGYRIVTLDgdlv 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1534 ----------TAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1603
Cdd:TIGR02168 656 rpggvitggsAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL 735
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1604 NEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRL 1683
Cdd:TIGR02168 736 ARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL 815
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1684 RAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRE 1763
Cdd:TIGR02168 816 NEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSE 895
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1764 LAEEAARLRALAEEAKRQRQLAEE------DAARQRAEAERVLTEKLAAISEatRLKTEAEIALkEKEAENERLRRLAED 1837
Cdd:TIGR02168 896 LEELSEELRELESKRSELRRELEElreklaQLELRLEGLEVRIDNLQERLSE--EYSLTLEEAE-ALENKIEDDEEEARR 972
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1838 EAFQ-RRRLEEQAALHKADIEErlaqLRKASE--SELERQKglvEDTLRQRRQVEEEI 1892
Cdd:TIGR02168 973 RLKRlENKIKELGPVNLAAIEE----YEELKEryDFLTAQK---EDLTEAKETLEEAI 1023
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1821-2573 |
2.82e-20 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 100.22 E-value: 2.82e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1821 LKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESE-LERQKGLVEDTlrqrrqveeeimalkvsf 1899
Cdd:PTZ00121 1042 LKEKDIIDEDIDGNHEGKAEAKAHVGQDEGLKPSYKDFDFDAKEDNRADEaTEEAFGKAEEA------------------ 1103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1900 EKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQrqlaaeeeqrrreaeervqrslaaEEEAARQRKVALEEVERl 1979
Cdd:PTZ00121 1104 KKTETGKAEEARKAEEAKKKAEDARKAEEARKAEDARK------------------------AEEARKAEDAKRVEIAR- 1158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1980 kaKVEEARRLRERAEQESARQLQLAQEAAQKRlQAEEKAHAFVVQQREEElqqtlqqeqnmldRLRSEAEAARRAAEEAE 2059
Cdd:PTZ00121 1159 --KAEDARKAEEARKAEDAKKAEAARKAEEVR-KAEELRKAEDARKAEAA-------------RKAEEERKAEEARKAED 1222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2060 EAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQ--KQAADAEMEKHKK 2137
Cdd:PTZ00121 1223 AKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKAEekKKADEAKKAEEKK 1302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2138 FAEQtLRQKAQVEQELTTLRLQLEETDHQKSILDE--ELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAE 2215
Cdd:PTZ00121 1303 KADE-AKKKAEEAKKADEAKKKAEEAKKKADAAKKkaEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKAD 1381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2216 NraliLRDKDNTQRfleeEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralaekmLKEKMQAVQEATRLKAEAE 2295
Cdd:PTZ00121 1382 A----AKKKAEEKK----KADEAKKKAEEDKKKADELKKAAAAKKKADE------------AKKKAEEKKKADEAKKKAE 1441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2296 LLQQQKELAQ--EQARRLQEDKEQmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKlrmAEMSRAQARAEEDAQRFRK 2373
Cdd:PTZ00121 1442 EAKKADEAKKkaEEAKKAEEAKKK-AEEAKKADEAKKKAEEAKKADEAKKKAEEAKKK---ADEAKKAAEAKKKADEAKK 1517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2374 QAE-EIGEKLHRTELATQEKvtlvqtlEIQRQQSDHDAERLREAiAELEREKEKLKQEAKllqlKSEEMQTVQQEQILQE 2452
Cdd:PTZ00121 1518 AEEaKKADEAKKAEEAKKAD-------EAKKAEEKKKADELKKA-EELKKAEEKKKAEEA----KKAEEDKNMALRKAEE 1585
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2453 TQALQKSFLSEKDSLLQrerfiEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMAsmEEARR----RQREAE 2528
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYE-----EEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEA--EEKKKaeelKKAEEE 1658
|
730 740 750 760
....*....|....*....|....*....|....*....|....*.
gi 254675251 2529 EGVRRKQEELQHLEQQRQQQEKLLAEENQRLR-ERLQRLEEEHRAA 2573
Cdd:PTZ00121 1659 NKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAaEALKKEAEEAKKA 1704
|
|
| CH_EHBP1L1 |
cd21255 |
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar ... |
127-226 |
4.41e-20 |
|
calponin homology (CH) domain found in EH domain-binding protein 1-like protein 1 and similar proteins; EHBP1L1 may act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409104 Cd Length: 105 Bit Score: 88.31 E-value: 4.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 206
Cdd:cd21255 1 SSSQSLLEWCQEVTAGYRGVRVTNFTTSWRNGLAFCAILHHFHPDLVDYESLDPLDIKENNKKAFEAFAS-LGVPRLLEP 79
|
90 100
....*....|....*....|.
gi 254675251 207 ED-VDVPQPDEKSIITYVSSL 226
Cdd:cd21255 80 ADmVLLPIPDKLIVMTYLCQL 100
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
127-227 |
1.43e-19 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 86.63 E-value: 1.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDP 206
Cdd:cd21200 1 SIKQMLLEWCQAKTRGYEHVDITNFSSSWSDGMAFCALIHHFFPDAFDYSSLDPKNRRKNFELAFSTAEELADIAPLLEV 80
|
90 100
....*....|....*....|...
gi 254675251 207 EDVDV--PQPDEKSIITYVSSLY 227
Cdd:cd21200 81 EDMVRmgNRPDWKCVFTYVQSLY 103
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1491-2431 |
1.48e-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: 1.48e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1491 EAAREKQRALQALDELRLQAEEAERRL----RQAE-AERARQVQVALETAQRSAEV-ELQSKRASFAEKTAQLERTLQEE 1564
Cdd:TIGR02168 176 ETERKLERTRENLDRLEDILNELERQLksleRQAEkAERYKELKAELRELELALLVlRLEELREELEELQEELKEAEEEL 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1565 HVTVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgka 1644
Cdd:TIGR02168 256 EELTAELQELEEK------------------LEELRLEVSELEEEIEELQKELYALANEISRLEQQK------------- 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1645 EEQAVRQRELAEQELEKQRQLAEgTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK 1724
Cdd:TIGR02168 305 QILRERLANLERQLEELEAQLEE-LESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1725 VRAEMEVLLASKARAEEEsRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAErvLTEKL 1804
Cdd:TIGR02168 384 LRSKVAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEE--LERLE 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1805 AAISEATRLKTEAEIALKEKEAENERLR-RLAEDEAFQRRRLEEQAALHKAdieerlaqlrKASESELERQKGLVEDTLR 1883
Cdd:TIGR02168 461 EALEELREELEEAEQALDAAERELAQLQaRLDSLERLQENLEGFSEGVKAL----------LKNQSGLSGILGVLSELIS 530
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1884 qrrqVEEEimalkvsFEKAaagkaeLELELGRIRSNAedTMRSKEQAELEAARQRQlaaeeeqrrreaeervqrslaaee 1963
Cdd:TIGR02168 531 ----VDEG-------YEAA------IEAALGGRLQAV--VVENLNAAKKAIAFLKQ------------------------ 567
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1964 eaARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEK---AHAFVVQQREEELQQTLQQEQNM 2040
Cdd:TIGR02168 568 --NELGRVTFLPLDSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKLRKALSyllGGVLVVDDLDNALELAKKLRPGY 645
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2041 ldRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQA 2120
Cdd:TIGR02168 646 --RIVTLDGDLVRPGGVITGGSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEE 723
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2121 ALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRv 2200
Cdd:TIGR02168 724 LSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALR- 802
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2201 qmEELGKLKARIEAENRAL--ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLK 2278
Cdd:TIGR02168 803 --EALDELRAELTLLNEEAanLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLN 880
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2279 EKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRtLEAERQRQLEMSAEAERLKLRMAEms 2358
Cdd:TIGR02168 881 ERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEG-LEVRIDNLQERLSEEYSLTLEEAE-- 957
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2359 RAQARAEEDAQRFRKQAEEIGEKLHR----TELATQEKVTLVQTLE-IQRQQSDHDA--ERLREAIAELEREKEKLKQEA 2431
Cdd:TIGR02168 958 ALENKIEDDEEEARRRLKRLENKIKElgpvNLAAIEEYEELKERYDfLTAQKEDLTEakETLEEAIEEIDREARERFKDT 1037
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1403-2219 |
2.36e-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: 97.05 E-value: 2.36e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1403 QQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEG-----------ELQALRARAEEAEAQKRQAQEEAERLRRQVQDE 1471
Cdd:TIGR02168 179 RKLERTRENLDRLEDILNELERQLKSLERQAEKAERykelkaelrelELALLVLRLEELREELEELQEELKEAEEELEEL 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1472 SQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEveLQSKRASFA 1551
Cdd:TIGR02168 259 TAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE--LESKLDELA 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1552 EKTAQLERTLQEEHVTVAQLREEaerraqqqaeaerareeaereLERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQK 1631
Cdd:TIGR02168 337 EELAELEEKLEELKEELESLEAE---------------------LEELEAELEELESRLEELEEQLETLRSKVAQLELQI 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1632 EEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAA 1711
Cdd:TIGR02168 396 ASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALEELREELEEA 473
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1712 TQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA---- 1785
Cdd:TIGR02168 474 EQALDAAERELAQLQARLDSLERLQENLEGFSEGVKAllKNQSGLSGILGVLSELISVDEGYEAAIEAALGGRLQAvvve 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1786 EEDAARQRAEAERVLTEKLAAISEATRLKteaeialkEKEAENERLRRLAEDEAFQR--RRLEEQAALHKADIEERLAQL 1863
Cdd:TIGR02168 554 NLNAAKKAIAFLKQNELGRVTFLPLDSIK--------GTEIQGNDREILKNIEGFLGvaKDLVKFDPKLRKALSYLLGGV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1864 RKASEselerqkglVEDTLRQRRQVEEEIM-------------ALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQA 1930
Cdd:TIGR02168 626 LVVDD---------LDNALELAKKLRPGYRivtldgdlvrpggVITGGSAKTNSSILERRREIEELEEKIEELEEKIAEL 696
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1931 ELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQK 2010
Cdd:TIGR02168 697 EKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2011 RLQAEEKAHAfvVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKqsaeeqa 2090
Cdd:TIGR02168 777 LAEAEAEIEE--LEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQI------- 847
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2091 QAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSIL 2170
Cdd:TIGR02168 848 EELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQL 927
|
810 820 830 840
....*....|....*....|....*....|....*....|....*....
gi 254675251 2171 DEELQRLKAEVteaARQRSQVEEElfsVRVQMEELGKLKARIEAENRAL 2219
Cdd:TIGR02168 928 ELRLEGLEVRI---DNLQERLSEE---YSLTLEEAEALENKIEDDEEEA 970
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1438-2332 |
3.07e-19 |
|
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: 96.58 E-value: 3.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1438 GELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERR 1516
Cdd:pfam02463 163 AGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKlKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1517 LRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHvtvaqlreeaeRRAQQQAEAERAREEAEREL 1596
Cdd:pfam02463 243 QELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLL-----------AKEEEELKSELLKLERRKVD 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1597 ERWQLKANEALRLRLQAEEVAQQKSLAQAdaEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1676
Cdd:pfam02463 312 DEEKLKESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1677 EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEA 1756
Cdd:pfam02463 390 AKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKLLKDELELKK 469
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1757 EagrFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAE 1836
Cdd:pfam02463 470 S---EDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAIS 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1837 DEAFQRRRLEEQAALHKADIEERLAQLRKASESeLERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRI 1916
Cdd:pfam02463 547 TAVIVEVSATADEVEERQKLVRALTELPLGARK-LRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVV 625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1917 RSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQE 1996
Cdd:pfam02463 626 EGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKE 705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1997 SARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQV 2076
Cdd:pfam02463 706 QREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEK 785
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2077 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTL 2156
Cdd:pfam02463 786 LKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITK 865
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2157 RLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAE 2236
Cdd:pfam02463 866 EELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEA 945
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2237 KMKQVAEEAarlsvaaqeaarLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE 2316
Cdd:pfam02463 946 DEKEKEENN------------KEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELEKERLEEEKKKLIRAIIE 1013
|
890
....*....|....*.
gi 254675251 2317 QMAQQLVEETQGFQRT 2332
Cdd:pfam02463 1014 ETCQRLKEFLELFVSI 1029
|
|
| CH_MICAL3 |
cd21251 |
calponin homology (CH) domain found in molecule interacting with CasL protein 3; MICAL-3 is a ... |
123-228 |
3.33e-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: 3.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 123 SEDMTAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTR 202
Cdd:cd21251 1 NESVARSSKLLGWCQRQTEGYAGVNVTDLTMSWKSGLALCAIIHRYRPDLIDFDSLDEQDVEKNNQLAFDIAEKEFGISP 80
|
90 100
....*....|....*....|....*..
gi 254675251 203 LLDPEDV-DVPQPDEKSIITYVSSLYD 228
Cdd:cd21251 81 IMTGKEMaSVGEPDKLSMVMYLTQFYE 107
|
|
| CH |
smart00033 |
Calponin homology domain; Actin binding domains present in duplicate at the N-termini of ... |
130-226 |
3.73e-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: 3.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 130 EKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN----LENLDQAFSVAERDLGVTRLLD 205
Cdd:smart00033 1 KTLLRWVNSLLAEYDKPPVTNFSSDLKDGVALCALLNSLSPGLVDKKKVAASLSrfkkIENINLALSFAEKLGGKVVLFE 80
|
90 100
....*....|....*....|.
gi 254675251 206 PEDVDVPQPDEKSIITYVSSL 226
Cdd:smart00033 81 PEDLVEGPKLILGVIWTLISL 101
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1279-1863 |
4.59e-19 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 96.14 E-value: 4.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1279 QEYVDLRTRYSELTTLTSQY-IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ----LAEAHAQAKAQAEL 1353
Cdd:COG4913 262 ERYAAARERLAELEYLRAALrLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREeldeLEAQIRGNGGDRLE 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1354 EAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1433
Cdd:COG4913 342 QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRREL 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1434 GGAEGELQALRARA---EEAEAQKRQAQEEAERLRR----------QVQDESQRKRQAeAELALR-------VKAEAEAA 1493
Cdd:COG4913 422 RELEAEIASLERRKsniPARLLALRDALAEALGLDEaelpfvgeliEVRPEEERWRGA-IERVLGgfaltllVPPEHYAA 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1494 rekqrALQALDEL----RLQAEEAERRLRQAEAER------ARQVQVALETAQRSAEVELQsKRASFA--EKTAQLERTl 1561
Cdd:COG4913 501 -----ALRWVNRLhlrgRLVYERVRTGLPDPERPRldpdslAGKLDFKPHPFRAWLEAELG-RRFDYVcvDSPEELRRH- 573
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1562 qEEHVTVAQLREEAERRAQQQAEAERAreeaerelERWQL-KANEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearr 1640
Cdd:COG4913 574 -PRAITRAGQVKGNGTRHEKDDRRRIR--------SRYVLgFDNRAKLAALEAELAELEEELAEAEERLEAL-------- 636
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1641 rgKAEEQAVRQRELAEQELEKQRQL---AEGTAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEATAATQKRQE 1717
Cdd:COG4913 637 --EAELDALQERREALQRLAEYSWDeidVASAEREIAELEAELERLDASSDDLAA----LEEQLEELEAELEELEEELDE 710
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1718 LEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1797
Cdd:COG4913 711 LKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELE 790
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1798 RVLTEklaAISEATRLKTEAEIALKEKEAENERLRRLAED------EAFQRRRLEE--------QAALHKA--DIEERLA 1861
Cdd:COG4913 791 RAMRA---FNREWPAETADLDADLESLPEYLALLDRLEEDglpeyeERFKELLNENsiefvadlLSKLRRAirEIKERID 867
|
..
gi 254675251 1862 QL 1863
Cdd:COG4913 868 PL 869
|
|
| CH_NAV2-like |
cd21212 |
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ... |
12-112 |
1.55e-18 |
|
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.
Pssm-ID: 409061 Cd Length: 105 Bit Score: 83.79 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 12 QKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGR--MRFHKLQNVQIALDYLRHRQVKLVN 87
Cdd:cd21212 1 EIEIYTDWANHYLEKGghKRIITDLQKDLGDGLTLVNLIEAVAGEKVPGIHSRpkTRAQKLENIQACLQFLAALGVDVQG 80
|
90 100
....*....|....*....|....*
gi 254675251 88 IRNDDIADGNPKLTLGLIWTIILHF 112
Cdd:cd21212 81 ITAEDIVDGNLKAILGLFFSLSRYK 105
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1297-1893 |
1.56e-18 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 93.95 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1297 QYIKFISETLRRMEEEERLAEQQR----------AEERERLAEVEAALEKQRQlaeahaqAKAQAELEAQELQRRMQEEV 1366
Cdd:PRK02224 213 SELAELDEEIERYEEQREQARETRdeadevleehEERREELETLEAEIEDLRE-------TIAETEREREELAEEVRDLR 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1367 ARREEaavdaqqqkrsIQEELQHLRQSSE---AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQAL 1443
Cdd:PRK02224 286 ERLEE-----------LEEERDDLLAEAGlddADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1444 RARAEEaeaqkrqAQEEAERLrrqvqdesqrkrqaEAELalrvkAEAEAAREKQRAlqALDELRLQAEEAERRLRQAEae 1523
Cdd:PRK02224 355 EERAEE-------LREEAAEL--------------ESEL-----EEAREAVEDRRE--EIEELEEEIEELRERFGDAP-- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1524 rarqvqVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELE--RWQL 1601
Cdd:PRK02224 405 ------VDLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALLEAGKCPECGQPVEGSPHVETIEedRERV 477
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1602 KANEALRLRLQAEEVAQQKSLAQADAEKqkeeaerearrrgKAEEQAVR---QRELAEQELEKQRQLAEGTAQQRLAAEQ 1678
Cdd:PRK02224 478 EELEAELEDLEEEVEEVEERLERAEDLV-------------EAEDRIERleeRREDLEELIAERRETIEEKRERAEELRE 544
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1679 ELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAeMEVLLASKARAEEESRSTSEKSKQRLEAEA 1758
Cdd:PRK02224 545 RAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIERLREKREALAELND 623
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1759 GRFRELAEEAARLRALAEEAKRQRqLAEEDAARQRAEaervltEKLAAISEATRLKTEAEIALKEK----EAENERLRRL 1834
Cdd:PRK02224 624 ERRERLAEKRERKRELEAEFDEAR-IEEAREDKERAE------EYLEQVEEKLDELREERDDLQAEigavENELEELEEL 696
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1835 aedeafqRRRLEEQAALHkadieERLAQLRKASEsELERQKGLVEDTLRQRRQVEEEIM 1893
Cdd:PRK02224 697 -------RERREALENRV-----EALEALYDEAE-ELESMYGDLRAELRQRNVETLERM 742
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
1655-2575 |
1.94e-18 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 94.12 E-value: 1.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1655 AEQELEKQRQLAEgtaQQRLAAEQELIRLRAETeqgeqQRQLLE--EELARLQHEA-TAATQKRQELEAELAKVRAEMEV 1731
Cdd:NF041483 74 AEQLLRNAQIQAD---QLRADAERELRDARAQT-----QRILQEhaEHQARLQAELhTEAVQRRQQLDQELAERRQTVES 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1732 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRA--LAEEAkRQRQLAEEDAARqrAEAERVLtekLAAISE 1809
Cdd:NF041483 146 HVNENVAWAEQLRARTESQARRLLDESRAEAEQALAAARAEAerLAEEA-RQRLGSEAESAR--AEAEAIL---RRARKD 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1810 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRR----LEEQAALHKADIEERLAQLRKASESELE-------RQKGLV 1878
Cdd:NF041483 220 AERLLNAASTQAQEATDHAEQLRSSTAAESDQARRqaaeLSRAAEQRMQEAEEALREARAEAEKVVAeakeaaaKQLASA 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1879 EDTLRQR-RQVEEEIMALKVSFEK-AAAGKAELELELGRIRSNAE-------DTMRSKEQAELEAARQRQLAAEEEQRRR 1949
Cdd:NF041483 300 ESANEQRtRTAKEEIARLVGEATKeAEALKAEAEQALADARAEAEklvaeaaEKARTVAAEDTAAQLAKAARTAEEVLTK 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1950 EAEERVQRSLAAEEEAARQRKVALEEVERLKAKV--------------------------EEARRLRERAEQ-------- 1995
Cdd:NF041483 380 ASEDAKATTRAAAEEAERIRREAEAEADRLRGEAadqaeqlkgaakddtkeyraktvelqEEARRLRGEAEQlraeavae 459
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1996 ------ESARQ-LQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRL----RSEAEAARRAAEEAEEAREQ 2064
Cdd:NF041483 460 gerirgEARREaVQQIEEAARTAEELLTKAKADADELRSTATAESERVRTEAIERAttlrRQAEETLERTRAEAERLRAE 539
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2065 AEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAAlkqkqAADAEMEK-HKKFAEQTL 2143
Cdd:NF041483 540 AEEQAEEVRAAAERAARELREETERAIAARQAEAAEELTRLHTEAEERLTAAEEALA-----DARAEAERiRREAAEETE 614
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2144 RQKAQVEQELTTLRLQLEetdhqksildEELQRLKaevTEAARQRSQVEEELFSVRVqmeelgKLKARIEAENRALILRD 2223
Cdd:NF041483 615 RLRTEAAERIRTLQAQAE----------QEAERLR---TEAAADASAARAEGENVAV------RLRSEAAAEAERLKSEA 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2224 KDNTQRFLEEEAEKMKQVAEEAAR-LSVAAQEAARLRQLAEEDLAQQRALAEkmlKEKMQAVQEATRLKAEAellQQQKE 2302
Cdd:NF041483 676 QESADRVRAEAAAAAERVGTEAAEaLAAAQEEAARRRREAEETLGSARAEAD---QERERAREQSEELLASA---RKRVE 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2303 LAQEQARRLQEDKEQMAQQLV---EETQGFQRTLEAERQRQlemsAEAERLKLRMAemsraqarAEEDAQRFRKQAEEIG 2379
Cdd:NF041483 750 EAQAEAQRLVEEADRRATELVsaaEQTAQQVRDSVAGLQEQ----AEEEIAGLRSA--------AEHAAERTRTEAQEEA 817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2380 EKLHRTELATQEKVTLVQTLEIQRQQSDHDAER------LREAIAELEREKEKLKQEAKLLQLK-SEEMQTVQQEQILQE 2452
Cdd:NF041483 818 DRVRSDAYAERERASEDANRLRREAQEETEAAKalaertVSEAIAEAERLRSDASEYAQRVRTEaSDTLASAEQDAARTR 897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2453 TQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASM-----EEARRRQREA 2527
Cdd:NF041483 898 ADAREDANRIRSDAAAQADRLIGEATSEAERLTAEARAEAERLRDEARAEAERVRADAAAQAEQLiaeatGEAERLRAEA 977
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|..
gi 254675251 2528 EEGVRRKQEELQHLEQQRQQQEKLLAEENQRL----RERLQRLEEEHRAALA 2575
Cdd:NF041483 978 AETVGSAQQHAERIRTEAERVKAEAAAEAERLrteaREEADRTLDEARKDAN 1029
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
1958-2570 |
4.74e-18 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 92.69 E-value: 4.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1958 SLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQE 2037
Cdd:COG1196 204 PLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2038 QNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2117
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2118 EQAALKQKQAADAEMEKhkkfAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFS 2197
Cdd:COG1196 364 EEALLEAEAELAEAEEE----LEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2198 VRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2277
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2278 KEKMQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMA 2355
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAalQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARAALAAALARGAIGA 599
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2356 EMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ 2435
Cdd:COG1196 600 AVDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2436 LKSEEMQTVQQEQILQETQALQKSFLSEKDS-LLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELM 2514
Cdd:COG1196 680 ELEELAERLAEEELELEEALLAEEEEERELAeAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEP 759
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 2515 ASMEEARRRQREAEEGVRRkqeelqhleqqrqqqekllAEENQRLRERLQRLEEEH 2570
Cdd:COG1196 760 PDLEELERELERLEREIEAlgpv-----------nllaIEEYEELEERYDFLSEQR 804
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
13-110 |
6.04e-18 |
|
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: 82.00 E-value: 6.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 13 KKTFTKWVNKHL-IKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPRE--KGRMRFHKLQNVQIALDYLRHRQV-KLVNI 88
Cdd:cd00014 1 EEELLKWINEVLgEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKInkKPKSPFKKRENINLFLNACKKLGLpELDLF 80
|
90 100
....*....|....*....|...
gi 254675251 89 RNDDI-ADGNPKLTLGLIWTIIL 110
Cdd:cd00014 81 EPEDLyEKGNLKKVLGTLWALAL 103
|
|
| CH_EHBP1 |
cd21254 |
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 ... |
127-226 |
8.78e-18 |
|
calponin homology (CH) domain found in EH domain-binding protein 1 and similar proteins; EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. Members of this subfamily contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409103 Cd Length: 107 Bit Score: 81.82 E-value: 8.78e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDP 206
Cdd:cd21254 1 NASQSLLAWCKEVTKGYRGVKITNFTTSWRNGLAFCAILHHFRPDLIDYKSLNPHDIKENNKKAYDGFAS-LGISRLLEP 79
|
90 100
....*....|....*....|.
gi 254675251 207 ED-VDVPQPDEKSIITYVSSL 226
Cdd:cd21254 80 SDmVLLAVPDKLTVMTYLYQI 100
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1296-2227 |
9.86e-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: 91.57 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1296 SQYIKFISETLRRMEEEERLAEQqrAEERERLAEVEAALEKQRqlaEAHAQAKAQAELEAQELQRRMQEEVARREEAAVD 1375
Cdd:pfam02463 156 LEIEEEAAGSRLKRKKKEALKKL--IEETENLAELIIDLEELK---LQELKLKEQAKKALEYYQLKEKLELEEEYLLYLD 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1376 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELqalraraEEAEAQKR 1455
Cdd:pfam02463 231 YLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEE-------EELKSELL 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1456 QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAarEKQRALQALDELRLQAEEAERRLRQAEAERARQVQValeta 1535
Cdd:pfam02463 304 KLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEEL--EKELKELEIKREAEEEEEEELEKLQEKLEQLEEELL----- 376
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1536 qrsAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEaerelerwqLKANEALRLRLQAEE 1615
Cdd:pfam02463 377 ---AKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEL---------EILEEEEESIELKQG 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1616 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1695
Cdd:pfam02463 445 KLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRI 524
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1696 LLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRL--EAEAGRFRELAEEAARLRA 1773
Cdd:pfam02463 525 ISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLipKLKLPLKSIAVLEIDPILN 604
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1774 LAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaaLHK 1853
Cdd:pfam02463 605 LAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQ--ELQ 682
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1854 ADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE 1933
Cdd:pfam02463 683 EKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEK 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1934 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEArrlRERAEQESARQLQLAQEAAQKRLQ 2013
Cdd:pfam02463 763 EEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAE---LLEEEQLLIEQEEKIKEEELEELA 839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2014 AEEKahaFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQ 2093
Cdd:pfam02463 840 LELK---EEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKE 916
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2094 AQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEE 2173
Cdd:pfam02463 917 NEIEERIKEEAEILLKYEEEPEELLLEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE 996
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2174 LQRLKAEVTEAARQRSQVEEELF------SVRVQMEELGKLKARIEAENRALILRDKDNT 2227
Cdd:pfam02463 997 KERLEEEKKKLIRAIIEETCQRLkeflelFVSINKGWNKVFFYLELGGSAELRLEDPDDP 1056
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1302-1933 |
2.21e-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: 90.51 E-value: 2.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1302 ISETLRRMEEEERLAEQQRAEERERLAEVEAALEKqrqLAEAHAQAKAQAELEAQELQRRMqEEVARREEAAVDAQQQKR 1381
Cdd:TIGR02169 239 KEAIERQLASLEEELEKLTEEISELEKRLEEIEQL---LEELNKKIKDLGEEEQLRVKEKI-GELEAEIASLERSIAEKE 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1382 SIQEELQHLRQSSEAEIQAKAQQVEAaersrmrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1455
Cdd:TIGR02169 315 RELEDAEERLAKLEAEIDKLLAEIEE-------LEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAetrdel 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1456 --------QAQEEAERLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQA-LDELRLQAEEAERRLRQAEAER-- 1524
Cdd:TIGR02169 388 kdyrekleKLKREINELKRELDRLQEELQRLSEELA-DLNAAIAGIEAKINELEEeKEDKALEIKKQEWKLEQLAADLsk 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1525 ARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEE-----------------HVTVAQLREEAerraqqqaeaer 1587
Cdd:TIGR02169 467 YEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVrggraveevlkasiqgvHGTVAQLGSVG------------ 534
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1588 areeaerelERWQLKANEALRLRLQA-----EEVAQQ--KSLAQADAE----------KQKEEAEREARRRG-------- 1642
Cdd:TIGR02169 535 ---------ERYATAIEVAAGNRLNNvvvedDAVAKEaiELLKRRKAGratflplnkmRDERRDLSILSEDGvigfavdl 605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1643 ----KAEEQAVR---QRELAEQELEKQRQL--------------------------AEGTAQQRLAAEQELIRLRAETEQ 1689
Cdd:TIGR02169 606 vefdPKYEPAFKyvfGDTLVVEDIEAARRLmgkyrmvtlegelfeksgamtggsraPRGGILFSRSEPAELQRLRERLEG 685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1690 GEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLL----ASKARAEEESRSTSEKSKQRLEAEAgrfrELA 1765
Cdd:TIGR02169 686 LKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEqeeeKLKERLEELEEDLSSLEQEIENVKS----ELK 761
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1766 EEAARLRALaEEAKRQRQLAEEDAARQRAEAE--------RVLTEKLAAISEATRlktEAEIALKEKEAENERLRRLAED 1837
Cdd:TIGR02169 762 ELEARIEEL-EEDLHKLEEALNDLEARLSHSRipeiqaelSKLEEEVSRIEARLR---EIEQKLNRLTLEKEYLEKEIQE 837
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1838 EAFQRRRLEEQAALHKADIEERLAQLRKAsESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIR 1917
Cdd:TIGR02169 838 LQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR 916
|
730
....*....|....*.
gi 254675251 1918 SNAEDTMRSKEQAELE 1933
Cdd:TIGR02169 917 KRLSELKAKLEALEEE 932
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1292-2016 |
2.88e-17 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 90.03 E-value: 2.88e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1292 TTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAaLEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREE 1371
Cdd:TIGR00618 134 DLLKLDYKTFTRVVLLPQGEFAQFLKAKSKEKKELLMNLFP-LDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPC 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1372 AAVDAQQQKRSIQEELQHLR--QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggaEGELQALRARAEE 1449
Cdd:TIGR00618 213 MPDTYHERKQVLEKELKHLReaLQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQ----EAVLEETQERINR 288
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1450 AEAQKRQA--QEEAERLRRQVQDESQRKRQAEAELA-LRVKAEAEAAREKQRALQALDELRLQAEEAERRlRQAEAERAR 1526
Cdd:TIGR00618 289 ARKAAPLAahIKAVTQIEQQAQRIHTELQSKMRSRAkLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIR-DAHEVATSI 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1527 QVQVALETAQRSAEVELQSKRASFAEK---TAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKA 1603
Cdd:TIGR00618 368 REISCQQHTLTQHIHTLQQQKTTLTQKlqsLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1604 NEALRLrLQAEEVAQQKSLAQADAEKQ---------KEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLA-------- 1666
Cdd:TIGR00618 448 TCTAQC-EKLEKIHLQESAQSLKEREQqlqtkeqihLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQdidnpgpl 526
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1667 ----EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1742
Cdd:TIGR00618 527 trrmQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEA 606
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1743 SRSTSEKS------------KQRLEAEAGRF-RELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAERVLTEKLAAISE 1809
Cdd:TIGR00618 607 EDMLACEQhallrklqpeqdLQDVRLHLQQCsQELALKLTALHALQLTLTQERV--REHALSIRVLPKELLASRQLALQK 684
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1810 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASES--ELERQK--GLVEDTLRQR 1885
Cdd:TIGR00618 685 MQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDLAAREDALNQSlkELMHQArtVLKARTEAHF 764
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1886 RQVEEEIMALKVSFEKAAAgKAELElelgrirsnaedtmrskEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEA 1965
Cdd:TIGR00618 765 NNNEEVTAALQTGAELSHL-AAEIQ-----------------FFNRLREEDTHLLKTLEAEIGQEIPSDEDILNLQCETL 826
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1966 ARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEE 2016
Cdd:TIGR00618 827 VQEEEQFLSRLEEKSATLGEITHQLLKYEECSKQLAQLTQEQAKIIQLSDK 877
|
|
| CH_MICAL2 |
cd21250 |
calponin homology (CH) domain found in molecule interacting with CasL protein 2; MICAL-2 is a ... |
131-228 |
5.40e-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: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 131 KLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLD-PEDV 209
Cdd:cd21250 8 KLLTWCQKQTEGYQNVNVTDLTTSWKSGLALCAIIHRFRPELIDFDSLNEDDAVKNNQLAFDVAEREFGIPPVTTgKEMA 87
|
90
....*....|....*....
gi 254675251 210 DVPQPDEKSIITYVSSLYD 228
Cdd:cd21250 88 SAEEPDKLSMVMYLSKFYE 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
929-1563 |
1.33e-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: 87.80 E-value: 1.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 929 HYQQLLQSLEQGEQEESRCQRcisELKDIRLQLEACETR-TVHRLRLpldkdpaRECAQRIAEQQK----AQAEVEGLGK 1003
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEE---ELEELTAELQELEEKlEELRLEV-------SELEEEIEELQKelyaLANEISRLEQ 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1004 GVARLSAEAEKVLA-LPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKE--- 1079
Cdd:TIGR02168 303 QKQILRERLANLERqLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEqle 382
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1080 --AQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQ-QRHGERDVEVERWRERVTQLLERWQAV 1156
Cdd:TIGR02168 383 tlRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAElKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1157 LAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAvPIANCQAAREQLRQEKALLEEIERHGEKVEEC--- 1233
Cdd:TIGR02168 463 LEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSE-GVKALLKNQSGLSGILGVLSELISVDEGYEAAiea 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1234 -------------QKFAKQYINAIKDYELQLITYKA--QLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSE----LTTL 1294
Cdd:TIGR02168 542 alggrlqavvvenLNAAKKAIAFLKQNELGRVTFLPldSIKGTEIQGNDREILKNIEGFLGVAKDLVKFDPKlrkaLSYL 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1295 TSQYikFISETL-------RRMEEEERL--------------------AEQQRAEERERLAEVEAALEK-QRQLAEAHAQ 1346
Cdd:TIGR02168 622 LGGV--LVVDDLdnalelaKKLRPGYRIvtldgdlvrpggvitggsakTNSSILERRREIEELEEKIEElEEKIAELEKA 699
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1347 ----AKAQAELEAQELQRRMQEEVARREEAAVDAQQQK-RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRV 1421
Cdd:TIGR02168 700 laelRKELEELEEELEQLRKELEELSRQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAE 779
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1422 VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQ 1501
Cdd:TIGR02168 780 AEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAA 859
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1502 ALDELRLQAEEAERRLRQAEAERArQVQVALETAqRSAEVELQSKRASFAEKTAQLERTLQE 1563
Cdd:TIGR02168 860 EIEELEELIEELESELEALLNERA-SLEEALALL-RSELEELSEELRELESKRSELRRELEE 919
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1311-1788 |
1.61e-16 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 86.75 E-value: 1.61e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1311 EEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQ-AELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1389
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAElEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1390 LRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR-GGAEGELQALRARAEEAEAQKRQAQEEAERLRRQV 1468
Cdd:COG4717 151 LEER-LEELRELEEELEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1469 QDESQRKRQAEAELALRvkaeaeAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALetaqrSAEVELQSKRA 1548
Cdd:COG4717 230 EQLENELEAAALEERLK------EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLA-----LLFLLLAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1549 SFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAE 1628
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1629 KQkeeaerearrrGKAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQqrqlLEEELARLQHEA 1708
Cdd:COG4717 379 AG-----------VEDEEELRAALEQAEEYQELKEELEE--LEEQLEELLGELEELLEALDEEE----LEEELEELEEEL 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1709 TAATQKRQELEAELAKVRAEMEVLlaskaraeeESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1788
Cdd:COG4717 442 EELEEELEELREELAELEAELEQL---------EEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREE 512
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1786-2572 |
3.71e-16 |
|
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: 86.56 E-value: 3.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1786 EEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAlhkadIEERLAQLRK 1865
Cdd:pfam02463 143 KIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAK-----KALEYYQLKE 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1866 ASESELERQKGLVEDTLRQRRQVEEEimalkvsfEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEE 1945
Cdd:pfam02463 218 KLELEEEYLLYLDYLKLNEERIDLLQ--------ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELK 289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1946 QRRREAEERVQRSLAAEeeaaRQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKahafvVQQ 2025
Cdd:pfam02463 290 LLAKEEEELKSELLKLE----RRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEE-----EEE 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2026 REEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERlKQSAEEQAQAQAQAQAAAEKLRK 2105
Cdd:pfam02463 361 LEKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQ-LEDLLKEEKKEELEILEEEEESI 439
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2106 EAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELqrlkaEVTEAA 2185
Cdd:pfam02463 440 ELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSG-----LKVLLA 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2186 RQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAE------EAARLSVAAQEAARLR 2259
Cdd:pfam02463 515 LIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQKLVRALTElplgarKLRLLIPKLKLPLKSI 594
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2260 QLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQR 2339
Cdd:pfam02463 595 AVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKE 674
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2340 QLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAE 2419
Cdd:pfam02463 675 LLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEK 754
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2420 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKA-KQLREE 2498
Cdd:pfam02463 755 SRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEeKIKEEE 834
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 2499 QQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRA 2572
Cdd:pfam02463 835 LEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQK 908
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2231-2652 |
4.72e-16 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 86.14 E-value: 4.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2231 LEEEAEKmkqvAEEAARLSVAAQEA-ARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQAR 2309
Cdd:COG1196 205 LERQAEK----AERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELE 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2310 RLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELAT 2389
Cdd:COG1196 281 LELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAEL 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2390 QEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQETQALQKSFLSEKDSLLQ 2469
Cdd:COG1196 361 AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLE-RLERLEEELEELEEALAELEEEEEE 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2470 RERFIEQEKAKLEQLFQDEVA----KAKQLREEQQRQQQQMEQEKQELMA-----SMEEARRRQREAEEGVRRKQEELQH 2540
Cdd:COG1196 440 EEEALEEAAEEEAELEEEEEAllelLAELLEEAALLEAALAELLEELAEAaarllLLLEAEADYEGFLEGVKAALLLAGL 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2541 LEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALPNGRDAPDGPSVEAEPEytfegLRQKVPAQ 2620
Cdd:COG1196 520 RGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLPLDKIRARA-----ALAAALAR 594
|
410 420 430
....*....|....*....|....*....|..
gi 254675251 2621 QLQEAGILSQEELQRLAQGHTTVAELTQREDV 2652
Cdd:COG1196 595 GAIGAAVDLVASDLREADARYYVLGDTLLGRT 626
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
129-227 |
6.96e-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: 76.57 E-value: 6.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 129 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 208
Cdd:cd21259 3 KQMLLDWCRAKTRGYENVDIQNFSSSWSDGMAFCALVHNFFPEAFDYSQLSPQNRRHNFEVAFSSAEKHADCPQLLDVED 82
|
90 100
....*....|....*....|
gi 254675251 209 -VDVPQPDEKSIITYVSSLY 227
Cdd:cd21259 83 mVRMREPDWKCVYTYIQEFY 102
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1754-2570 |
7.62e-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: 7.62e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1754 LEAEAGRFRELAEEAA---RLRALAEEAKRQRQLAEEDAAR------------QRAEAERVLTEKLAAISEATRlKTEAE 1818
Cdd:TIGR02168 150 IEAKPEERRAIFEEAAgisKYKERRKETERKLERTRENLDRledilnelerqlKSLERQAEKAERYKELKAELR-ELELA 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1819 IALKEKEAENERLRRLAED-EAFQRRRLEEQAALHKAdiEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMA 1894
Cdd:TIGR02168 229 LLVLRLEELREELEELQEElKEAEEELEELTAELQEL--EEKLEELRLEVselEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1895 LKVSFEKAAAGKAELELELgrirsnaEDTMRSKEQAELEAARQRQlaaeeeqrRREAEERVQRSLAAEEEAARqrkvalE 1974
Cdd:TIGR02168 307 LRERLANLERQLEELEAQL-------EELESKLDELAEELAELEE--------KLEELKEELESLEAELEELE------A 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1975 EVERLKAKVEEARRLRERAEQESArQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARR 2053
Cdd:TIGR02168 366 ELEELESRLEELEEQLETLRSKVA-QLELQIASLNNEIErLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2054 AAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADaeme 2133
Cdd:TIGR02168 445 LEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG---- 520
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2134 khkkfAEQTLRQKAQVEQElttLRLQLEETdhqksiLDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIE 2213
Cdd:TIGR02168 521 -----ILGVLSELISVDEG---YEAAIEAA------LGGRLQAVVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEI 586
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2214 AENRALILRDKDNTQRF---LEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEED------------------LAQQRA 2271
Cdd:TIGR02168 587 QGNDREILKNIEGFLGVakdLVKFDPKLRKALSYLlGGVLVVDDLDNALELAKKLRpgyrivtldgdlvrpggvITGGSA 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2272 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLK 2351
Cdd:TIGR02168 667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2352 LRMAEMSRAQARAEEdaqrfrkQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEA 2431
Cdd:TIGR02168 747 ERIAQLSKELTELEA-------EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEA 819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2432 KLLQLKSEEMQTvQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEQEKQ 2511
Cdd:TIGR02168 820 ANLRERLESLER-RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEEL-ESELEALLNERASLEEALALLRSELE 897
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 2512 ELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEH 2570
Cdd:TIGR02168 898 ELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEA 956
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1197-1902 |
7.76e-16 |
|
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: 85.41 E-value: 7.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1197 QIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSES 1276
Cdd:TIGR00618 222 QVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1277 VIQEYVDLRTRYSELttltsqyikfisetlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ 1356
Cdd:TIGR00618 302 VTQIEQQAQRIHTEL------------------QSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEV 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1357 ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVR----LQLETTERQ 1432
Cdd:TIGR00618 364 ATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKkqqeLQQRYAELC 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1433 RGGAEGELQALRARAEEAE--AQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQA 1510
Cdd:TIGR00618 444 AAAITCTAQCEKLEKIHLQesAQSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNP 523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1511 EEAERRLRQAEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQlreeaerraqqqaeaerare 1590
Cdd:TIGR00618 524 GPLTRRMQRGEQTYAQ-----LETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQC-------------------- 578
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1591 eaerelerWQLKANEALRLRLQAEEVaqQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTA 1670
Cdd:TIGR00618 579 --------DNRSKEDIPNLQNITVRL--QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL 648
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1671 QQ---RLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLAS-KARAEEESRST 1746
Cdd:TIGR00618 649 HAlqlTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYdREFNEIENASS 728
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1747 SEKSK--QRLEAEA---GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLkteaeiaL 1821
Cdd:TIGR00618 729 SLGSDlaAREDALNqslKELMHQARTVLKARTEAHFNNNEEVTAALQTGAELSHLAAEIQFFNRLREEDTHL-------L 801
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1822 KEKEAENERLRRLAEDEafqrrrLEEQAALHKADIEERLAQLRKASES--ELERQKGLVEDTLRQRRQVEEEIMALKVSF 1899
Cdd:TIGR00618 802 KTLEAEIGQEIPSDEDI------LNLQCETLVQEEEQFLSRLEEKSATlgEITHQLLKYEECSKQLAQLTQEQAKIIQLS 875
|
...
gi 254675251 1900 EKA 1902
Cdd:TIGR00618 876 DKL 878
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1378-2321 |
1.12e-15 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 84.73 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1378 QQKRSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEA----- 1452
Cdd:TIGR02169 153 VERRKIIDEIAGVAEF-DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREYEGyellk 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1453 QKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAR------EKQRALQALDELRLQAEEAE-----RRLRQAE 1521
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnKKIKDLGEEEQLRVKEKIGEleaeiASLERSI 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1522 AERARQVQVALETaqrsaEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQaeaerareeaerelerwql 1601
Cdd:TIGR02169 311 AEKERELEDAEER-----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEEL------------------- 366
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1602 kanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQR-ELAEQELEKQRQLAEGTAQQRLAAEQEL 1680
Cdd:TIGR02169 367 ---EDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEElQRLSEELADLNAAIAGIEAKINELEEEK 443
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1681 IRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE---SRSTSEKSKQRLEAE 1757
Cdd:TIGR02169 444 EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERvrgGRAVEEVLKASIQGV 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1758 AGRFRELAEeaarlralaeeAKRQRQLAEEDAARQRAEAERVLTEKLAAiseatrlktEAEIALKEKEAENER---LRRL 1834
Cdd:TIGR02169 524 HGTVAQLGS-----------VGERYATAIEVAAGNRLNNVVVEDDAVAK---------EAIELLKRRKAGRATflpLNKM 583
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1835 AEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELeRQKGLVEDTLRQRRQVEEEIMalkVS-----FEKAAAgkael 1909
Cdd:TIGR02169 584 RDERRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVF-GDTLVVEDIEAARRLMGKYRM---VTlegelFEKSGA----- 654
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1910 eLELGRIRSNAEDTMRSKEQAELEAARQRqlaaeeeqrrreaeervqrslaaEEEAARQRKVALEEVERLKAKVEEARRL 1989
Cdd:TIGR02169 655 -MTGGSRAPRGGILFSRSEPAELQRLRER-----------------------LEGLKRELSSLQSELRRIENRLDELSQE 710
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1990 RERAEQE----SARQLQLAQEAAQKRLQAEEkahafvVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQA 2065
Cdd:TIGR02169 711 LSDASRKigeiEKEIEQLEQEEEKLKERLEE------LEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL 784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2066 EREAAQSRKQVEEAERLKQsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQ 2145
Cdd:TIGR02169 785 EARLSHSRIPEIQAELSKL----------------EEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQ 848
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2146 KAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENraliLRDKD 2225
Cdd:TIGR02169 849 IKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQL---RELERKIEELEAQIEKKR----KRLSE 921
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2226 NTQRfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALaEKMLKEKMQAVQEATRLKAEAELLQQQKELAQ 2305
Cdd:TIGR02169 922 LKAK-LEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEI-RALEPVNMLAIQEYEEVLKRLDELKEKRAKLE 999
|
970
....*....|....*.
gi 254675251 2306 EQARRLQEDKEQMAQQ 2321
Cdd:TIGR02169 1000 EERKAILERIEEYEKK 1015
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3428-3466 |
1.36e-15 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 73.13 E-value: 1.36e-15
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3428 LLEAQVATGGIIDPVHSHRLPVDVAYQRGYFDEEMNRVL 3466
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
132-227 |
1.87e-15 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 75.09 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 132 LLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDPED-VD 210
Cdd:cd21199 13 LLKWCQEKTQGYKGIDITNFSSSWNDGLAFCALLHSYLPDKIPYSELNPQDKRRNFTLAFKAAE-SVGIPTTLTIDEmVS 91
|
90
....*....|....*..
gi 254675251 211 VPQPDEKSIITYVSSLY 227
Cdd:cd21199 92 MERPDWQSVMSYVTAIY 108
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1600-2460 |
1.92e-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: 83.96 E-value: 1.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1600 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA---- 1675
Cdd:TIGR02169 231 EKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLersi 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1676 --AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQR 1753
Cdd:TIGR02169 311 aeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDY 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1754 LEAEAGRFRELAEEAARLRALAEEAKRqrqlAEEDAARQRAEAERVLTEKLAAISEatrlKTEAEIALKEKEAENERLRR 1833
Cdd:TIGR02169 391 REKLEKLKREINELKRELDRLQEELQR----LSEELADLNAAIAGIEAKINELEEE----KEDKALEIKKQEWKLEQLAA 462
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1834 LAEDEAFQRRRLEEQAalhkADIEERLAQLRKaSESELERQKGLVEDTLRQRRQVEEEImalkvsfEKAAAGKAELELEL 1913
Cdd:TIGR02169 463 DLSKYEQELYDLKEEY----DRVEKELSKLQR-ELAEAEAQARASEERVRGGRAVEEVL-------KASIQGVHGTVAQL 530
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1914 GRIrsnaedtmRSKEQAELEAARQRQLaaeeeqrrreaeervqRSLAAEEEAarqrkVALEEVERLKA------------ 1981
Cdd:TIGR02169 531 GSV--------GERYATAIEVAAGNRL----------------NNVVVEDDA-----VAKEAIELLKRrkagratflpln 581
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1982 KVEEARRLRERAEQESARQLQLAQEAAQKRLqaeEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEA 2061
Cdd:TIGR02169 582 KMRDERRDLSILSEDGVIGFAVDLVEFDPKY---EPAFKYVFGDTLVVEDIEAARRLMGKYRMVTLEGELFEKSGAMTGG 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2062 REQAEREAAQSRKQVEEAERL---KQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKF 2138
Cdd:TIGR02169 659 SRAPRGGILFSRSEPAELQRLrerLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2139 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVteAARQRSQVEEELFSVRVQMEELGKLKARIEAENRA 2218
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAL--NDLEARLSHSRIPEIQAELSKLEEEVSRIEARLRE 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2219 L--ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvAAQEAARLRQLaEEDLAQQRALAEKmLKEKMQAVQEatrLKAEAEL 2296
Cdd:TIGR02169 817 IeqKLNRLTLEKEYLEKEIQELQEQRIDL-----KEQIKSIEKEI-ENLNGKKEELEEE-LEELEAALRD---LESRLGD 886
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2297 LQQQKELAQEQARRLQEDKEQMAQQlVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2376
Cdd:TIGR02169 887 LKKERDELEAQLRELERKIEELEAQ-IEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEE 965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2377 EIgeklhrtelatqEKVTLVQTLEIQrqqsdhDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2456
Cdd:TIGR02169 966 EI------------RALEPVNMLAIQ------EYEEVLKRLDELKEKRAKLEEERKAILERIEEYEKKKREVFMEAFEAI 1027
|
....
gi 254675251 2457 QKSF 2460
Cdd:TIGR02169 1028 NENF 1031
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
2297-2718 |
1.94e-15 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 83.83 E-value: 1.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2297 LQQQKELAqEQARRLQEDKEQM-AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQA 2375
Cdd:COG1196 205 LERQAEKA-ERYRELKEELKELeAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELEL 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2376 EEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2455
Cdd:COG1196 284 EEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEA 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2456 LQKSFLSEKDSLLQRERFIEQEKAKLEQLfqdevaKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQ 2535
Cdd:COG1196 364 EEALLEAEAELAEAEEELEELAEELLEAL------RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEE 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2536 EELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALpngrdapdgpsveaepeytFEGLRQ 2615
Cdd:COG1196 438 EEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAAR-------------------LLLLLE 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2616 KVPAQQLQEAGILSQEELQRLAQGHTTVAELTQREDVYRYLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTALILLE 2695
Cdd:COG1196 499 AEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFLP 578
|
410 420
....*....|....*....|...
gi 254675251 2696 AQAASGFLLDPVRNRRLTVNEAV 2718
Cdd:COG1196 579 LDKIRARAALAAALARGAIGAAV 601
|
|
| CH_SMTNL2 |
cd21261 |
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 ... |
129-228 |
2.11e-15 |
|
calponin homology (CH) domain found in smoothelin-like protein 2; Smoothelin-like protein 2 (SMTNL2) is highly expressed in skeletal muscle and could be associated with differentiating myocytes. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409110 Cd Length: 107 Bit Score: 75.00 E-value: 2.11e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 129 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 208
Cdd:cd21261 3 KQILLEWCRSKTIGYKNIDLQNFSSSWSDGMAFCALVHSFFPEAFDYDSLSPSNRKHNFELAFSMAEKLANCDRLIEVED 82
|
90 100
....*....|....*....|..
gi 254675251 209 VDV--PQPDEKSIITYVSSLYD 228
Cdd:cd21261 83 MMVmgRKPDPMCVFTYVQSLYN 104
|
|
| CH_SMTNA |
cd21258 |
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are ... |
129-232 |
3.17e-15 |
|
calponin homology (CH) domain found in smoothelin-A and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. This model corresponds to the single CH domain of smoothelin-A. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409107 Cd Length: 111 Bit Score: 74.70 E-value: 3.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 129 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 208
Cdd:cd21258 3 KQMLLDWCRAKTRGYEHVDIQNFSSSWSDGMAFCALVHNFFPDAFDYSQLSPQNRRQNFEVAFSAAEMLADCVPLVEVED 82
|
90 100
....*....|....*....|....*.
gi 254675251 209 VDV--PQPDEKSIITYVSSLYDAMPR 232
Cdd:cd21258 83 MMImgKKPDSKCVFTYVQSLYNHLRR 108
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4006-4044 |
3.26e-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: 3.26e-15
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 4006 LLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEMNEIL 4044
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_CTX_rpt1 |
cd21225 |
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ... |
9-108 |
3.77e-15 |
|
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409074 Cd Length: 111 Bit Score: 74.49 E-value: 3.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 9 DRVQKKTFTKWVNKHLIKAQ-RHISDLYEDLRDGHNLISLLEVLSGDSLPRE---KGRMRFHKLQNVQIALDYLRHR-QV 83
Cdd:cd21225 2 EKVQIKAFTAWVNSVLEKRGiPKISDLATDLSDGVRLIFFLELVSGKKFPKKfdlEPKNRIQMIQNLHLAMLFIEEDlKI 81
|
90 100
....*....|....*....|....*
gi 254675251 84 KLVNIRNDDIADGNPKLTLGLIWTI 108
Cdd:cd21225 82 RVQGIGAEDFVDNNKKLILGLLWTL 106
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2769-2807 |
5.06e-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: 5.06e-15
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 2769 LLEAQIATGGIIDPVHSHRVPVDVAYKRGYFDEEMNRIL 2807
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_FIM_rpt3 |
cd21219 |
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
6-111 |
1.25e-14 |
|
third calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409068 Cd Length: 113 Bit Score: 72.70 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 6 DERDrvqKKTFTKWVNKHLIKAQrhISDLYEDLRDGhnlISLLEVLsgDSL-P---------REKGRMRFHKLQNVQIAL 75
Cdd:cd21219 2 GSRE---ERAFRMWLNSLGLDPL--INNLYEDLRDG---LVLLQVL--DKIqPgcvnwkkvnKPKPLNKFKKVENCNYAV 71
|
90 100 110
....*....|....*....|....*....|....*.
gi 254675251 76 DYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTIILH 111
Cdd:cd21219 72 DLAKKLGFSLVGIGGKDIADGNRKLTLALVWQLMRY 107
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3687-3725 |
1.28e-14 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 70.43 E-value: 1.28e-14
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3687 LLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPELHDRL 3725
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1030-1895 |
1.70e-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: 80.88 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1030 SELELTLGKLEQVRslsaiylEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATK--ASLKKLRAQAEAQ 1107
Cdd:TIGR02169 170 RKKEKALEELEEVE-------ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGYEllKEKEALERQKEAI 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1108 QPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLaqtdvrQRELEQLGRQLRYYRESADPLSAW 1187
Cdd:TIGR02169 243 ERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV------KEKIGELEAEIASLERSIAEKERE 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1188 LQDAKRRQEQIQAvpiancqaareqlrQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKK 1267
Cdd:TIGR02169 317 LEDAEERLAKLEA--------------EIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAE 382
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1268 PKvqsgsesviQEYVDLRTRYSELTtltsQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAhaqa 1347
Cdd:TIGR02169 383 TR---------DELKDYREKLEKLK----REINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKED---- 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1348 kAQAELEAQElqRRMQEEVARREeaavDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLE 1427
Cdd:TIGR02169 446 -KALEIKKQE--WKLEQLAADLS----KYEQELYDLKEEYDRV----EKELSKLQRELAEAEAQARASEERVRGGRAVEE 514
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1428 TTERQRGGAEGELQALraraEEAEAQKRQAQEEAERLRRQ---VQDESQRKRQAEaeLALRVKA------EAEAAREKQR 1498
Cdd:TIGR02169 515 VLKASIQGVHGTVAQL----GSVGERYATAIEVAAGNRLNnvvVEDDAVAKEAIE--LLKRRKAgratflPLNKMRDERR 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1499 ALQALDE-----LRLQAEEAERRLRQAEAERARQVQV--ALETAQR--------SAEVELQSKRA-----SFAEKTAQLE 1558
Cdd:TIGR02169 589 DLSILSEdgvigFAVDLVEFDPKYEPAFKYVFGDTLVveDIEAARRlmgkyrmvTLEGELFEKSGamtggSRAPRGGILF 668
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1559 RTLQEEhvtvaqlreeaerraqqqaeaerareeaerelerwqlkanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREA 1638
Cdd:TIGR02169 669 SRSEPA----------------------------------------ELQRLRERLEGLKRELSSLQSELRRIENRLDELS 708
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1639 RRRGKAEEQAV---RQRELAEQELEKQRQLAEG-------TAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLqhEA 1708
Cdd:TIGR02169 709 QELSDASRKIGeieKEIEQLEQEEEKLKERLEEleedlssLEQEIENVKSELKELEARIEELEEDLHKLEEALNDL--EA 786
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1709 TAATQKRQELEAELAKVRAEmevllaskaRAEEESRSTS-EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE 1787
Cdd:TIGR02169 787 RLSHSRIPEIQAELSKLEEE---------VSRIEARLREiEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIE 857
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1788 DAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIE---ERLAQLR 1864
Cdd:TIGR02169 858 NLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEaleEELSEIE 937
|
890 900 910
....*....|....*....|....*....|...
gi 254675251 1865 KASESELERQKGL--VEDTLRQRRQVEEEIMAL 1895
Cdd:TIGR02169 938 DPKGEDEEIPEEElsLEDVQAELQRVEEEIRAL 970
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1066-1564 |
1.85e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 80.96 E-value: 1.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1066 AEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDvEVERWRER 1145
Cdd:PTZ00121 1338 AEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKAD-ELKKAAAA 1416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1146 VTQLLErwqavLAQTDVRQRELEQLGRQLRYYREsADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEIER 1225
Cdd:PTZ00121 1417 KKKADE-----AKKKAEEKKKADEAKKKAEEAKK-ADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKK 1490
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1226 hgeKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESViqeyvdlrtRYSELTTLTSQYIKfiSET 1305
Cdd:PTZ00121 1491 ---KAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEA---------KKAEEKKKADELKK--AEE 1556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1306 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQlaeahaQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1385
Cdd:PTZ00121 1557 LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAE------EARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEE 1630
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1386 ELQHLRQ--SSEAEIQAKAQQVEAAERsrmriEEEIRVVRLQLETTERQRGGAEgelqalrarAEEAEAQKRQAQEEAER 1463
Cdd:PTZ00121 1631 EKKKVEQlkKKEAEEKKKAEELKKAEE-----ENKIKAAEEAKKAEEDKKKAEE---------AKKAEEDEKKAAEALKK 1696
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1464 LRRQVQDESQRKRQAEAELAlrvKAEAEAAREKQRALQAlDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVEL 1543
Cdd:PTZ00121 1697 EAEEAKKAEELKKKEAEEKK---KAEELKKAEEENKIKA-EEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
|
490 500
....*....|....*....|.
gi 254675251 1544 QSKrasfaEKTAQLERTLQEE 1564
Cdd:PTZ00121 1773 IRK-----EKEAVIEEELDEE 1788
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1691-2561 |
1.87e-14 |
|
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: 80.79 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1691 EQQRQLLEEELARLQHEAtaatQKRQELEaELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAAR 1770
Cdd:pfam02463 152 PERRLEIEEEAAGSRLKR----KKKEALK-KLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYL 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1771 L--RALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKtEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1848
Cdd:pfam02463 227 LylDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLK-ENKEEEKEKKLQEEELKLLAKEEEELKSELLKL 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1849 AALHKADIEERlaqlrKASESE---LERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDT-- 1923
Cdd:pfam02463 306 ERRKVDDEEKL-----KESEKEkkkAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKkk 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1924 ----MRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESAR 1999
Cdd:pfam02463 381 leseRLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEEKEELEKQELKL 460
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2000 QLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEA 2079
Cdd:pfam02463 461 LKDELELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVEN 540
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2080 ERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLR---QKAQVEQELTTL 2156
Cdd:pfam02463 541 YKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLaqlDKATLEADEDDK 620
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2157 RLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAE 2236
Cdd:pfam02463 621 RAKVVEGILKDTELTKLKESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLE 700
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2237 KMKQVAEEAARLSVAAQEA----ARLRQLAEEDLAQQRALAEKMLKEKMQaVQEATRLKAEAELLQQQKELAQEQARRLQ 2312
Cdd:pfam02463 701 IKKKEQREKEELKKLKLEAeellADRVQEAQDKINEELKLLKQKIDEEEE-EEEKSRLKKEEKEEEKSELSLKEKELAEE 779
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2313 EDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKlhrtELATQEK 2392
Cdd:pfam02463 780 REKTEKLKVEEEKEEKLKAQEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKL----EKLAEEE 855
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2393 VTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRER 2472
Cdd:pfam02463 856 LERLEEEITKEELLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEE 935
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2473 FIEQEK-AKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREaeegVRRKQEELQHLEQQRQQQEKL 2551
Cdd:pfam02463 936 EPEELLlEEADEKEKEENNKEEEEERNKRLLLAKEELGKVNLMAIEEFEEKEERY----NKDELEKERLEEEKKKLIRAI 1011
|
890
....*....|
gi 254675251 2552 LAEENQRLRE 2561
Cdd:pfam02463 1012 IEETCQRLKE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
931-1840 |
2.07e-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: 80.88 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 931 QQLLQSLEQGEQEESRCQRCISELKDirlQLEACETRTVHRLRLPLDKDPARECAQ--RIAEQQKAQAEVEGLGKGVARL 1008
Cdd:TIGR02169 173 EKALEELEEVEENIERLDLIIDEKRQ---QLERLRREREKAERYQALLKEKREYEGyeLLKEKEALERQKEAIERQLASL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1009 SAEAEKVLALpepspaaptlRSELELTLGKLEQVRSLSAIYLEKL-----KTISLVIRSTQG----AEEVLKTHEEQLKE 1079
Cdd:TIGR02169 250 EEELEKLTEE----------ISELEKRLEEIEQLLEELNKKIKDLgeeeqLRVKEKIGELEAeiasLERSIAEKERELED 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1080 AQAVPATLQ-ELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllerwqavla 1158
Cdd:TIGR02169 320 AEERLAKLEaEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKD---------- 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1159 qtdvRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAvpiancqaareqlrqekalleEIERHGEKVEECQKFAK 1238
Cdd:TIGR02169 390 ----YREKLEKLKREINELKRELDRLQEELQRLSEELADLNA---------------------AIAGIEAKINELEEEKE 444
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1239 QYINAIKDYELQLITYKAQLepvaspakkpkvqsgsESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQ 1318
Cdd:TIGR02169 445 DKALEIKKQEWKLEQLAADL----------------SKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1319 QRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQElqrRMQEEVARREEAAVDAQQQKRS-------------IQE 1385
Cdd:TIGR02169 509 GRAVEEVLKASIQGVHGTVAQLGSVGERYATAIEVAAGN---RLNNVVVEDDAVAKEAIELLKRrkagratflplnkMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1386 ELQHLRQSSEAEIQAKA-------QQVEAAER-------------SRMRIEEEIRVVRLQLETTERQ---RGGA-EGELQ 1441
Cdd:TIGR02169 586 ERRDLSILSEDGVIGFAvdlvefdPKYEPAFKyvfgdtlvvedieAARRLMGKYRMVTLEGELFEKSgamTGGSrAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1442 ALRARAEEAEAQkrQAQEEAERLRRQVQDESQRKRQAEAELalrvkaeAEAAREKQRALQALDELRLQAEEAERRlRQAE 1521
Cdd:TIGR02169 666 ILFSRSEPAELQ--RLRERLEGLKRELSSLQSELRRIENRL-------DELSQELSDASRKIGEIEKEIEQLEQE-EEKL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1522 AERARQVQVALETAQRSAEvELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERraqqqaeaerareeaerelERWQL 1601
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIE-NVKSELKELEARIEELEEDLHKLEEALNDLEARLSH-------------------SRIPE 795
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1602 KANEALRLRlqAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAvRQRELAEQELEKQRQLAEGTAQQRlAAEQELI 1681
Cdd:TIGR02169 796 IQAELSKLE--EEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQE-QRIDLKEQIKSIEKEIENLNGKKE-ELEEELE 871
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1682 RLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE--AEAG 1759
Cdd:TIGR02169 872 ELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEipEEEL 951
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1760 RFRELAEE----AARLRALAEEAKRQRQLAEEDAARQRAeaervLTEKLAaiseatRLKTEAEiALKEKEAENERLRRLA 1835
Cdd:TIGR02169 952 SLEDVQAElqrvEEEIRALEPVNMLAIQEYEEVLKRLDE-----LKEKRA------KLEEERK-AILERIEEYEKKKREV 1019
|
....*
gi 254675251 1836 EDEAF 1840
Cdd:TIGR02169 1020 FMEAF 1024
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1066-1564 |
2.08e-14 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 80.47 E-value: 2.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1066 AEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAqaeaqqpvfnTLRDELRGAQEVGERLQQRHGERDVEVERWRER 1145
Cdd:PRK02224 239 ADEVLEEHEERREELETLEAEIEDLRETIAETERERE----------ELAEEVRDLRERLEELEEERDDLLAEAGLDDAD 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1146 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQ---AVPIANCQAAREQLRQEKALLEE 1222
Cdd:PRK02224 309 AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELReeaAELESELEEAREAVEDRREEIEE 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1223 IERHGEKVEECQKFAkqyinaikdyelqlitykaqlepvasPAKKPKVQSGSESVIQEYVDLRTRYSELTTLtsqyikfI 1302
Cdd:PRK02224 389 LEEEIEELRERFGDA--------------------------PVDLGNAEDFLEELREERDELREREAELEAT-------L 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1303 SETLRRMEEEERLAEQQR-----------------AEERERLAEVEAALE----KQRQLAEAHAQAKAQAELEAQ----- 1356
Cdd:PRK02224 436 RTARERVEEAEALLEAGKcpecgqpvegsphvetiEEDRERVEELEAELEdleeEVEEVEERLERAEDLVEAEDRierle 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1357 ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvRLQLETTERQRGGA 1436
Cdd:PRK02224 516 ERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNS--KLAELKERIESLER 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1437 EGELQALRARAE---EAEAQKRQAQEEAERLRR-QVQDESQRKRQAEAELAlrvKAEAEAARE-KQRALQALdelrlqaE 1511
Cdd:PRK02224 594 IRTLLAAIADAEdeiERLREKREALAELNDERReRLAEKRERKRELEAEFD---EARIEEAREdKERAEEYL-------E 663
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 1512 EAERRLRQAEAERARqVQVALETAQRSAE--VELQSKRASFAEKTAQLErTLQEE 1564
Cdd:PRK02224 664 QVEEKLDELREERDD-LQAEIGAVENELEelEELRERREALENRVEALE-ALYDE 716
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1070-1546 |
2.36e-14 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 79.81 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1070 LKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRH---GERDVEVERWrERV 1146
Cdd:COG4717 73 LKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEaleAELAELPERL-EEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1147 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAW-LQDAKRRQEQIQavpiANCQAAREQLRQEKALLEEIER 1225
Cdd:COG4717 152 EERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEeLQDLAEELEELQ----QRLAELEEELEEAQEELEELEE 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1226 HGEKVEEcQKFAKQYINAIKDYELQLITYKAQLEPVAspakkpkVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISET 1305
Cdd:COG4717 228 ELEQLEN-ELEAAALEERLKEARLLLLIAAALLALLG-------LGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKAS 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1306 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRmqeevARREEAAVDAQQQKRSIQE 1385
Cdd:COG4717 300 LGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE-----AEELEEELQLEELEQEIAA 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1386 ELQHLRQSSEAEIQAKAQQVEAAErsrmRIEEEIRVVRLQLE--TTERQRGGAEGELQALRARAEEAEAQKRQAQEEAER 1463
Cdd:COG4717 375 LLAEAGVEDEEELRAALEQAEEYQ----ELKEELEELEEQLEelLGELEELLEALDEEELEEELEELEEELEELEEELEE 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1464 LRRQVQDESQRKRQAEAElalrvkaeaeaarekqralQALDELRLQAEEAERRLRQAEAERARQ--VQVALETAQRSAEV 1541
Cdd:COG4717 451 LREELAELEAELEQLEED-------------------GELAELLQELEELKAELRELAEEWAALklALELLEEAREEYRE 511
|
....*
gi 254675251 1542 ELQSK 1546
Cdd:COG4717 512 ERLPP 516
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
583-761 |
2.81e-14 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 74.79 E-value: 2.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 583 LHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQ 662
Cdd:cd00176 2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 663 AALQTQWSWMLQLCCCIEAHLKENTAYFQFFSDVREAEEQLQKLQETLRRKYSCDrtiTVTRLEDLLQDAQDEKEQLNEY 742
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGK---DLESVEELLKKHKELEEELEAH 158
|
170
....*....|....*....
gi 254675251 743 KGHLSGLAKRAKAIVQLKP 761
Cdd:cd00176 159 EPRLKSLNELAEELLEEGH 177
|
|
| CH_DIXDC1 |
cd21213 |
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ... |
12-112 |
2.85e-14 |
|
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409062 Cd Length: 107 Bit Score: 71.56 E-value: 2.85e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 12 QKKTFTKWVNKHLIK--AQRHISDLYEDLRDGHNLISLLEVLSGDSL------PREKGRMRfhklQNVQIALDYLRHRQV 83
Cdd:cd21213 1 QLQAYVAWVNSQLKKrpGIRPVQDLRRDLRDGVALAQLIEILAGEKLpgidwnPTTDAERK----ENVEKVLQFMASKRI 76
|
90 100
....*....|....*....|....*....
gi 254675251 84 KLVNIRNDDIADGNPKLTLGLIWTIILHF 112
Cdd:cd21213 77 RMHQTSAKDIVDGNLKAIMRLILALAAHF 105
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1107-2017 |
3.24e-14 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 80.22 E-value: 3.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1107 QQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQA----------VLAQTDVRQRELEQLGRQLRY 1176
Cdd:pfam01576 3 QEEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAetelcaeaeeMRARLAARKQELEEILHELES 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1177 YRESADPLSAWLQ-DAKRRQEQIQAVP--IANCQAAREQLRQEKALLE-EIERHGEKVEECQKFAKQYINAIKDYELQLI 1252
Cdd:pfam01576 83 RLEEEEERSQQLQnEKKKMQQHIQDLEeqLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLSKERKLLEERIS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1253 TYKAQLEPVASPAKK-PKVQSGSESVIQEyVDLRTRYSElttltsqyikfisETLRRMEEEERLAEQQRAEERERLAEVE 1331
Cdd:pfam01576 163 EFTSNLAEEEEKAKSlSKLKNKHEAMISD-LEERLKKEE-------------KGRQELEKAKRKLEGESTDLQEQIAELQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1332 AalekqrQLAEAHAQAkAQAELEAQELQRRMQEEVARREEaavdAQQQKRSIQEELQHLRQSSEAEIQAKAQqveaAERS 1411
Cdd:pfam01576 229 A------QIAELRAQL-AKKEEELQAALARLEEETAQKNN----ALKKIRELEAQISELQEDLESERAARNK----AEKQ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1412 RMRIEEEIRVVRLQLETTErqrgGAEGELQALRARAE-EAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvkaeA 1490
Cdd:pfam01576 294 RRDLGEELEALKTELEDTL----DTTAAQQELRSKREqEVTELKKALEEETRSHEAQLQEMRQKHTQALEEL-------T 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1491 EAAREKQRALQALDELRlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEktAQLERTLQEEHVTVAQ 1570
Cdd:pfam01576 363 EQLEQAKRNKANLEKAK-QALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSE--SERQRAELAEKLSKLQ 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1571 LREEAERRAQQQAEAERAREEAERELERWQLKANEALRlrlqAEEVAQQKSLAqadaekqkeeaereaRRRGKAEEQAVR 1650
Cdd:pfam01576 440 SELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELL----QEETRQKLNLS---------------TRLRQLEDERNS 500
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1651 QRELAEQELEKQRQLaegtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK------ 1724
Cdd:pfam01576 501 LQEQLEEEEEAKRNV----ERQLSTLQAQLSDMKKKLEEDAGTLEALEEGKKRLQRELEALTQQLEEKAAAYDKlektkn 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1725 -VRAEMEVLLAS-------------------KARAEEESRSTS-EKSKQRLEAEAgrfRELAEEAARLRALAEEAKRQRQ 1783
Cdd:pfam01576 577 rLQQELDDLLVDldhqrqlvsnlekkqkkfdQMLAEEKAISARyAEERDRAEAEA---REKETRALSLARALEEALEAKE 653
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1784 LAEEDAARQRAEAERVLTEKLAA---ISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERL 1860
Cdd:pfam01576 654 ELERTNKQLRAEMEDLVSSKDDVgknVHELERSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDL 733
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1861 AQLRKASEselERQKGLVedtlRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQL 1940
Cdd:pfam01576 734 QARDEQGE---EKRRQLV----KQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1941 AAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESAR-QLQLAQEAAQKRLQAEEK 2017
Cdd:pfam01576 807 MKDLQRELEEARASRDEILAQSKESEKKLKNLEAELLQLQEDLAASERARRQAQQERDElADEIASGASGKSALQDEK 884
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
1958-2651 |
4.70e-14 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 79.80 E-value: 4.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1958 SLAAEEEAARQRKVALEEVERLKAKVEEARRlRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQE 2037
Cdd:PTZ00121 1075 SYKDFDFDAKEDNRADEATEEAFGKAEEAKK-TETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKR 1153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2038 QNMLDRLRSEaeaarraaeeaeeareqaereaaqsrKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQA 2117
Cdd:PTZ00121 1154 VEIARKAEDA--------------------------RKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARK 1207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2118 EQAALKQKQAADAEMEKHK---KFAEQTlRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEE 2194
Cdd:PTZ00121 1208 AEEERKAEEARKAEDAKKAeavKKAEEA-KKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEARKADELKKA 1286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2195 lfSVRVQMEELGKLKARIEAENraliLRDKDNTQRFLEE---EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRA 2271
Cdd:PTZ00121 1287 --EEKKKADEAKKAEEKKKADE----AKKKAEEAKKADEakkKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAE 1360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2272 LAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLveetqgfqRTLEAERQRQLEMSAEAErlK 2351
Cdd:PTZ00121 1361 AAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKK-ADEL--------KKAAAAKKKADEAKKKAE--E 1429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2352 LRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvqtleiQRQQSDHDAERLREAiAELEREKEKLKQEA 2431
Cdd:PTZ00121 1430 KKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAK---------KADEAKKKAEEAKKA-DEAKKKAEEAKKKA 1499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2432 KLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQ 2511
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2512 ELMAsmEEARRRQREAEEGVRRKQEElqhlEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAlahSEIATTQAASTKALP 2591
Cdd:PTZ00121 1580 LRKA--EEAKKAEEARIEEVMKLYEE----EKKMKAEEAKKAEEAKIKAEELKKAEEEKKKV---EQLKKKEAEEKKKAE 1650
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 2592 NGRDAPDGPSVEAEPEY--TFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTVAELTQRED 2651
Cdd:PTZ00121 1651 ELKKAEEENKIKAAEEAkkAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEA 1712
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1339-1709 |
5.41e-14 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 79.01 E-value: 5.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1339 QLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQsseAEIQAKAQQVeaAERSRMRIEEE 1418
Cdd:pfam17380 273 QLLHIVQHQKAVSERQQQEKFEKMEQERLRQEKEEKAREVERRRKLEEAEKARQ---AEMDRQAAIY--AEQERMAMERE 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1419 IRVVRLQLEttERQRggaegELQALRaraEEAEAQKRQAQEEAERLRRQVQDESQRKRQaEAELALRVK-AEAEAAREKQ 1497
Cdd:pfam17380 348 RELERIRQE--ERKR-----ELERIR---QEEIAMEISRMRELERLQMERQQKNERVRQ-ELEAARKVKiLEEERQRKIQ 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1498 RALQALDELRLQAEEA-ERRLRQAEAERARqvqvaletaqrsaevELQSKRASFAEKTAQLERTLQEEhvtvaqlreeae 1576
Cdd:pfam17380 417 QQKVEMEQIRAEQEEArQREVRRLEEERAR---------------EMERVRLEEQERQQQVERLRQQE------------ 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1577 rraqqqaeAERAREEAERELE-RWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQavrQRELA 1655
Cdd:pfam17380 470 --------EERKRKKLELEKEkRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE---RRREA 538
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1656 EQELEKQRQLAE--GTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEAT 1709
Cdd:pfam17380 539 EEERRKQQEMEErrRIQEQMRKATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| CH_SMTNL1 |
cd21260 |
calponin homology (CH) domain found in smoothelin-like protein 1; Smoothelin-like protein 1 ... |
129-230 |
5.66e-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: 71.27 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 129 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 208
Cdd:cd21260 3 KNMLLEWCRAKTRGYEHVDIQNFSSSWSSGMAFCALIHKFFPDAFDYAELDPANRRHNFTLAFSTAEKHADCAPLLEVED 82
|
90 100
....*....|....*....|...
gi 254675251 209 -VDVPQPDEKSIITYVSSLYDAM 230
Cdd:cd21260 83 mVRMSVPDSKCVYTYIQELYRSL 105
|
|
| CH_FLN_rpt2 |
cd21230 |
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ... |
127-224 |
7.41e-14 |
|
second calponin homology (CH) domain found in filamins; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. Members of this family contain two copies of the CH domain. The model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409079 Cd Length: 103 Bit Score: 70.49 E-value: 7.41e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI----DMNKVYRqtnLENLDQAFSVAERDLGVTR 202
Cdd:cd21230 1 TPKQRLLGWIQNKIPQ---LPITNFTTDWNDGRALGALVDSCAPGLCpdweTWDPNDA---LENATEAMQLAEDWLGVPQ 74
|
90 100
....*....|....*....|..
gi 254675251 203 LLDPEDVDVPQPDEKSIITYVS 224
Cdd:cd21230 75 LITPEEIINPNVDEMSVMTYLS 96
|
|
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
127-227 |
7.76e-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: 70.87 E-value: 7.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 206
Cdd:cd21256 14 SKRNALLKWCQKKTEGYQNIDITNFSSSWNDGLAFCALLHTYLPAHIPYQELNSQDKRRNFTLAFQAAE-SVGIKSTLDI 92
|
90 100
....*....|....*....|..
gi 254675251 207 ED-VDVPQPDEKSIITYVSSLY 227
Cdd:cd21256 93 NEmVRTERPDWQSVMTYVTAIY 114
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
953-1553 |
2.49e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 77.26 E-value: 2.49e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 953 ELKDIRLQLEAcETRTVHRLRlpldkdPARECAQRIAEQQKAQAEVEGLGKGVARLSAEAEKVLAlpepSPAAPTLRSEL 1032
Cdd:COG4913 236 DLERAHEALED-AREQIELLE------PIRELAERYAAARERLAELEYLRAALRLWFAQRRLELL----EAELEELRAEL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1033 ELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEvlktheEQLKeaqavpatlQELEATKASLKKLRAQAEAQQPVFN 1112
Cdd:COG4913 305 ARLEAELERLEARLDALREELDELEAQIRGNGGDRL------EQLE---------REIERLERELEERERRRARLEALLA 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1113 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQllERWQAVLAQTDVRqRELEQLGRQLRYYRESADPLSAWLQDAK 1192
Cdd:COG4913 370 ALGLPLPASAEEFAALRAEAAALLEALEEELEALEE--ALAEAEAALRDLR-RELRELEAEIASLERRKSNIPARLLALR 446
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1193 RRQEQ-----IQAVPIAnC---QAAREQLRQEKAlleeIER--HGEKV-----EECQKFAKQYINAIKDyELQLITYKAQ 1257
Cdd:COG4913 447 DALAEalgldEAELPFV-GeliEVRPEEERWRGA----IERvlGGFALtllvpPEHYAAALRWVNRLHL-RGRLVYERVR 520
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1258 LEPVASPAKKPKVQSGSEsviqeyvdlrtrysELTTLTSQYIKFISETLRRM------EEEERLAEQQRAEERERLA-EV 1330
Cdd:COG4913 521 TGLPDPERPRLDPDSLAG--------------KLDFKPHPFRAWLEAELGRRfdyvcvDSPEELRRHPRAITRAGQVkGN 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1331 EAALEK--QRQLAEAH------AQAKAQAELEAQELQRRMQEEVARREEAAvDAQQQKRSIQEELQHLRQSSEAEIqaka 1402
Cdd:COG4913 587 GTRHEKddRRRIRSRYvlgfdnRAKLAALEAELAELEEELAEAEERLEALE-AELDALQERREALQRLAEYSWDEI---- 661
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1403 qQVEAAERSRMRIEEEIRvvrlQLETterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1482
Cdd:COG4913 662 -DVASAEREIAELEAELE----RLDA-------SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEEL 729
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1483 -ALRVKAEAEAAREKQRALQALDELRlqAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEK 1553
Cdd:COG4913 730 dELQDRLEAAEDLARLELRALLEERF--AAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFNRE 799
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3021-3059 |
3.17e-13 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 66.20 E-value: 3.17e-13
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3021 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPELHEKL 3059
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1113-1938 |
3.88e-13 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 76.53 E-value: 3.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1113 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQRelEQLGRqlryYRESADPLSAw 1187
Cdd:PRK04863 290 ELRRELYTSRRQLAAEQYRLVEMARELAELNEAESDLEQDYQAAsdhlnLVQTALRQQ--EKIER----YQADLEELEE- 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1188 lqdakRRQEQIQAVPIANCQAAREQLRQEKAlLEEIER-------HGEKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1259
Cdd:PRK04863 363 -----RLEEQNEVVEEADEQQEENEARAEAA-EEEVDElksqladYQQALDVQQTRAIQYQQAVQALErAKQLCGLPDLT 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1260 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERlaeveaALEKQRQ 1339
Cdd:PRK04863 437 ADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQFEQAYQLVRKIAGEVSRSEAWDVARELLR------RLREQRH 510
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1340 LAEAHAQAKAQ-AELEAQELQRRMQEEVARReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEE 1418
Cdd:PRK04863 511 LAEQLQQLRMRlSELEQRLRQQQRAERLLAE---FCKRLGKNLDDEDELEQLQEELEARLESLSESVSEARERRMALRQQ 587
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1419 IRvvrlqletterqrggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDE---SQRKRQAEAELALRVKAEAEAARE 1495
Cdd:PRK04863 588 LE------------------QLQARIQRLAARAPAWLAAQDALARLREQSGEEfedSQDVTEYMQQLLERERELTVERDE 649
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1496 KQRALQALDE--LRLQAEEAER--RLRQAeAERARQV-------QVALETA---------QRSAEVELQSKRAsfAEKTA 1555
Cdd:PRK04863 650 LAARKQALDEeiERLSQPGGSEdpRLNAL-AERFGGVllseiydDVSLEDApyfsalygpARHAIVVPDLSDA--AEQLA 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1556 QLERTLQE------------EHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANEAL--RLRLQAEEVAQQks 1621
Cdd:PRK04863 727 GLEDCPEDlyliegdpdsfdDSVFSVEELEKAVVVKIADRQWRYSRFPEVPLFGR---AAREKRieQLRAEREELAER-- 801
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1622 LAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEEL 1701
Cdd:PRK04863 802 YATLSFDVQKLQRLHQAFSRFIGSHLAVAFEADPEAELRQLN-------RRRVELERALADHESQEQQQRSQLEQAKEGL 874
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1702 ARL-QHEATAATQKRQELEAELAKVRAEMEvllaskaRAEEESRSTSEKSKQ--RLEAEAGRFRELAEEAARLRALAEEA 1778
Cdd:PRK04863 875 SALnRLLPRLNLLADETLADRVEEIREQLD-------EAEEAKRFVQQHGNAlaQLEPIVSVLQSDPEQFEQLKQDYQQA 947
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1779 KRQRQlaeedAARQRAEAervLTEklaAISEATRLKTEAEIALKEKEAE-NERLR-RLAEDEAfQRRRLEEQAALHKA-- 1854
Cdd:PRK04863 948 QQTQR-----DAKQQAFA---LTE---VVQRRAHFSYEDAAEMLAKNSDlNEKLRqRLEQAEQ-ERTRAREQLRQAQAql 1015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1855 -DIEERLAQLRKASeselerqkglveDTLRQRRQ-VEEEIMALKVSF-----EKAAAGKAELELEL--GRIRSNAEDTMR 1925
Cdd:PRK04863 1016 aQYNQVLASLKSSY------------DAKRQMLQeLKQELQDLGVPAdsgaeERARARRDELHARLsaNRSRRNQLEKQL 1083
|
890
....*....|...
gi 254675251 1926 SKEQAELEAARQR 1938
Cdd:PRK04863 1084 TFCEAEMDNLTKK 1096
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1360-1884 |
4.16e-13 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 76.49 E-value: 4.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1360 RRMQEEVA---RREEAAVDAQQQKRSiqeeLQHLRQSSEaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggA 1436
Cdd:COG4913 228 DALVEHFDdleRAHEALEDAREQIEL----LEPIRELAE-RYAAARERLAELEYLRAALRLWFAQRRLELLEAELEE--L 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1437 EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAER 1515
Cdd:COG4913 301 RAELARLEAELERLEARLDALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAE 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1516 RLrQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTlqeehvtvaqlreeaerraqqqaeaerareeaERE 1595
Cdd:COG4913 381 EF-AALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELREL--------------------------------EAE 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1596 LERwqLKAN--------EALRLRLQAE---------------EVAQ-----------------------QKSLAQA---- 1625
Cdd:COG4913 428 IAS--LERRksniparlLALRDALAEAlgldeaelpfvgeliEVRPeeerwrgaiervlggfaltllvpPEHYAAAlrwv 505
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1626 DAEKQKEEAEREARRRGKAEEQAVR--QRELAEqELEKQRQLAEGTAQQRLAA---------EQELIRL-RAETEQG--- 1690
Cdd:COG4913 506 NRLHLRGRLVYERVRTGLPDPERPRldPDSLAG-KLDFKPHPFRAWLEAELGRrfdyvcvdsPEELRRHpRAITRAGqvk 584
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1691 ------------------------EQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1746
Cdd:COG4913 585 gngtrhekddrrrirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVA 664
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1747 S--------EKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEklaaiseatrlkteaE 1818
Cdd:COG4913 665 SaereiaelEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEE---------------L 729
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1819 IALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQ 1884
Cdd:COG4913 730 DELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
|
|
| CH_ASPM_rpt1 |
cd21223 |
first calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
30-109 |
5.73e-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: 5.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 30 HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM----RFHKLQNVQIALDYLRHRQV----KLVNIRNDDIADGNPKLT 101
Cdd:cd21223 25 AVTNLAVDLRDGVRLCRLVELLTGDWSLLSKLRVpaisRLQKLHNVEVALKALKEAGVlrggDGGGITAKDIVDGHREKT 104
|
....*...
gi 254675251 102 LGLIWTII 109
Cdd:cd21223 105 LALLWRII 112
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
127-227 |
7.05e-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: 67.75 E-value: 7.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAErDLGVTRLLDP 206
Cdd:cd21257 8 SKRNALLKWCQKKTEGYPNIDITNFSSSWSDGLAFCALLHTYLPAHIPYQELSSQDKKRNLLLAFQAAE-SVGIKPSLEL 86
|
90 100
....*....|....*....|..
gi 254675251 207 ED-VDVPQPDEKSIITYVSSLY 227
Cdd:cd21257 87 SEmMYTDRPDWQSVMQYVAQIY 108
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1051-1901 |
7.13e-13 |
|
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: 75.78 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1051 EKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQ--PVFNTLRDELRGAQEVGERL 1128
Cdd:pfam02463 180 EETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEEriDLLQELLRDEQEEIESSKQE 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1129 QQRHGERDVEVERWR---ERVTQLLERWQAVLAqtdvrqRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIAN 1205
Cdd:pfam02463 260 IEKEEEKLAQVLKENkeeEKEKKLQEEELKLLA------KEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKE 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1206 CQAAREQLRQEKALLEEIERHGEKVEEC-QKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDL 1284
Cdd:pfam02463 334 KEEIEELEKELKELEIKREAEEEEEEELeKLQEKLEQLEEELLAKKKLESERLSSAAKLKEEELELKSEEEKEAQLLLEL 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1285 RTRYSELTTLTSQYIKFISEtlrrmEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQE 1364
Cdd:pfam02463 414 ARQLEDLLKEEKKEELEILE-----EEEESIELKQGKLTEEKEELEKQELKLLKDELELKKSEDLLKETQLVKLQEQLEL 488
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1365 EVARREEAAVDAQQQKrsiqeelqhlrqSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALR 1444
Cdd:pfam02463 489 LLSRQKLEERSQKESK------------ARSGLKVLLALIKDGVGGRIISAHGRLGDLGVAVENYKVAISTAVIVEVSAT 556
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1445 ARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAER 1524
Cdd:pfam02463 557 ADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDDKRAKVVEGILKDTELTK 636
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1525 ARQVQVALETaQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKAN 1604
Cdd:pfam02463 637 LKESAKAKES-GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKL 715
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1605 EALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLR 1684
Cdd:pfam02463 716 KLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLKVEEEKEEK 795
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1685 ----AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR 1760
Cdd:pfam02463 796 lkaqEEELRALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEKLAEEELERLEEEITKEELLQELLLK 875
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1761 FRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE--AENERLRRLAEDE 1838
Cdd:pfam02463 876 EEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELllEEADEKEKEENNK 955
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 1839 AFQRRRlEEQAALHKADIEERLAQLRKASESELERQKGLVEDtlrQRRQVEEEIMALKVSFEK 1901
Cdd:pfam02463 956 EEEEER-NKRLLLAKEELGKVNLMAIEEFEEKEERYNKDELE---KERLEEEKKKLIRAIIEE 1014
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1310-2017 |
1.10e-12 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 75.10 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1310 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElEAQELQRRMQE----EVARREEAAVdaqQQKRSIQE 1385
Cdd:TIGR02169 169 DRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRREREKAE-RYQALLKEKREyegyELLKEKEALE---RQKEAIER 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1386 ELQHLRQS---SEAEIQAKAQQVEAAERSRMRIEEEIRVVrlqletterqrggAEGELQALRARAEEAEAqkrqaqeEAE 1462
Cdd:TIGR02169 245 QLASLEEElekLTEEISELEKRLEEIEQLLEELNKKIKDL-------------GEEEQLRVKEKIGELEA-------EIA 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1463 RLRRQVQDESQRKRQAEAELAlrvKAEAEaarekqralqaLDELRLQAEEAERRLRQAEAERArqvqvALETAQRSAEVE 1542
Cdd:TIGR02169 305 SLERSIAEKERELEDAEERLA---KLEAE-----------IDKLLAEIEELEREIEEERKRRD-----KLTEEYAELKEE 365
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1543 LQSKRASFAEKTAQLERTLQEehvtvaqlreeaerraqqqaeaeraREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1622
Cdd:TIGR02169 366 LEDLRAELEEVDKEFAETRDE-------------------------LKDYREKLEKLKREINELKRELDRLQEELQRLSE 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1623 AQADAEKQkeeaeREARRRGKAEEQAVRqrELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1702
Cdd:TIGR02169 421 ELADLNAA-----IAGIEAKINELEEEK--EDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1703 RLQHEATAATQ-----KRQELE------------AELAKVRAEMEVLLASKA----------------------RAEEES 1743
Cdd:TIGR02169 494 EAEAQARASEErvrggRAVEEVlkasiqgvhgtvAQLGSVGERYATAIEVAAgnrlnnvvveddavakeaiellKRRKAG 573
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1744 RST-----------SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEE-DAARQRAEAERVLT------EKLA 1805
Cdd:TIGR02169 574 RATflplnkmrderRDLSILSEDGVIGFAVDLVEFDPKYEPAFKYVFGDTLVVEDiEAARRLMGKYRMVTlegelfEKSG 653
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1806 AI-----------SEATRLKTEA-EIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLR-KASESELE 1872
Cdd:TIGR02169 654 AMtggsraprggiLFSRSEPAELqRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEiEQLEQEEE 733
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1873 RQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELeaaRQRQLAAEEEQRRREAE 1952
Cdd:TIGR02169 734 KLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRI---PEIQAELSKLEEEVSRI 810
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1953 ERVQRSLAAEEEAARQRKVALE-EVERLKAKVE--EARRLRERAEQESARQLQLAQEAAQKRLQAEEK 2017
Cdd:TIGR02169 811 EARLREIEQKLNRLTLEKEYLEkEIQELQEQRIdlKEQIKSIEKEIENLNGKKEELEEELEELEAALR 878
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1065-1561 |
1.22e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 74.95 E-value: 1.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1065 GAEEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELrgAQEVGERLQQRHGERDVEVERWRE 1144
Cdd:COG4913 239 RAHEALEDAREQIELLEPIRELAERYAAARERLAELEYLRAALRLWFAQRRLEL--LEAELEELRAELARLEAELERLEA 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1145 RVTQLLERWQAVLAQ-TDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEI 1223
Cdd:COG4913 317 RLDALREELDELEAQiRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL 396
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1224 ErhgEKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIS 1303
Cdd:COG4913 397 E---EELEALEEALAEAEAALRDLRRELRELEAEIA---------SLERRKSNIPARLLALRDALAEALGLDEAELPFVG 464
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1304 ETLRRMEEEERLaeqQRAEER-------------ERLAEVEAALEKQR-------QLAEAHAQAKAQAELEAQELQRRM- 1362
Cdd:COG4913 465 ELIEVRPEEERW---RGAIERvlggfaltllvppEHYAAALRWVNRLHlrgrlvyERVRTGLPDPERPRLDPDSLAGKLd 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1363 ----------QEEVARREEAA-VDAQQQ----KRSIQEELQ--------------HLR------QSSEAEIQAKAQQVEA 1407
Cdd:COG4913 542 fkphpfrawlEAELGRRFDYVcVDSPEElrrhPRAITRAGQvkgngtrhekddrrRIRsryvlgFDNRAKLAALEAELAE 621
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1408 AERSRMRIEEEIRVVRLQLETTERQRGGAEG---------ELQALRARAEEAEAQKRQAQE---EAERLRRQVQDESQRK 1475
Cdd:COG4913 622 LEEELAEAEERLEALEAELDALQERREALQRlaeyswdeiDVASAEREIAELEAELERLDAssdDLAALEEQLEELEAEL 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1476 RQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQV--QVALETAQRSAEVELQSKRASFAEK 1553
Cdd:COG4913 702 EELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERfaAALGDAVERELRENLEERIDALRAR 781
|
....*...
gi 254675251 1554 TAQLERTL 1561
Cdd:COG4913 782 LNRAEEEL 789
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4275-4313 |
1.51e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 64.27 E-value: 1.51e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 4275 LLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMVDRI 4313
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_PLS_rpt3 |
cd21298 |
third calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
14-115 |
1.91e-12 |
|
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: 66.88 E-value: 1.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 14 KTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSL-------PREKGRMRFHKLQNVQIALDYLRHRQVKLV 86
Cdd:cd21298 9 KTYRNWMNS--LGVNPFVNHLYSDLRDGLVLLQLYDKIKPGVVdwsrvnkPFKKLGANMKKIENCNYAVELGKKLKFSLV 86
|
90 100
....*....|....*....|....*....
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILHFQIS 115
Cdd:cd21298 87 GIGGKDIYDGNRTLTLALVWQLMRAYTLS 115
|
|
| CH_SF |
cd00014 |
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ... |
129-228 |
2.11e-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: 66.21 E-value: 2.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 129 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTN---LENLDQAFSVAER-DLGVTRLL 204
Cdd:cd00014 1 EEELLKWINEVLGEELPVSITDLFESLRDGVLLCKLINKLSPGSIPKINKKPKSPfkkRENINLFLNACKKlGLPELDLF 80
|
90 100
....*....|....*....|....
gi 254675251 205 DPEDVdVPQPDEKSIITYVSSLYD 228
Cdd:cd00014 81 EPEDL-YEKGNLKKVLGTLWALAL 103
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1324-1849 |
3.27e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 73.35 E-value: 3.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1324 RERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQ 1403
Cdd:COG3899 722 AEALRYLERALELLPPDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYANLGLL 801
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1404 QVEAAERSRMRIEEEIRVV-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL--RRQVQDESQRKRQAEA 1480
Cdd:COG3899 802 LLGDYEEAYEFGELALALAeRLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETgdAALALLALAAAAAAAA 881
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1481 ELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERT 1560
Cdd:COG3899 882 AAAALAAAAAAAARLLAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALA 961
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1561 LQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARR 1640
Cdd:COG3899 962 AAAAAAAAAALAAAAAAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAA 1041
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1641 RGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA 1720
Cdd:COG3899 1042 ALALLAALAAAAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALA 1121
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1721 ELAKVRAEMEVLLASKARAEEESRSTsekskqRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1800
Cdd:COG3899 1122 ALALAAAARAAAALLLLAAALALALA------ALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAAL 1195
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 254675251 1801 TEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1849
Cdd:COG3899 1196 LAALLALAARLAALLALALLALEAAALLLLLLLAALALAAALLALRLLA 1244
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1438-2016 |
3.35e-12 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 73.35 E-value: 3.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1438 GELQALRARAEEA--EAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAeAEAARekqralqaldeLRLQAEEAER 1515
Cdd:COG3899 699 GERDRAARLLLRAarRALARGAYAEALRYLERALELLPPDPEEEYRLALLLEL-AEALY-----------LAGRFEEAEA 766
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1516 RLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQlreeaerrAQQQAEAERAREEAERE 1595
Cdd:COG3899 767 LLERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAE--------RLGDRRLEARALFNLGF 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1596 LERWQLKANEALRLRLQAEEVAQQKSLAQADAekqkeeaEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLA 1675
Cdd:COG3899 839 ILHWLGPLREALELLREALEAGLETGDAALAL-------LALAAAAAAAAAAAALAAAAAAAARLLAAAAAALAAAAAAA 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1676 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstsekskQRLE 1755
Cdd:COG3899 912 ALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAA---------AAAA 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1756 AEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1835
Cdd:COG3899 983 AAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAAAAAAAL 1062
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1836 EDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGR 1915
Cdd:COG3899 1063 AAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALLLLAAAL 1142
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1916 IRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQ 1995
Cdd:COG3899 1143 ALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLALEAAAL 1222
|
570 580
....*....|....*....|.
gi 254675251 1996 ESARQLQLAQEAAQKRLQAEE 2016
Cdd:COG3899 1223 LLLLLLAALALAAALLALRLL 1243
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3097-3135 |
3.57e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.50 E-value: 3.57e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3097 LLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKETNRAL 3135
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt2 |
cd21229 |
second calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
129-224 |
3.75e-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: 65.49 E-value: 3.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 129 KEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPE 207
Cdd:cd21229 5 KKLMLAWLQAVLPE---LKITNFSTDWNDGIALSALLDYCKPGLCpNWRKLDPSNSLENCRRAMDLAKREFNIPMVLSPE 81
|
90
....*....|....*..
gi 254675251 208 DVDVPQPDEKSIITYVS 224
Cdd:cd21229 82 DLSSPHLDELSGMTYLS 98
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3352-3390 |
3.78e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 63.12 E-value: 3.78e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3352 LLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPELHEKL 3390
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1075-1797 |
4.30e-12 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 73.06 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1075 EQLKEAQAvpATLQELEATKASLKKLRAQAEAQQPV------FNTLRDELRGAQEVGERLQQRHGERDVEVERWRERV-- 1146
Cdd:COG3096 316 EELSARES--DLEQDYQAASDHLNLVQTALRQQEKIeryqedLEELTERLEEQEEVVEEAAEQLAEAEARLEAAEEEVds 393
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1147 --TQLLERWQAVlaqtDVRQRE----------LEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQ------A 1208
Cdd:COG3096 394 lkSQLADYQQAL----DVQQTRaiqyqqavqaLEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQklsvadA 469
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1209 AREQLRQEKALLEEIERHGEKVEECQKfAKQYINAIKDYELQLitykAQLEPVAspakkpkvqsgsesviQEYVDLRTRY 1288
Cdd:COG3096 470 ARRQFEKAYELVCKIAGEVERSQAWQT-ARELLRRYRSQQALA----QRLQQLR----------------AQLAELEQRL 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1289 S---ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAE---------LEAQ 1356
Cdd:COG3096 529 RqqqNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKelaarapawLAAQ 608
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1357 ELQRRMQEEVArreEAAVDAQQQKRSIQEELQHLRQsseaeiqAKAQQVEAAERsRMRIEEEIRvvRLQletterQRGGA 1436
Cdd:COG3096 609 DALERLREQSG---EALADSQEVTAAMQQLLERERE-------ATVERDELAAR-KQALESQIE--RLS------QPGGA 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1437 E-GELQALRAR-----------------AEEAEAQ---KRQA--QEEAERLRRQVQ-------------------DESQR 1474
Cdd:COG3096 670 EdPRLLALAERlggvllseiyddvtledAPYFSALygpARHAivVPDLSAVKEQLAgledcpedlyliegdpdsfDDSVF 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1475 KRQaEAELALRVKAE---------------AEAAREKQralqaLDELRLQAEE-----AERRLRQAEAER---------A 1525
Cdd:COG3096 750 DAE-ELEDAVVVKLSdrqwrysrfpevplfGRAAREKR-----LEELRAERDElaeqyAKASFDVQKLQRlhqafsqfvG 823
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1526 RQVQVALETaqrSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRA-------QQQAEAERAREEAERELER 1598
Cdd:COG3096 824 GHLAVAFAP---DPEAELAALRQRRSELERELAQHRAQEQQLRQQLDQLKEQLQllnkllpQANLLADETLADRLEELRE 900
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1599 WQLKANEALR-LRLQAEEVAQQKSLAQA-DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ-LAEGTAQQRLA 1675
Cdd:COG3096 901 ELDAAQEAQAfIQQHGKALAQLEPLVAVlQSDPEQFEQLQADYLQAKEQQRRLKQQIFALSEVVQRRPhFSYEDAVGLLG 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1676 AEQELI-RLRAETEQGEQQRQLLEEELARLQHEATAATQKR--------------QELEAELakvrAEMEVLLAskARAE 1740
Cdd:COG3096 981 ENSDLNeKLRARLEQAEEARREAREQLRQAQAQYSQYNQVLaslkssrdakqqtlQELEQEL----EELGVQAD--AEAE 1054
|
810 820 830 840 850
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1741 EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAE 1797
Cdd:COG3096 1055 ERARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVV 1111
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1308-2431 |
6.64e-12 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 72.52 E-value: 6.64e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1308 RMEEEERLAEQQRAEERERLAEVEAAL----EKQRQLAEAHA----QAKAQAEL--EAQELQRRMQ------EEVARREE 1371
Cdd:pfam01576 2 RQEEEMQAKEEELQKVKERQQKAESELkeleKKHQQLCEEKNalqeQLQAETELcaEAEEMRARLAarkqelEEILHELE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1372 AAVDaQQQKRSIQeeLQHLRQSSEAEIQAKAQQVEAAERSRMrieeeirvvRLQLETTErqrggAEGELQALRARAEEAE 1451
Cdd:pfam01576 82 SRLE-EEEERSQQ--LQNEKKKMQQHIQDLEEQLDEEEAARQ---------KLQLEKVT-----TEAKIKKLEEDILLLE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1452 AQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKaeaeaAREKQRALQALDELRLQAEEAERRlrqaEAERARQVQVA 1531
Cdd:pfam01576 145 DQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSK-----LKNKHEAMISDLEERLKKEEKGRQ----ELEKAKRKLEG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1532 LETAQRSAEVELQskrASFAEKTAQLERtlQEEHVTVAQLreeaerraqqqaeaerareeaerELERWQLKANEALRlrl 1611
Cdd:pfam01576 216 ESTDLQEQIAELQ---AQIAELRAQLAK--KEEELQAALA-----------------------RLEEETAQKNNALK--- 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1612 QAEEVAQQKSLAQADAEKQKEeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTaQQRLAAEQELiRLRAETEQGE 1691
Cdd:pfam01576 265 KIRELEAQISELQEDLESERA-----------ARNKAEKQRRDLGEELEALKTELEDT-LDTTAAQQEL-RSKREQEVTE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1692 QQRQLLEEEL---ARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEK----SKQRLEAEAGRfREL 1764
Cdd:pfam01576 332 LKKALEEETRsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAElrtlQQAKQDSEHKR-KKL 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1765 AEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-------------LTEKLAAIS-----------EATRLKTEAEIA 1820
Cdd:pfam01576 411 EGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaegknikLSKDVSSLEsqlqdtqellqEETRQKLNLSTR 490
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1821 LKEKEAENERLRRLAEDEAFQRRRLEEQAALHKAdieeRLAQLRKASESELERQKGLVEDtlrqRRQVEEEIMALKVSFE 1900
Cdd:pfam01576 491 LRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLSDMKKKLEEDAGTLEALEEG----KKRLQRELEALTQQLE 562
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1901 KAAAGKAELELELGRIRSNAEDTMrskeqaeLEAARQRQLAAEEEQRRREAEErvqrsLAAEEEAARQRKVALEEVERLK 1980
Cdd:pfam01576 563 EKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEKKQKKFDQ-----MLAEEKAISARYAEERDRAEAE 630
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1981 AKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahafvvqqreeelqqtlqqeqnmLDRLRSEAEAARRAAEEAEE 2060
Cdd:pfam01576 631 AREKETRALSLARALEEALEAKEELERTNKQLRAE-------------------------MEDLVSSKDDVGKNVHELER 685
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2061 AREQAEREAAQSRKQVEEAERLKQSaeeqaqaqaqaqAAAEKLRKEAEQEAARRAQAeqaalKQKQAADAEMEKHKKfae 2140
Cdd:pfam01576 686 SKRALEQQVEEMKTQLEELEDELQA------------TEDAKLRLEVNMQALKAQFE-----RDLQARDEQGEEKRR--- 745
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2141 QTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALI 2220
Cdd:pfam01576 746 QLVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQMKDLQRELEEARASRDEIL 825
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2221 LRDKDNTQRFLEEEAEKMkQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2300
Cdd:pfam01576 826 AQSKESEKKLKNLEAELL-QLQEDLAASERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEEQSN 904
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2301 KELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQrqleMSAEAERLKLRMAEMSRAQ---------------ARAE 2365
Cdd:pfam01576 905 TELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQ----LERQNKELKAKLQEMEGTVkskfkssiaaleakiAQLE 980
|
1130 1140 1150 1160 1170 1180
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 2366 EDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEA 2431
Cdd:pfam01576 981 EQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQLKRQLEEAEEEA 1046
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2693-2731 |
6.93e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 6.93e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 2693 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPELHHKL 2731
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_MICAL1 |
cd21196 |
calponin homology (CH) domain found in molecule interacting with CasL protein 1; MICAL-1, also ... |
129-229 |
7.48e-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: 64.68 E-value: 7.48e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 129 KEKLLLWSQRMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERDLGVTRLLDPED 208
Cdd:cd21196 5 QEELLRWCQEQTAGYPGVHVSDLSSSWADGLALCALVYRLQPGLLEPSELQGLGALEATAWALKVAENELGITPVVSAQA 84
|
90 100
....*....|....*....|.
gi 254675251 209 VdVPQPDEKSIITYVSSLYDA 229
Cdd:cd21196 85 V-VAGSDPLGLIAYLSHFHSA 104
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3930-3968 |
9.03e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 9.03e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3930 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEFKDKL 3968
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3763-3801 |
9.20e-12 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 62.35 E-value: 9.20e-12
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3763 LLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDTHDQL 3801
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1391-2017 |
1.72e-11 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 71.02 E-value: 1.72e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1391 RQSSEAEIQAKAQQVEA--AERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE----RL 1464
Cdd:pfam12128 209 DGVVPPKSRLNRQQVEHwiRDIQAIAGIMKIRPEFTKLQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQetsaEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1465 RRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVeLQ 1544
Cdd:pfam12128 289 NQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKA-LT 367
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1545 SKRASFAEKTAQLERTLQEEHVT-VAQLREEAERRAQQQAEAERAREEAERELE---RWQLKAN------EALRLRLQAE 1614
Cdd:pfam12128 368 GKHQDVTAKYNRRRSKIKEQNNRdIAGIKDKLAKIREARDRQLAVAEDDLQALEselREQLEAGklefneEEYRLKSRLG 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1615 EVAQQKSLAQADAEK--QKEEAEREARRRGKAEEQAVRQRELAEQELekqrqlaegtAQQRLAAEQELIRLRAETEQGEQ 1692
Cdd:pfam12128 448 ELKLRLNQATATPELllQLENFDERIERAREEQEAANAEVERLQSEL----------RQARKRRDQASEALRQASRRLEE 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1693 QRQLLEEelarLQHEATAATQKRQE-LEAELAKVRAEMEVLLASK--ARAEEESRSTSEKSKQRLEAEAGRFRELAEEAA 1769
Cdd:pfam12128 518 RQSALDE----LELQLFPQAGTLLHfLRKEAPDWEQSIGKVISPEllHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVP 593
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1770 RLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQA 1849
Cdd:pfam12128 594 EWAASEEELRERLDKAEEALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQSEKDKKNKAL 673
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1850 ALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEkaaagkAELELELGRIRSN--AEDTMRSK 1927
Cdd:pfam12128 674 AERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVE------GALDAQLALLKAAiaARRSGAKA 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1928 EQAELEAARQRQLAAE-EEQRRREAEERVQRSLAAEEEAARQRKVA------------LEEVERLKAKVEEARRLRERAE 1994
Cdd:pfam12128 748 ELKALETWYKRDLASLgVDPDVIAKLKREIRTLERKIERIAVRRQEvlryfdwyqetwLQRRPRLATQLSNIERAISELQ 827
|
650 660
....*....|....*....|...
gi 254675251 1995 QESARQlqlaQEAAQKRLQAEEK 2017
Cdd:pfam12128 828 QQLARL----IADTKLRRAKLEM 846
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1643-1859 |
1.95e-11 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 69.41 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1643 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1722
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAEL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1723 AKVRAEMEVLLASKARAEEESRST---SEKSKQRLEAEAGRFRELAEE-AARLRALAEEAKRQRQLAEEdAARQRAEAER 1798
Cdd:COG4942 100 EAQKEELAELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPArREQAEELRADLAELAALRAE-LEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1799 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEER 1859
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
927-1563 |
2.97e-11 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 70.38 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 927 SRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACEtrtvhrLRLPLDKDPARECAQRIAEQQKAQA-EVEGLGKGV 1005
Cdd:TIGR00618 162 SKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLT------LRSQLLTLCTPCMPDTYHERKQVLEkELKHLREAL 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1006 ARLSAEAEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVlKTHEEQLKEAQAVPA 1085
Cdd:TIGR00618 236 QQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHI-KAVTQIEQQAQRIHT 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1086 TLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVE-------------RWRERVTQLLER 1152
Cdd:TIGR00618 315 ELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREiscqqhtltqhihTLQQQKTTLTQK 394
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1153 WQAVLAQTDVRQRELEQLGRQLRYYR-------------ESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKAL 1219
Cdd:TIGR00618 395 LQSLCKELDILQREQATIDTRTSAFRdlqgqlahakkqqELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQ 474
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1220 LEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVA-----SPAKKPKVQSGSESVIQEYVDLRTRYSELTTL 1294
Cdd:TIGR00618 475 LQTKEQIHLQETRKKAVVLARLLELQEEPCPLCGSCIHPNPARqdidnPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSE 554
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1295 TSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAV 1374
Cdd:TIGR00618 555 RKQ-RASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLH 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1375 DAQQQKRsIQEELQHLRQssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALraraEEAEAQK 1454
Cdd:TIGR00618 634 LQQCSQE-LALKLTALHA--LQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEML----AQCQTLL 706
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1455 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAeaarekqralQALDELRLQAEEAERRLRQAEAERARQVQVALET 1534
Cdd:TIGR00618 707 RELETHIEEYDREFNEIENASSSLGSDLAAREDALN----------QSLKELMHQARTVLKARTEAHFNNNEEVTAALQT 776
|
650 660 670
....*....|....*....|....*....|.
gi 254675251 1535 AQRSAEV--ELQSKRASFAEKTAQLERTLQE 1563
Cdd:TIGR00618 777 GAELSHLaaEIQFFNRLREEDTHLLKTLEAE 807
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1278-1776 |
4.02e-11 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 69.99 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1278 IQEYVDLRTRYSELTTLTSQYIkfiSETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEahaqakaqaeleaqE 1357
Cdd:PRK04863 249 IRVTQSDRDLFKHLITESTNYV---AADYMRHANERRVHLEEALELRRELYTSRRQLAAEQYRLV--------------E 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1358 LQRRMQEEVARREEAAVDAQQQKrsiqeelQHLRQSSEAEIQAKA--QQVEAAERSRMRIEEEIRVVRLQLEtterqrgg 1435
Cdd:PRK04863 312 MARELAELNEAESDLEQDYQAAS-------DHLNLVQTALRQQEKieRYQADLEELEERLEEQNEVVEEADE-------- 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1436 aegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQR----------KRQAEAELAlRVKA-------EAEAAREKQR 1498
Cdd:PRK04863 377 ----------QQEENEARAEAAEEEVDELKSQLADYQQAldvqqtraiqYQQAVQALE-RAKQlcglpdlTADNAEDWLE 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1499 ALQA-LDELRLQAEEAERRLRQAEAERaRQVQVALETAQR-SAEVElqskRASFAEKTAQLERTLQEEHVTVAQLreeae 1576
Cdd:PRK04863 446 EFQAkEQEATEELLSLEQKLSVAQAAH-SQFEQAYQLVRKiAGEVS----RSEAWDVARELLRRLREQRHLAEQL----- 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1577 rraqqqaeaerareeaerelerwqlkanEALRLRLQAeevAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAE 1656
Cdd:PRK04863 516 ----------------------------QQLRMRLSE---LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELE 564
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1657 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQL---LEEELARLQHEATAATQKRQELEAELAKvraemevlL 1733
Cdd:PRK04863 565 ARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAwlaAQDALARLREQSGEEFEDSQDVTEYMQQ--------L 636
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 254675251 1734 ASKARAEEESRSTSEKSKQRLEAEAGRFREL-AEEAARLRALAE 1776
Cdd:PRK04863 637 LERERELTVERDELAARKQALDEEIERLSQPgGSEDPRLNALAE 680
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1618-1827 |
4.65e-11 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 68.29 E-value: 4.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1618 QQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAegtaQQRLAAeQELIRLRAETEQGEQQRQLL 1697
Cdd:PRK09510 68 QQQQKSAKRAEEQRKK---------KEQQQAEELQQKQAAEQERLKQLE----KERLAA-QEQKKQAEEAAKQAALKQKQ 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1698 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1777
Cdd:PRK09510 134 AEEAAAKAAAAAKAKAEAEAKRAAAAAKKAAAE---AKKKAEAEAAKKAAAEAKKKAEAEA---AAKAAAEAKKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1778 AKRQRQLAEEDAARQ-RAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1827
Cdd:PRK09510 208 KKKAAAEAKKKAAAEaKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1284-1940 |
6.33e-11 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 69.01 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1284 LRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLaEVEAALEKQRQLAEAHAQAKAQ---AELEAQELQR 1360
Cdd:pfam07111 53 LELEGSQALSQQAELISRQLQELRRLEEEVRLLRETSLQQKMRL-EAQAMELDALAVAEKAGQAEAEglrAALAGAEMVR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1361 RMQEEVARREeaavdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSrmrieeeirvvrlqLETTERQRGGAEGEL 1440
Cdd:pfam07111 132 KNLEEGSQRE-----LEEIQRLHQEQLSSLTQAHEEALSSLTSKAEGLEKS--------------LNSLETKRAGEAKQL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1441 QalraraeeaeaqkrQAQEEAERLRRQVqdeSQRKRQAEAELALrvkaeAEAAReKQRALQALDELRLQAEEAERRLRQA 1520
Cdd:pfam07111 193 A--------------EAQKEAELLRKQL---SKTQEELEAQVTL-----VESLR-KYVGEQVPPEVHSQTWELERQELLD 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1521 EAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLreeaerraqqqaeaeraREEAERELERWQ 1600
Cdd:pfam07111 250 TMQHLQEDRADLQATVELLQVRVQSLTHMLALQEEELTRKIQPSDSLEPEF-----------------PKKCRSLLNRWR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1601 LKANeALRLRLQAEEVAQQKSLAQADAEkqkeEAEREARRRGKAEEQAVRQRELAEQ--ELEKQRQLAEGTAQQRLAAEQ 1678
Cdd:pfam07111 313 EKVF-ALMVQLKAQDLEHRDSVKQLRGQ----VAELQEQVTSQSQEQAILQRALQDKaaEVEVERMSAKGLQMELSRAQE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1679 ELIRLRAETEQGEQQRQL-----------LEEELARLQHEATAATQKRQELEAELAKVRAeMEVLLASK---ARAEEESR 1744
Cdd:pfam07111 388 ARRRQQQQTASAEEQLKFvvnamsstqiwLETTMTRVEQAVARIPSLSNRLSYAVRKVHT-IKGLMARKvalAQLRQESC 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1745 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1824
Cdd:pfam07111 467 PPPPPAPPVDADLSLELEQLREERNRLDAELQLSAHLIQ-QEVGRAREQGEAERQQLSEVAQQLEQELQRAQESLASVGQ 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1825 EAENER--LRRLAEDEAFQRRRLEEQAALHKADIEERLAQLrkasESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKA 1902
Cdd:pfam07111 546 QLEVARqgQQESTEEAASLRQELTQQQEIYGQALQEKVAEV----ETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHR 621
|
650 660 670
....*....|....*....|....*....|....*...
gi 254675251 1903 AAGKAELELELGRIRSNAEdtmrsKEQAELEAARQRQL 1940
Cdd:pfam07111 622 ATQEKERNQELRRLQDEAR-----KEEGQRLARRVQEL 654
|
|
| CH_FIMB_rpt3 |
cd21300 |
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
7-106 |
7.89e-11 |
|
third calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409149 Cd Length: 119 Bit Score: 62.06 E-value: 7.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 7 ERDRvQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDS--------LPREKGRMRFHKLQNVQIALDYL 78
Cdd:cd21300 4 EGER-EARVFTLWLNS--LDVEPAVNDLFEDLRDGLILLQAYDKVIPGSvnwkkvnkAPASAEISRFKAVENTNYAVELG 80
|
90 100
....*....|....*....|....*...
gi 254675251 79 RHRQVKLVNIRNDDIADGNPKLTLGLIW 106
Cdd:cd21300 81 KQLGFSLVGIQGADITDGSRTLTLALVW 108
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1321-1837 |
1.05e-10 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 68.45 E-value: 1.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1321 AEERERLaeVEAALEKQRQLAEAHAQAKAQaeleaQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRqssEAEIQA 1400
Cdd:PRK04863 278 ANERRVH--LEEALELRRELYTSRRQLAAE-----QYRLVEMARELAELNEAESDLEQDYQAASDHLNLVQ---TALRQQ 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1401 KA--QQVEAAERSRMRIEEEIRVVRLQLEtterqrggaegelqalraRAEEAEAQKRQAQEEAERLRRQVQDESQRkrqa 1478
Cdd:PRK04863 348 EKieRYQADLEELEERLEEQNEVVEEADE------------------QQEENEARAEAAEEEVDELKSQLADYQQA---- 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1479 eaelalrVKAEAEAAREKQRALQALDELR-------LQAEEAERRLRQAEAERARQVQVALETAQRsaeVELQSKRASFA 1551
Cdd:PRK04863 406 -------LDVQQTRAIQYQQAVQALERAKqlcglpdLTADNAEDWLEEFQAKEQEATEELLSLEQK---LSVAQAAHSQF 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1552 EKTAQLERTLQEEHVtvaqlreeaerraqqqaeaerareeaerelerwqlkanealrlRLQAEEVAQQkslaqadaekqk 1631
Cdd:PRK04863 476 EQAYQLVRKIAGEVS-------------------------------------------RSEAWDVARE------------ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1632 eeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEgtAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAA 1711
Cdd:PRK04863 501 ------------LLRRLREQRHLAEQLQQLRMRLSE--LEQRLRQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEAR 566
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1712 tqkRQELEAELAKVRAEMEVLlaskaRAEEESrstSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEdAAR 1791
Cdd:PRK04863 567 ---LESLSESVSEARERRMAL-----RQQLEQ---LQARIQRLAARAPAWLAAQDALARLREQSGEEFEDSQDVTE-YMQ 634
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 254675251 1792 QRAEAERVLTEKLAAISEA-TRLKTEAEIALKEKEAENERLRRLAED 1837
Cdd:PRK04863 635 QLLERERELTVERDELAARkQALDEEIERLSQPGGSEDPRLNALAER 681
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1507-1846 |
1.43e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 67.84 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1507 RLQAEEAER----RLRQAEAERARQVQV--ALETAQRSAEVELQSKRASFAEKtaqlERTLQEEHvtvaqlreeaerraq 1580
Cdd:pfam17380 287 RQQQEKFEKmeqeRLRQEKEEKAREVERrrKLEEAEKARQAEMDRQAAIYAEQ----ERMAMERE--------------- 347
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1581 qqaeaerareeaeRELERWQL----KANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGkAEEQAVRQRELAE 1656
Cdd:pfam17380 348 -------------RELERIRQeerkRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEA-ARKVKILEEERQR 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1657 QELEKQRQLAEGTAQQRLAAEQELIRLraETEQGEQQRQLLEEELARLQHeataaTQKRQELEAELAKVRAEMEVLLASK 1736
Cdd:pfam17380 414 KIQQQKVEMEQIRAEQEEARQREVRRL--EEERAREMERVRLEEQERQQQ-----VERLRQQEEERKRKKLELEKEKRDR 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1737 ARAEEESRSTSEKskqrlEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDaARQRAEAER---VLTEKLAAISEATRL 1813
Cdd:pfam17380 487 KRAEEQRRKILEK-----ELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE-RRREAEEERrkqQEMEERRRIQEQMRK 560
|
330 340 350
....*....|....*....|....*....|...
gi 254675251 1814 KTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1846
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVESEK-ARAEYE 592
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2123-2325 |
1.47e-10 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 66.71 E-value: 1.47e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2123 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2202
Cdd:COG4942 27 AELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEEL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2203 EEL----------GKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRAL 2272
Cdd:COG4942 107 AELlralyrlgrqPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 254675251 2273 AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2325
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1290-1507 |
1.71e-10 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 66.82 E-value: 1.71e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1290 ELTTLTSQYIK-----FISETLRRMEEEERLAEQQRAEeRERLAEVE-AALEKQRQLAEAHAQ--------AKAQAELEA 1355
Cdd:COG2268 170 ELESVAITDLEdennyLDALGRRKIAEIIRDARIAEAE-AERETEIAiAQANREAEEAELEQEreietariAEAEAELAK 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1356 QELQRRMQEEVARRE-EAAVDAQQQKRSIQEELQhlrqsseAEIQAKAQQVEAAERSRMRIEEEirvvrlqLETTERQRg 1434
Cdd:COG2268 249 KKAEERREAETARAEaEAAYEIAEANAEREVQRQ-------LEIAEREREIELQEKEAEREEAE-------LEADVRKP- 313
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 1435 gAEGELQALRARAEeAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELR 1507
Cdd:COG2268 314 -AEAEKQAAEAEAE-AEAEAIRAKGLAEAEGKRALAEAWNKLGDAAILLMLIEKLPEIAEAAAKPLEKIDKIT 384
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1618-1813 |
2.20e-10 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 65.98 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1618 QQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1697
Cdd:PRK09510 70 QQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKA 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1698 EEELARLQHEATAATQKRQELEAELAKVRAEMEvllASKARAEEESRSTSEKSKQRLEAEAgrfRELAEEAARLRALAEE 1777
Cdd:PRK09510 150 EAEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAE---AKKKAEAEAAAKAAAEAKKKAEAEA---KKKAAAEAKKKAAAEA 223
|
170 180 190
....*....|....*....|....*....|....*.
gi 254675251 1778 AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRL 1813
Cdd:PRK09510 224 KAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4351-4389 |
2.23e-10 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 58.11 E-value: 2.23e-10
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 4351 FLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTAQKL 4389
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1608-2020 |
2.35e-10 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 67.10 E-value: 2.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1608 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQL--AEGTAQQRLAAEQELIRLRA 1685
Cdd:COG4717 67 ELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLlqLLPLYQELEALEAELAELPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1686 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1765
Cdd:COG4717 147 RLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1766 EEAARLRALAEEAKRQRQLAEED---------------AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENER 1830
Cdd:COG4717 227 EELEQLENELEAAALEERLKEARlllliaaallallglGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLGKEAEE 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1831 LRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVE-DTLRQRRQVEEEIMALKVSFEKAAAGKAEl 1909
Cdd:COG4717 307 LQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREaEELEEELQLEELEQEIAALLAEAGVEDEE- 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1910 elelgRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAE-EEAARQRKVALEEVERLKAKVEEAR- 1987
Cdd:COG4717 386 -----ELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELEELREELAELEa 460
|
410 420 430
....*....|....*....|....*....|...
gi 254675251 1988 RLRERAEQESARQLQLAQEAAQKRLQAEEKAHA 2020
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWA 493
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1321-1809 |
2.65e-10 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 67.28 E-value: 2.65e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1321 AEERERLaeVEAALEKQRQLAEAHAQAkaqaeLEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELqhlrqsseAEIQA 1400
Cdd:COG3096 277 ANERREL--SERALELRRELFGARRQL-----AEEQYRLVEMARELEELSARESDLEQDYQAASDHL--------NLVQT 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1401 KAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEGELqalraraEEAEAQKRQAQEEAERLRRQVQDesqrKRQAEA 1480
Cdd:COG3096 342 ALRQQEKIERYQEDLEE----LTERLEEQEEVVEEAAEQL-------AEAEARLEAAEEEVDSLKSQLAD----YQQALD 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1481 ELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVElqSKRASFAEKTAQLERT 1560
Cdd:COG3096 407 VQQTRAIQYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVAD--AARRQFEKAYELVCKI 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1561 LQEehVTVAQlreeaerraqqqaeaerareeaereleRWQlKANEALR----LRLQAEEVAQ-QKSLAQAdaekqkeeae 1635
Cdd:COG3096 485 AGE--VERSQ---------------------------AWQ-TARELLRryrsQQALAQRLQQlRAQLAEL---------- 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1636 rearrrgkaeEQAVRQRELAEQELEkqrQLAEGTAQQRLAAEQelirLRAETEQGEQQRQLLEEELARLQHEATAATQKR 1715
Cdd:COG3096 525 ----------EQRLRQQQNAERLLE---EFCQRIGQQLDAAEE----LEELLAELEAQLEELEEQAAEAVEQRSELRQQL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1716 QELEAELAKVRAEMEVLLASKARAE----------EESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLA 1785
Cdd:COG3096 588 EQLRARIKELAARAPAWLAAQDALErlreqsgealADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPG 667
|
490 500
....*....|....*....|....
gi 254675251 1786 EEDAARQRAEAERVLTEKLAAISE 1809
Cdd:COG3096 668 GAEDPRLLALAERLGGVLLSEIYD 691
|
|
| CH_PLS_FIM_rpt1 |
cd21217 |
first calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
13-109 |
3.70e-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: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 13 KKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR-----FHKLQNVQIALDYL 78
Cdd:cd21217 3 KEAFVEHINslladdpdlKHLLPIDPDGDDLFEALRDGVLLCKLINKIVPGTIDERKLNKKkpkniFEATENLNLALNAA 82
|
90 100 110
....*....|....*....|....*....|.
gi 254675251 79 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 109
Cdd:cd21217 83 KKIGCKVVNIGPQDILDGNPHLVLGLLWQII 113
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1682-2236 |
3.94e-10 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 66.60 E-value: 3.94e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1682 RLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEesrsTSEKSKQRLEAEAGRF 1761
Cdd:PRK02224 175 RLGVERVLSDQRGSLDQLKAQIEEKEEKDLHERLNGLESELAELDEEIERYEEQREQARE----TRDEADEVLEEHEERR 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1762 RELA---EEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKE---AENERLRRLA 1835
Cdd:PRK02224 251 EELEtleAEIEDLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREeleDRDEELRDRL 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1836 EDEAFQRRRLEEQA---ALHKADIEERLAQLRKAS---ESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAEL 1909
Cdd:PRK02224 331 EECRVAAQAHNEEAeslREDADDLEERAEELREEAaelESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNA 410
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1910 ELELGRIRSNAEDTmRSKE---QAELEAARQR------------------QLAAEEEQRRREAEERVQRSLAAEEEAARQ 1968
Cdd:PRK02224 411 EDFLEELREERDEL-REREaelEATLRTARERveeaealleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEE 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1969 RKVALEE-VERLKAKVEEARRLRERAEQESArqlqLAQEAAQKRLQAEEKAHAfvvqqreeelqqtlqqeqnmLDRLRSE 2047
Cdd:PRK02224 490 EVEEVEErLERAEDLVEAEDRIERLEERRED----LEELIAERRETIEEKRER--------------------AEELRER 545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2048 AEAARRAAEEAEEAREQAereaaqsRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQA 2127
Cdd:PRK02224 546 AAELEAEAEEKREAAAEA-------EEEAEEAREEVAELNSKLAELKERIESLERIRTLLAAIADAEDEIERLREKREAL 618
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2128 ADAEMEKHKKFAEQTLRqKAQVEQELTTLRlqLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGK 2207
Cdd:PRK02224 619 AELNDERRERLAEKRER-KRELEAEFDEAR--IEEAREDKERAEEYLEQVEEKLDELREERDDLQAEIGAVENELEELEE 695
|
570 580 590
....*....|....*....|....*....|
gi 254675251 2208 LKARIEA-ENRALILRDkdntqrfLEEEAE 2236
Cdd:PRK02224 696 LRERREAlENRVEALEA-------LYDEAE 718
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1340-1564 |
4.54e-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: 4.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1340 LAEAHAQAKAQAELEAQelQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEI 1419
Cdd:COG4942 12 ALAAAAQADAAAEAEAE--LEQLQQEIAELEKELAALKKEEKALLKQLAAL----ERRIAALARRIRALEQELAALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1420 RVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR-------QAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEA 1492
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAELLRALYRLGRQPPlalllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAAL 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1493 AREKQRALQALDELRLQAEEAERRLRQAEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1564
Cdd:COG4942 166 RAELEAERAELEALLAELEEERAALEALKAERQKLLA-RLEKELAELAAELAELQQEAEELEALIARLEAEA 236
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
1424-1865 |
5.40e-10 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 65.76 E-value: 5.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1424 LQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAL 1503
Cdd:COG4995 17 LALALLALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1504 DELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQA 1583
Cdd:COG4995 97 ALAAAALAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1584 EAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQR 1663
Cdd:COG4995 177 LALLALLLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1664 QLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEES 1743
Cdd:COG4995 257 LLALAAALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1744 RSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKE 1823
Cdd:COG4995 337 LLLAAAALLAAALAAALALAAALALALLAALLLLLAALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLRLLLAAL 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1824 KEAENERLRRLAEDEAFQR-------RRLEEQAALHK---ADIEERLAQLRK 1865
Cdd:COG4995 417 ALLLALAAYAAARLALLALieyiilpDRLYAFVQLYQlliAPIEAELPGIKR 468
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1318-1884 |
7.08e-10 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 65.59 E-value: 7.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1318 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQeevarreeAAVDAQQQKRSIQEELQHLRQSSEAE 1397
Cdd:PRK10246 219 QSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLDELQQEASRRQQ--------ALQQALAAEEKAQPQLAALSLAQPAR 290
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1398 I-----QAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRggAEGELQALRARAEEAEAQKRQAQ--EEAERLR----- 1465
Cdd:PRK10246 291 QlrphwERIQEQSAALAHTRQQIEE----VNTRLQSTMALR--ARIRHHAAKQSAELQAQQQSLNTwlAEHDRFRqwnne 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1466 ---------RQVQDESQRKRQAEAELALRVK----------------AEAEAAREKQRAL-QALDELRLQAEEAERRLRQ 1519
Cdd:PRK10246 365 lagwraqfsQQTSDREQLRQWQQQLTHAEQKlnalpaitltltadevAAALAQHAEQRPLrQRLVALHGQIVPQQKRLAQ 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1520 AEAERARqvqvaLETAQRSAEVELQSKRASFAEKTAQLE--RTLQEEHVTVAQLREEAERRAQQQAEAE--RAREEAERE 1595
Cdd:PRK10246 445 LQVAIQN-----VTQEQTQRNAALNEMRQRYKEKTQQLAdvKTICEQEARIKDLEAQRAQLQAGQPCPLcgSTSHPAVEA 519
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1596 LERWQLKANEALRLRLQaEEVAQQKS-----LAQADAEKQKEEaerearrrgKAEEQAVRQRElAEQELEKQRQLAEGTA 1670
Cdd:PRK10246 520 YQALEPGVNQSRLDALE-KEVKKLGEegaalRGQLDALTKQLQ---------RDESEAQSLRQ-EEQALTQQWQAVCASL 588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1671 QQRLAAEQELIRLRAETEQGEQQRQLLEEELArLQHEATAATQKRQELEAELAKVRAEMEVLLASKA------RAEEESR 1744
Cdd:PRK10246 589 NITLQPQDDIQPWLDAQEEHERQLRLLSQRHE-LQGQIAAHNQQIIQYQQQIEQRQQQLLTALAGYAltlpqeDEEASWL 667
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1745 STSEKSKQRLEAEAGRFRELAEEAARLRALAEeakrqrQLAEEDAArqRAEAERVLTEKLAAISEATrLKTEAEIALKEK 1824
Cdd:PRK10246 668 ATRQQEAQSWQQRQNELTALQNRIQQLTPLLE------TLPQSDDL--PHSEETVALDNWRQVHEQC-LSLHSQLQTLQQ 738
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1825 EAENERlRRLAE-----DEAFQRRRLEEQAALHKADIEE----RLAQLRKASESELERQKGLVEDTLRQ 1884
Cdd:PRK10246 739 QDVLEA-QRLQKaqaqfDTALQASVFDDQQAFLAALLDEetltQLEQLKQNLENQRQQAQTLVTQTAQA 806
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
487-676 |
7.24e-10 |
|
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here
Pssm-ID: 238103 [Multi-domain] Cd Length: 213 Bit Score: 62.08 E-value: 7.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 487 LRYLQDLLAWVEENQRRIDSAEWGVDLPSVEAQLGSHRGMHQSIEEFRAKIERARNDESQLSPATRGAY---RDCLGRLD 563
Cdd:cd00176 6 LRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAeeiQERLEELN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 564 LQYAKLLNSSKARLRSLE---SLHGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEI 640
Cdd:cd00176 86 QRWEELRELAEERRQRLEealDLQQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHEPRLKSL 165
|
170 180 190
....*....|....*....|....*....|....*..
gi 254675251 641 QNTGDRLLREDHP-ARPTVESFQAALQTQWSWMLQLC 676
Cdd:cd00176 166 NELAEELLEEGHPdADEEIEEKLEELNERWEELLELA 202
|
|
| CH_PARV_rpt2 |
cd21222 |
second calponin homology (CH) domain found in the parvin family; The parvin family includes ... |
5-112 |
8.27e-10 |
|
second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409071 Cd Length: 121 Bit Score: 59.52 E-value: 8.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 5 PDERDRVqKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLP----REKGRMRFHKLQNVQIALDYLRH 80
Cdd:cd21222 11 PEKLAEV-KELLLQFVNKHLAKLNIEVTDLATQFHDGVYLILLIGLLEGFFVPlheyHLTPSTDDEKLHNVKLALELMED 89
|
90 100 110
....*....|....*....|....*....|..
gi 254675251 81 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 112
Cdd:cd21222 90 AGISTPKIRPEDIVNGDLKSILRVLYSLFSKY 121
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2223-2569 |
9.52e-10 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 65.14 E-value: 9.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2223 DKDNTQRFLEEEAEKMKQVAEEAARlsvaaqEAARLRQLAEEDLAQQRALAEkmlkekmqavqeatrlkaEAELLQQQKE 2302
Cdd:pfam17380 286 ERQQQEKFEKMEQERLRQEKEEKAR------EVERRRKLEEAEKARQAEMDR------------------QAAIYAEQER 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2303 LAQEQARRLQEDKEQmaqqlveetqgfQRTLEAERQRQLEMSAEAERlklrMAEMSRAQARAEEDAQRFRKQAEEIGE-K 2381
Cdd:pfam17380 342 MAMERERELERIRQE------------ERKRELERIRQEEIAMEISR----MRELERLQMERQQKNERVRQELEAARKvK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2382 LHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEakllqlkseEMQTVQQEQILQETQALQKSFL 2461
Cdd:pfam17380 406 ILEEERQRKIQQQKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLE---------EQERQQQVERLRQQEEERKRKK 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2462 SEKDSLLQRERFIEQEKAKLEQLFQDEVAKAkqlreeqqrqqqQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHL 2541
Cdd:pfam17380 477 LELEKEKRDRKRAEEQRRKILEKELEERKQA------------MIEEERKRKLLEKEMEERQKAIYEEERRREAEEERRK 544
|
330 340
....*....|....*....|....*...
gi 254675251 2542 EQQRqqqekllaEENQRLRERLQRLEEE 2569
Cdd:pfam17380 545 QQEM--------EERRRIQEQMRKATEE 564
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
1613-2016 |
1.02e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 65.06 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1613 AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGEQ 1692
Cdd:PRK02224 278 AEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQ-AHNEEAESLREDADDLEE 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1693 QRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLR 1772
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREAELEATLR 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1773 ALAEEAKRQRQLAEE----DAARQRAEAERV--LTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLE 1846
Cdd:PRK02224 437 TARERVEEAEALLEAgkcpECGQPVEGSPHVetIEEDRERVEELEAELEDLEEEVEEVEERLERAEDLVEAED-RIERLE 515
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1847 EQAalhkADIEERLAQLRKASESELERQkglveDTLRQRRQVEEEIMALKvsfeKAAAGKAELELELGRIRSNAEDtmrs 1926
Cdd:PRK02224 516 ERR----EDLEELIAERRETIEEKRERA-----EELRERAAELEAEAEEK----REAAAEAEEEAEEAREEVAELN---- 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1927 KEQAELEAARQRqlaaeeeqrrreaeERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLA-- 2004
Cdd:PRK02224 579 SKLAELKERIES--------------LERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEfd 644
|
410
....*....|....*.
gi 254675251 2005 ----QEAAQKRLQAEE 2016
Cdd:PRK02224 645 eariEEAREDKERAEE 660
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
2124-2430 |
1.05e-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: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2124 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEEL------FS 2197
Cdd:TIGR02169 217 LKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEK-------LTEEISELEKRLEEIEQLLEELNKKIkdlgeeEQ 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2198 VRVQmEELGKLKARIEaenralilrdkdNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRalaekml 2277
Cdd:TIGR02169 290 LRVK-EKIGELEAEIA------------SLERSIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEER------- 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2278 KEKMQAVQEATRLKAEAELLQQQkelAQEQARRLQEDKEQMAqQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEM 2357
Cdd:TIGR02169 350 KRRDKLTEEYAELKEELEDLRAE---LEEVDKEFAETRDELK-DYREKLEKLKREINELKRELDRLQEELQRLSEELADL 425
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 2358 SRAQARAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQsdhdAERLREAIAELEREKEKLKQE 2430
Cdd:TIGR02169 426 NAAIAGIEAKINELEEEKEDKALEI---KKQEWKLEQLAADLSKYEQE----LYDLKEEYDRVEKELSKLQRE 491
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1277-1842 |
1.09e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 65.09 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1277 VIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQAELEAQ 1356
Cdd:PRK03918 170 VIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELE-KLEKEVKELEELKEEIEELEKELE 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1357 ELQRRMQEEvarrEEAAVDAQQQKRSIQEELQHLRQSSE--AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRG 1434
Cdd:PRK03918 249 SLEGSKRKL----EEKIRELEERIEELKKEIEELEEKVKelKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEIN 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1435 GAEGELQAL---RARAEEAEAQKRQAQEEAERLRRQVQdESQRKRQAEAELAlRVKAEaEAAREKQRALQALDELRLQAE 1511
Cdd:PRK03918 325 GIEERIKELeekEERLEELKKKLKELEKRLEELEERHE-LYEEAKAKKEELE-RLKKR-LTGLTPEKLEKELEELEKAKE 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1512 EAERRLRQAEAERARQVQ---------VALETAQRSAEV----------------------ELQSKRASFAEKTAQLERT 1560
Cdd:PRK03918 402 EIEEEISKITARIGELKKeikelkkaiEELKKAKGKCPVcgrelteehrkelleeytaelkRIEKELKEIEEKERKLRKE 481
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1561 LQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARR 1640
Cdd:PRK03918 482 LRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAEL 561
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1641 RGKAEEQAVRQRELaEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA 1720
Cdd:PRK03918 562 EKKLDELEEELAEL-LKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAETEK 640
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1721 ELAKVRAEMEVLLasKARAEEESRSTSEKskqrleaeagrFRELAEEAARLRALAEEAKRQRQLAEEDAarqraeaeRVL 1800
Cdd:PRK03918 641 RLEELRKELEELE--KKYSEEEYEELREE-----------YLELSRELAGLRAELEELEKRREEIKKTL--------EKL 699
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 254675251 1801 TEKLAAISEATRLKTEAEIALKEKEAENERLRR---LAEDEAFQR 1842
Cdd:PRK03918 700 KEELEEREKAKKELEKLEKALERVEELREKVKKykaLLKERALSK 744
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1306-1522 |
1.13e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 63.63 E-value: 1.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1306 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1385
Cdd:COG4942 29 LEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1386 ---ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1462
Cdd:COG4942 109 llrALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERA 188
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1463 RLRRQVqdesQRKRQAEAELALRVKAEAEAAREKQRALQALDEL--RLQAEEAERRLRQAEA 1522
Cdd:COG4942 189 ALEALK----AERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAA 246
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2122-2638 |
1.16e-09 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 65.08 E-value: 1.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2122 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQ 2201
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRER 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2202 MEELGKLKARIEAEnRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKM 2281
Cdd:TIGR02168 311 LANLERQLEELEAQ-LEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVA 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2282 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVE-ETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRA 2360
Cdd:TIGR02168 390 QLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaELKELQAELEELEEELEELQEELERLEEALEELREE 469
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2361 QARAEEDAQRFRKQAEEIGEKLHRTE-----------------------------LATQEKVT----------------- 2394
Cdd:TIGR02168 470 LEEAEQALDAAERELAQLQARLDSLErlqenlegfsegvkallknqsglsgilgvLSELISVDegyeaaieaalggrlqa 549
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2395 -LVQTLEIQRQ--QSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEE-----------------------MQTVQQEQ 2448
Cdd:TIGR02168 550 vVVENLNAAKKaiAFLKQNELGRVTFLPLDSIKGTEIQGNDREILKNIEgflgvakdlvkfdpklrkalsylLGGVLVVD 629
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2449 ILQETQALQKS------------------------FLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQ 2504
Cdd:TIGR02168 630 DLDNALELAKKlrpgyrivtldgdlvrpggvitggSAKTNSSILERRREIEELEEKIEEL-EEKIAELEKALAELRKELE 708
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2505 QMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQA 2584
Cdd:TIGR02168 709 ELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELE 788
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 2585 ASTKALPNGRDAPDGPSVEAEPEYT---FEGLRQKVPAQQLQEAGILSQEELQRLAQ 2638
Cdd:TIGR02168 789 AQIEQLKEELKALREALDELRAELTllnEEAANLRERLESLERRIAATERRLEDLEE 845
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
885-1505 |
1.44e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.94 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 885 EEQRQALRNLELHYQAFLRDSQDAGGFGPEDRLV----AEREYGSCSRHYQQLLQSLEQGEQEESRCQRCISELKDIRLQ 960
Cdd:COG4913 248 REQIELLEPIRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDE 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 961 LEacetrtvhrlrlpldkdparecaQRIAEQqkaqaeveglgkGVARLSAeaekvlalpepspaaptLRSELELTLGKLE 1040
Cdd:COG4913 328 LE-----------------------AQIRGN------------GGDRLEQ-----------------LEREIERLERELE 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1041 QVRSLSAIYLEKLKTISLVIRSTqgaeevlkthEEQLKEAQA-VPATLQELEATKASLKKLRAQAEAQqpvFNTLRDELR 1119
Cdd:COG4913 356 ERERRRARLEALLAALGLPLPAS----------AEEFAALRAeAAALLEALEEELEALEEALAEAEAA---LRDLRRELR 422
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1120 GAQEVGERLQQRHGERDVEVERWRERVTQLL--------------------ERWQAVLaqtdvrQRELEQLGRQL----R 1175
Cdd:COG4913 423 ELEAEIASLERRKSNIPARLLALRDALAEALgldeaelpfvgelievrpeeERWRGAI------ERVLGGFALTLlvppE 496
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1176 YYREsadpLSAWLQDAKRRQE-QIQAVPIANCQAAREQLrQEKALLEEIErhgEKVEECQKFAKQYINAIKDYELqlity 1254
Cdd:COG4913 497 HYAA----ALRWVNRLHLRGRlVYERVRTGLPDPERPRL-DPDSLAGKLD---FKPHPFRAWLEAELGRRFDYVC----- 563
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1255 kaqlepVASPAkkpkvqsgsesviqeyvDLRtRYSELTTLTSQyIKFiSETLRRMEEEERL---------AEQQRAEERE 1325
Cdd:COG4913 564 ------VDSPE-----------------ELR-RHPRAITRAGQ-VKG-NGTRHEKDDRRRIrsryvlgfdNRAKLAALEA 617
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1326 RLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRmqEEVARREEAAVDAQQQKRSIQEELQHLRQSSeAEIQAKAQQV 1405
Cdd:COG4913 618 ELAELEEELAEAEERLEALEAELDALQERREALQRL--AEYSWDEIDVASAEREIAELEAELERLDASS-DDLAALEEQL 694
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1406 EAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQ-EEAERLRRQVQDESQRKRQAEAELAL 1484
Cdd:COG4913 695 EELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELrALLEERFAAALGDAVERELRENLEER 774
|
650 660
....*....|....*....|.
gi 254675251 1485 RVKAEAEAAREKQRALQALDE 1505
Cdd:COG4913 775 IDALRARLNRAEEELERAMRA 795
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4273-4310 |
1.51e-09 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 55.95 E-value: 1.51e-09
10 20 30
....*....|....*....|....*....|....*...
gi 254675251 4273 QRLLEAQACTGGIIDPSTGERFPVTEAVNKGLVDKIMV 4310
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1119-1544 |
1.59e-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: 64.59 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1119 RGAQEvgERLQQRHGERDVEVERWR---------ERVTQLLERW-------------QAVLAQTDVRQRELEqlgRQLRY 1176
Cdd:COG3096 780 RAARE--KRLEELRAERDELAEQYAkasfdvqklQRLHQAFSQFvgghlavafapdpEAELAALRQRRSELE---RELAQ 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1177 YRESADPLSAWLQDAKRRQEQIQA-VPIANCQAArEQLRQekaLLEEIERHGEKVEECQKFAKQYINAIkdyelqlityk 1255
Cdd:COG3096 855 HRAQEQQLRQQLDQLKEQLQLLNKlLPQANLLAD-ETLAD---RLEELREELDAAQEAQAFIQQHGKAL----------- 919
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1256 AQLEPVASPAKKPKVQSgsESVIQEYVDLRTRYSELttltSQYIKFISETLRRM------EEEERLAEQQRAEE--RERL 1327
Cdd:COG3096 920 AQLEPLVAVLQSDPEQF--EQLQADYLQAKEQQRRL----KQQIFALSEVVQRRphfsyeDAVGLLGENSDLNEklRARL 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1328 AEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevarreeaavdAQQQKRSIQEELQHLrqsseaEIQAKAQQVEA 1407
Cdd:COG3096 994 EQAEEARREAREQLRQAQAQYSQYNQVLASLKSSRDA-----------KQQTLQELEQELEEL------GVQADAEAEER 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1408 AERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQAEA 1480
Cdd:COG3096 1057 ARIRRDELHEELSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQEREQVVqakagwcAVLRLARDNDVERRLHRR 1136
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1481 ELalrvkaeaeaarekqrALQALDELRLQAEEAERRLRQAEAERArQVQVALETAQ--RSAEVELQ 1544
Cdd:COG3096 1137 EL----------------AYLSADELRSMSDKALGALRLAVADNE-HLRDALRLSEdpRRPERKVQ 1185
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1346-2492 |
1.59e-09 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 64.43 E-value: 1.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1346 QAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQhlrqsSEAEIQAKAQQVEAAERSRMRIEEEIrvvrlq 1425
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQ-----AETELCAEAEEMRARLAARKQELEEI------ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1426 letterqrggaegeLQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkrQAEAELALRVKAEAEAAREKQRALQALDE 1505
Cdd:pfam01576 77 --------------LHELESRLEEEEERSQQLQNEKKKMQQHIQDLEE---QLDEEEAARQKLQLEKVTTEAKIKKLEED 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1506 LRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKT-AQLERTLQEEHVTVAQLREEAERRAQQQAE 1584
Cdd:pfam01576 140 ILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAMiSDLEERLKKEEKGRQELEKAKRKLEGESTD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1585 AERAREEAERELE--RWQL--KANEALRLRLQAEEVAQQKSLAQA---DAEKQKEEAEREARRRGKAEEQAVRQRELAEQ 1657
Cdd:pfam01576 220 LQEQIAELQAQIAelRAQLakKEEELQAALARLEEETAQKNNALKkirELEAQISELQEDLESERAARNKAEKQRRDLGE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1658 ELEKQRQLAEGTaQQRLAAEQELiRLRAETEQGEQQRQLLEEEL---ARLQHEATAATQKRQELEAELAKVRAEMEVLLA 1734
Cdd:pfam01576 300 ELEALKTELEDT-LDTTAAQQEL-RSKREQEVTELKKALEEETRsheAQLQEMRQKHTQALEELTEQLEQAKRNKANLEK 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1735 SKARAEEESRSTSEK----SKQRLEAEAGRfRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV----------- 1799
Cdd:pfam01576 378 AKQALESENAELQAElrtlQQAKQDSEHKR-KKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVssllneaegkn 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1800 --LTEKLAAIS-----------EATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKAdieeRLAQLRKA 1866
Cdd:pfam01576 457 ikLSKDVSSLEsqlqdtqellqEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQA----QLSDMKKK 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1867 SESELERQKGLVEDtlrqRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMrskeqaeLEAARQRQLAAEEEQ 1946
Cdd:pfam01576 533 LEEDAGTLEALEEG----KKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLL-------VDLDHQRQLVSNLEK 601
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1947 RRREAEErvqrsLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEekahafvvqqr 2026
Cdd:pfam01576 602 KQKKFDQ-----MLAEEKAISARYAEERDRAEAEAREKETRALSLARALEEALEAKEELERTNKQLRAE----------- 665
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2027 eeelqqtlqqeqnmLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQaqaqaqaqaaaeKLRKE 2106
Cdd:pfam01576 666 --------------MEDLVSSKDDVGKNVHELERSKRALEQQVEEMKTQLEELEDELQATEDA------------KLRLE 719
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2107 AEQeaarraqaeqaalkqkQAAdaemekhkkfaeqtlrqKAQVEQELTTLRLQLEEtdhQKSILDEELQRLKAEVTEAAR 2186
Cdd:pfam01576 720 VNM----------------QAL-----------------KAQFERDLQARDEQGEE---KRRQLVKQVRELEAELEDERK 763
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2187 QRSQveeeLFSVRVQME-ELGKLKARIEAENRAlilRDkdntqrfleeeaEKMKQVAEEAARLSVAAQEAARLRQLAEED 2265
Cdd:pfam01576 764 QRAQ----AVAAKKKLElDLKELEAQIDAANKG---RE------------EAVKQLKKLQAQMKDLQRELEEARASRDEI 824
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2266 LAQQRAlAEKMLKekmqavqeatrlKAEAELLQQQKELA-QEQARR-LQEDKEQMAQQLVEETQGfqRTLEAERQRQLEm 2343
Cdd:pfam01576 825 LAQSKE-SEKKLK------------NLEAELLQLQEDLAaSERARRqAQQERDELADEIASGASG--KSALQDEKRRLE- 888
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2344 saeaERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHrTELATQEkvTLVQTLEIQRQQSDHDAERLREAIAELERE 2423
Cdd:pfam01576 889 ----ARIAQLEEELEEEQSNTELLNDRLRKSTLQV-EQLT-TELAAER--STSQKSESARQQLERQNKELKAKLQEMEGT 960
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 2424 -KEKLKQ-----EAKLLQLKSEEMQTVQQEQilQETQALQKSFLSEKDSLLQRErfieqekakleqlfqDEVAKA 2492
Cdd:pfam01576 961 vKSKFKSsiaalEAKIAQLEEQLEQESRERQ--AANKLVRRTEKKLKEVLLQVE---------------DERRHA 1018
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1332-1564 |
1.70e-09 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 64.20 E-value: 1.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1332 AALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLR--QSSEAEIQAKAQQVEAA 1408
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLEREKAAREARHKKAAEArAAKDKDAVAAALARVKakKAAATQPIVIKAGARPD 515
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1409 ERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1488
Cdd:PRK05035 516 NSAVIAAREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAA 595
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1489 EAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASfAEKTAQLERTLQEE 1564
Cdd:PRK05035 596 QQAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAK-ARKAAQQQANAEPE 670
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1316-1527 |
1.74e-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: 1.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1316 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMqeevARREEAAVDAQQQKRSIQEEL-------Q 1388
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRI----AALARRIRALEQELAALEAELaelekeiA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1389 HLRQSSEAEIQAKAQQVEAAERSRMR-----------IEEEIRVVRLQLETTERQRggaeGELQALRARAEEAEAQKRQA 1457
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQpplalllspedFLDAVRRLQYLKYLAPARR----EQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1458 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1527
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAA 239
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1130-1938 |
2.04e-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: 64.20 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1130 QRHGERDVEVER-WRERVTQLLERwQAVLAQTdvrQRELEQLGRQLRYYRESADPLSAWL---QDAKRRQEQIQAVpIAN 1205
Cdd:COG3096 281 RELSERALELRReLFGARRQLAEE-QYRLVEM---ARELEELSARESDLEQDYQAASDHLnlvQTALRQQEKIERY-QED 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1206 CQAAREQLRQEKALLEEIErhgEKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpkVQSGSESVIQEYVDLR 1285
Cdd:COG3096 356 LEELTERLEEQEEVVEEAA---EQLAEAEARLEAAEEEVDSLKSQLADYQQALD----------VQQTRAIQYQQAVQAL 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1286 TRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAA---LEKQRQLAEAHAQA--KAQAELEAQELQR 1360
Cdd:COG3096 423 EKARALCGLPDLTPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAArrqFEKAYELVCKIAGEveRSQAWQTARELLR 502
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1361 RMQEEVARreeaAVDAQQQKRSIQEELQHLRQSSEAEIQAK------AQQVEAA---ERSRMRIEEEIRVVRLQLETTER 1431
Cdd:COG3096 503 RYRSQQAL----AQRLQQLRAQLAELEQRLRQQQNAERLLEefcqriGQQLDAAeelEELLAELEAQLEELEEQAAEAVE 578
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1432 QRGGAEGELQALRARAEEAEAQK---RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRL 1508
Cdd:COG3096 579 QRSELRQQLEQLRARIKELAARApawLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALES 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1509 QAeeaeRRLRQAE-AERARQVQ----------------VALETA---------QRSAEVELQSKRAsfAEKTAQLERTLQ 1562
Cdd:COG3096 659 QI----ERLSQPGgAEDPRLLAlaerlggvllseiyddVTLEDApyfsalygpARHAIVVPDLSAV--KEQLAGLEDCPE 732
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1563 E------------EHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANE--ALRLRLQAEEVAQQksLAQADAE 1628
Cdd:COG3096 733 DlyliegdpdsfdDSVFDAEELEDAVVVKLSDRQWRYSRFPEVPLFGR---AAREkrLEELRAERDELAEQ--YAKASFD 807
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1629 KQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegtaqQRLAAEQELIRLRAETEQGEQQRQLLEEE---LARLQ 1705
Cdd:COG3096 808 VQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALRQ-------RRSELERELAQHRAQEQQLRQQLDQLKEQlqlLNKLL 880
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1706 HEATA-----ATQKRQELEAELAKvraemevllaskarAEEESRSTSEKSKQ--RLEAEAGRFRELAEEAARLRALAEEA 1778
Cdd:COG3096 881 PQANLladetLADRLEELREELDA--------------AQEAQAFIQQHGKAlaQLEPLVAVLQSDPEQFEQLQADYLQA 946
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1779 KRQRQlaeedAARQRAEAERVLTEKLAAISEAtrlktEAEIALKEKEAENERLR---RLAEDEAFQRRRLEEQAALHKAD 1855
Cdd:COG3096 947 KEQQR-----RLKQQIFALSEVVQRRPHFSYE-----DAVGLLGENSDLNEKLRarlEQAEEARREAREQLRQAQAQYSQ 1016
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1856 IEERLAQLRKASESELErqkglvedtlrQRRQVEEEIMALKVSF-----EKAAAGKAELELELGRIRS--NAEDTMRSKE 1928
Cdd:COG3096 1017 YNQVLASLKSSRDAKQQ-----------TLQELEQELEELGVQAdaeaeERARIRRDELHEELSQNRSrrSQLEKQLTRC 1085
|
890
....*....|
gi 254675251 1929 QAELEAARQR 1938
Cdd:COG3096 1086 EAEMDSLQKR 1095
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1608-2016 |
2.06e-09 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 64.17 E-value: 2.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1608 RLRLQAEEVAQQ-KSLAQADAEKQKEEAEREARRRGKAE------EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQEL 1680
Cdd:COG4913 239 RAHEALEDAREQiELLEPIRELAERYAAARERLAELEYLraalrlWFAQRRLELLEAELEELRAELARLEAELERLEARL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1681 IRLRAETEQGEQQRQLLE-EELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAG 1759
Cdd:COG4913 319 DALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEALEE 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1760 RFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV---LTEKLAAISEATRLKTEA------EIALKEKEAE--- 1827
Cdd:COG4913 399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIparLLALRDALAEALGLDEAElpfvgeLIEVRPEEERwrg 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1828 -------NERLRRLAEDEAFQ-------RRRLEEQAALHKADIEERLAQLRKAS-------------------ESELERQ 1874
Cdd:COG4913 479 aiervlgGFALTLLVPPEHYAaalrwvnRLHLRGRLVYERVRTGLPDPERPRLDpdslagkldfkphpfrawlEAELGRR 558
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1875 KGLV----EDTLRQ-RRQVEEEIM--ALKVSFEK---------------AAAGKAELELELGRIRSNAEDTmrskeQAEL 1932
Cdd:COG4913 559 FDYVcvdsPEELRRhPRAITRAGQvkGNGTRHEKddrrrirsryvlgfdNRAKLAALEAELAELEEELAEA-----EERL 633
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1933 EAAR------QRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALE----EVERLKAKVEEARRLRERAEQESARQLQ 2002
Cdd:COG4913 634 EALEaeldalQERREALQRLAEYSWDEIDVASAEREIAELEAELERLDassdDLAALEEQLEELEAELEELEEELDELKG 713
|
490
....*....|....
gi 254675251 2003 LAQEAAQKRLQAEE 2016
Cdd:COG4913 714 EIGRLEKELEQAEE 727
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1399-1631 |
2.39e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.86 E-value: 2.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1399 QAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1478
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1479 EAELALRVKAEAEAAREKQR-ALQALDELRLQAEEAERRLRQAEA-ERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1556
Cdd:COG4942 96 RAELEAQKEELAELLRALYRlGRQPPLALLLSPEDFLDAVRRLQYlKYLAPARREQAEELRADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1557 LERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRL--RLQAEEVAQQKSLAQADAEKQK 1631
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALiaRLEAEAAAAAERTPAAGFAALK 252
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1343-1798 |
2.51e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 63.88 E-value: 2.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1343 AHAQAKAQAELEAQELQRRMQEEVARReeaAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVV 1422
Cdd:COG3903 475 EYAAERLAEAGERAAARRRHADYYLAL---AERAAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAAAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1423 RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA 1502
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1503 LDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQ 1582
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1583 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1662
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1663 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1742
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1743 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAER 1798
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAA 927
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1314-1895 |
3.42e-09 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 63.72 E-value: 3.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1314 RLAEQQRAEERERLAEVEAalekqRQLAEAHAQAKAQAELEA---QELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL 1390
Cdd:COG3899 674 RALEARGPEPLEERLFELA-----HHLNRAGERDRAARLLLRaarRALARGAYAEALRYLERALELLPPDPEEEYRLALL 748
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1391 RQSSEAEIQAkaQQVEAAERSRmrieEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1470
Cdd:COG3899 749 LELAEALYLA--GRFEEAEALL----ERALAARALAALAALRHGNPPASARAYANLGLLLLGDYEEAYEFGELALALAER 822
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1471 ESQRKRQAEAELAL-RVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRAS 1549
Cdd:COG3899 823 LGDRRLEARALFNLgFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARLLAAAAA 902
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1550 FAEKTAQLERTLQEEH---VTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQAD 1626
Cdd:COG3899 903 ALAAAAAAAALAAAELarlAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAAAAAAAA 982
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1627 AEKQKEeaerearrrgkAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH 1706
Cdd:COG3899 983 AAAAAA-----------AALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAA 1051
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1707 EATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE 1786
Cdd:COG3899 1052 AAAAAAAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARA 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1787 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKA 1866
Cdd:COG3899 1132 AAALLLLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLA 1211
|
570 580
....*....|....*....|....*....
gi 254675251 1867 SESELERQKGLVEDTLRQRRQVEEEIMAL 1895
Cdd:COG3899 1212 LALLALEAAALLLLLLLAALALAAALLAL 1240
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1335-1556 |
3.51e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 62.13 E-value: 3.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1335 EKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEaavdaQQQKRSIQEELQhlRQSSEAEIQAKAQQVEAAERsrmr 1414
Cdd:PRK09510 69 QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQ-----LEKERLAAQEQK--KQAEEAAKQAALKQKQAEEA---- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1415 ieeeirvvrlQLETTERQRGGAEGELQALRARAEEAEAQ-KRQAQEEAerlrrQVQDESQRKRQAEAELALRVKAEAEAA 1493
Cdd:PRK09510 138 ----------AAKAAAAAKAKAEAEAKRAAAAAKKAAAEaKKKAEAEA-----AKKAAAEAKKKAEAEAAAKAAAEAKKK 202
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 1494 REKQRALQAldelrlqAEEAErrlRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQ 1556
Cdd:PRK09510 203 AEAEAKKKA-------AAEAK---KKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| CH_FLNC_rpt2 |
cd21314 |
second calponin homology (CH) domain found in filamin-C (FLN-C) and similar proteins; ... |
127-229 |
3.72e-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: 57.39 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 127 TAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGVTRLLD 205
Cdd:cd21314 11 TPKQRLLGWIQNKVPQ---LPITNFNRDWQDGKALGALVDNCAPGLCpDWESWDPNQPVQNAREAMQQADDWLGVPQVIA 87
|
90 100
....*....|....*....|....
gi 254675251 206 PEDVDVPQPDEKSIITYVSSLYDA 229
Cdd:cd21314 88 PEEIVDPNVDEHSVMTYLSQFPKA 111
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1616-1850 |
4.47e-09 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 62.09 E-value: 4.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1616 VAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQ 1695
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1696 LLEEELARLQHEAtaatqKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKS-KQRLEAEAGRFRELAEEAARLRAL 1774
Cdd:COG4942 94 ELRAELEAQKEEL-----AELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYlAPARREQAEELRADLAELAALRAE 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1775 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1850
Cdd:COG4942 169 LEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1297-2014 |
4.77e-09 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 63.21 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1297 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDA 1376
Cdd:pfam15921 82 EYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKCLK 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1377 QQQKRSIQEELQHLRQ---SSEAEIQA-KAQQVEAAERSRMRIEEEIRVVRLQLetteRQRGGA--------EGELQALR 1444
Cdd:pfam15921 162 EDMLEDSNTQIEQLRKmmlSHEGVLQEiRSILVDFEEASGKKIYEHDSMSTMHF----RSLGSAiskilrelDTEISYLK 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1445 AR----AEEAEAQKRQAQEEAERLRRQVQDE-SQRKRQAEAELAlRVKAEAEAAREKQRALQAldelrlQAEEAERRLRQ 1519
Cdd:pfam15921 238 GRifpvEDQLEALKSESQNKIELLLQQHQDRiEQLISEHEVEIT-GLTEKASSARSQANSIQS------QLEIIQEQARN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1520 AEAERARQVQvALETAQRSAEVELQSKRASFAEKTAQLERTL------------------QEEHVTVAQLREEAERRAQQ 1581
Cdd:pfam15921 311 QNSMYMRQLS-DLESTVSQLRSELREAKRMYEDKIEELEKQLvlanseltearterdqfsQESGNLDDQLQKLLADLHKR 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1582 QAEAERAREEAERELERWQLKANEALRLRLQAE----EVAQQKSLAQA-DAEKQKEEAEREARRRGKAEEQAVRQRELAE 1656
Cdd:pfam15921 390 EKELSLEKEQNKRLWDRDTGNSITIDHLRRELDdrnmEVQRLEALLKAmKSECQGQMERQMAAIQGKNESLEKVSSLTAQ 469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1657 QELEKQ--RQLAEGTAQQRL---AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAE---LAKVRAE 1728
Cdd:pfam15921 470 LESTKEmlRKVVEELTAKKMtleSSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQHLKNEgdhLRNVQTE 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1729 MEVL---LASKARAEEESRSTSEK-----------------SKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEED 1788
Cdd:pfam15921 550 CEALklqMAEKDKVIEILRQQIENmtqlvgqhgrtagamqvEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSD 629
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1789 AARQRAEAERVLTEKLAAISEatrLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLrKASE 1868
Cdd:pfam15921 630 LELEKVKLVNAGSERLRAVKD---IKQERDQLLNEVKTSRNELNSLSEDYEVLKRNFRNKSEEMETTTNKLKMQL-KSAQ 705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1869 SELERQKglveDTLRQRRQVEEEIMALKVSFEKA-AAGKAELELELGRIRSNAED-TMRSKEQAELEAARQRQLAAEEEQ 1946
Cdd:pfam15921 706 SELEQTR----NTLKSMEGSDGHAMKVAMGMQKQiTAKRGQIDALQSKIQFLEEAmTNANKEKHFLKEEKNKLSQELSTV 781
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1947 RRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVE--EARRLRERAEQESARqLQLAQEAAQKRLQA 2014
Cdd:pfam15921 782 ATEKNKMAGELEVLRSQERRLKEKVANMEVALDKASLQfaECQDIIQRQEQESVR-LKLQHTLDVKELQG 850
|
|
| CH_AtFIM_like_rpt3 |
cd21299 |
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The ... |
12-111 |
5.38e-09 |
|
third calponin homology (CH) domain found in the Arabidopsis thaliana fimbrin family; The Arabidopsis thaliana fimbrin (AtFIM) family includes Fimbrin-1, -2, -3, -4, and -5, which cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Members of this family contain four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409148 Cd Length: 114 Bit Score: 56.74 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 12 QKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG-----RMRFHKLQNVQIALDYLRHRQVKLV 86
Cdd:cd21299 5 EERCFRLWINS--LGIDTYVNNVFEDVRDGWVLLEVLDKVSPGSVNWKHAnkppiKMPFKKVENCNQVVKIGKQLKFSLV 82
|
90 100
....*....|....*....|....*
gi 254675251 87 NIRNDDIADGNPKLTLGLIWTIILH 111
Cdd:cd21299 83 NVAGNDIVQGNKKLILALLWQLMRY 107
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2139-2573 |
5.82e-09 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 62.48 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2139 AEQTLRQKAQVEQELTTLRLQLEEtdhqksiLDEELQRLKAEVTEAARQRSQVEEELfSVRVQMEELGKLKARIEAENRA 2218
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEE-------LEEELEELEAELEELREELEKLEKLL-QLLPLYQELEALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2219 LI-LRDKDNTQRFLEEEAEKMKQVAEEAARlsVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2297
Cdd:COG4717 148 LEeLEERLEELRELEEELEELEAELAELQE--ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEEL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2298 QQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAE-AERLKLRMAEMSRAQARAEEDAQRFRKQAE 2376
Cdd:COG4717 226 EEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTiAGVLFLVLGLLALLFLLLAREKASLGKEAE 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2377 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvqQEQILQETQAL 2456
Cdd:COG4717 306 ELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQE---IAALLAEAGVE 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2457 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQElmASMEEARRRQREAEEGVRRKQE 2536
Cdd:COG4717 383 DEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELE--EELEELEEELEELREELAELEA 460
|
410 420 430
....*....|....*....|....*....|....*..
gi 254675251 2537 ELQHLEQQRQQQEKLLAEEnqRLRERLQRLEEEHRAA 2573
Cdd:COG4717 461 ELEQLEEDGELAELLQELE--ELKAELRELAEEWAAL 495
|
|
| CH_dFLNA-like_rpt2 |
cd21315 |
second calponin homology (CH) domain found in Drosophila melanogaster filamin-A (dFLNA) and ... |
122-224 |
6.32e-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: 6.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 122 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 200
Cdd:cd21315 11 DGKGPTPKQRLLGWIQSKVPD---LPITNFTNDWNDGKAIGALVDALAPGLCpDWEDWDPKDAVKNAKEAMDLAEDWLDV 87
|
90 100
....*....|....*....|....
gi 254675251 201 TRLLDPEDVDVPQPDEKSIITYVS 224
Cdd:cd21315 88 PQLIKPEEMVNPKVDELSMMTYLS 111
|
|
| SPEC |
cd00176 |
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ... |
1067-1257 |
7.45e-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: 7.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1067 EEVLKTHEEQLKEAQaVPATLQELEATKASLKKLRAQAEAQQPVFNTLrdelrgaQEVGERLQQRHGERDVEVerwRERV 1146
Cdd:cd00176 13 EAWLSEKEELLSSTD-YGDDLESVEALLKKHEALEAELAAHEERVEAL-------NELGEQLIEEGHPDAEEI---QERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1147 TQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADpLSAWLQDAKRRQEQIQavPIANCQAAREQLRQEKALLEEIERH 1226
Cdd:cd00176 82 EELNQRWEELRELAEERRQRLEEALDLQQFFRDADD-LEQWLEEKEAALASED--LGKDLESVEELLKKHKELEEELEAH 158
|
170 180 190
....*....|....*....|....*....|.
gi 254675251 1227 GEKVEECQKFAKQYINAIKDYELQLITYKAQ 1257
Cdd:cd00176 159 EPRLKSLNELAEELLEEGHPDADEEIEEKLE 189
|
|
| CH_ASPM_rpt2 |
cd21224 |
second calponin homology (CH) domain found in abnormal spindle-like microcephaly-associated ... |
131-226 |
8.38e-09 |
|
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: 56.93 E-value: 8.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 131 KLLL-WSQrMVEGYQGLRCDNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNL-----------------------EN 186
Cdd:cd21224 3 SLLLkWCQ-AVCAHYGVKVENFTVSFADGRALCYLIHHYLPSLLPLDAIRQPTTQtvdraqdeaedfwvaefspstgdSG 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 254675251 187 LDQAFSVAER-----------DLG-VTRLLDPEDVDVPQPDEKSIITYVSSL 226
Cdd:cd21224 82 LSSELLANEKrnfklvqqavaELGgVPALLRASDMSNTIPDEKVVILFLSYL 133
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1012-1558 |
9.63e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.00 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1012 AEKVLALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEaqaVPATLQELE 1091
Cdd:PRK03918 203 EEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEE---LKKEIEELE 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1092 ATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLqqrhgerdveverwrERVTQLLERWQAVLAQTDVRQRELEQLG 1171
Cdd:PRK03918 280 EKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRL---------------SRLEEEINGIEERIKELEEKEERLEELK 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1172 RQLRYYRESADPLSAW---LQDAKRRQEQIqavpiancqaarEQLRQEKALL--EEIERHGEKVEECQKFAKQYINAIKD 1246
Cdd:PRK03918 345 KKLKELEKRLEELEERhelYEEAKAKKEEL------------ERLKKRLTGLtpEKLEKELEELEKAKEEIEEEISKITA 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1247 YELQLITYKAQLEPVASPAKKPKVQS---GSESVIQEYVDLRTRYSElttltsqYIKFISETLRRMEEEERlaeqqraEE 1323
Cdd:PRK03918 413 RIGELKKEIKELKKAIEELKKAKGKCpvcGRELTEEHRKELLEEYTA-------ELKRIEKELKEIEEKER-------KL 478
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1324 RERLAEVEAALEKQRQLAEAHAQAKAQAELEaQELQRRMQEEVARREEAAvdaqqqkRSIQEELQHLrqssEAEIQAKAQ 1403
Cdd:PRK03918 479 RKELRELEKVLKKESELIKLKELAEQLKELE-EKLKKYNLEELEKKAEEY-------EKLKEKLIKL----KGEIKSLKK 546
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1404 QVEAAERsrmrIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1483
Cdd:PRK03918 547 ELEKLEE----LKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELK 622
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1484 lRVKAEAEAAREK-QRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLE 1558
Cdd:PRK03918 623 -KLEEELDKAFEElAETEKRLEELRKELEELEKKYSEEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLE 697
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1307-1514 |
9.63e-09 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 60.98 E-value: 9.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1307 RRMEEEERLAEQQRAEERErlaEVEAALEKQRQLaeahaqakAQAELEAQElQRRMQEEVARREeaavdAQQQKrsiQEE 1386
Cdd:PRK09510 76 RAEEQRKKKEQQQAEELQQ---KQAAEQERLKQL--------EKERLAAQE-QKKQAEEAAKQA-----ALKQK---QAE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1387 LQHLRQSSEAEIQAKAQQVEAAERSRmRIEEEIRvVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlrr 1466
Cdd:PRK09510 136 EAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAK-KKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKK--- 210
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254675251 1467 qVQDESQRKRQAEAELAL-RVKAEAEAAREKQRALQALDELRLQAEEAE 1514
Cdd:PRK09510 211 -AAAEAKKKAAAEAKAAAaKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1300-1542 |
1.23e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.32 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1300 KFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQ 1379
Cdd:pfam13868 88 KRQEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAER 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1380 KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEeirvVRLQLETTERQRGGAEGELQALRARAEEaEAQKRQAQE 1459
Cdd:pfam13868 168 EEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDE----LRAKLYQEEQERKERQKEREEAEKKARQ-RQELQQARE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1460 EAERLRRQVQDESQRKRQAEAELALRVKAEAE------AAREKQRALQALDELRLQAEEAER-RLRQAEAERARQVQVAL 1532
Cdd:pfam13868 243 EQIELKERRLAEEAEREEEEFERMLRKQAEDEeieqeeAEKRRMKRLEHRRELEKQIEEREEqRAAEREEELEEGERLRE 322
|
250
....*....|
gi 254675251 1533 ETAQRSAEVE 1542
Cdd:pfam13868 323 EEAERRERIE 332
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1307-1540 |
1.26e-08 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 60.32 E-value: 1.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1307 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKrsIQEE 1386
Cdd:pfam13868 36 AEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVER--IQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1387 LQHLRQSSEAEIQAKAQQVEAAERSRMRI---------EEEIRVVRLQLETTERQRggAEGELQALRARAEEAEAQKRQA 1457
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWkelekeeerEEDERILEYLKEKAEREE--EREAEREEIEEEKEREIARLRA 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1458 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQR 1537
Cdd:pfam13868 192 QQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQA 271
|
...
gi 254675251 1538 SAE 1540
Cdd:pfam13868 272 EDE 274
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1126-1433 |
1.49e-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: 61.29 E-value: 1.49e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1126 ERLQQRHGERDVEVERWR-----ERVTQL-LERWQAVLAQTD----VRQRELEQLGrqlryyresadplsawLQDAKRRQ 1195
Cdd:pfam17380 299 ERLRQEKEEKAREVERRRkleeaEKARQAeMDRQAAIYAEQErmamERERELERIR----------------QEERKREL 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1196 EQIQAVPIAncqAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVaspakKPKVQSGSE 1275
Cdd:pfam17380 363 ERIRQEEIA---MEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQI-----RAEQEEARQ 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1276 SVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAELEA 1355
Cdd:pfam17380 435 REVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAE---EQRRKILEKELEERKQAMIEE 511
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1356 QELQRRMQEEVARREEAAvdAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQR 1433
Cdd:pfam17380 512 ERKRKLLEKEMEERQKAI--YEEERRREAEEERRKQQEMEERRRIQEQMRKATeERSRLEAMEREREMMRQIVESEKAR 588
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1798-2536 |
1.53e-08 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 61.24 E-value: 1.53e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1798 RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaalhKADIEERLAQLRKASESELERQKGL 1877
Cdd:TIGR02169 156 RKIIDEIAGVAEFDRKKEKALEELEEVEENIERLDLIIDEKRQQLERLRRE----REKAERYQALLKEKREYEGYELLKE 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1878 VEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAED-TMRSKEQAELEAARQRQLAAEEEQRRREAEERVQ 1956
Cdd:TIGR02169 232 KEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEElNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIA 311
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1957 RSLAAEEEAARQRKVALEEVERLKAKVEEarrLRERAEQESARQLQLAQEAAQK---------RLQAEEKAHAFVVqqre 2027
Cdd:TIGR02169 312 EKERELEDAEERLAKLEAEIDKLLAEIEE---LEREIEEERKRRDKLTEEYAELkeeledlraELEEVDKEFAETR---- 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2028 eelqqtlqqeqnmlDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAaeklrkea 2107
Cdd:TIGR02169 385 --------------DELKDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEE-------- 442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2108 eqeaarraqaeqaalkqKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAE---VTEA 2184
Cdd:TIGR02169 443 -----------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQaraSEER 505
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2185 ARQRSQVEEELFS----VRVQMEELGKLKAR------IEAENR--ALILRDKDNTQR---FLEEEA---------EKMKQ 2240
Cdd:TIGR02169 506 VRGGRAVEEVLKAsiqgVHGTVAQLGSVGERyataieVAAGNRlnNVVVEDDAVAKEaieLLKRRKagratflplNKMRD 585
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2241 VAEEAARLSVAA-------------QEAARLRQ-----LAEEDLAQQRALAEKM--------LKEKMQAVQEATRLKAEA 2294
Cdd:TIGR02169 586 ERRDLSILSEDGvigfavdlvefdpKYEPAFKYvfgdtLVVEDIEAARRLMGKYrmvtlegeLFEKSGAMTGGSRAPRGG 665
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2295 ELLQQQKElaqEQARRLQEDKEQMAQQLveetQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2374
Cdd:TIGR02169 666 ILFSRSEP---AELQRLRERLEGLKREL----SSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKER 738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2375 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELER-----------------EKEKLKQEAKLLQLK 2437
Cdd:TIGR02169 739 LEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEArlshsripeiqaelsklEEEVSRIEARLREIE 818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2438 SEEMQTVQQEQILQ-ETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEQEKQELMAS 2516
Cdd:TIGR02169 819 QKLNRLTLEKEYLEkEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-EEELEELEAALRDLESRLGDLKKERDELEAQ 897
|
810 820
....*....|....*....|
gi 254675251 2517 MEEARRRQREAEEGVRRKQE 2536
Cdd:TIGR02169 898 LRELERKIEELEAQIEKKRK 917
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1385-1759 |
1.58e-08 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 60.68 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1385 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERL 1464
Cdd:pfam07888 30 ELLQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSAS 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1465 RRQVQDESQRKRQAEAELALRVKA-EAEAAREKQRALQA---LDELRLQAEEAERRLRQAEAERaRQVQVALETAQ---R 1537
Cdd:pfam07888 110 SEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLEReteLERMKERAKKAGAQRKEEEAER-KQLQAKLQQTEeelR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1538 SAEVELQSKRASFAEKTAQLERtLQEehvTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1617
Cdd:pfam07888 189 SLSKEFQELRNSLAQRDTQVLQ-LQD---TITTLTQKLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1618 QQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1697
Cdd:pfam07888 265 AQRDRTQAELHQARLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEERMEREKL 344
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 1698 EEELARlqhEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSE---KSKQRLEAEAG 1759
Cdd:pfam07888 345 EVELGR---EKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEyirQLEQRLETVAD 406
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2129-2590 |
1.69e-08 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 61.14 E-value: 1.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2129 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKaevtEAARQRSQVEEELFSVRVQMEELGKL 2208
Cdd:TIGR00618 200 TLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSHAYLTQKR----EAQEEQLKKQQLLKQLRARIEELRAQ 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2209 KARIEAENRALILRDKDNTqrfLEEEAEKMKQVAEEAARLSVAAQEAARLR----------QLAEEDLAQQRALAEKMLK 2278
Cdd:TIGR00618 276 EAVLEETQERINRARKAAP---LAAHIKAVTQIEQQAQRIHTELQSKMRSRakllmkraahVKQQSSIEEQRRLLQTLHS 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2279 EKMQAVQEATRLKAEAELLQQQKELAQeQARRLQEDKEQMAQQLVEETQgfqrtlEAERQRQLEMSAEAERLKLRMAEMS 2358
Cdd:TIGR00618 353 QEIHIRDAHEVATSIREISCQQHTLTQ-HIHTLQQQKTTLTQKLQSLCK------ELDILQREQATIDTRTSAFRDLQGQ 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2359 RAQARAEEDAQRFRKQAEEigekLHRTELATQEKVTLVQTLEIQrQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKS 2438
Cdd:TIGR00618 426 LAHAKKQQELQQRYAELCA----AAITCTAQCEKLEKIHLQESA-QSLKEREQQLQTKEQIHLQETRKKAVVLARLLELQ 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2439 EEMQTVQqEQILQETQALQKSFLSEKDS-----LLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQEL 2513
Cdd:TIGR00618 501 EEPCPLC-GSCIHPNPARQDIDNPGPLTrrmqrGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCD 579
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 2514 MASMEEArrrqreaeEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKAL 2590
Cdd:TIGR00618 580 NRSKEDI--------PNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTAL 648
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1321-1541 |
1.84e-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: 1.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1321 AEERERLAEVEAALEKQRQLAEAHAQ-AKAQAELEAQELQRRMQEEVARREEAAvdAQQQKRSIQEELQhlRQSSEAEIQ 1399
Cdd:COG2268 188 ALGRRKIAEIIRDARIAEAEAERETEiAIAQANREAEEAELEQEREIETARIAE--AEAELAKKKAEER--REAETARAE 263
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1400 AKAQQVEAAERSRMRIEEEIRVVRLQLETterqrggaegelqalraRAEEAEAQKRQAQEEAERlrrqvqdesqrkrqae 1479
Cdd:COG2268 264 AEAAYEIAEANAEREVQRQLEIAEREREI-----------------ELQEKEAEREEAELEADV---------------- 310
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1480 aelalRVKAEAEAAREKQRALQALDELRLQAE-EAERRLRQAEAERA-RQVQVALETAQRSAEV 1541
Cdd:COG2268 311 -----RKPAEAEKQAAEAEAEAEAEAIRAKGLaEAEGKRALAEAWNKlGDAAILLMLIEKLPEI 369
|
|
| CH_FLNB_rpt2 |
cd21313 |
second calponin homology (CH) domain found in filamin-B (FLN-B) and similar proteins; ... |
122-229 |
1.92e-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: 55.10 E-value: 1.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 122 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 200
Cdd:cd21313 3 DAKKQTPKQRLLGWIQNKIPY---LPITNFNQNWQDGKALGALVDSCAPGLCpDWESWDPQKPVDNAREAMQQADDWLGV 79
|
90 100
....*....|....*....|....*....
gi 254675251 201 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 229
Cdd:cd21313 80 PQVITPEEIIHPDVDEHSVMTYLSQFPKA 108
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1316-2105 |
2.05e-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: 60.96 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1316 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQ-HLRQSS 1394
Cdd:pfam01576 290 AEKQRRDLGEELEALKTELEDTLDTTAAQQELRSKREQEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTeQLEQAK 369
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1395 EAEIQ-AKAQQVEAAERSRMriEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQ 1473
Cdd:pfam01576 370 RNKANlEKAKQALESENAEL--QAELRTLQQAKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSS 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1474 RKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERA--RQVQVALETAQRSAEVELQSKRASFA 1551
Cdd:pfam01576 448 LLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNslQEQLEEEEEAKRNVERQLSTLQAQLS 527
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1552 EktaqLERTLQEEHVTVAQLREEaerraqqqaeaerareeaerelERWQLKANEALRLRLQAEEVAQQKslaqadAEKQK 1631
Cdd:pfam01576 528 D----MKKKLEEDAGTLEALEEG----------------------KKRLQRELEALTQQLEEKAAAYDK------LEKTK 575
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1632 EEAEREARRRGKAEEQavrQRELAEQELEKQRQLAEGTAQQRLAAEQELI-RLRAETEQGEQQRQLLEeelarLQHEATA 1710
Cdd:pfam01576 576 NRLQQELDDLLVDLDH---QRQLVSNLEKKQKKFDQMLAEEKAISARYAEeRDRAEAEAREKETRALS-----LARALEE 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1711 ATQKRQELEAELAKVRAEMEVLLASKARAEEeSRSTSEKSKQRLEAEAGRFRELAEEA---------ARLR------ALA 1775
Cdd:pfam01576 648 ALEAKEELERTNKQLRAEMEDLVSSKDDVGK-NVHELERSKRALEQQVEEMKTQLEELedelqatedAKLRlevnmqALK 726
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1776 EEAKRQRQLAEEDA-------ARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1848
Cdd:pfam01576 727 AQFERDLQARDEQGeekrrqlVKQVRELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKGREEAVKQLKKLQAQ 806
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1849 AALHKADIEE-RLAQ---LRKASESElERQKGLVEDTL----------RQRRQVEEEIMALKVSFEKAAAGKAELELEL- 1913
Cdd:pfam01576 807 MKDLQRELEEaRASRdeiLAQSKESE-KKLKNLEAELLqlqedlaaseRARRQAQQERDELADEIASGASGKSALQDEKr 885
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1914 ---GRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREaeervqrsLAAEEEAARQRKVALEEVER----LKAKVEEA 1986
Cdd:pfam01576 886 rleARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTE--------LAAERSTSQKSESARQQLERqnkeLKAKLQEM 957
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1987 RRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQae 2066
Cdd:pfam01576 958 EGTVKSKFKSSIAALEAKIAQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSRMKQL-- 1035
|
810 820 830
....*....|....*....|....*....|....*....
gi 254675251 2067 reaaqsRKQVEEAERLKQsaeeqaqaqaQAQAAAEKLRK 2105
Cdd:pfam01576 1036 ------KRQLEEAEEEAS----------RANAARRKLQR 1058
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1324-1793 |
2.11e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.80 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1324 RERLAEVEAALEKQRQLAEAHAQAKAQAEleaQELQRRMQEEVARREEAAVDaqqqkrSIQEELQHLRQSSEAEIqakAQ 1403
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAA---AELRGPDQLAWLARLDAEHD------NLRAALRWALAHGDAEL---AL 545
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1404 QVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1483
Cdd:COG3903 546 RLAAALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLL 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1484 LRvkAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQE 1563
Cdd:COG3903 626 LA--ALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAAL 703
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1564 EHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGK 1643
Cdd:COG3903 704 AAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAA 783
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1644 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1723
Cdd:COG3903 784 AALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAA 863
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1724 KVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQR 1793
Cdd:COG3903 864 AAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAAAAA 933
|
|
| CH_NAV3 |
cd21286 |
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ... |
14-108 |
2.79e-08 |
|
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409135 Cd Length: 105 Bit Score: 54.65 E-value: 2.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 14 KTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGD------SLPREKGRMrfhkLQNVQIALDYLRHRQVKL 85
Cdd:cd21286 3 KIYTDWANHYLAKSghKRLIKDLQQDIADGVLLAEIIQIIANEkvedinGCPRSQSQM----IENVDVCLSFLAARGVNV 78
|
90 100
....*....|....*....|...
gi 254675251 86 VNIRNDDIADGNPKLTLGLIWTI 108
Cdd:cd21286 79 QGLSAEEIRNGNLKAILGLFFSL 101
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1461-1917 |
3.16e-08 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 60.42 E-value: 3.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1461 AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAldelRLQAEEAERRLRQAEAERARQVQVALETAqrSAE 1540
Cdd:COG3903 478 AERLAEAGERAAARRRHADYYLALAERAAAELRGPDQLAWLA----RLDAEHDNLRAALRWALAHGDAELALRLA--AAL 551
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1541 VELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQK 1620
Cdd:COG3903 552 APFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAA 631
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1621 SLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE 1700
Cdd:COG3903 632 AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAAL 711
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1701 LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKR 1780
Cdd:COG3903 712 AAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAA 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1781 QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERL 1860
Cdd:COG3903 792 AAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALA 871
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1861 AQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIR 1917
Cdd:COG3903 872 AAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAA 928
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1113-1905 |
3.56e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 60.35 E-value: 3.56e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1113 TLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAV-----LAQTDVRQREleQLGRqlryYRESADPLSAw 1187
Cdd:COG3096 289 ELRRELFGARRQLAEEQYRLVEMARELEELSARESDLEQDYQAAsdhlnLVQTALRQQE--KIER----YQEDLEELTE- 361
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1188 lqdakRRQEQIQAVPIANCQAAREQLRQEKALlEEIERHG-------EKVEECQKFAKQYINAIKDYE-LQLITYKAQLE 1259
Cdd:COG3096 362 -----RLEEQEEVVEEAAEQLAEAEARLEAAE-EEVDSLKsqladyqQALDVQQTRAIQYQQAVQALEkARALCGLPDLT 435
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1260 PVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFIsETLRRMEEE-ERLAEQQRAEER-ERLAEVEAALEK- 1336
Cdd:COG3096 436 PENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAY-ELVCKIAGEvERSQAWQTARELlRRYRSQQALAQRl 514
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1337 ---QRQLAEAHAQAKAQAELE--AQELQRRmqeevarreeaavdaQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERS 1411
Cdd:COG3096 515 qqlRAQLAELEQRLRQQQNAErlLEEFCQR---------------IGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1412 RMrieeeirvvrlqleTTERQRGGAEGELQALRARAEEAeaqkRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1491
Cdd:COG3096 580 RS--------------ELRQQLEQLRARIKELAARAPAW----LAAQDALERLREQSGEALADSQEVTAAMQQLLERERE 641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1492 AAREKQRALQALDELRLQAeeaeRRLRQAE-AERARQVQ----------------VALETA---------QRSAEVELQS 1545
Cdd:COG3096 642 ATVERDELAARKQALESQI----ERLSQPGgAEDPRLLAlaerlggvllseiyddVTLEDApyfsalygpARHAIVVPDL 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1546 KRAsfAEKTAQLERTLQE------------EHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANE--ALRLRL 1611
Cdd:COG3096 718 SAV--KEQLAGLEDCPEDlyliegdpdsfdDSVFDAEELEDAVVVKLSDRQWRYSRFPEVPLFGR---AAREkrLEELRA 792
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1612 QAEEVAQQksLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaQQRLAAEQELIRLRAETEQGE 1691
Cdd:COG3096 793 ERDELAEQ--YAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPDPEAELAALR-------QRRSELERELAQHRAQEQQLR 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1692 QQRQLLEEE---LARLQHEATA-----ATQKRQELEAELAKVR-AEMEVLLASKARAE-EESRSTSEKSKQRLEAEAGRF 1761
Cdd:COG3096 864 QQLDQLKEQlqlLNKLLPQANLladetLADRLEELREELDAAQeAQAFIQQHGKALAQlEPLVAVLQSDPEQFEQLQADY 943
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1762 RELAEEAARLR----ALAEEAKRQRQLAEEDAARQRAEAeRVLTEKL-AAISEATRLKTEAEIALKEKEAE-NERLRRLA 1835
Cdd:COG3096 944 LQAKEQQRRLKqqifALSEVVQRRPHFSYEDAVGLLGEN-SDLNEKLrARLEQAEEARREAREQLRQAQAQySQYNQVLA 1022
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1836 E-DEAFQRRR--------------------LEEQAALHKADIEERLAQLRkASESELERQKGLVE---DTLRQR-RQVEE 1890
Cdd:COG3096 1023 SlKSSRDAKQqtlqeleqeleelgvqadaeAEERARIRRDELHEELSQNR-SRRSQLEKQLTRCEaemDSLQKRlRKAER 1101
|
890
....*....|....*
gi 254675251 1891 EIMALKVSFEKAAAG 1905
Cdd:COG3096 1102 DYKQEREQVVQAKAG 1116
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1741-2024 |
3.85e-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: 3.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1741 EESRSTSEKSKQ----RLEAEagRFRELAEEAARlralaeEAKRQRQLAEEDAARQrAEAERvlteKLAAISEATRLKTE 1816
Cdd:pfam17380 279 QHQKAVSERQQQekfeKMEQE--RLRQEKEEKAR------EVERRRKLEEAEKARQ-AEMDR----QAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1817 AE-----IALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQ----LRKASESELERQKGLVEDT--LRQR 1885
Cdd:pfam17380 346 RErelerIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQeleaARKVKILEEERQRKIQQQKveMEQI 425
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1886 RQVEEEIMALKV---------SFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQ 1956
Cdd:pfam17380 426 RAEQEEARQREVrrleeerarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERK 505
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1957 RSLAAEEeaaRQRKVALEEVE-RLKAKVEEARR------LRERAEQESARQLQLAQEAA---QKRLQAEEKAHAFVVQ 2024
Cdd:pfam17380 506 QAMIEEE---RKRKLLEKEMEeRQKAIYEEERRreaeeeRRKQQEMEERRRIQEQMRKAteeRSRLEAMEREREMMRQ 580
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2239-2459 |
3.86e-08 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 59.01 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2239 KQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQAVQEATR----LKAEAELLQQQKELAQEQARRLQED 2314
Cdd:COG4942 20 DAAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARriraLEQELAALEAELAELEKEIAELRAE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2315 KEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVT 2394
Cdd:COG4942 99 LEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEA 178
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 2395 LVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKS 2459
Cdd:COG4942 179 LLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERT 243
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1653-2567 |
4.23e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.80 E-value: 4.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1653 ELAEQELEKQR-QLAEGTAQQRLAA-EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAeME 1730
Cdd:pfam01576 111 QLDEEEAARQKlQLEKVTTEAKIKKlEEDILLLEDQNSKLSKERKLLEERISEFTSNLAEEEEKAKSLSKLKNKHEA-MI 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1731 VLLASKARAEEESRSTSEKSKQRLEAEAGrfrELAEEAARLRALAEEAKRQRQLAEEDaarqraeaervLTEKLAAISEA 1810
Cdd:pfam01576 190 SDLEERLKKEEKGRQELEKAKRKLEGEST---DLQEQIAELQAQIAELRAQLAKKEEE-----------LQAALARLEEE 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1811 TRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQaalhKADIEErlaqlrkasesELERQKGLVEDTLRQRRQVEE 1890
Cdd:pfam01576 256 TAQKNNALKKIRELEAQISELQEDLESERAARNKAEKQ----RRDLGE-----------ELEALKTELEDTLDTTAAQQE 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1891 EimalkvsfekaaagKAELELELGRIRSNAEDTMRSKEqAELEAARQRQLaaeeeqrrreaeervqrslAAEEEAARQrk 1970
Cdd:pfam01576 321 L--------------RSKREQEVTELKKALEEETRSHE-AQLQEMRQKHT-------------------QALEELTEQ-- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1971 vaLEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFV--VQQREEELQQTLQQEQNMLDRLRSEA 2048
Cdd:pfam01576 365 --LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLqeLQARLSESERQRAELAEKLSKLQSEL 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2049 EAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAA 2128
Cdd:pfam01576 443 ESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQELLQEETRQKLNLSTRLRQLEDERNSLQEQLEEEEEAKRNVERQLSTL 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2129 DAEMEKHKKFAEQTL-------RQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAA----RQRSQVEeelfs 2197
Cdd:pfam01576 523 QAQLSDMKKKLEEDAgtlealeEGKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQELDDLLvdldHQRQLVS----- 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2198 vrvQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKmkqvAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2277
Cdd:pfam01576 598 ---NLEKKQKKFDQMLAEEKAISARYAEERDRAEAEAREK----ETRALSLARALEEALEAKEELERTNKQLRAEMEDLV 670
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2278 --------------KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaERQRQL-- 2341
Cdd:pfam01576 671 sskddvgknvheleRSKRALEQQVEEMKTQLEELEDELQATEDAKLRLEVNMQALKAQFERDLQARDEQGE-EKRRQLvk 749
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2342 ---EMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKlhRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIA 2418
Cdd:pfam01576 750 qvrELEAELEDERKQRAQAVAAKKKLELDLKELEAQIDAANKG--REEAVKQLKKLQAQMKDLQRELEEARASRDEILAQ 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2419 ELEREKEKLKQEAKLLQLKSE----EMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEvakakq 2494
Cdd:pfam01576 828 SKESEKKLKNLEAELLQLQEDlaasERARRQAQQERDELADEIASGASGKSALQDEKRRLEARIAQLEEELEEE------ 901
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 2495 lreeqqrqqqqmeqekqelMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAE---ENQRLRERLQRLE 2567
Cdd:pfam01576 902 -------------------QSNTELLNDRLRKSTLQVEQLTTELAAERSTSQKSESARQQlerQNKELKAKLQEME 958
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1648-2020 |
4.47e-08 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 59.97 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1648 AVRQRELAEQELEKQRQLAeGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEE-------LARLQhEATAATQK----RQ 1716
Cdd:COG3096 277 ANERRELSERALELRRELF-GARRQLAEEQYRLVEMARELEELSARESDLEQDyqaasdhLNLVQ-TALRQQEKieryQE 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1717 ELEAELAKVRAEMEVLLA---SKARAEEESRSTSEKSK----------QRLEAE---AGRFR------ELAEEAARLRAL 1774
Cdd:COG3096 355 DLEELTERLEEQEEVVEEaaeQLAEAEARLEAAEEEVDslksqladyqQALDVQqtrAIQYQqavqalEKARALCGLPDL 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1775 AEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERlrrlaeDEAFQR-RRLEEQAALHK 1853
Cdd:COG3096 435 TPENAEDYLAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKIAGEVER------SQAWQTaRELLRRYRSQQ 508
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1854 AdIEERLAQLRkASESELERQkglvedtLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE 1933
Cdd:COG3096 509 A-LAQRLQQLR-AQLAELEQR-------LRQQQNAERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQ 579
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1934 AARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQ 2013
Cdd:COG3096 580 RSELRQQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQ 659
|
....*..
gi 254675251 2014 AEEKAHA 2020
Cdd:COG3096 660 IERLSQP 666
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1304-1526 |
4.54e-08 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 58.70 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1304 ETLRRMEEEERLAEQQRAEERERLAEVE--AALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQkr 1381
Cdd:TIGR02794 68 ERQKKLEQQAEEAEKQRAAEQARQKELEqrAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAK-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1382 siqEELQHlrqssEAEIQAKAQQVEAAERSRmrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRQAQEE- 1460
Cdd:TIGR02794 146 ---EEAAK-----QAEEEAKAKAAAEAKKKA-----------------------EEAKKKAEAEAKAKAEAEAKAKAEEa 194
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1461 ---AERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERAR 1526
Cdd:TIGR02794 195 kakAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDK 263
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1735-2018 |
6.65e-08 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 59.19 E-value: 6.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1735 SKARAEEESRSTSEKSKQRLEAEAGRF-RELAEEAARlralAEEAKRQRQLAEEDAarqRAEAERVLTEKLAAISEATRL 1813
Cdd:PRK05035 436 AEIRAIEQEKKKAEEAKARFEARQARLeREKAAREAR----HKKAAEARAAKDKDA---VAAALARVKAKKAAATQPIVI 508
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1814 KTEAEIALKEKEAEnERLRRLAEDEAFQRRRLEEQAALHKADIEERL--AQLRKASESELERQKGLVEDTlrQRRQVEEE 1891
Cdd:PRK05035 509 KAGARPDNSAVIAA-REARKAQARARQAEKQAAAAADPKKAAVAAAIarAKAKKAAQQAANAEAEEEVDP--KKAAVAAA 585
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1892 ImalkvsfEKAAAGKAELelelgrirsnAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKV 1971
Cdd:PRK05035 586 I-------ARAKAKKAAQ----------QAASAEPEEQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAV 648
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 254675251 1972 ALeEVERLKAKVEEARRLRERAEQESARQLQlAQEAAQKRLQAEEKA 2018
Cdd:PRK05035 649 AA-AIARAKARKAAQQQANAEPEEAEDPKKA-AVAAAIARAKAKKAA 693
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1674-2569 |
6.84e-08 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 59.42 E-value: 6.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1674 LAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQElEAELAKVRAEMEVLLASKARAEEESRSTSEKskqR 1753
Cdd:pfam01576 8 QAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQA-ETELCAEAEEMRARLAARKQELEEILHELES---R 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1754 LEAEAGRFRELAEEAARLRALAEEAkrQRQLAEEDAARQRAEAERVLTE-KLAAISEATRLKTEAEIAL-KEKEAENERL 1831
Cdd:pfam01576 84 LEEEEERSQQLQNEKKKMQQHIQDL--EEQLDEEEAARQKLQLEKVTTEaKIKKLEEDILLLEDQNSKLsKERKLLEERI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1832 RRLA------EDEAFQRRRLEEQAALHKADIEERLAQLRK-------------ASESELERQ----KGLVEDTLRQRRQV 1888
Cdd:pfam01576 162 SEFTsnlaeeEEKAKSLSKLKNKHEAMISDLEERLKKEEKgrqelekakrkleGESTDLQEQiaelQAQIAELRAQLAKK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1889 EEEIMALKVSFEKAAAGKAELE---LELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEA 1965
Cdd:pfam01576 242 EEELQAALARLEEETAQKNNALkkiRELEAQISELQEDLESERAARNKAEKQRRDLGEELEALKTELEDTLDTTAAQQEL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1966 ARQRKvalEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLR 2045
Cdd:pfam01576 322 RSKRE---QEVTELKKALEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQ 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2046 SEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAeqeaarraqaeqaalKQK 2125
Cdd:pfam01576 399 AKQDSEHKRKKLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSSLLNEAEGKNIKLS---------------KDV 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2126 QAADAEMEKHKKFAEQTLRQK-------AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQrsqVEEELFSV 2198
Cdd:pfam01576 464 SSLESQLQDTQELLQEETRQKlnlstrlRQLEDERNSLQEQLEEEEEAKRNVERQLSTLQAQLSDMKKK---LEEDAGTL 540
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2199 RvQMEElGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQvaeEAARLSVAAQeaaRLRQLAEEDLAQQRALAEKMLK 2278
Cdd:pfam01576 541 E-ALEE-GKKRLQRELEALTQQLEEKAAAYDKLEKTKNRLQQ---ELDDLLVDLD---HQRQLVSNLEKKQKKFDQMLAE 612
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2279 EKMQAVQEA-TRLKAEAELLQQQKElAQEQARRLQEdkeqmAQQLVEETQGFQRTLEAERQrqlEMSAEAERLKLRMAEM 2357
Cdd:pfam01576 613 EKAISARYAeERDRAEAEAREKETR-ALSLARALEE-----ALEAKEELERTNKQLRAEME---DLVSSKDDVGKNVHEL 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2358 SRAQARAEEDAQRFRKQAEEIGEKLHRTELAtqeKVTLVQTLEIQRQQSDHD---------------AERLREAIAELER 2422
Cdd:pfam01576 684 ERSKRALEQQVEEMKTQLEELEDELQATEDA---KLRLEVNMQALKAQFERDlqardeqgeekrrqlVKQVRELEAELED 760
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2423 EKE--------KLKQEAKLLQLKSE-EMQTVQQEQILQETQALQKSFlseKDslLQRErfIEQEKAKLEQLFqdevAKAK 2493
Cdd:pfam01576 761 ERKqraqavaaKKKLELDLKELEAQiDAANKGREEAVKQLKKLQAQM---KD--LQRE--LEEARASRDEIL----AQSK 829
|
890 900 910 920 930 940 950
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 2494 QLREEQQRQQQQMEQEKQELMASmeEARRRQREAEegvrrkQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEE 2569
Cdd:pfam01576 830 ESEKKLKNLEAELLQLQEDLAAS--ERARRQAQQE------RDELADEIASGASGKSALQDEKRRLEARIAQLEEE 897
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
982-1566 |
6.85e-08 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 59.20 E-value: 6.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 982 RECAQRIAEQQKAQaeveglgkgvaRLSAEAEKVLALPEPSPA-APTLRSELELTLGKL-EQVRSLSAIYLE-------- 1051
Cdd:PRK04863 523 SELEQRLRQQQRAE-----------RLLAEFCKRLGKNLDDEDeLEQLQEELEARLESLsESVSEARERRMAlrqqleql 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1052 -----KLKTISLVIRSTQGAEEVLKTH-EEQLKEAQAVPATLQELeatkasLKKLRAQAEAqqpvfntlRDELRGAQEV- 1124
Cdd:PRK04863 592 qariqRLAARAPAWLAAQDALARLREQsGEEFEDSQDVTEYMQQL------LERERELTVE--------RDELAARKQAl 657
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1125 ---GERLQQRHGERDveverwrERVTQLLERWQAVLAQTDVRQRELEQLGrqlrYYresadplSAWLQDAKrrqeqiQAV 1201
Cdd:PRK04863 658 deeIERLSQPGGSED-------PRLNALAERFGGVLLSEIYDDVSLEDAP----YF-------SALYGPAR------HAI 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1202 PIANCQAAREQLRQEKALLEEI-------ERHGEKVEECQKFAKQYINAIKDYELQLITYKAqlEPVASPAKKPK----V 1270
Cdd:PRK04863 714 VVPDLSDAAEQLAGLEDCPEDLyliegdpDSFDDSVFSVEELEKAVVVKIADRQWRYSRFPE--VPLFGRAAREKrieqL 791
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1271 QSGSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQ 1350
Cdd:PRK04863 792 RAEREELAERYATLSFDVQKLQRLHQAFSRFIGSHLAVAFEAD--PEAELRQLNRRRVELERALADHESQEQQQRSQLEQ 869
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1351 AELEAQELQRRM------------------QEEVARREEAAVDAQQQKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE- 1409
Cdd:PRK04863 870 AKEGLSALNRLLprlnlladetladrveeiREQLDEAEEAKRFVQQHGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQq 949
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1410 ---RSRMRIE--EEIRVVRLQLETTERQR-GGAEGELQ-ALRARAEEAEAQKRQAQEEAerlrRQVQDESQRKRQAEAEL 1482
Cdd:PRK04863 950 tqrDAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLEQAEQERTRAREQL----RQAQAQLAQYNQVLASL 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1483 alrvKAEAEAAREK-QRALQALDELRLQA-EEAERRLRQAEAE------RARQVQVALETAQRSAEVELQS--KRASFAE 1552
Cdd:PRK04863 1026 ----KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElharlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLE 1101
|
650
....*....|....
gi 254675251 1553 KTAQLERTLQEEHV 1566
Cdd:PRK04863 1102 RDYHEMREQVVNAK 1115
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1307-1568 |
7.03e-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: 58.12 E-value: 7.03e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1307 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQ 1384
Cdd:pfam15558 21 QRMRELQQQAALAWEELRRRDQKRQETLERERRLLLQQSQEQWQAEKEQRKARLGREERRRAdrREKQVIEKESRWREQA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1385 EELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrlqletterqRGGAEGELQALRARAEEAEaQKRQAQEEAERL 1464
Cdd:pfam15558 101 EDQENQRQEKLERARQEAEQRKQCQEQRLKEKEEEL------------QALREQNSLQLQERLEEAC-HKRQLKEREEQK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1465 RRQVQDESQR-KRQA-EAELALRVKAEAEAARE--KQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAE 1540
Cdd:pfam15558 168 KVQENNLSELlNHQArKVLVDCQAKAEELLRRLslEQSLQRSQENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEE 247
|
250 260
....*....|....*....|....*...
gi 254675251 1541 VELQSKRASFAEKTAQLERTLQEEHVTV 1568
Cdd:pfam15558 248 ERQEHKEALAELADRKIQQARQVAHKTV 275
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1685-2247 |
8.45e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 58.92 E-value: 8.45e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1685 AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTS--EKSKQRLEAEAGRFR 1762
Cdd:PRK03918 186 KRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEELEKELEslEGSKRKLEEKIRELE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1763 E-LAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-LTEKLAAIS-EATRLKTEA---EIALKEKEAENERLRRLAE 1836
Cdd:PRK03918 266 ErIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEeYLDELREIEkRLSRLEEEIngiEERIKELEEKEERLEELKK 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1837 DEAFQRRRLEEQAALHKA--DIEERLAQLRKASES----ELERQKGLVEDTLRQRRQVEEEImalkvsfEKAAAGKAELE 1910
Cdd:PRK03918 346 KLKELEKRLEELEERHELyeEAKAKKEELERLKKRltglTPEKLEKELEELEKAKEEIEEEI-------SKITARIGELK 418
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1911 LELGRIRSNAEdtmrskeqaELEAARQ------RQLAAEEEQRRREAEERVQRSLAAE----EEAARQRKVALEEVERLK 1980
Cdd:PRK03918 419 KEIKELKKAIE---------ELKKAKGkcpvcgRELTEEHRKELLEEYTAELKRIEKElkeiEEKERKLRKELRELEKVL 489
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1981 AKVEEARRLRERAEQESARQLQLAQEAAQKrlqAEEKAHAFvvqqreeelqqtlQQEQNMLDRLRSEAEAARRAAEEAEE 2060
Cdd:PRK03918 490 KKESELIKLKELAEQLKELEEKLKKYNLEE---LEKKAEEY-------------EKLKEKLIKLKGEIKSLKKELEKLEE 553
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2061 AREQAEREAAQSRKQVEE-AERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFA 2139
Cdd:PRK03918 554 LKKKLAELEKKLDELEEElAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFE 633
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2140 EQTLRQKA--QVEQELTTLRLQLEETDHQKSI-----LDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARI 2212
Cdd:PRK03918 634 ELAETEKRleELRKELEELEKKYSEEEYEELReeyleLSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL 713
|
570 580 590
....*....|....*....|....*....|....*
gi 254675251 2213 EAENRALilrdkdntqRFLEEEAEKMKQVAEEAAR 2247
Cdd:PRK03918 714 EKLEKAL---------ERVEELREKVKKYKALLKE 739
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
1518-2436 |
8.89e-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: 58.83 E-value: 8.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1518 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREeaerelE 1597
Cdd:TIGR00618 56 RRSEVIRSLNSLYAAPSEAAFAELEFSLGTKIYRVHRTLRCTRSHRKTEQPEQLYLEQKKGRGRILAAKKSET------E 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1598 RWQLKAnealrLRLQAEEVAQQKSLAQADAEKqkeeaereaRRRGKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAE 1677
Cdd:TIGR00618 130 EVIHDL-----LKLDYKTFTRVVLLPQGEFAQ---------FLKAKSKEKKELLMNL--FPLDQYTQLALMEFAKKKSLH 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1678 QELIrlrAETEQGEQQRQLLEEELARLqheataaTQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK--QRLE 1755
Cdd:TIGR00618 194 GKAE---LLTLRSQLLTLCTPCMPDTY-------HERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKkqQLLK 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1756 AEAGRFRELAEEAARLRALAEEAKRQRQLAEedaarqraeaervLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLA 1835
Cdd:TIGR00618 264 QLRARIEELRAQEAVLEETQERINRARKAAP-------------LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1836 EDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQR-RQVEEEIMALKVSFEKAAAGKAELELELG 1914
Cdd:TIGR00618 331 AAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHiHTLQQQKTTLTQKLQSLCKELDILQREQA 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1915 RIrsNAEDTMRSKEQAELEAAR-QRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERA 1993
Cdd:TIGR00618 411 TI--DTRTSAFRDLQGQLAHAKkQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRK 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1994 EQESARQLQLAQEaaQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAaqsr 2073
Cdd:TIGR00618 489 KAVVLARLLELQE--EPCPLCGSCIHPNPARQDIDNPGPLTRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLK---- 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2074 kqvEEAERLKQSAEEQAQAQAQAQAAAEKLRKeaEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQEL 2153
Cdd:TIGR00618 563 ---EQMQEIQQSFSILTQCDNRSKEDIPNLQN--ITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQC 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2154 TTlRLQLEETdhqkSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEE 2233
Cdd:TIGR00618 638 SQ-ELALKLT----ALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETH 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2234 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAT-RLKAEAELLQQQKELAQE---QAR 2309
Cdd:TIGR00618 713 IEEYDREFNEIENASSSLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNNNeEVTAALQTGAELSHLAAEiqfFNR 792
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2310 RLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAraeedaqRFRKQAEEIGEKLHRTELAT 2389
Cdd:TIGR00618 793 LREEDTHLLKTLEAEIGQEIPSDEDILNLQCETLVQEEEQFLSRLEEKSATLG-------EITHQLLKYEECSKQLAQLT 865
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|.
gi 254675251 2390 QEKVTLVQTLE----IQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQL 2436
Cdd:TIGR00618 866 QEQAKIIQLSDklngINQIKIQFDGDALIKFLHEITLYANVRLANQSEGRF 916
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1709-1862 |
9.00e-08 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 57.96 E-value: 9.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1709 TAATQKRQELEAELAKVRAEMEVLLASKARAEEESRstseKSKQRLEAEAGRFRELAEEAARLRAlaEEAKRQRQLAEED 1788
Cdd:COG2268 212 TEIAIAQANREAEEAELEQEREIETARIAEAEAELA----KKKAEERREAETARAEAEAAYEIAE--ANAEREVQRQLEI 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1789 AARQR------AEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAALHKADIEERLAQ 1862
Cdd:COG2268 286 AEREReielqeKEAEREEAELEADVRKPAEAEKQAAEAEAEAEAEAIRAKGLAEAEG-KRALAEAWNKLGDAAILLMLIE 364
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4004-4040 |
9.86e-08 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 50.56 E-value: 9.86e-08
10 20 30
....*....|....*....|....*....|....*..
gi 254675251 4004 IRLLEAQIATGGIIDPEESHRLPVEVAYKRGLFDEEM 4040
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1031-1479 |
1.04e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1031 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEatkaslkKLRAQAEAQQPV 1110
Cdd:COG4717 75 ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELE-------ALEAELAELPER 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1111 FNTLRDELRGAQEVGERLQqrhgERDVEVERWRERVTQLLERWQAVLAQTDVR-QRELEQLGRQLRYYRESADPLSAWLQ 1189
Cdd:COG4717 148 LEELEERLEELRELEEELE----ELEAELAELQEELEELLEQLSLATEEELQDlAEELEELQQRLAELEEELEEAQEELE 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1190 DAKRRQEQIQAVPIAncQAAREQLRQEK----------ALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLE 1259
Cdd:COG4717 224 ELEEELEQLENELEA--AALEERLKEARlllliaaallALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1260 PVASPAKKPKVQSGSESviQEYVDLRTRYSELTTLTSQYIkfisETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ 1339
Cdd:COG4717 302 KEAEELQALPALEELEE--EELEELLAALGLPPDLSPEEL----LELLDRIEELQELLREAEELEEELQLEELEQEIAAL 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1340 LAEAHAQAKAQAELEAQELQRRmQEEVARREEAAVDAQQQKRSIQEELQHLRQSS-EAEIQAKAQQVEAAERSRMRIEEE 1418
Cdd:COG4717 376 LAEAGVEDEEELRAALEQAEEY-QELKEELEELEEQLEELLGELEELLEALDEEElEEELEELEEELEELEEELEELREE 454
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1419 IRVVRLQLETTERqrggaEGELQALRARAEEAEAQKRQAQEEAERLR------RQVQDESQRKRQAE 1479
Cdd:COG4717 455 LAELEAELEQLEE-----DGELAELLQELEELKAELRELAEEWAALKlalellEEAREEYREERLPP 516
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
930-1566 |
1.12e-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: 58.81 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 930 YQQLLQSLEQGEQeesrcqrcISELKDirLQLEACETR-TVHRLRLPLDKDPARECAQRIAEQQKAQAEVEGLGKGVARL 1008
Cdd:COG3096 415 YQQAVQALEKARA--------LCGLPD--LTPENAEDYlAAFRAKEQQATEEVLELEQKLSVADAARRQFEKAYELVCKI 484
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1009 SAEAEKVLALPEpspAAPTLR--SELELTLGKLEQVRSlsaiyleKLKTISLVIRSTQGAEEVL----KTHEEQLKEAQA 1082
Cdd:COG3096 485 AGEVERSQAWQT---ARELLRryRSQQALAQRLQQLRA-------QLAELEQRLRQQQNAERLLeefcQRIGQQLDAAEE 554
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1083 VPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRG--------------AQEVGERLQQRHGERDVEVERWRERVTQ 1148
Cdd:COG3096 555 LEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRArikelaarapawlaAQDALERLREQSGEALADSQEVTAAMQQ 634
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1149 LLERWQAVLAQTD---VRQRELEQLGRQLRYYRESADP-------------LS-----AWLQDA----KRRQEQIQAVPI 1203
Cdd:COG3096 635 LLEREREATVERDelaARKQALESQIERLSQPGGAEDPrllalaerlggvlLSeiyddVTLEDApyfsALYGPARHAIVV 714
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1204 ANCQAAREQLRQEKALLEE---IERH----GEKVEECQKFAKQYINAIKDYELQLITYKAqlEPV----ASPAKKPKVQS 1272
Cdd:COG3096 715 PDLSAVKEQLAGLEDCPEDlylIEGDpdsfDDSVFDAEELEDAVVVKLSDRQWRYSRFPE--VPLfgraAREKRLEELRA 792
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1273 GSESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAE 1352
Cdd:COG3096 793 ERDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQL 869
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1353 LEAQELQRRMQEEV---------ARREEAAVD---AQQQKRSIQEELQHLRQSSE--AEIQAKAQQVEAAERSRMRIEEE 1418
Cdd:COG3096 870 KEQLQLLNKLLPQAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQ 949
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1419 IRVVRLQL----ETTER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDESQrkRQAEAELA 1483
Cdd:COG3096 950 QRRLKQQIfalsEVVQRrphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQ--VLASLKSS 1027
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1484 LRVKAE--AEAARE-KQRALQALDELRLQAEEAERRLRQA-EAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1559
Cdd:COG3096 1028 RDAKQQtlQELEQElEELGVQADAEAEERARIRRDELHEElSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQER 1107
|
....*..
gi 254675251 1560 TLQEEHV 1566
Cdd:COG3096 1108 EQVVQAK 1114
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1491-1938 |
1.28e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1491 EAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvaq 1570
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL------ 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1571 lreeaerraqqqaeaerareeaereLERW-QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRgKAEEQAV 1649
Cdd:COG4717 145 -------------------------PERLeELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATE-EELQDLA 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1650 RQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEM 1729
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGV 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1730 EVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISE 1809
Cdd:COG4717 279 LFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLRE 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1810 ATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALH--KADIEERLAQLRKASESELERQKGLVEDTLRQR-R 1886
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQelKEELEELEEQLEELLGELEELLEALDEEELEEElE 435
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1887 QVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQR 1938
Cdd:COG4717 436 ELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQELEELKAELRE 487
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1612-1795 |
1.37e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 57.12 E-value: 1.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1612 QAEEVAQQKslaQADAEKQKEEAEREArrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQ----RLAAEQELIRLRAET 1687
Cdd:PRK09510 88 QAEELQQKQ---AAEQERLKQLEKERL----AAQEQKKQAEEAAKQAALKQKQAEEAAAKAaaaaKAKAEAEAKRAAAAA 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1688 EQGEQQRQLLEEELARLQHEATAatqkRQELEAElAKVRAEMEvllaSKARAEEESRSTSEK-SKQRLEAEAGRFRELAE 1766
Cdd:PRK09510 161 KKAAAEAKKKAEAEAAKKAAAEA----KKKAEAE-AAAKAAAE----AKKKAEAEAKKKAAAeAKKKAAAEAKAAAAKAA 231
|
170 180
....*....|....*....|....*....
gi 254675251 1767 EAArlRALAEEAKRQRQLAEEDAARQRAE 1795
Cdd:PRK09510 232 AEA--KAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1195-1766 |
1.39e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 57.86 E-value: 1.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1195 QEQIQAVPIANCQAAREQL-----RQEKALLEEIERHGEKVEECQKFAKQYINAIKdyelQLITYKAQLEPVASPAKKPK 1269
Cdd:COG4717 40 LAFIRAMLLERLEKEADELfkpqgRKPELNLKELKELEEELKEAEEKEEEYAELQE----ELEELEEELEELEAELEELR 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1270 VQSGSESVIQEYVDLRTRYSELTtltsqyikfisETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKA 1349
Cdd:COG4717 116 EELEKLEKLLQLLPLYQELEALE-----------AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1350 QAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAERSRMRIEE--EIRVV 1422
Cdd:COG4717 185 QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEeleqlENELEAAALEERLKEARLLLLIAAAllALLGL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1423 RLQLETTERQRGGA----EGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQR 1498
Cdd:COG4717 265 GGSLLSLILTIAGVlflvLGLLALLFLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1499 ALQALDELRLQAEEAERRLRQAEAERARqvQVALETAQRSAEVELQSKRASFAEKTAQLERtlqeehvtvaqlreeaerr 1578
Cdd:COG4717 345 RIEELQELLREAEELEEELQLEELEQEI--AALLAEAGVEDEEELRAALEQAEEYQELKEE------------------- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1579 aqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVAQQKSLAQADAEKQKEeaerearrrgKAEEQAVRQRELAEQE 1658
Cdd:COG4717 404 -------------------------LEELEEQLEELLGELEELLEALDEEELEE----------ELEELEEELEELEEEL 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1659 LEKQRQLAEGTAQ-QRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAE-LAKVRAEMEVLLASK 1736
Cdd:COG4717 449 EELREELAELEAElEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREErLPPVLERASEYFSRL 528
|
570 580 590
....*....|....*....|....*....|
gi 254675251 1737 ARAEEESRSTSEKSKQRLEAEAGRFRELAE 1766
Cdd:COG4717 529 TDGRYRLIRIDEDLSLKVDTEDGRTRPVEE 558
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1676-1876 |
1.49e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 57.15 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1676 AEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLE 1755
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1756 A---------------EAGRFRELAEEAARLRALAEEAKR---QRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA 1817
Cdd:COG3883 94 AlyrsggsvsyldvllGSESFSDFLDRLSALSKIADADADlleELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1818 EIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKG 1876
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAA 232
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1612-1798 |
1.68e-07 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 56.78 E-value: 1.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1612 QAEEVAQQKSlAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGE 1691
Cdd:TIGR02794 51 QANRIQQQKK-PAAKKEQERQK---------KLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1692 QQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAE---EA 1768
Cdd:TIGR02794 121 AEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKakaEA 200
|
170 180 190
....*....|....*....|....*....|
gi 254675251 1769 ARLRALAEEAKRQRQLAeedAARQRAEAER 1798
Cdd:TIGR02794 201 AKAKAAAEAAAKAEAEA---AAAAAAEAER 227
|
|
| CH_PLS3_rpt3 |
cd21331 |
third calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
7-114 |
2.32e-07 |
|
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: 52.70 E-value: 2.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 7 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL-------SGDSLPREKGRMRFHKLQNVQIALDYLR 79
Cdd:cd21331 18 EGETREERTFRNWMNS--LGVNPHVNHLYGDLQDALVILQLYEKIkvpvdwnKVNKPPYPKLGANMKKLENCNYAVELGK 95
|
90 100 110
....*....|....*....|....*....|....*.
gi 254675251 80 HR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQI 114
Cdd:cd21331 96 HPaKFSLVGIGGQDLNDGNPTLTLALVWQLMRRYTL 131
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2172-2440 |
2.35e-07 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 57.62 E-value: 2.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2172 EELQRLKAEVTEAARQRSQVE------EELFSVRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkQVAEEA 2245
Cdd:COG4913 235 DDLERAHEALEDAREQIELLEpirelaERYAAARERLAELEYLRAALRLWFAQRRLELLEAELEELRAELA---RLEAEL 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2246 ARLSVAAQEAARLRQLAEEDLAQQralaekmlkekmqAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEE 2325
Cdd:COG4913 312 ERLEARLDALREELDELEAQIRGN-------------GGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2326 TQGFQRTLEAERQRQLEMSAEAERLklrmaemSRAQARAEEDAQRFRKQAEEIgeklhRTELAtqekvtlvqtlEIQRQQ 2405
Cdd:COG4913 379 AEEFAALRAEAAALLEALEEELEAL-------EEALAEAEAALRDLRRELREL-----EAEIA-----------SLERRK 435
|
250 260 270
....*....|....*....|....*....|....*...
gi 254675251 2406 SDHDAE--RLREAIAE-LEREKEKLKQEAKLLQLKSEE 2440
Cdd:COG4913 436 SNIPARllALRDALAEaLGLDEAELPFVGELIEVRPEE 473
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
1976-2651 |
2.62e-07 |
|
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: 57.37 E-value: 2.62e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1976 VERLKAKVEEARRLRERAEQESARQLQLA----QEAAQKRLQAEEKAHAfvVQQREEELQQTLQQEQNMLDRLRSEAEAA 2051
Cdd:TIGR02168 202 LKSLERQAEKAERYKELKAELRELELALLvlrlEELREELEELQEELKE--AEEELEELTAELQELEEKLEELRLEVSEL 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2052 RRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAE 2131
Cdd:TIGR02168 280 EEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAE 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2132 MEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEE--LGKLK 2209
Cdd:TIGR02168 360 LEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEaeLKELQ 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2210 ARIEAENRAlilrdkdntqrfLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEkMLKEKMQAVQEATR 2289
Cdd:TIGR02168 440 AELEELEEE------------LEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLD-SLERLQENLEGFSE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2290 lkAEAELLQQQKELAQEQARrlqedkeqmAQQLVEETQGFQRTLEA---ERQRQLEMS------------AEAERLKLRM 2354
Cdd:TIGR02168 507 --GVKALLKNQSGLSGILGV---------LSELISVDEGYEAAIEAalgGRLQAVVVEnlnaakkaiaflKQNELGRVTF 575
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2355 AEMSRAQARAEEDAQRFRKQAEE--IGEKLHRTELATQEKVTL---------VQTLEI---QRQQSDHDA---------- 2410
Cdd:TIGR02168 576 LPLDSIKGTEIQGNDREILKNIEgfLGVAKDLVKFDPKLRKALsyllggvlvVDDLDNaleLAKKLRPGYrivtldgdlv 655
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2411 ------------------------ERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQETQALQKSFLSEKDS 2466
Cdd:TIGR02168 656 rpggvitggsaktnssilerrreiEELEEKIEELEEKIAELEKALAELRKELEELEE-ELEQLRKELEELSRQISALRKD 734
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2467 LLQRERFIEQEKAKLEQL-------------FQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRR 2533
Cdd:TIGR02168 735 LARLEAEVEQLEERIAQLskelteleaeieeLEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTL 814
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2534 KQEELQHLEQQRQQQEKLLAEENQRLRERLQRLE--EEHRAALAHS-----EIATTQAASTKALPNGRDAPDGPSVEAEP 2606
Cdd:TIGR02168 815 LNEEAANLRERLESLERRIAATERRLEDLEEQIEelSEDIESLAAEieeleELIEELESELEALLNERASLEEALALLRS 894
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 254675251 2607 EYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTVAELTQRED 2651
Cdd:TIGR02168 895 ELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRID 939
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1299-1539 |
2.80e-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: 2.80e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1299 IKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQ 1378
Cdd:COG3883 18 IQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1379 QKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAE----EAEAQK 1454
Cdd:COG3883 98 SGGSVSYLDVLLGSESFSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEaakaELEAQQ 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1455 RQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALET 1534
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGA 257
|
....*
gi 254675251 1535 AQRSA 1539
Cdd:COG3883 258 AAGSA 262
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1338-1550 |
2.89e-07 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 56.95 E-value: 2.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1338 RQLAEAHAQAKAQAELEAQELQRRMQEEVARR--EEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAER 1410
Cdd:COG3206 147 PELAAAVANALAEAYLEQNLELRREEARKALEflEEQLPELRKELEEAEAALEEFRQknglvDLSEEAKLLLQQLSELES 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1411 SRMRIEEEIRVVRLQLETTERQRGGAEGE---------LQALRARAEEAEAQKRQAQE-------EAERLRRQVQDESQR 1474
Cdd:COG3206 227 QLAEARAELAEAEARLAALRAQLGSGPDAlpellqspvIQQLRAQLAELEAELAELSArytpnhpDVIALRAQIAALRAQ 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1475 KRQAEAELALRVKAEAEAAREKQRALQA-LDELRLQAE---EAERRLR--QAEAERARQVQVALETAQRSAEVELQSKRA 1548
Cdd:COG3206 307 LQQEAQRILASLEAELEALQAREASLQAqLAQLEARLAelpELEAELRrlEREVEVARELYESLLQRLEEARLAEALTVG 386
|
..
gi 254675251 1549 SF 1550
Cdd:COG3206 387 NV 388
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1317-1720 |
3.11e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 57.27 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1317 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRM------------------QEEVARREEAAVDAQQ 1378
Cdd:PRK04863 836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSALNRLLprlnlladetladrveeiREQLDEAEEAKRFVQQ 915
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1379 QKRSIQ--EELQHLRQSSEAEIQAKAQQVEAAE----RSRMRIE--EEIRVVRLQLETTERQR-GGAEGELQ-ALRARAE 1448
Cdd:PRK04863 916 HGNALAqlEPIVSVLQSDPEQFEQLKQDYQQAQqtqrDAKQQAFalTEVVQRRAHFSYEDAAEmLAKNSDLNeKLRQRLE 995
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1449 EAEAQKRQAQEEAerlrRQVQDESQRKRQAEAELalrvKAEAEAAREK-QRALQALDELRLQA-EEAERRLRQAEAE--- 1523
Cdd:PRK04863 996 QAEQERTRAREQL----RQAQAQLAQYNQVLASL----KSSYDAKRQMlQELKQELQDLGVPAdSGAEERARARRDElha 1067
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1524 ---RARQVQVALETAQRSAEVELQS--KRASFAEKTAQLERTLQEEHVT--VAQLREEAERRAQQQAEAERAREEAEREL 1596
Cdd:PRK04863 1068 rlsANRSRRNQLEKQLTFCEAEMDNltKKLRKLERDYHEMREQVVNAKAgwCAVLRLVKDNGVERRLHRRELAYLSADEL 1147
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1597 ERWQLKANEALRLrlqaeevaqqkslAQADAEKqkEEAEREARRRGKAEEQAVRQRELAEQEL-EKQRQLAEGTAQQRLA 1675
Cdd:PRK04863 1148 RSMSDKALGALRL-------------AVADNEH--LRDVLRLSEDPKRPERKVQFYIAVYQHLrERIRQDIIRTDDPVEA 1212
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 254675251 1676 AEQ---ELIRLRAETEQGEQQRQLLEEELA-----RLQHEATAATQKRQELEA 1720
Cdd:PRK04863 1213 IEQmeiELSRLTEELTSREQKLAISSESVAniirkTIQREQNRIRMLNQGLQN 1265
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
1717-2568 |
3.43e-07 |
|
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: 57.00 E-value: 3.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1717 ELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRleaeaGRFRELAEEAARLRALAEEaKRQRQLAEEDAARQRAEA 1796
Cdd:TIGR02169 167 EFDRKKEKALEELEEV---EENIERLDLIIDEKRQQL-----ERLRREREKAERYQALLKE-KREYEGYELLKEKEALER 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1797 ERVLTEKlaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHkadIEERLAQLrkasESELERQKG 1876
Cdd:TIGR02169 238 QKEAIER--QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLR---VKEKIGEL----EAEIASLER 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1877 LVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNaedtmRSKEQAELEAARQRqlaaeeEQRRREAEERVQ 1956
Cdd:TIGR02169 309 SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKR-----RDKLTEEYAELKEE------LEDLRAELEEVD 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1957 RSLAAEEEAARQRKVALEEVERLKAKVE-EARRLRERAEQESARQLQLAQEAAQKRLQ-AEEKAHAFVVQQREEELQQTL 2034
Cdd:TIGR02169 378 KEFAETRDELKDYREKLEKLKREINELKrELDRLQEELQRLSEELADLNAAIAGIEAKiNELEEEKEDKALEIKKQEWKL 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2035 QQEQNMLDRLRSEAEAARRAAEEAEEAREqaereaaQSRKQVEEAERLKQSAEEQAQAQAqaqaaaeklrkeaeqeaarr 2114
Cdd:TIGR02169 458 EQLAADLSKYEQELYDLKEEYDRVEKELS-------KLQRELAEAEAQARASEERVRGGR-------------------- 510
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2115 aqaeqaalkqkqAADAEMEKHKKFAEQTLRQKAQVEQELTTL-------RLQL----EETDHQKSIldEELQRLKA-EVT 2182
Cdd:TIGR02169 511 ------------AVEEVLKASIQGVHGTVAQLGSVGERYATAievaagnRLNNvvveDDAVAKEAI--ELLKRRKAgRAT 576
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2183 EAARQRSQVEEELFSVRVQMEELGKLKARIEAENR-----ALILRDKDNTQRfLEEEAEKMKQV---------------- 2241
Cdd:TIGR02169 577 FLPLNKMRDERRDLSILSEDGVIGFAVDLVEFDPKyepafKYVFGDTLVVED-IEAARRLMGKYrmvtlegelfeksgam 655
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2242 ----AEEAARLSVAAQEAARLRQLAEE---------DLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQA 2308
Cdd:TIGR02169 656 tggsRAPRGGILFSRSEPAELQRLRERleglkrelsSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL 735
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2309 RRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARaeEDAQRFRKQAEEIGEKLHRTELA 2388
Cdd:TIGR02169 736 KERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSH--SRIPEIQAELSKLEEEVSRIEAR 813
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2389 TQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMqtvqqEQILQETQALQKSfLSEKDSLL 2468
Cdd:TIGR02169 814 LREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEEL-----EEELEELEAALRD-LESRLGDL 887
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2469 QRERfiEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEqekqelmASMEEARRRQREAEEGVRRKQEElqhleQQRQQQ 2548
Cdd:TIGR02169 888 KKER--DELEAQLREL-ERKIEELEAQIEKKRKRLSELK-------AKLEALEEELSEIEDPKGEDEEI-----PEEELS 952
|
890 900
....*....|....*....|
gi 254675251 2549 EKLLAEENQRLRERLQRLEE 2568
Cdd:TIGR02169 953 LEDVQAELQRVEEEIRALEP 972
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1396-1533 |
3.57e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.44 E-value: 3.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1396 AEIQAKAQQVEAAersrmrieeeIRVVRLQLETTERQRGgAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDE--SQ 1473
Cdd:COG1566 79 TDLQAALAQAEAQ----------LAAAEAQLARLEAELG-AEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGavSQ 147
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1474 RKRQaEAELALRV-KAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERArQVQVALE 1533
Cdd:COG1566 148 QELD-EARAALDAaQAQLEAAQAQLAQAQAGLREEEELAAAQAQVAQAEAALA-QAELNLA 206
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1337-1465 |
4.04e-07 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 55.44 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1337 QRQLAEAHAQ-AKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKaQQVEAAERSRMRI 1415
Cdd:COG1566 82 QAALAQAEAQlAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQALYKKGAVSQ-QELDEARAALDAA 160
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 254675251 1416 EEEIRVVRLQLETTERQRGGAEgELQALRARAEEAEAQKRQAQEEAERLR 1465
Cdd:COG1566 161 QAQLEAAQAQLAQAQAGLREEE-ELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1039-1485 |
4.05e-07 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 56.67 E-value: 4.05e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1039 LEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEaqaVPATLQE----LEATKASLKKLRAQAEAQQPVFNTL 1114
Cdd:pfam15921 460 LEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSD---LTASLQEkeraIEATNAEITKLRSRVDLKLQELQHL 536
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1115 RDE---LRGAQEVGERLQQRHGERDVEVERWR---ERVTQLLERW----QAVLAQTDVRQRELEQLGRQLRYYRESADPL 1184
Cdd:pfam15921 537 KNEgdhLRNVQTECEALKLQMAEKDKVIEILRqqiENMTQLVGQHgrtaGAMQVEKAQLEKEINDRRLELQEFKILKDKK 616
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1185 SAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQkfaKQYINAIKDYELQLITYKAQLEPVASP 1264
Cdd:pfam15921 617 DAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSR---NELNSLSEDYEVLKRNFRNKSEEMETT 693
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1265 AKKPKVQsgsesviqeyvdLRTRYSELTTLTSqyikfiseTLRRMEEEERLAeqqraeererlaeVEAALEKQRQLAEAH 1344
Cdd:pfam15921 694 TNKLKMQ------------LKSAQSELEQTRN--------TLKSMEGSDGHA-------------MKVAMGMQKQITAKR 740
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1345 AQAKAqaeleaqelqrrMQEEVARREEAAVDAQQQKRSIQEELQHLRQsseaeiqakaqqveaaersrmrieeeirvvrl 1424
Cdd:pfam15921 741 GQIDA------------LQSKIQFLEEAMTNANKEKHFLKEEKNKLSQ-------------------------------- 776
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1425 QLETTERQRGGAEGELQALRA---RAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR 1485
Cdd:pfam15921 777 ELSTVATEKNKMAGELEVLRSqerRLKEKVANMEVALDKASLQFAECQDIIQRQEQESVRLKLQ 840
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1792-2182 |
4.39e-07 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 56.29 E-value: 4.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1792 QRAEAERVLTEKLAAIsEATRLKTEAEialkEKEAENERLRRLAEDEAFQRRRLEEQAALHKAdiEERLAQLRkasESEL 1871
Cdd:pfam17380 281 QKAVSERQQQEKFEKM-EQERLRQEKE----EKAREVERRRKLEEAEKARQAEMDRQAAIYAE--QERMAMER---EREL 350
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1872 ERQKglVEDTLRQRRQVEEEIMALKVSFEKaaagkaELE-LELGRIRSNaedtmrSKEQAELEAARQRQLAaeeeqrrre 1950
Cdd:pfam17380 351 ERIR--QEERKRELERIRQEEIAMEISRMR------ELErLQMERQQKN------ERVRQELEAARKVKIL--------- 407
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1951 aeervqrslaaEEEAARQRKVALEEVERLKAKVEEARRLR-ERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQReee 2029
Cdd:pfam17380 408 -----------EEERQRKIQQQKVEMEQIRAEQEEARQREvRRLEEERAREMERVRLEEQERQQQVERLRQQEEERK--- 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2030 lqqtlqqeqnmldRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAeq 2109
Cdd:pfam17380 474 -------------RKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEERRREA-- 538
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 2110 eaarraqaeqaalKQKQAADAEMEKHKKFAEQTLRqkaqVEQELTTLRLQLEETDHQKSILDEELQRLKAEVT 2182
Cdd:pfam17380 539 -------------EEERRKQQEMEERRRIQEQMRK----ATEERSRLEAMEREREMMRQIVESEKARAEYEAT 594
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1388-1676 |
4.64e-07 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 56.11 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1388 QHLRQSsEAEIQAKAQQVEAAERSRMRIEEeiRVVRLQLETTERQrggaegelqalrARAEEAEAQKRQAQEEA-----E 1462
Cdd:PRK05035 429 QYYRQA-KAEIRAIEQEKKKAEEAKARFEA--RQARLEREKAARE------------ARHKKAAEARAAKDKDAvaaalA 493
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1463 RLRRQVQDESQRKRQAEAELALRVKAEAEA-AREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEV 1541
Cdd:PRK05035 494 RVKAKKAAATQPIVIKAGARPDNSAVIAAReARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEE 573
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1542 ELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAeaerareeaerelerwqlkANEALRLRLQAEEVAQQKS 1621
Cdd:PRK05035 574 EVDPKKAAVAAAIARAKAKKAAQQAASAEPEEQVAEVDPKKA-------------------AVAAAIARAKAKKAEQQAN 634
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 1622 LAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAA 1676
Cdd:PRK05035 635 AEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPEEAEDPKKAAVAAAIARAKA 689
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
1067-1729 |
4.88e-07 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 56.34 E-value: 4.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1067 EEVLKTHEEQLKE-----AQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVER 1141
Cdd:pfam01576 337 EEETRSHEAQLQEmrqkhTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQE 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1142 WRERVTQ-------LLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKR-RQEQIQAVpiANCQAAREQL 1213
Cdd:pfam01576 417 LQARLSEserqraeLAEKLSKLQSELESVSSLLNEAEGKNIKLSKDVSSLESQLQDTQElLQEETRQK--LNLSTRLRQL 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1214 RQEKALLEEieRHGEKVEECQKFAKQyinaIKDYELQLITYKAQLEPVASPAK-----KPKVQSGSESVIQEY------- 1281
Cdd:pfam01576 495 EDERNSLQE--QLEEEEEAKRNVERQ----LSTLQAQLSDMKKKLEEDAGTLEaleegKKRLQRELEALTQQLeekaaay 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1282 ------------------VDLRTRYSELTTLTSQYIKFisetlRRMEEEERLAEQQRAEERERlAEVEAALEKQRQLAEA 1343
Cdd:pfam01576 569 dklektknrlqqelddllVDLDHQRQLVSNLEKKQKKF-----DQMLAEEKAISARYAEERDR-AEAEAREKETRALSLA 642
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1344 HAQAKAQAELEAQELQRRMQE--------------------EVARR--EEAAVDAQQQKRSIQEEL-------------- 1387
Cdd:pfam01576 643 RALEEALEAKEELERTNKQLRaemedlvsskddvgknvhelERSKRalEQQVEEMKTQLEELEDELqatedaklrlevnm 722
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1388 QHLRQSSEAEIQAKAqqvEAAERSRMRIEEEIRVVRLQLETTERQRGGA-------EGELQALRARAEEAEAQKRQAQEE 1460
Cdd:pfam01576 723 QALKAQFERDLQARD---EQGEEKRRQLVKQVRELEAELEDERKQRAQAvaakkklELDLKELEAQIDAANKGREEAVKQ 799
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1461 AERLRRQVQDesqrkRQAEAELALRVKAEAEA-AREKQRALQALDELRLQAEE----AERRLRQAEAERAR-QVQVALET 1534
Cdd:pfam01576 800 LKKLQAQMKD-----LQRELEEARASRDEILAqSKESEKKLKNLEAELLQLQEdlaaSERARRQAQQERDElADEIASGA 874
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1535 AQRSAeveLQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELE-----RWQL-KANEALR 1608
Cdd:pfam01576 875 SGKSA---LQDEKRRLEARIAQLEEELEEEQSNTELLNDRLRKSTLQVEQLTTELAAERSTSQksesaRQQLeRQNKELK 951
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1609 LRLQAEEVA---QQKSLAQA------DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQE 1679
Cdd:pfam01576 952 AKLQEMEGTvksKFKSSIAAleakiaQLEEQLEQESRERQAANKLVRRTEKKLKEVLLQVEDERRHADQYKDQAEKGNSR 1031
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|
gi 254675251 1680 LIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEM 1729
Cdd:pfam01576 1032 MKQLKRQLEEAEEEASRANAARRKLQRELDDATESNESMNREVSTLKSKL 1081
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2281-2426 |
4.91e-07 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 56.18 E-value: 4.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2281 MQAVQEATRlkaeaELLQQQKELA-------QEQARRLQ-EDKEQMAQQLVEEtQGFQRTLEAERQRQLEMSAEAERLKL 2352
Cdd:PTZ00491 638 VEPVDERTR-----DSLQKSVQLAieittksQEAAARHQaELLEQEARGRLER-QKMHDKAKAEEQRTKLLELQAESAAV 711
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 2353 RMAEMSRAQARAEEDAQRFRKQAEeigekLHRTEL-ATQEKVTLVQTLEIQRQQSDHDAERlREAIAELEREKEK 2426
Cdd:PTZ00491 712 ESSGQSRAEALAEAEARLIEAEAE-----VEQAELrAKALRIEAEAELEKLRKRQELELEY-EQAQNELEIAKAK 780
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2239-2455 |
5.79e-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: 5.79e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2239 KQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM 2318
Cdd:TIGR02794 46 GAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQAEEAK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2319 AQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKvtlvQT 2398
Cdd:TIGR02794 126 AKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAE----AA 201
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 2399 LEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQA 2455
Cdd:TIGR02794 202 KAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAG 258
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1642-1850 |
5.87e-07 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 55.73 E-value: 5.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1642 GKAEEQAVRQRELAEQELEKQRQlAEGTAQQRLAAEQ-ELIRLRAETEQGEQ--QRQLLEEELARlqheataATQKRQEL 1718
Cdd:pfam15709 307 GNMESEEERSEEDPSKALLEKRE-QEKASRDRLRAERaEMRRLEVERKRREQeeQRRLQQEQLER-------AEKMREEL 378
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1719 EAELAKVRAEMEvlLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEeakRQRQLAEEDAARQRAEAER 1798
Cdd:pfam15709 379 ELEQQRRFEEIR--LRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEFRRKLQE---LQRKKQQEEAERAEAEKQR 453
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1799 VLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAA 1850
Cdd:pfam15709 454 QKELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAA 505
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1119-1544 |
6.68e-07 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 56.12 E-value: 6.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1119 RGAQEvgERLQQRHGERDVEVERW--RERVTQLLERWQ-----------AVLAQTDVRQrELEQLGRQLRY-YRESADpl 1184
Cdd:PRK04863 781 RAARE--KRIEQLRAEREELAERYatLSFDVQKLQRLHqafsrfigshlAVAFEADPEA-ELRQLNRRRVElERALAD-- 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1185 sawlQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEiERHGEKVEECQ---KFAKQYINAIKDYELQLitykAQLEPV 1261
Cdd:PRK04863 856 ----HESQEQQQRSQLEQAKEGLSALNRLLPRLNLLAD-ETLADRVEEIReqlDEAEEAKRFVQQHGNAL----AQLEPI 926
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1262 AS-----PAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKF-ISETLRRMEEEERLAEQQRAeereRLAEVEAALE 1335
Cdd:PRK04863 927 VSvlqsdPEQFEQLKQDYQQAQQTQRDAKQQAFALTEVVQRRAHFsYEDAAEMLAKNSDLNEKLRQ----RLEQAEQERT 1002
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1336 KQRqlaEAHAQAKAQAeleAQELQRRMQEEVARREeaavdAQQQKRSIQEELQHL--RQSSEAEIQAKAQqveaaersRM 1413
Cdd:PRK04863 1003 RAR---EQLRQAQAQL---AQYNQVLASLKSSYDA-----KRQMLQELKQELQDLgvPADSGAEERARAR--------RD 1063
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1414 RIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE-------RLRRQVQDESQRKRQAEAELALRV 1486
Cdd:PRK04863 1064 ELHARLSANRSRRNQLEKQLTFCEAEMDNLTKKLRKLERDYHEMREQVVnakagwcAVLRLVKDNGVERRLHRRELAYLS 1143
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1487 KAEAEAAREKqrALQALdelrlqaeeaerRLRQAEAERARQVQVALETAQRsAEVELQ 1544
Cdd:PRK04863 1144 ADELRSMSDK--ALGAL------------RLAVADNEHLRDVLRLSEDPKR-PERKVQ 1186
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3685-3720 |
7.06e-07 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 48.25 E-value: 7.06e-07
10 20 30
....*....|....*....|....*....|....*.
gi 254675251 3685 RLLLEAQAATGFLLDPVKGERLTVDEAVRKGLVGPE 3720
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1311-1506 |
8.25e-07 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 54.81 E-value: 8.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1311 EEERLAEQQRAEERERLAEveAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVAR-REEAAVDAQQQKRSIQEElqh 1389
Cdd:PRK09510 107 EKERLAAQEQKKQAEEAAK--QAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAAKKaAAEAKKKAEAEAAKKAAA--- 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1390 lRQSSEAEIQAKAQQVEAAErsrmrieeeirvvrlqletterQRGGAEGELQALRARAEEAEAQKRQAQEEAErlrrqvq 1469
Cdd:PRK09510 182 -EAKKKAEAEAAAKAAAEAK----------------------KKAEAEAKKKAAAEAKKKAAAEAKAAAAKAA------- 231
|
170 180 190
....*....|....*....|....*....|....*..
gi 254675251 1470 desqRKRQAEAELALRVKAEAEAAREKQRAlqALDEL 1506
Cdd:PRK09510 232 ----AEAKAAAEKAAAAKAAEKAAAAKAAA--EVDDL 262
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1457-1992 |
8.55e-07 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 55.46 E-value: 8.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1457 AQEEAERLRRQVQDESQRKR---QAEAELALRVKaeaEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALE 1533
Cdd:PRK03918 163 AYKNLGEVIKEIKRRIERLEkfiKRTENIEELIK---EKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1534 TAQRSAEVE-LQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERraqqqaeaerareeaereLERWQLKANEALRLRLQ 1612
Cdd:PRK03918 240 IEELEKELEsLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKE------------------LKELKEKAEEYIKLSEF 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1613 AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAE--------GTAQQRLAAEQELIRLR 1684
Cdd:PRK03918 302 YEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEEleerhelyEEAKAKKEELERLKKRL 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1685 AETEQGEQQRQLLEEELAR--LQHEATAATQKRQELEAELAKVRAEMEVLLASKARA-------EEESR----------- 1744
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKeeIEEEISKITARIGELKKEIKELKKAIEELKKAKGKCpvcgrelTEEHRkelleeytael 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1745 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAE--------------EDAARQRAEAERVLTEKLAAISEA 1810
Cdd:PRK03918 462 KRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELAEqlkeleeklkkynlEELEKKAEEYEKLKEKLIKLKGEI 541
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1811 TRLKTEAEIA---LKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKA---------SESELERQKGLV 1878
Cdd:PRK03918 542 KSLKKELEKLeelKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFyneylelkdAEKELEREEKEL 621
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1879 EDTLRQRRQVEEEIMALKVSFEKAaagKAELElELGRIRSnaEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRS 1958
Cdd:PRK03918 622 KKLEEELDKAFEELAETEKRLEEL---RKELE-ELEKKYS--EEEYEELREEYLELSRELAGLRAELEELEKRREEIKKT 695
|
570 580 590
....*....|....*....|....*....|....
gi 254675251 1959 LAAEEEAARQRKVALEEVERLKAKVEEARRLRER 1992
Cdd:PRK03918 696 LEKLKEELEEREKAKKELEKLEKALERVEELREK 729
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1655-1870 |
8.94e-07 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 54.84 E-value: 8.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1655 AEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLA 1734
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1735 SKARAEE---------ESRSTSE--KSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEK 1803
Cdd:COG3883 94 ALYRSGGsvsyldvllGSESFSDflDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1804 LAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESE 1870
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 240
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4107-4135 |
9.40e-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: 9.40e-07
10 20
....*....|....*....|....*....
gi 254675251 4107 IVDPETGKEMSVYEAYRKGLIDHQTYLEL 4135
Cdd:pfam00681 11 IIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1312-1689 |
1.09e-06 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 54.90 E-value: 1.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1312 EERLAEQQRaEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevarREEAAVDAQQQKRSIQEELQHLR 1391
Cdd:pfam07888 33 QNRLEECLQ-ERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAE----LKEELRQSREKHEELEEKYKELS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1392 QSSEAEIQAKAQQVEAAERSRMRIEE-EIRVVRLQLETTERqrggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD 1470
Cdd:pfam07888 108 ASSEELSEEKDALLAQRAAHEARIRElEEDIKTLTQRVLER-----ETELERMKERAKKAGAQRKEEEAERKQLQAKLQQ 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1471 ESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEA--ERARQVQVALETAQRSAEvelqSKRA 1548
Cdd:pfam07888 183 TEEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAllEELRSLQERLNASERKVE----GLGE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1549 SFAEKTAQLERTLQEEH---VTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALrLRLQAEEVAQQKSLAQA 1625
Cdd:pfam07888 259 ELSSMAAQRDRTQAELHqarLQAAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRI-EKLSAELQRLEERLQEE 337
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1626 DAEKQKEEAEREARRRGKAEEQAVRQRELaeQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQ 1689
Cdd:pfam07888 338 RMEREKLEVELGREKDCNRVQLSESRREL--QELKASLRVAQKEKEQLQAEKQELLEYIRQLEQ 399
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1285-1404 |
1.10e-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: 53.45 E-value: 1.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1285 RTRYSELTTLTSQYIKFI----SETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELeaqelqR 1360
Cdd:pfam12037 56 QTRQAELQAKIKEYEAAQeqlkIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEEL------L 129
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 254675251 1361 RMQEEVARREEAAVDAQQQKRSIQEEL----QHLRQSSEAEIQAKAQQ 1404
Cdd:pfam12037 130 RKQEESVAKQEAMRIQAQRRQTEEHEAelrrETERAKAEAEAEARAKE 177
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1306-1786 |
1.29e-06 |
|
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.
Pssm-ID: 461677 [Multi-domain] Cd Length: 660 Bit Score: 54.75 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1306 LRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAeahaQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQE 1385
Cdd:pfam05557 57 IRLLEKREAEAEEALREQAELNRLKKKYLEALNKKL----NEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNS 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1386 ELQHLRQSSE------AEIQAKAQQVEAAERSRMRIEEEIR--VVRLQLET-------TERQRGGAEGELQALRARAEEA 1450
Cdd:pfam05557 133 ELEELQERLDllkakaSEAEQLRQNLEKQQSSLAEAEQRIKelEFEIQSQEqdseivkNSKSELARIPELEKELERLREH 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1451 EAQKRQAQEEAERLRRQVQDESQRKRQAEaelalrvKAEAEAAR---EKQRALQALDELRLQAEEAERRLRQAEAERARQ 1527
Cdd:pfam05557 213 NKHLNENIENKLLLKEEVEDLKRKLEREE-------KYREEAATlelEKEKLEQELQSWVKLAQDTGLNLRSPEDLSRRI 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1528 VQValetaqRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAEREL-----ERWQLK 1602
Cdd:pfam05557 286 EQL------QQREIVLKEENSSLTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRLQRRVllltkERDGYR 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1603 AN-EALRLRLQAEEVAQQKSLAQADAE----KQKEEAEREARRRGKAEEQAVRQRELA---EQELEKQRQlAEGTAQQRL 1674
Cdd:pfam05557 360 AIlESYDKELTMSNYSPQLLERIEEAEdmtqKMQAHNEEMEAQLSVAEEELGGYKQQAqtlERELQALRQ-QESLADPSY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1675 AAE------QELIRLRAETEQGEQQRQLLEEELAR--------------LQHEATAATQKRQELEAELAKVRAEMEVLla 1734
Cdd:pfam05557 439 SKEevdslrRKLETLELERQRLREQKNELEMELERrclqgdydpkktkvLHLSMNPAAEAYQQRKNQLEKLQAEIERL-- 516
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 254675251 1735 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEeaarLRALAEEA-KRQRQLAE 1786
Cdd:pfam05557 517 -KRLLKKLEDDLEQVLRLPETTSTMNFKEVLD----LRKELESAeLKNQRLKE 564
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
2129-2590 |
1.32e-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: 55.23 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2129 DAEMEKHKKFAEQTLRQKAQVEQELTT--------LRLQLEETDHQKSILDEELQRLKAEV---TEAARQRSQVEEELFS 2197
Cdd:pfam12128 364 KALTGKHQDVTAKYNRRRSKIKEQNNRdiagikdkLAKIREARDRQLAVAEDDLQALESELreqLEAGKLEFNEEEYRLK 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2198 VRvqmeeLGKLKARIeaeNRALILRDKDNTQRFLEEEAEKMKQVAEEA-ARLSVAAQEAARLRQLAEEDLAQQRaLAEKM 2276
Cdd:pfam12128 444 SR-----LGELKLRL---NQATATPELLLQLENFDERIERAREEQEAAnAEVERLQSELRQARKRRDQASEALR-QASRR 514
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2277 LKEKMQAVQEATR------------LKAEAELLQQQ--KELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLE 2342
Cdd:pfam12128 515 LEERQSALDELELqlfpqagtllhfLRKEAPDWEQSigKVISPELLHRTDLDPEVWDGSVGGELNLYGVKLDLKRIDVPE 594
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2343 MSAEAERLKLRMAEMSRA-------QARAEEDAQRFRKQAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLR 2414
Cdd:pfam12128 595 WAASEEELRERLDKAEEAlqsarekQAAAEEQLVQANGELEKASREETFARTALKNaRLDLRRLFDEKQSEKDKKNKALA 674
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2415 EAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQ---ETQALQKSFLSEKDSLLQR-----ERFIEQEKAKLEQLfQ 2486
Cdd:pfam12128 675 ERKDSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREartEKQAYWQVVEGALDAQLALlkaaiAARRSGAKAELKAL-E 753
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2487 DEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRL 2566
Cdd:pfam12128 754 TWYKRDLASLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLRYFDWYQETWLQRRPRLATQLSNIERAISELQQQLARL 833
|
490 500
....*....|....*....|....
gi 254675251 2567 EEEHRAALAhsEIATTQAASTKAL 2590
Cdd:pfam12128 834 IADTKLRRA--KLEMERKASEKQQ 855
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
2132-2435 |
1.36e-06 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 54.64 E-value: 1.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2132 MEKHKKFAEQTLRQKAQVEQELTTlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKAR 2211
Cdd:TIGR04523 389 LESQINDLESKIQNQEKLNQQKDE---QIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRES 465
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2212 IEAENRAL------ILRDKDNTQRFLEEEAEKMKQVAEEAarlsvaaqeaarlRQLAEE--DLAQQRALaekmLKEKMQa 2283
Cdd:TIGR04523 466 LETQLKVLsrsinkIKQNLEQKQKELKSKEKELKKLNEEK-------------KELEEKvkDLTKKISS----LKEKIE- 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2284 vqeatrlKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEaerqrqlemsaeaeRLKLRMAEMSRAQAR 2363
Cdd:TIGR04523 528 -------KLESEKKEKESKISDLEDELNKDDFELKKENLEKEIDEKNKEIE--------------ELKQTQKSLKKKQEE 586
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 2364 AEEDAQRFRKQAEEIGEKLhrtelatQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ 2435
Cdd:TIGR04523 587 KQELIDQKEKEKKDLIKEI-------EEKEKKISSLEKELEKAKKENEKLSSIIKNIKSKKNKLKQEVKQIK 651
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1268-1461 |
1.43e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 54.64 E-value: 1.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1268 PKVQSGSESVIQEYVDLRTRYSELTTltSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQA 1347
Cdd:COG3206 185 PELRKELEEAEAALEEFRQKNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELLQS 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1348 KAQAELEAQ--ELQRRMQEEVARREE---AAVDAQQQ----KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEE 1418
Cdd:COG3206 263 PVIQQLRAQlaELEAELAELSARYTPnhpDVIALRAQiaalRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEAR 342
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 254675251 1419 IRV---VRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEA 1461
Cdd:COG3206 343 LAElpeLEAELRRLEREVEVARELYESLLQRLEEARLAEALTVGNV 388
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1345-1559 |
1.55e-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: 1.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1345 AQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAqqveaAERSRMRIEEEIRvvrl 1424
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQ-----AEQAAKQAEEKQK---- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1425 qletterqrggaegelQALRARAEEAEAQKRQAQEEAERlrrQVQDESQRKRQAEAelalRVKAEAEAAREKQRALQALD 1504
Cdd:TIGR02794 120 ----------------QAEEAKAKQAAEAKAKAEAEAER---KAKEEAAKQAEEEA----KAKAAAEAKKKAEEAKKKAE 176
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1505 ELRLQAEEAERRLRQ--AEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1559
Cdd:TIGR02794 177 AEAKAKAEAEAKAKAeeAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAE 233
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2068-2657 |
2.06e-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: 54.59 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2068 EAAQSRKQVEEAERLKQ-SAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEqtlRQK 2146
Cdd:pfam02463 212 YYQLKEKLELEEEYLLYlDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQE---EEL 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2147 AQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKDN 2226
Cdd:pfam02463 289 KLLAKEEEELKSELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKL 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2227 TQR-------------FLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDL---AQQRALAEKMLKEKMQAVQEATRL 2290
Cdd:pfam02463 369 EQLeeellakkkleseRLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLkeeKKEELEILEEEEESIELKQGKLTE 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2291 KAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETqgfQRTLEAERQRQLEMSAeAERLKLRMAEMSRAQARAEED--- 2367
Cdd:pfam02463 449 EKEELEKQELKLLKDELELKKSEDLLKETQLVKLQE---QLELLLSRQKLEERSQ-KESKARSGLKVLLALIKDGVGgri 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2368 ---AQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQqsdhdaeRLREAIAELEREKEKLKQEAKLLQLKSEEMQTV 2444
Cdd:pfam02463 525 isaHGRLGDLGVAVENYKVAISTAVIVEVSATADEVEERQ-------KLVRALTELPLGARKLRLLIPKLKLPLKSIAVL 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2445 QQEQILQETQALQKSFLSEKDSLLQRErFIEQEKAKLEQLFQdEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQ 2524
Cdd:pfam02463 598 EIDPILNLAQLDKATLEADEDDKRAKV-VEGILKDTELTKLK-ESAKAKESGLRKGVSLEEGLAEKSEVKASLSELTKEL 675
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2525 REAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALpngrdapdgPSVEA 2604
Cdd:pfam02463 676 LEIQELQEKAESELAKEEILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLL---------KQKID 746
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 254675251 2605 EPEYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHTTvaELTQREDVYRYLK 2657
Cdd:pfam02463 747 EEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTE--KLKVEEEKEEKLK 797
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1458-1994 |
2.17e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.00 E-value: 2.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1458 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQR 1537
Cdd:COG4717 52 EKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLY 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1538 SAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAerraqqqaeaerareeaerelerwqlkaNEALRLRLQAEEVA 1617
Cdd:COG4717 132 QELEALEAELAELPERLEELEERLEELRELEEELEELE----------------------------AELAELQEELEELL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1618 QQKSLAQAdaekqkeeaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLL 1697
Cdd:COG4717 184 EQLSLATE-----------------EELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEERLK 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1698 EEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRStseKSKQRLEAEAGRFRELAEEAARLRALAEE 1777
Cdd:COG4717 247 EARLLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLA---REKASLGKEAEELQALPALEELEEEELEE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1778 AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALH--KAD 1855
Cdd:COG4717 324 LLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEEYQelKEE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1856 IEERLAQLRKASESELERQKGLVEDTLRQR-RQVEEEImalkvsfekaaagkAELELELGRIRsnaedtmrsKEQAELEA 1934
Cdd:COG4717 404 LEELEEQLEELLGELEELLEALDEEELEEElEELEEEL--------------EELEEELEELR---------EELAELEA 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1935 ARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEAR--RLRERAE 1994
Cdd:COG4717 461 ELEQLEEDGELAELLQELEELKAELRELAEEWAALKLALELLEEAREEYREERlpPVLERAS 522
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
2184-2432 |
2.33e-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: 53.23 E-value: 2.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2184 AARQRSQVEEELFSVRVQMEELGKLKARIEAEnRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAE 2263
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE-EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2264 EDLAQQRALaekmLKEKMQAVQEATRLKAEAELLQQQKELaqeQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEM 2343
Cdd:COG4942 97 AELEAQKEE----LAELLRALYRLGRQPPLALLLSPEDFL---DAVRRLQYLKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2344 SAEAERLKLRMAEMSRAQARAEEDAQRFRKQAeeigeklhrTELATQEKVTLVQTLEIQRQqsdhdAERLREAIAELERE 2423
Cdd:COG4942 170 EAERAELEALLAELEEERAALEALKAERQKLL---------ARLEKELAELAAELAELQQE-----AEELEALIARLEAE 235
|
....*....
gi 254675251 2424 KEKLKQEAK 2432
Cdd:COG4942 236 AAAAAERTP 244
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1643-2016 |
2.43e-06 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 53.72 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1643 KAEEQAVRQRElaEQELEKQRQLAEGTAQQRLAAEQelIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1722
Cdd:pfam02029 14 RAREERRRQKE--EEEPSGQVTESVEPNEHNSYEED--SELKPSGQGGLDEEEAFLDRTAKREERRQKRLQEALERQKEF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1723 AKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRElAEEAARLRALAEEAKRQ--RQLAEEDAARQRAEAERVL 1800
Cdd:pfam02029 90 DPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKE-EETEIREKEYQENKWSTevRQAEEEGEEEEDKSEEAEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1801 TEKLAAISEatrlKTEAEIALKEKEAENERLRRLAedeafQRRRLEEQAAlhkadieerlaqlrKASESELERQKGLVED 1880
Cdd:pfam02029 169 VPTENFAKE----EVKDEKIKKEKKVKYESKVFLD-----QKRGHPEVKS--------------QNGEEEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1881 TLRQRRQVEEEimalkvsfEKAAAGKAELELELGRIR-SNAEdtmrsKEQAELEAARQRQLAAEEEQRRREAEERVQRSL 1959
Cdd:pfam02029 226 RQGGLSQSQER--------EEEAEVFLEAEQKLEELRrRRQE-----KESEEFEKLRQKQQEAELELEELKKKREERRKL 292
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1960 AAEEEaaRQRKValEEVERLKAKVEEARRLRERAEQESArqlqlaqEAAQKRLQAEE 2016
Cdd:pfam02029 293 LEEEE--QRRKQ--EEAERKLREEEEKRRMKEEIERRRA-------EAAEKRQKLPE 338
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1327-1739 |
2.46e-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: 2.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1327 LAEVEAALEKQRQLAEAHAQAKaqaelEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE----------- 1395
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVAR-----EDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAvvlllplpltg 959
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1396 --------AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ 1467
Cdd:COG1020 960 ngkldrlaLPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLL 1039
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1468 VQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKR 1547
Cdd:COG1020 1040 FLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLL 1119
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1548 ASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADA 1627
Cdd:COG1020 1120 ALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLL 1199
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1628 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1707
Cdd:COG1020 1200 LLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALL 1279
|
410 420 430
....*....|....*....|....*....|..
gi 254675251 1708 ATAATQKRQELEAELAKVRAEMEVLLASKARA 1739
Cdd:COG1020 1280 LPALARARAARTARALALLLLLALLLLLALAL 1311
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3890-3927 |
2.48e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.71 E-value: 2.48e-06
10 20 30
....*....|....*....|....*....|....*...
gi 254675251 3890 QKFLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTA 3927
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| CH_PLS3_rpt1 |
cd21325 |
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is ... |
12-120 |
2.48e-06 |
|
first calponin homology (CH) domain found in plastin-3; Plastin-3, also called T-plastin, is an actin-bundling protein found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Plastin- 3 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409174 Cd Length: 148 Bit Score: 50.06 E-value: 2.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 12 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 78
Cdd:cd21325 25 EKYAFVNWINKalendpdcrHVIPMNPNTDDLFKAVGDGIVLCKMINLSVPDTIDErainKKKLTPFIIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 254675251 79 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQVS 120
Cdd:cd21325 105 SAIGCHVVNIGAEDLRAGKPHLVLGLLWQIIKIGLFADIELS 146
|
|
| DUF4659 |
pfam15558 |
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ... |
1304-1537 |
2.80e-06 |
|
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.
Pssm-ID: 464768 [Multi-domain] Cd Length: 374 Bit Score: 53.12 E-value: 2.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1304 ETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARReEAAVDAQQQKRSI 1383
Cdd:pfam15558 51 ERRLLLQQSQEQWQAEKEQRKARLGREERRRADRREKQVIEKESRWREQAEDQENQRQEKLERARQ-EAEQRKQCQEQRL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1384 QEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEA------EAQKRQA 1457
Cdd:pfam15558 130 KEKEEELQALREQNSLQLQERLEEACHKRQLKEREEQKKVQENNLSELLNHQARKVLVDCQAKAEELlrrlslEQSLQRS 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1458 QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQ----RALQALDELRL-QAEEAERRLRQAEAERARQVQVAL 1532
Cdd:pfam15558 210 QENYEQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERqehkEALAELADRKIqQARQVAHKTVQDKAQRARELNLER 289
|
....*
gi 254675251 1533 ETAQR 1537
Cdd:pfam15558 290 EKNHH 294
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1447-1563 |
2.98e-06 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 53.34 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1447 AEEAEAQKRQAQEEAErLRRQVQDESQRKRQAEAELAlRVKAEAEAAREKQRALQALdELRLQAEEAErrlrqaeaeraR 1526
Cdd:COG2268 212 TEIAIAQANREAEEAE-LEQEREIETARIAEAEAELA-KKKAEERREAETARAEAEA-AYEIAEANAE-----------R 277
|
90 100 110
....*....|....*....|....*....|....*..
gi 254675251 1527 QVQVALETAQRSAEVELQSKRAsfAEKTAQLERTLQE 1563
Cdd:COG2268 278 EVQRQLEIAEREREIELQEKEA--EREEAELEADVRK 312
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
1066-1714 |
3.01e-06 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 53.80 E-value: 3.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1066 AEEVLKTHEEQLKEAQAVPATL-QELEATKASLKKLRAQAEA---QQPVFNTLRDE----LRGAQEVGERLQQR-HGERD 1136
Cdd:COG3096 562 LEAQLEELEEQAAEAVEQRSELrQQLEQLRARIKELAARAPAwlaAQDALERLREQsgeaLADSQEVTAAMQQLlERERE 641
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1137 VEVER-----WRERVTQLLERWQAVLAQTDVRQREL-EQLGRQL--RYYR----ESADPLSAWLQDAKrrqeqiQAVPIA 1204
Cdd:COG3096 642 ATVERdelaaRKQALESQIERLSQPGGAEDPRLLALaERLGGVLlsEIYDdvtlEDAPYFSALYGPAR------HAIVVP 715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1205 NCQAAREQLRQEKALLEE---IERH----GEKVEECQKFAKQYINAIKDYELQLITYKAqlEPV----ASPAKKPKVQSG 1273
Cdd:COG3096 716 DLSAVKEQLAGLEDCPEDlylIEGDpdsfDDSVFDAEELEDAVVVKLSDRQWRYSRFPE--VPLfgraAREKRLEELRAE 793
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1274 SESVIQEYVDLRTRYSELTTLTSQYIKFISETLRRMEEEErlAEQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAEL 1353
Cdd:COG3096 794 RDELAEQYAKASFDVQKLQRLHQAFSQFVGGHLAVAFAPD--PEAELAALRQRRSELERELAQHRA-QEQQLRQQLDQLK 870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1354 EAQELQRRMQEEV---------ARREEAAVD---AQQQKRSIQEELQHLRQSSE--AEIQAKAQQVEAAERSRMRIEEEI 1419
Cdd:COG3096 871 EQLQLLNKLLPQAnlladetlaDRLEELREEldaAQEAQAFIQQHGKALAQLEPlvAVLQSDPEQFEQLQADYLQAKEQQ 950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1420 RVVRLQL----ETTER----------QRGGAEGEL-QALRARAEEAEAQKRQAQEEAERLRRQVQDESQRkrQAEAELAL 1484
Cdd:COG3096 951 RRLKQQIfalsEVVQRrphfsyedavGLLGENSDLnEKLRARLEQAEEARREAREQLRQAQAQYSQYNQV--LASLKSSR 1028
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1485 RVKAE--AEAARE-KQRALQALDELRLQAEEAERRLRQA-EAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERT 1560
Cdd:COG3096 1029 DAKQQtlQELEQElEELGVQADAEAEERARIRRDELHEElSQNRSRRSQLEKQLTRCEAEMDSLQKRLRKAERDYKQERE 1108
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1561 LQEEHVtvaqlreeaerraqqqaeaerareeaerelERW----QLKANEALRLRLQAEEVAQQkslaqaDAEKQKEEAer 1636
Cdd:COG3096 1109 QVVQAK------------------------------AGWcavlRLARDNDVERRLHRRELAYL------SADELRSMS-- 1150
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1637 earrrgkaeEQAVRQRELAEQELEKQRQLAEGTAQQR---------LAAEQEL-IRLRAETEQGEQQRQLLEE---ELAR 1703
Cdd:COG3096 1151 ---------DKALGALRLAVADNEHLRDALRLSEDPRrperkvqfyIAVYQHLrERIRQDIIRTDDPVEAIEQmeiELAR 1221
|
730
....*....|.
gi 254675251 1704 LQHEATAATQK 1714
Cdd:COG3096 1222 LTEELTSREQK 1232
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
1067-1783 |
3.05e-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: 53.60 E-value: 3.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1067 EEVLKTHEEQLKEAQAVPATLQELEATKASLKKLRAQAEAqqpvfntLRDELRGAQEVGERLQQRHGERDVEVERW-RER 1145
Cdd:pfam07111 80 EEVRLLRETSLQQKMRLEAQAMELDALAVAEKAGQAEAEG-------LRAALAGAEMVRKNLEEGSQRELEEIQRLhQEQ 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1146 VTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESAdplSAWLQDAKRRQEQIQAvpiaNCQAAREQLRQEKALLEEIER 1225
Cdd:pfam07111 153 LSSLTQAHEEALSSLTSKAEGLEKSLNSLETKRAGE---AKQLAEAQKEAELLRK----QLSKTQEELEAQVTLVESLRK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1226 H-GEKV------EECQKFAKQYINAIKDYELQLITYKAQLEPVaspakKPKVQSGSESVIQEYVDLRTRYSELTTLTSQY 1298
Cdd:pfam07111 226 YvGEQVppevhsQTWELERQELLDTMQHLQEDRADLQATVELL-----QVRVQSLTHMLALQEEELTRKIQPSDSLEPEF 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1299 IKFISETLRRMEEEE-RLAEQQRAEERERLAEVEaalEKQRQLAEAHAQAKAQAELEAQeLQRRMQEEVARREEAAVDAq 1377
Cdd:pfam07111 301 PKKCRSLLNRWREKVfALMVQLKAQDLEHRDSVK---QLRGQVAELQEQVTSQSQEQAI-LQRALQDKAAEVEVERMSA- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1378 qqkRSIQEELQhlrQSSEAEIQAKaQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQA 1457
Cdd:pfam07111 376 ---KGLQMELS---RAQEARRRQQ-QQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQAVARIPSLSNRLSYAVRKVHTI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1458 QEEAER--LRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQAldELRLQA----EEAERRLRQAEAERARQVQVA 1531
Cdd:pfam07111 449 KGLMARkvALAQLRQESCPPPPPAPPVDADLSLELEQLREERNRLDA--ELQLSAhliqQEVGRAREQGEAERQQLSEVA 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1532 LETAQrsaevELQSKRASFAEKTAQLERTLQEEhvtvaqlreeaerraqqqaeaerareeaerelerwQLKANEALRLRl 1611
Cdd:pfam07111 527 QQLEQ-----ELQRAQESLASVGQQLEVARQGQ-----------------------------------QESTEEAASLR- 565
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1612 qAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRlAAEQELIRLRAETEQGE 1691
Cdd:pfam07111 566 -QELTQQQEIYGQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEK-ERNQELRRLQDEARKEE 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1692 QQR-----QLLEEE----LARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR-----STSEKSKQRLEAE 1757
Cdd:pfam07111 644 GQRlarrvQELERDknlmLATLQQEGLLSRYKQQRLLAVLPSGLDKKSVVSSPRPECSASAPipaavPTRESIKGSLTVL 723
|
730 740
....*....|....*....|....*.
gi 254675251 1758 AGRFRELAEEAARLRALAEEAKRQRQ 1783
Cdd:pfam07111 724 LDNLQGLSEAISREEAVCQEDNQDTC 749
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1269-1483 |
3.19e-06 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 52.84 E-value: 3.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1269 KVQSGSESVIQEYVDLRTRYSELTTL---TSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHA 1345
Cdd:COG4942 45 ALKKEEKALLKQLAALERRIAALARRiraLEQELAALEAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1346 QAKAQAELEAQELQRRMQEEVARREEAAVDAQQQkrsiQEELQHLRQSSEAEIQAKAQQVEAAERSRmrieeeirvVRLQ 1425
Cdd:COG4942 125 LLSPEDFLDAVRRLQYLKYLAPARREQAEELRAD----LAELAALRAELEAERAELEALLAELEEER---------AALE 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1426 LETTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA 1483
Cdd:COG4942 192 ALKAERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAERTP 244
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1310-1475 |
3.33e-06 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 52.54 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1310 EEEERLAEQQRAEERERLAEVEAAleKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1389
Cdd:TIGR02794 101 EKAAKQAEQAAKQAEEKQKQAEEA--KAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAE 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1390 LRQSSEAEIQAKAQQVEA-AERSRMRIEEEI----RVVRLQLETTERQRGGAEGELQALRARAEEAEAQK------RQAQ 1458
Cdd:TIGR02794 179 AKAKAEAEAKAKAEEAKAkAEAAKAKAAAEAaakaEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKqggargAAAG 258
|
170
....*....|....*..
gi 254675251 1459 EEAERLRRQVQDESQRK 1475
Cdd:TIGR02794 259 SEVDKYAAIIQQAIQQN 275
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3095-3131 |
3.74e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 3.74e-06
10 20 30
....*....|....*....|....*....|....*..
gi 254675251 3095 LRLLDAQLSTGGIVDPSKSHRVPLDVAYARGYLDKET 3131
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| CH_PLS1_rpt1 |
cd21323 |
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
12-119 |
3.80e-06 |
|
first calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409172 Cd Length: 145 Bit Score: 49.66 E-value: 3.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 12 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 78
Cdd:cd21323 25 EKVAFVNWINKalegdpdckHVVPMNPTDESLFKSLADGILLCKMINLSQPDTIDErainKKKLTPFTISENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254675251 79 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 119
Cdd:cd21323 105 SAIGCTVVNIGSLDLKEGKPHLVLGLLWQIIKVGLFADIEI 145
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2768-2803 |
4.00e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 46.32 E-value: 4.00e-06
10 20 30
....*....|....*....|....*....|....*.
gi 254675251 2768 RLLEAQIATGGIIDPVHSHRVPVDVAYKRGYFDEEM 2803
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1645-1870 |
4.05e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 53.10 E-value: 4.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1645 EEQAVRQRELAEQELEK-QRQLAEgtAQQRL-AAEQELIRLRAETE--QGEQQRQLLEEELARLQHEATAATQKRQELEA 1720
Cdd:COG3206 163 EQNLELRREEARKALEFlEEQLPE--LRKELeEAEAALEEFRQKNGlvDLSEEAKLLLQQLSELESQLAEARAELAEAEA 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1721 ELAKVRAEMEVLLASKARAEEeSRSTSEKSKQRLEAEAgrfrELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVL 1800
Cdd:COG3206 241 RLAALRAQLGSGPDALPELLQ-SPVIQQLRAQLAELEA----ELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL 315
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1801 TEklaAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfQRRRLEEQAALHKADIEERLAQLRKASESE 1870
Cdd:COG3206 316 AS---LEAELEALQAREASLQAQLAQLEARLAELPELEA-ELRRLEREVEVARELYESLLQRLEEARLAE 381
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2124-2309 |
4.43e-06 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 53.11 E-value: 4.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2124 QKQAADAEMEKHKKFAEQTLRQKAQvEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSVRVQME 2203
Cdd:pfam05667 309 TNEAPAATSSPPTKVETEEELQQQR-EEELEELQEQLEDLESSIQELEKEIKKLESSI-------KQVEEELEELKEQNE 380
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2204 ELGKLKARIEaenRAL-ILRDKDNT----QRFLEEEAEKMKQVAE--EAARLSVAAQEAARLRQLAEEDLAQQRALAE-K 2275
Cdd:pfam05667 381 ELEKQYKVKK---KTLdLLPDAEENiaklQALVDASAQRLVELAGqwEKHRVPLIEEYRALKEAKSNKEDESQRKLEEiK 457
|
170 180 190
....*....|....*....|....*....|....*.
gi 254675251 2276 MLKEKMQAVQEATRLKAE--AELLQQQKELAQEQAR 2309
Cdd:pfam05667 458 ELREKIKEVAEEAKQKEElyKQLVAEYERLPKDVSR 493
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2249-2527 |
4.51e-06 |
|
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.
Pssm-ID: 467957 [Multi-domain] Cd Length: 1848 Bit Score: 53.30 E-value: 4.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2249 SVAAQEAARLRQLAEEDLAQQRALAEKmlkekmqavqeatrlkaeaellqqqkELAQEQARRLQEDKeqmaQQLVEETQG 2328
Cdd:NF012221 1538 SESSQQADAVSKHAKQDDAAQNALADK--------------------------ERAEADRQRLEQEK----QQQLAAISG 1587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2329 FQRTLEAERQRQLEMSAEAERlklrmaemsraQARAEEdaqrfrkqAEEIgeklhrtelaTQEKVTLVQTLEIQRQQSDH 2408
Cdd:NF012221 1588 SQSQLESTDQNALETNGQAQR-----------DAILEE--------SRAV----------TKELTTLAQGLDALDSQATY 1638
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2409 DAE---RLREAIAE--LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSllqrerfiEQEKAKLEQ 2483
Cdd:NF012221 1639 AGEsgdQWRNPFAGglLDRVQEQLDDAKKISGKQLADAKQRHVDNQQKVKDAVAKSEAGVAQG--------EQNQANAEQ 1710
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 254675251 2484 LFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRR-QREA 2527
Cdd:NF012221 1711 DIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRgEQDA 1755
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1327-1421 |
4.84e-06 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 53.03 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1327 LAEVEAALEKQRQLAEAHAQAKAQAeleaQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLR-QSSEAEIQAKAQQV 1405
Cdd:PRK11448 144 LHALQQEVLTLKQQLELQAREKAQS----QALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQeKAAETSQERKQKRK 219
|
90
....*....|....*....
gi 254675251 1406 EAAERSRMRI---EEEIRV 1421
Cdd:PRK11448 220 EITDQAAKRLelsEEETRI 238
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
1540-2374 |
4.98e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 53.20 E-value: 4.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1540 EVELQSKRASFAEKTAQ-LERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELerwQLKANEALRLRLQAEEVAQ 1618
Cdd:pfam15921 58 EVELDSPRKIIAYPGKEhIERVLEEYSHQVKDLQRRLNESNELHEKQKFYLRQSVIDL---QTKLQEMQMERDAMADIRR 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1619 QKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQqrlaaeqELIRLRAETEQGEQQRQLLE 1698
Cdd:pfam15921 135 RESQSQEDLRNQLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKMMLSHEGVLQ-------EIRSILVDFEEASGKKIYEH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1699 EELARLQHEA--TAATQKRQELEAELA-------KVRAEMEVLLA-SKARAEEESRSTSEKSKQRLEAEAGRFRELAEEA 1768
Cdd:pfam15921 208 DSMSTMHFRSlgSAISKILRELDTEISylkgrifPVEDQLEALKSeSQNKIELLLQQHQDRIEQLISEHEVEITGLTEKA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1769 ARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQ 1848
Cdd:pfam15921 288 SSARSQANSIQSQLEIIQEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQ 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1849 AALHKADIEERLAQL-----RKASESELERQkglvedtlrQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEdT 1923
Cdd:pfam15921 368 FSQESGNLDDQLQKLladlhKREKELSLEKE---------QNKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLK-A 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1924 MRSKEQAELEaarqRQLAaeeeqrrreaeervqrslaaeeeAARQRKVALEEVERLKAKVEEARR-LRERAEQESARQLQ 2002
Cdd:pfam15921 438 MKSECQGQME----RQMA-----------------------AIQGKNESLEKVSSLTAQLESTKEmLRKVVEELTAKKMT 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2003 LAQE---------AAQKRLQAEEKAHAFV--VQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREaaq 2071
Cdd:pfam15921 491 LESSertvsdltaSLQEKERAIEATNAEItkLRSRVDLKLQELQHLKNEGDHLRNVQTECEALKLQMAEKDKVIEIL--- 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2072 sRKQVEEAERLkqsaeeqaqaqaqaqaaaeklrkeaeqeaarraqaeqaalkqkqaadaeMEKHKKFAEQTLRQKAQVEQ 2151
Cdd:pfam15921 568 -RQQIENMTQL-------------------------------------------------VGQHGRTAGAMQVEKAQLEK 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2152 ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQV----EEELFSVRVQMEELGKLKARIE---------AENRA 2218
Cdd:pfam15921 598 EINDRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLvnagSERLRAVKDIKQERDQLLNEVKtsrnelnslSEDYE 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2219 LILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEK----MLKEKMQAVQEA- 2287
Cdd:pfam15921 678 VLKRNFRNKSEEMETTTNKLKmqlksaQSELEQTRNTLKSMEGSDGHAMKVAMGMQKQITAKRgqidALQSKIQFLEEAm 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2288 TRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLvEETQGFQRTLeaeRQRQLEMSAEAERLKLRMAEMSRAQARAEED 2367
Cdd:pfam15921 758 TNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQERRL---KEKVANMEVALDKASLQFAECQDIIQRQEQE 833
|
....*..
gi 254675251 2368 AQRFRKQ 2374
Cdd:pfam15921 834 SVRLKLQ 840
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1304-1540 |
5.00e-06 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 52.29 E-value: 5.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1304 ETLRRMEEE--ERLAEQQRAEERERLAE---VEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQ 1378
Cdd:PRK07735 13 EAARRAKEEarKRLVAKHGAEISKLEEEnreKEKALPKNDDMTIEEAKRRAAAAAKAKAAALAKQKREGTEEVTEEEKAK 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1379 QKRSIQEElqhlrqsseaeiqAKAQQVEAAERSRMRIEEeirvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQ 1458
Cdd:PRK07735 93 AKAKAAAA-------------AKAKAAALAKQKREGTEE---------VTEEEKAAAKAKAAAAAKAKAAALAKQKREGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1459 EEAERLRRQVQDESQRKRQAEAelalrVKAEAeAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRS 1538
Cdd:PRK07735 151 EEVTEEEEETDKEKAKAKAAAA-----AKAKA-AALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKAS 224
|
..
gi 254675251 1539 AE 1540
Cdd:PRK07735 225 QG 226
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1702-2432 |
5.10e-06 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 52.80 E-value: 5.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1702 ARLQHEATAATQKRQELEAELAKVRAEME---VLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEA 1778
Cdd:pfam05483 81 SKLYKEAEKIKKWKVSIEAELKQKENKLQenrKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCNLL 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1779 KRQRQLAEEDAAR---QRAEAERVLT------EKLAAISEATRLKTE---AEIALKEKEaENERLRRLAEDEAFQRRRLE 1846
Cdd:pfam05483 161 KETCARSAEKTKKyeyEREETRQVYMdlnnniEKMILAFEELRVQAEnarLEMHFKLKE-DHEKIQHLEEEYKKEINDKE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1847 EQAALHKADIEERlaqlrkasESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRS 1926
Cdd:pfam05483 240 KQVSLLLIQITEK--------ENKMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMST 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1927 keqaeleaarQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR---KVALEEVERLKAKVEEARRLRERAEQESARQLQL 2003
Cdd:pfam05483 312 ----------QKALEEDLQIATKTICQLTEEKEAQMEELNKAKaahSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKI 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2004 AQEAAQKRLQAEEKAHAFVVQQREEelqqtlqqeqnmLDRLRSEAEAARRAAEEaeeareqaereaaqsRKQVEE-AERL 2082
Cdd:pfam05483 382 ITMELQKKSSELEEMTKFKNNKEVE------------LEELKKILAEDEKLLDE---------------KKQFEKiAEEL 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2083 KQSAEEQAQAQAQAQAAAEKLRkeaeQEAARRAQAEQAALKQKQAADAEMEKHK-KFAEQT------LRQKAQVEQELTT 2155
Cdd:pfam05483 435 KGKEQELIFLLQAREKEIHDLE----IQLTAIKTSEEHYLKEVEDLKTELEKEKlKNIELTahcdklLLENKELTQEASD 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2156 LRLQLEetDHQKSILDEELQ--RLKAEVTEAARQRSQVEEELFSVRVQMEELGKlkarieaENRALILRDKDNTQRFLEE 2233
Cdd:pfam05483 511 MTLELK--KHQEDIINCKKQeeRMLKQIENLEEKEMNLRDELESVREEFIQKGD-------EVKCKLDKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2234 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ---EATRLKAEAELLQQQKELAQEQARR 2310
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKKGSAENKQLNAyeiKVNKLELELASAKQKFEEIIDNYQK 661
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2311 LQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSaeaERLKLRMAEMSraqARAEEDAQRFRKQAEEIGEKLHRTELATQ 2390
Cdd:pfam05483 662 EIEDKKISEEKLLEEVEKAKAIADEAVKLQKEID---KRCQHKIAEMV---ALMEKHKHQYDKIIEERDSELGLYKNKEQ 735
|
730 740 750 760
....*....|....*....|....*....|....*....|..
gi 254675251 2391 EKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAK 2432
Cdd:pfam05483 736 EQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAK 777
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1114-1564 |
5.29e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.85 E-value: 5.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1114 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKR 1193
Cdd:COG4717 47 LLERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1194 RQEQIQAVpiancQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLepvaspakkpkvqsg 1273
Cdd:COG4717 127 LLPLYQEL-----EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQL--------------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1274 SESVIQEYVDLRTRYSELttltSQYIKFISETLRRMEEEERLAEQQraeeRERLAEVEAALEKQRQLAEAHAQAKAQAEL 1353
Cdd:COG4717 187 SLATEEELQDLAEELEEL----QQRLAELEEELEEAQEELEELEEE----LEQLENELEAAALEERLKEARLLLLIAAAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1354 EAQELQRRMQEEVARREEAAVDAQQQ------KRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLE 1427
Cdd:COG4717 259 LALLGLGGSLLSLILTIAGVLFLVLGllallfLLLAREKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1428 TTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESqrkrqaEAELALRVKAEAEAAREKQRALQALDELR 1507
Cdd:COG4717 339 LLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGVED------EEELRAALEQAEEYQELKEELEELEEQLE 412
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1508 LQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEE 1564
Cdd:COG4717 413 ELLGELEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDG 469
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1691-1882 |
5.64e-06 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 52.12 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1691 EQQRQLLEEELAR-LQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQRLEAEAGRFR----ELA 1765
Cdd:PRK09510 78 EEQRKKKEQQQAEeLQQKQAAEQERLKQLEKERLAAQEQ-------KKQAEEAAKQAALKQKQAEEAAAKAAAaakaKAE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1766 EEAARLRALAEEAKRQRQLAEEDAARQRAEAE-RVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAfqrrr 1844
Cdd:PRK09510 151 AEAKRAAAAAKKAAAEAKKKAEAEAAKKAAAEaKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKA----- 225
|
170 180 190
....*....|....*....|....*....|....*...
gi 254675251 1845 LEEQAALHKADIEERLAQLRKASESELERQKGLVEDTL 1882
Cdd:PRK09510 226 AAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVDDLF 263
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2129-2584 |
5.82e-06 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 52.73 E-value: 5.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2129 DAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEE-TDHQKSILDE-ELQRLKAEVTEAAR-----QRSQVEEELFSVRVQ 2201
Cdd:PRK02224 257 EAEIEDLRETIAETEREREELAEEVRDLRERLEElEEERDDLLAEaGLDDADAEAVEARReeledRDEELRDRLEECRVA 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2202 MEELGK----LKARI-EAENRALILRDKDNTqrfLEEEAEKMK-QVAEEAARLSVAAQEAARLRQL---AEEDLAQQRAL 2272
Cdd:PRK02224 337 AQAHNEeaesLREDAdDLEERAEELREEAAE---LESELEEAReAVEDRREEIEELEEEIEELRERfgdAPVDLGNAEDF 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2273 AEKMLKEKMQAVQEATRLKAEaelLQQQKELAQEQARRLQEDKEQMAQQLVEETqGFQRTLEAERQRQLEMSAEAERLKL 2352
Cdd:PRK02224 414 LEELREERDELREREAELEAT---LRTARERVEEAEALLEAGKCPECGQPVEGS-PHVETIEEDRERVEELEAELEDLEE 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2353 RMAEMSRAQARAEE------DAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEK 2426
Cdd:PRK02224 490 EVEEVEERLERAEDlveaedRIERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2427 LKQEAKLLQLKSEEM-QTVQQEQILQETQALQKSFLSEKDSLL-QRERFIEQEKAKLEQLFQDEVAKAKQLREEQQrqqq 2504
Cdd:PRK02224 570 AREEVAELNSKLAELkERIESLERIRTLLAAIADAEDEIERLReKREALAELNDERRERLAEKRERKRELEAEFDE---- 645
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2505 qmeqekqelmASMEEARRRQREAEE------GVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALA-HS 2577
Cdd:PRK02224 646 ----------ARIEEAREDKERAEEyleqveEKLDELREERDDLQAEIGAVENELEELEELRERREALENRVEALEAlYD 715
|
....*..
gi 254675251 2578 EIATTQA 2584
Cdd:PRK02224 716 EAEELES 722
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3426-3462 |
6.80e-06 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 45.55 E-value: 6.80e-06
10 20 30
....*....|....*....|....*....|....*..
gi 254675251 3426 IRLLEAQVATGGIIDPVHSHRLPVDVAYQRGYFDEEM 3462
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1657-2045 |
6.82e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.46 E-value: 6.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1657 QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQH--EATAATQKRQELEAELAKVRAEMEvlla 1734
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKllQLLPLYQELEALEAELAELPERLE---- 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1735 sKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRaeaervlteklaaISEATRLK 1814
Cdd:COG4717 150 -ELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR-------------LAELEEEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1815 TEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVedtlrqrrQVEEEIMA 1894
Cdd:COG4717 216 EEAQEELEELEEELEQLENELEAAALEERLKEARLLLLIAAALLALLGLGGSLLSLILTIAGVL--------FLVLGLLA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1895 LKVSF---EKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKV 1971
Cdd:COG4717 288 LLFLLlarEKASLGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEE 367
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1972 ALEEVERL--KAKVEEARRLRERAEQ-ESARQLQLAQEAAQKRLQAEEK-AHAFVVQQREEELQQTLQQEQNMLDRLR 2045
Cdd:COG4717 368 LEQEIAALlaEAGVEDEEELRAALEQaEEYQELKEELEELEEQLEELLGeLEELLEALDEEELEEELEELEEELEELE 445
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2215-2491 |
6.94e-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: 52.66 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2215 ENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA 2294
Cdd:TIGR00618 163 KEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRSQLLTLCTPCMPDTYHERKQVLEKELKHLREALQQTQQSH 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2295 ELLQQQKELAQEQARRLQEDKEQMAQqlvEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2374
Cdd:TIGR00618 243 AYLTQKREAQEEQLKKQQLLKQLRAR---IEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQSK 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2375 AEEIGEKLHRT------ELATQEKVTLVQTLEIQ----RQQSDHDAER---------LREAIAELEREKEKLKQeakLLQ 2435
Cdd:TIGR00618 320 MRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQeihiRDAHEVATSIreiscqqhtLTQHIHTLQQQKTTLTQ---KLQ 396
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 2436 LKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAK 2491
Cdd:TIGR00618 397 SLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQ 452
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
584-676 |
7.05e-06 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 47.71 E-value: 7.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 584 HGFVAAATKELMWLNEKEEEEVGFDWSDRNTNMAAKKESYSALMRELEMKEKKIKEIQNTGDRLLREDHPARPTVESFQA 663
Cdd:smart00150 1 QQFLRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLIEEGHPDAEEIEERLE 80
|
90
....*....|...
gi 254675251 664 ALQTQWSWMLQLC 676
Cdd:smart00150 81 ELNERWEELKELA 93
|
|
| CH_FLNA_rpt2 |
cd21312 |
second calponin homology (CH) domain found in filamin-A (FLN-A) and similar proteins; ... |
122-229 |
7.48e-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: 47.88 E-value: 7.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 122 QSEDMTAKEKLLLWSQRMVEGyqgLRCDNFTTSWRDGRLFNAIIHRHKPMLI-DMNKVYRQTNLENLDQAFSVAERDLGV 200
Cdd:cd21312 7 EAKKQTPKQRLLGWIQNKLPQ---LPITNFSRDWQSGRALGALVDSCAPGLCpDWDSWDASKPVTNAREAMQQADDWLGI 83
|
90 100
....*....|....*....|....*....
gi 254675251 201 TRLLDPEDVDVPQPDEKSIITYVSSLYDA 229
Cdd:cd21312 84 PQVITPEEIVDPNVDEHSVMTYLSQFPKA 112
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1291-1530 |
7.71e-06 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 52.33 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1291 LTTLTSQYIKFISEtLRRMEEEERLA--EQQRAEERERLAEVEAALEKQRQlAEAHAQAKAQAELEAQELQRrMQEEVAR 1368
Cdd:COG3206 154 ANALAEAYLEQNLE-LRREEARKALEflEEQLPELRKELEEAEAALEEFRQ-KNGLVDLSEEAKLLLQQLSE-LESQLAE 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1369 REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggAEGELQALRAR-A 1447
Cdd:COG3206 231 ARAELAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIA--LRAQIAALRAQlQ 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1448 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEaAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1527
Cdd:COG3206 309 QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAE-LRRLEREVEVARELYESLLQRLEEARLAEALTVGN 387
|
...
gi 254675251 1528 VQV 1530
Cdd:COG3206 388 VRV 390
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
2231-2593 |
7.87e-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: 52.67 E-value: 7.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2231 LEEEAEKMKQVAEEAARLSVAAQEaaRLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARR 2310
Cdd:pfam02463 171 KKEALKKLIEETENLAELIIDLEE--LKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDYLKLNEERIDLLQELLRD 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2311 LQEDKEQMAQQLVEETQgfqrtLEAERQRQLEMSAEAERLKLrmaemsraqaraEEDAQRFRKQAEEIGEKLHRtELATQ 2390
Cdd:pfam02463 249 EQEEIESSKQEIEKEEE-----KLAQVLKENKEEEKEKKLQE------------EELKLLAKEEEELKSELLKL-ERRKV 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2391 EKVTLVQTLEIQRQQSDHDAERLREAIAELEREKeKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQR 2470
Cdd:pfam02463 311 DDEEKLKESEKEKKKAEKELKKEKEEIEELEKEL-KELEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSA 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2471 ERFIEQEKAKLEQLFQdevaKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVR-RKQEELQHLEQQRQQQE 2549
Cdd:pfam02463 390 AKLKEEELELKSEEEK----EAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTeEKEELEKQELKLLKDEL 465
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 254675251 2550 KLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAASTKALPNG 2593
Cdd:pfam02463 466 ELKKSEDLLKETQLVKLQEQLELLLSRQKLEERSQKESKARSGL 509
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
1746-2189 |
8.16e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1746 TSEKSKQRLEAEAGRFRELAEEAARLRALAEE-AKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1824
Cdd:COG4717 65 KPELNLKELKELEEELKEAEEKEEEYAELQEElEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAEL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1825 EAENERLRRLAEdeafQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAA 1904
Cdd:COG4717 145 PERLEELEERLE----ELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQE 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1905 GKAELELELGRIRSNAEDTMRSKEQAELEAArQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK-- 1982
Cdd:COG4717 221 ELEELEEELEQLENELEAAALEERLKEARLL-LLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKas 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1983 -VEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEA 2061
Cdd:COG4717 300 lGKEAEELQALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEA 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2062 REQAEREAAQSRKQVEEAERLKQsaeeqaqaqaQAQAAAEKLRKEAEQEAARRAQAEQAALKQK-QAADAEMEKHKKFAE 2140
Cdd:COG4717 380 GVEDEEELRAALEQAEEYQELKE----------ELEELEEQLEELLGELEELLEALDEEELEEElEELEEELEELEEELE 449
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 254675251 2141 QTLRQKAQVEQELTTLrlqleETDHQKSILDEELQRLKAEVTEAARQRS 2189
Cdd:COG4717 450 ELREELAELEAELEQL-----EEDGELAELLQELEELKAELRELAEEWA 493
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1317-1499 |
8.16e-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: 8.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1317 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRrmqeEVARREEAAVDAQQQKRSIQEELQHLRqsSEA 1396
Cdd:COG1579 16 DSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEK----EIKRLELEIEEVEARIKKYEEQLGNVR--NNK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1397 EIQAKAQQVEAAERSRMRIEEEIRVVRLQLETterqrggAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR 1476
Cdd:COG1579 90 EYEALQKEIESLKRRISDLEDEILELMERIEE-------LEEELAELEAELAELEAELEEKKAELDEELAELEAELEELE 162
|
170 180
....*....|....*....|...
gi 254675251 1477 QAEAELALRVKAEAEAAREKQRA 1499
Cdd:COG1579 163 AEREELAAKIPPELLALYERIRK 185
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2144-2429 |
1.01e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 52.27 E-value: 1.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2144 RQKAQVEQELTTLRLQLeeTDHQKSiLDEE-------------LQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKlkA 2210
Cdd:PRK04863 383 ARAEAAEEEVDELKSQL--ADYQQA-LDVQqtraiqyqqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATE--E 457
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2211 RIEAENRaliLRDKDNTQRFLEEEAEKMKQVAEEaarlsVAAQEAARLRQLAEEDLAQQRALAEKM---------LKEKM 2281
Cdd:PRK04863 458 LLSLEQK---LSVAQAAHSQFEQAYQLVRKIAGE-----VSRSEAWDVARELLRRLREQRHLAEQLqqlrmrlseLEQRL 529
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2282 QAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEEtqgfqrtLEAERQRQLEMSAEAERLKLRMAE-MSRA 2360
Cdd:PRK04863 530 RQQQRAERLLAEFCKRLGKNLDDEDELEQLQEELEARLESLSES-------VSEARERRMALRQQLEQLQARIQRlAARA 602
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 2361 QA--RAEEDAQRFRKQAEEigeklhrtELATQEKVT--LVQTLEIQRQQSDHDaERLREAIAELEREKEKLKQ 2429
Cdd:PRK04863 603 PAwlAAQDALARLREQSGE--------EFEDSQDVTeyMQQLLERERELTVER-DELAARKQALDEEIERLSQ 666
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1307-1422 |
1.07e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 51.49 E-value: 1.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1307 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQA-ELEAQELQRRMQEEVARREEAAVD---------A 1376
Cdd:pfam15709 383 QRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfRRKLQELQRKKQQEEAERAEAEKQrqkelemqlA 462
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 254675251 1377 QQQKR----SIQEELQHLRQSSEAEIQAkaqQVEAAERsRMRIEEEIRVV 1422
Cdd:pfam15709 463 EEQKRlmemAEEERLEYQRQKQEAEEKA---RLEAEER-RQKEEEAARLA 508
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2141-2534 |
1.08e-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: 52.04 E-value: 1.08e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2141 QTLRQKAQVE------QELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRS----QVEEELFSVRVQMEELGKLKA 2210
Cdd:pfam15921 445 QMERQMAAIQgkneslEKVSSLTAQLESTKEMLRKVVEELTAKKMTLESSERTVSdltaSLQEKERAIEATNAEITKLRS 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2211 RIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedLAQQRALAEKMLKEKMQAVQEAT 2288
Cdd:pfam15921 525 RVDLKLQELQhLKNEGDHLRNVQTECEALKlQMAEKDKVIEILRQQIENMTQL----VGQHGRTAGAMQVEKAQLEKEIN 600
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2289 RLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDA 2368
Cdd:pfam15921 601 DRRLELQEFKILKDKKDAKIRELEARVSDLELEKVKLVNAGSERLRAVKDIKQERDQLLNEVKTSRNELNSLSEDYEVLK 680
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2369 QRFRKQAEEIgeklhrtELATQEkvtlvqtLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQlkseEMQTVQQEQ 2448
Cdd:pfam15921 681 RNFRNKSEEM-------ETTTNK-------LKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMGMQ----KQITAKRGQ 742
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2449 IlqetQALQK--SFLSEKDSLLQRER-FIEQEKAKLEQLFQdEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRR-- 2523
Cdd:pfam15921 743 I----DALQSkiQFLEEAMTNANKEKhFLKEEKNKLSQELS-TVATEKNKMAGELEVLRSQERRLKEKVANMEVALDKas 817
|
410 420
....*....|....*....|.
gi 254675251 2524 ----------QREAEEGVRRK 2534
Cdd:pfam15921 818 lqfaecqdiiQRQEQESVRLK 838
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1675-1770 |
1.10e-05 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 51.88 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1675 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLlasKARAEEESRSTSEKSKQRL 1754
Cdd:PRK11448 146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQL---QEKAAETSQERKQKRKEIT 222
|
90
....*....|....*.
gi 254675251 1755 EAEAGRFrELAEEAAR 1770
Cdd:PRK11448 223 DQAAKRL-ELSEEETR 237
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1316-1744 |
1.11e-05 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 51.45 E-value: 1.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1316 AEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSE 1395
Cdd:COG5278 84 ARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLAL 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1396 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1475
Cdd:COG5278 164 ALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1476 RQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1555
Cdd:COG5278 244 LLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAA 323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1556 QLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAE 1635
Cdd:COG5278 324 ALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAA 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1636 REARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKR 1715
Cdd:COG5278 404 AEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALAALAAAAAA 483
|
410 420
....*....|....*....|....*....
gi 254675251 1716 QELEAELAKVRAEMEVLLASKARAEEESR 1744
Cdd:COG5278 484 LAEAEAAAALAAAAALSLALALAALLLAA 512
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3892-3930 |
1.12e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 45.01 E-value: 1.12e-05
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3892 FLEGTSCIAGVFVDATKERLSVYQAMKKGIIRPGTAFEL 3930
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2228-2491 |
1.23e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 50.69 E-value: 1.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2228 QRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQ 2307
Cdd:pfam13868 34 IKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQEE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2308 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAE-RLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTE 2386
Cdd:pfam13868 114 DQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDeRILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQ 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2387 LATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQIlQETQALQKSFLSEKDS 2466
Cdd:pfam13868 194 EKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEA-EREEEEFERMLRKQAE 272
|
250 260
....*....|....*....|....*
gi 254675251 2467 LLQRERFIEQEKAKLEQLFQDEVAK 2491
Cdd:pfam13868 273 DEEIEQEEAEKRRMKRLEHRRELEK 297
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1450-1660 |
1.26e-05 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 50.96 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1450 AEAQKRQAQEEAERLRRQVQDESQRKRQAEaELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQ 1529
Cdd:PRK09510 61 VEQYNRQQQQQKSAKRAEEQRKKKEQQQAE-ELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1530 VALETAQRSAEVElqSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEaerelerwqlKANEALRL 1609
Cdd:PRK09510 140 KAAAAAKAKAEAE--AKRAAAAAKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEA----------KKKAEAEA 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1610 RLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1660
Cdd:PRK09510 208 KKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAE 258
|
|
| CH_NAV2 |
cd21285 |
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ... |
9-108 |
1.62e-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: 47.27 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 9 DRVQKKTFTKWVNKHLIKA--QRHISDLYEDLRDGHNLISLLEVLSGDSLPREKG--RMRFHKLQNVQIALDYLRHRQVK 84
Cdd:cd21285 8 NGFDKQIYTDWANHYLAKSghKRLIKDLQQDVTDGVLLAEIIQVVANEKIEDINGcpKNRSQMIENIDACLSFLAAKGIN 87
|
90 100
....*....|....*....|....
gi 254675251 85 LVNIRNDDIADGNPKLTLGLIWTI 108
Cdd:cd21285 88 IQGLSAEEIRNGNLKAILGLFFSL 111
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
915-1528 |
1.70e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 51.19 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 915 DRLVAEREYGSCSRhyQQLLQSLEQGEQEESRCQRCISELKDIRLQLEACETrtvhrlrlplDKDPAREcaqRIAEQQKA 994
Cdd:PRK02224 223 ERYEEQREQARETR--DEADEVLEEHEERREELETLEAEIEDLRETIAETER----------EREELAE---EVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 995 ----QAEVEGLGKGVARLSAEAEKVLALPEpspaapTLRSELELTLGKLEQVRSlsaiyleklkTISLVIRSTQGAEEVL 1070
Cdd:PRK02224 288 leelEEERDDLLAEAGLDDADAEAVEARRE------ELEDRDEELRDRLEECRV----------AAQAHNEEAESLREDA 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1071 KTHEEQLKEAQAVPATLQ-ELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTql 1149
Cdd:PRK02224 352 DDLEERAEELREEAAELEsELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELREREA-- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1150 lerwqavlaqtdvrqrELEqlgrqlryyresadplsawlqdakrrqeqiqavpiANCQAAREQLRQEKALLEEierhgEK 1229
Cdd:PRK02224 430 ----------------ELE-----------------------------------ATLRTARERVEEAEALLEA-----GK 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1230 VEECQKFAKQ--YINAIKDYELQLITYKAQLEPVASpakkpkvqsgsesviqEYVDLRTRYSELTTLTSQyikfiSETLR 1307
Cdd:PRK02224 454 CPECGQPVEGspHVETIEEDRERVEELEAELEDLEE----------------EVEEVEERLERAEDLVEA-----EDRIE 512
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1308 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevARREEAAVDAQQQkrSIQEEL 1387
Cdd:PRK02224 513 RLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEE--AREEVAELNSKLA--ELKERI 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1388 QHLR--QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQAlrARAEEAEAQKRQAQEEAErlr 1465
Cdd:PRK02224 589 ESLEriRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERKRELEAEFDE--ARIEEAREDKERAEEYLE--- 663
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1466 rQVQDESQRKRQAEAELALRVKA------EAEAAREKQRAL----QALDELRLQAEEAERRLRQAEAE-RARQV 1528
Cdd:PRK02224 664 -QVEEKLDELREERDDLQAEIGAveneleELEELRERREALenrvEALEALYDEAEELESMYGDLRAElRQRNV 736
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
1616-1937 |
1.83e-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: 51.37 E-value: 1.83e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1616 VAQQKSLAQADA--EKQKEEAEREARRRGKAEEQAVRQRelaeQELEKQRQLAEGTAQQrlaAEQELIRLRAETEQGEQQ 1693
Cdd:NF012221 1535 VATSESSQQADAvsKHAKQDDAAQNALADKERAEADRQR----LEQEKQQQLAAISGSQ---SQLESTDQNALETNGQAQ 1607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1694 RQLLEEELARLQHEATAATQKRQELEAELAKV-------RAEMEVLLasKARAEEESRSTSEKSKQRLEAEAGRF----R 1762
Cdd:NF012221 1608 RDAILEESRAVTKELTTLAQGLDALDSQATYAgesgdqwRNPFAGGL--LDRVQEQLDDAKKISGKQLADAKQRHvdnqQ 1685
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1763 ELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQR 1842
Cdd:NF012221 1686 KVKDAVAKSEAGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQA 1765
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1843 RRLEEQAALHKADIEERlaqlRKASESELERQKGLVEDtlrqrrqVEEEIMALKVSFEKAAAGKaelelelgrirsNAED 1922
Cdd:NF012221 1766 QADAKGAKQDESDKPNR----QGAAGSGLSGKAYSVEG-------VAEPGSHINPDSPAAADGR------------FSEG 1822
|
330
....*....|....*
gi 254675251 1923 tMRSKEQAELEAARQ 1937
Cdd:NF012221 1823 -LTEQEQEALEGATN 1836
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
2146-2571 |
1.84e-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: 51.26 E-value: 1.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2146 KAQVEQELTTLRLQLEETDHQKSILDEELQRlkaEVTEAARQRSQVEEELFSVRVQMEELGKLKAriEAENRALILRDKD 2225
Cdd:pfam05483 203 RVQAENARLEMHFKLKEDHEKIQHLEEEYKK---EINDKEKQVSLLLIQITEKENKMKDLTFLLE--ESRDKANQLEEKT 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2226 NTQ-RFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ---- 2300
Cdd:pfam05483 278 KLQdENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEfeat 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2301 ----KELAQEQARRLQEDKEQMaQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEmsraqaraEEDAQRFRKQAE 2376
Cdd:pfam05483 358 tcslEELLRTEQQRLEKNEDQL-KIITMELQKKSSELEEMTKFKNNKEVELEELKKILAE--------DEKLLDEKKQFE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2377 EIGEKLHRTElatQEKVTLVQTleiqRQQSDHDAERLREAIAELE----REKEKLKQEAKLLQLKSEEMQTVQQEQILQE 2452
Cdd:pfam05483 429 KIAEELKGKE---QELIFLLQA----REKEIHDLEIQLTAIKTSEehylKEVEDLKTELEKEKLKNIELTAHCDKLLLEN 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2453 TQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQqqmeqEKQELMASMEEARRRQREAEEGVR 2532
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELES-----VREEFIQKGDEVKCKLDKSEENAR 576
|
410 420 430
....*....|....*....|....*....|....*....
gi 254675251 2533 RKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHR 2571
Cdd:pfam05483 577 SIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQ 615
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3058-3094 |
1.89e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 44.40 E-value: 1.89e-05
10 20 30
....*....|....*....|....*....|....*..
gi 254675251 3058 KLLSAEKAVTGYRDPYSGQSVSLFQALKKGLIPREQG 3094
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1914-2579 |
1.90e-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: 51.13 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1914 GRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEARRLRERA 1993
Cdd:pfam02463 142 GKIEIIAMMKPERRLEIEEEAAGSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLEL 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1994 EQEsaRQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSR 2073
Cdd:pfam02463 222 EEE--YLLYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELK 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2074 KQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKAQVEQEL 2153
Cdd:pfam02463 300 SELLKLERRKVDDEEKLKESEKEKKKAEKELKKEKEEIEELEKELKELEIKREAEEEEEEELEKLQEKLEQLEEELLAKK 379
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2154 TTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM--EELGKLKARIEAENRALILRDKDNTQRFL 2231
Cdd:pfam02463 380 KLESERLSSAAKLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEEleILEEEEESIELKQGKLTEEKEELEKQELK 459
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2232 EEEAEKM-KQVAEEAARLSVAA----QEAARLRQLAEEDLAQQRA--------LAEKMLKEKMQAVQEATRLKAEAELLQ 2298
Cdd:pfam02463 460 LLKDELElKKSEDLLKETQLVKlqeqLELLLSRQKLEERSQKESKarsglkvlLALIKDGVGGRIISAHGRLGDLGVAVE 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2299 QQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEI 2378
Cdd:pfam02463 540 NYKVAISTAVIVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPLKSIAVLEIDPILNLAQLDKATLEADEDD 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2379 GEKLHRTELATQEKVTLVQTLEIQRQQsdhdaeRLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQK 2458
Cdd:pfam02463 620 KRAKVVEGILKDTELTKLKESAKAKES------GLRKGVSLEEGLAEKSEVKASLSELTKELLEIQELQEKAESELAKEE 693
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2459 SFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEgvRRKQEEL 2538
Cdd:pfam02463 694 ILRRQLEIKKKEQREKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEE--EKSELSL 771
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 254675251 2539 QHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEI 2579
Cdd:pfam02463 772 KEKELAEEREKTEKLKVEEEKEEKLKAQEEELRALEEELKE 812
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2249-2454 |
1.97e-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: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2249 SVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQaVQEATRLKAEAELLQQQKelaQEQARRLQEDKEQMAQQLVEETQG 2328
Cdd:pfam15709 316 SEEDPSKALLEKREQEKASRDRLRAERAEMRRLE-VERKRREQEEQRRLQQEQ---LERAEKMREELELEQQRRFEEIRL 391
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2329 FQRTLEAERQRQlemsAEAERLKLRMAEMsrAQARAEEDAQRFRKQAEEIGEKLHRTELATQE------KVTLVQTLEIQ 2402
Cdd:pfam15709 392 RKQRLEEERQRQ----EEEERKQRLQLQA--AQERARQQQEEFRRKLQELQRKKQQEEAERAEaekqrqKELEMQLAEEQ 465
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 254675251 2403 RQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQ 2454
Cdd:pfam15709 466 KRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAARLALEEAMKQAQ 517
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1122-1527 |
2.05e-05 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 51.20 E-value: 2.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1122 QEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKrrqeqiqav 1201
Cdd:TIGR00606 694 QEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELRNKLQKVNRDIQRLK--------- 764
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1202 piancqaarEQLRQEKALLEEIERHGEKVEECQK---FAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVI 1278
Cdd:TIGR00606 765 ---------NDIEEQETLLGTIMPEEESAKVCLTdvtIMERFQMELKDVERKIAQQAAKLQGSDLDRTVQQVNQEKQEKQ 835
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1279 QEYVDLRTRYSELTTLTSQYIKFISETLRRMEE--EERLAEQQRAEERERLAEVEAALEKQRQ-LAEAHAQAKAQAELEA 1355
Cdd:TIGR00606 836 HELDTVVSKIELNRKLIQDQQEQIQHLKSKTNElkSEKLQIGTNLQRRQQFEEQLVELSTEVQsLIREIKDAKEQDSPLE 915
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1356 Q---ELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL------------------RQSSEAEIQAKAQQVEAAERSRMR 1414
Cdd:TIGR00606 916 TfleKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIhgymkdienkiqdgkddyLKQKETELNTVNAQLEECEKHQEK 995
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1415 IEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeAAR 1494
Cdd:TIGR00606 996 INEDMRLMRQDIDTQKIQERWLQDNLTLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQKLEENIDL-------IKR 1068
|
410 420 430
....*....|....*....|....*....|...
gi 254675251 1495 EKQRALQALDELRLQAEEAERRLRQAEAERARQ 1527
Cdd:TIGR00606 1069 NHVLALGRQKGYEKEIKHFKKELREPQFRDAEE 1101
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1600-1796 |
2.09e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 50.64 E-value: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1600 QLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRqlaegtaqQRLAAEQE 1679
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKKKAEERREAET--------ARAEAEAA 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1680 lirlrAETEQGEQQRQL-LEEELARLQHEATAATQKRQELEAEL-AKVRAEMEvllASKARAEEESRSTSEKSKQRLEAE 1757
Cdd:COG2268 268 -----YEIAEANAEREVqRQLEIAEREREIELQEKEAEREEAELeADVRKPAE---AEKQAAEAEAEAEAEAIRAKGLAE 339
|
170 180 190
....*....|....*....|....*....|....*....
gi 254675251 1758 AGRFRELAEEAARLRALAEEAKRQRQLAEedAARQRAEA 1796
Cdd:COG2268 340 AEGKRALAEAWNKLGDAAILLMLIEKLPE--IAEAAAKP 376
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2133-2577 |
2.10e-05 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 2.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2133 EKHKKFAEQTlRQKAQVEQELTTLRLQLEET-----DHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEEL-G 2206
Cdd:COG4913 259 ELAERYAAAR-ERLAELEYLRAALRLWFAQRrlellEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNgG 337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2207 KLKARIEAENRAL--ILRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQA 2283
Cdd:COG4913 338 DRLEQLEREIERLerELEERERRRARLEALLAALGlPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDL 417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2284 VQEATRLKAEAELLQQQK---ELAQEQARR-----LQEDKEQM---------------------------AQQLVEETQG 2328
Cdd:COG4913 418 RRELRELEAEIASLERRKsniPARLLALRDalaeaLGLDEAELpfvgelievrpeeerwrgaiervlggfALTLLVPPEH 497
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2329 FQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQS-- 2406
Cdd:COG4913 498 YAAALRWVNRLHLRGRLVYERVRTGLPDPERPRLDPDSLAGKLDFKPHPFRAWLEA-ELGRRFDYVCVDSPEELRRHPra 576
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2407 --------------DHDAERL-----------REAIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQKS 2459
Cdd:COG4913 577 itragqvkgngtrhEKDDRRRirsryvlgfdnRAKLAALEAELAELEEELAEAEERLEALEAELDalQERREALQRLAEY 656
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2460 FLSEKDsLLQRERFIEQEKAKLEQL--FQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEE 2537
Cdd:COG4913 657 SWDEID-VASAEREIAELEAELERLdaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDR 735
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 254675251 2538 LQHLEQQRQQQEKLLAEEnQRLRERLQRLEEEHRAALAHS 2577
Cdd:COG4913 736 LEAAEDLARLELRALLEE-RFAAALGDAVERELRENLEER 774
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1457-1714 |
2.11e-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: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1457 AQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELRLQAEEAERRLRQAEAERArqvqvALETAQ 1536
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELA-------ALKKEEKALLKQLAALERRIAALARRIRALEQELA-----ALEAEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1537 RSAEVELQSKRASFAEKTAQLERtlqeehvtvaQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEV 1616
Cdd:COG4942 86 AELEKEIAELRAELEAQKEELAE----------LLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1617 AQQKslaQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtaqqrlaAEQELIRLRAETEQGEQQRQL 1696
Cdd:COG4942 156 RADL---AELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLAR--------LEKELAELAAELAELQQEAEE 224
|
250
....*....|....*...
gi 254675251 1697 LEEELARLQHEATAATQK 1714
Cdd:COG4942 225 LEALIARLEAEAAAAAER 242
|
|
| MutS2 |
COG1193 |
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair]; |
1365-1530 |
2.11e-05 |
|
dsDNA-specific endonuclease/ATPase MutS2 [Replication, recombination and repair];
Pssm-ID: 440806 [Multi-domain] Cd Length: 784 Bit Score: 50.91 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1365 EVARR----EEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRggaegel 1440
Cdd:COG1193 490 EIARRlglpEEIIERARELLGEESIDVEKLIEELERERRELEEEREEAERLREELEKLREELEEKLEELEEEK------- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1441 QALRARA-EEAEAQKRQAQEEAERLRRQVQDEsqrkrqaeaelalrvKAEAEAAREKQRALQALDElRLQAEEAERRLRQ 1519
Cdd:COG1193 563 EEILEKArEEAEEILREARKEAEELIRELREA---------------QAEEEELKEARKKLEELKQ-ELEEKLEKPKKKA 626
|
170
....*....|.
gi 254675251 1520 AEAERARQVQV 1530
Cdd:COG1193 627 KPAKPPEELKV 637
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
2175-2459 |
2.25e-05 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 50.80 E-value: 2.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2175 QRLKAEVTEAARQRSQVEEELFSVRVQmeelgKLKARIEAENRALILRDKDNTQRFLEEEAE--KMKQVAEEAARLSVAA 2252
Cdd:pfam05667 220 QEWEEEWNSQGLASRLTPEEYRKRKRT-----KLLKRIAEQLRSAALAGTEATSGASRSAQDlaELLSSFSGSSTTDTGL 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2253 QEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATrlkaeaelLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQ 2330
Cdd:pfam05667 295 TKGSRFTHTEKLQFTNEAPAATSSPPTKVETEEELQ--------QQREEELEelQEQLEDLESSIQELEKEIKKLESSIK 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2331 RTLEAERQRQLEMSAEAE--RLKLRMAE--------MSRAQARAEEDAQRFRKQAEEIGEklHRT--------------- 2385
Cdd:pfam05667 367 QVEEELEELKEQNEELEKqyKVKKKTLDllpdaeenIAKLQALVDASAQRLVELAGQWEK--HRVplieeyralkeaksn 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2386 -ELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEA-------KLLQL-KSEEMQTVQQEQILQETQAL 2456
Cdd:pfam05667 445 kEDESQRKLEEIKELREKIKEVAEEAKQKEELYKQLVAEYERLPKDVsrsaytrRILEIvKNIKKQKEEITKILSDTKSL 524
|
...
gi 254675251 2457 QKS 2459
Cdd:pfam05667 525 QKE 527
|
|
| CH_PLS2_rpt1 |
cd21324 |
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
12-119 |
2.27e-05 |
|
first calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409173 Cd Length: 145 Bit Score: 47.31 E-value: 2.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 12 QKKTFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 78
Cdd:cd21324 25 EKYAFVNWINKalendpdckHVIPMNPNTDDLFKAVGDGIVLCKMINFSVPDTIDErtinKKKLTPFTIQENLNLALNSA 104
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254675251 79 RHRQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQISDIQV 119
Cdd:cd21324 105 SAIGCHVVNIGAEDLKEGKPYLVLGLLWQVIKIGLFADIEL 145
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2171-2390 |
2.30e-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: 2.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2171 DEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIlRDKDNTQRFLEEEAEKMKQVAEEAARLSV 2250
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQ-AEIDKLQAEIAEAEAEIEERREELGERAR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2251 AAQEAARLRQLAE--------EDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQM---A 2319
Cdd:COG3883 94 ALYRSGGSVSYLDvllgsesfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAkaeL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 2320 QQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQ 2390
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 244
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1345-1502 |
2.38e-05 |
|
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: 49.73 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1345 AQAKAQAEL-EAQELQRRMQEEVARReEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAER--SRMRIEEEIRV 1421
Cdd:pfam00529 59 ALDSAEAQLaKAQAQVARLQAELDRL-QALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIdlARRRVLAPIGG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1422 V-RLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKR-QAEAELALrvkAEAEAAREKQRA 1499
Cdd:pfam00529 138 IsRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIaEAEAELKL---AKLDLERTEIRA 214
|
...
gi 254675251 1500 LQA 1502
Cdd:pfam00529 215 PVD 217
|
|
| CH_PLS1_rpt3 |
cd21329 |
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called ... |
7-115 |
2.45e-05 |
|
third calponin homology (CH) domain found in plastin-1; Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. It contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409178 Cd Length: 118 Bit Score: 46.52 E-value: 2.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 7 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEV---------LSGDSLPREKGRMRfhKLQNVQIALDY 77
Cdd:cd21329 2 EGESSEERTFRNWMNS--LGVNPYVNHLYSDLCDALVIFQLYEMtrvpvdwghVNKPPYPALGGNMK--KIENCNYAVEL 77
|
90 100 110
....*....|....*....|....*....|....*....
gi 254675251 78 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 115
Cdd:cd21329 78 GKNKaKFSLVGIAGSDLNEGNKTLTLALIWQLMRRYTLN 116
|
|
| COG4995 |
COG4995 |
Uncharacterized conserved protein, contains CHAT domain [Function unknown]; |
2242-2692 |
2.47e-05 |
|
Uncharacterized conserved protein, contains CHAT domain [Function unknown];
Pssm-ID: 444019 [Multi-domain] Cd Length: 711 Bit Score: 50.74 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2242 AEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQ 2321
Cdd:COG4995 23 ALALLLLLAALAAAALLLLALLALLLALAAAAAAALAAAALALALLAAAALALLLLALALAALALALLAAALALALAAAA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2322 LVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEI 2401
Cdd:COG4995 103 LAALALLAALLALAAAAALLALLAALALLALLAALAAALAAAAAAALAAALAAAAAAAAAAALLALALALAAAALALLAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2402 QRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKL 2481
Cdd:COG4995 183 LLAALAAALAAAAAALALLLALLLLAALAAALAAALAALLLALLALAAALLALLLLALLALAAAAAALAAAAAALLALAA 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2482 EQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRE 2561
Cdd:COG4995 263 ALLLLAALAALAAAAAAAALAALALAAALALAAAALALALLLAAAAAAALAALALLLLAALLLLLAALALLALLLLLAAA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2562 RLQRLEEEHRAALAHSEIATTQAASTKALpngrdapdgpsvEAEPEYTFEGLRQKVPAQQLQEAGILSQEELQRLAQGHT 2641
Cdd:COG4995 343 ALLAAALAAALALAAALALALLAALLLLL------------AALLALLLEALLLLLLALLAALLLLAAALLALAAAQLLR 410
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 254675251 2642 TVAELTQREDVYRYLKGRSSIAGLLLKP--TNEKLSVYTALQRQLLSPGTALI 2692
Cdd:COG4995 411 LLLAALALLLALAAYAAARLALLALIEYiiLPDRLYAFVQLYQLLIAPIEAEL 463
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
1542-1937 |
2.47e-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: 50.07 E-value: 2.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1542 ELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKS 1621
Cdd:pfam19220 21 DLRSLKADFSQLIEPIEAILRELPQAKSRLLELEALLAQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1622 LAQADAEKQKEEAEREARRRGKAEEQ---AVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRaeteqgeQQRQLLE 1698
Cdd:pfam19220 101 EAEAAKEELRIELRDKTAQAEALERQlaaETEQNRALEEENKALREEAQAAEKALQRAEGELATAR-------ERLALLE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1699 EELARLQH-------EATAATQKRQELEAELAKVRAEMEVLLASKAraeeESRSTSEKSKQRLEAEAGRFR-ELAEEAAR 1770
Cdd:pfam19220 174 QENRRLQAlseeqaaELAELTRRLAELETQLDATRARLRALEGQLA----AEQAERERAEAQLEEAVEAHRaERASLRMK 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1771 LRALAEEAKRQRQLAEEDAARQRaeaervltEKLAAISEATRLKTEAEIALKEKEAENERLRrlAEDEAFQRRRLEEQAA 1850
Cdd:pfam19220 250 LEALTARAAATEQLLAEARNQLR--------DRDEAIRAAERRLKEASIERDTLERRLAGLE--ADLERRTQQFQEMQRA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1851 lhKADIEERLAQLRKA---SESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAG-KAELElelgrirsnAEDTMRS 1926
Cdd:pfam19220 320 --RAELEERAEMLTKAlaaKDAALERAEERIASLSDRIAELTKRFEVERAALEQANRRlKEELQ---------RERAERA 388
|
410
....*....|.
gi 254675251 1927 KEQAELEAARQ 1937
Cdd:pfam19220 389 LAQGALEIARE 399
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2128-2369 |
2.48e-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: 2.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2128 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGK 2207
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEI---EERREELGE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2208 LKARI----EAENRALILRDKDNTQRFLEEeAEKMKQVAEEAARLsVAAQEAARlrqlaeEDLAQQRALAEKMLKEKMQA 2283
Cdd:COG3883 91 RARALyrsgGSVSYLDVLLGSESFSDFLDR-LSALSKIADADADL-LEELKADK------AELEAKKAELEAKLAELEAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2284 VQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAR 2363
Cdd:COG3883 163 KAELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
....*.
gi 254675251 2364 AEEDAQ 2369
Cdd:COG3883 243 AASAAG 248
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2217-2413 |
2.57e-05 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 50.55 E-value: 2.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2217 RALILRDKDNTQRFLEEEAEKMKQVAEEAarLSVAAQEAARLRQLAEEDLAQQRalaekmlkEKMQAVQEatRLKAEAEL 2296
Cdd:PRK12704 30 EAKIKEAEEEAKRILEEAKKEAEAIKKEA--LLEAKEEIHKLRNEFEKELRERR--------NELQKLEK--RLLQKEEN 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2297 LQQQKELAQEQARRLQEDKEQMAQQL--VEETQGFQRTLEAERQRQLE----MSAEAERLKLrmaeMSRAQARAEEDAQR 2370
Cdd:PRK12704 98 LDRKLELLEKREEELEKKEKELEQKQqeLEKKEEELEELIEEQLQELErisgLTAEEAKEIL----LEKVEEEARHEAAV 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254675251 2371 FRKQAEEIGEklhrtELATQE-KVTLVQTleIQRQQSDHDAERL 2413
Cdd:PRK12704 174 LIKEIEEEAK-----EEADKKaKEILAQA--IQRCAADHVAETT 210
|
|
| WEMBL |
pfam05701 |
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required ... |
1323-1837 |
2.62e-05 |
|
Weak chloroplast movement under blue light; WEMBL consists of several plant proteins required for the chloroplast avoidance response under high intensity blue light. This avoidance response consists in the relocation of chloroplasts on the anticlinal side of exposed cells. Acts in association with PMI2 to maintain the velocity of chloroplast photo-relocation movement via the regulation of cp-actin filaments. Thus several member-sequences are described as "myosin heavy chain-like".
Pssm-ID: 461718 [Multi-domain] Cd Length: 562 Bit Score: 50.41 E-value: 2.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1323 ERERLAEVEAALEKQ-----RQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRsiQEELQHLRQ----- 1392
Cdd:pfam05701 35 ERRKLVELELEKVQEeipeyKKQSEAAEAAKAQVLEELESTKRLIEELKLNLERAQTEEAQAKQ--DSELAKLRVeemeq 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1393 --SSEAEIQAKAQqVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQd 1470
Cdd:pfam05701 113 giADEASVAAKAQ-LEVAKARHAAAVAELKSVKEELESLRKEYASLVSERDIAIKRAEEAVSASKEIEKTVEELTIELI- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1471 esqrkrQAEAELALRVKAEAEAAREKQRALQALDELRL-------QAEEAERRLRQaEAERARQVQVALETAqrsaEVEL 1543
Cdd:pfam05701 191 ------ATKESLESAHAAHLEAEEHRIGAALAREQDKLnwekelkQAEEELQRLNQ-QLLSAKDLKSKLETA----SALL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1544 QSKRASFAektAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERwqlKANEALRLRLQAEevaqqkSLa 1623
Cdd:pfam05701 260 LDLKAELA---AYMESKLKEEADGEGNEKKTSTSIQAALASAKKELEEVKANIEK---AKDEVNCLRVAAA------SL- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1624 QADAEKQKeeaerearrrgkAEEQAVRQRELA--------EQELEKQRQLAEgTAQQRLAAEQE--------LIRLRAET 1687
Cdd:pfam05701 327 RSELEKEK------------AELASLRQREGMasiavsslEAELNRTKSEIA-LVQAKEKEAREkmvelpkqLQQAAQEA 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1688 EQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK------ARAEEESRSTSEKSKQR-------L 1754
Cdd:pfam05701 394 EEAKSLAQAAREELRKAKEEAEQAKAAASTVESRLEAVLKEIEAAKASEklalaaIKALQESESSAESTNQEdsprgvtL 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1755 EAE-----AGRFRElAEEAARLRalAEEAKRQRQLAEEDAAR---QRAEAERVLTEKLAAISEATrlkTEAEIALKEKEA 1826
Cdd:pfam05701 474 SLEeyyelSKRAHE-AEELANKR--VAEAVSQIEEAKESELRsleKLEEVNREMEERKEALKIAL---EKAEKAKEGKLA 547
|
570
....*....|.
gi 254675251 1827 ENERLRRLAED 1837
Cdd:pfam05701 548 AEQELRKWRAE 558
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1351-1510 |
2.74e-05 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 49.66 E-value: 2.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1351 AELEAQELQRRMQEevARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEeeirvvRLQlette 1430
Cdd:COG1566 74 ARLDPTDLQAALAQ--AEAQLAAAEAQLARLEAELGAEAEIAAAEAQLAAAQAQLDLAQRELERYQ------ALY----- 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1431 RQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQrKRQAEAELalrvkAEAEAAREKqrALQALDELRLQA 1510
Cdd:COG1566 141 KKGAVSQQELDEARAALDAAQAQLEAAQAQLAQAQAGLREEEE-LAAAQAQV-----AQAEAALAQ--AELNLARTTIRA 212
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2131-2580 |
2.90e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 50.45 E-value: 2.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2131 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDE---ELQRLKAEVTEAARQRSQVEE---ELFSVRVQMEE 2204
Cdd:PRK03918 294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEEkeeRLEELKKKLKELEKRLEELEErheLYEEAKAKKEE 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2205 LGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSvaaQEAARL------------------RQLAEED- 2265
Cdd:PRK03918 374 LERLKKRLTGLTPEKLEKELEELEKAKEEIEEEISKITARIGELK---KEIKELkkaieelkkakgkcpvcgRELTEEHr 450
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2266 ---LAQQRALAEKMLKEKMQAVQEATRLKAEAE----LLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAE 2336
Cdd:PRK03918 451 kelLEEYTAELKRIEKELKEIEEKERKLRKELRelekVLKKESELIklKELAEQLKELEEKLKKYNLEELEKKAEEYEKL 530
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2337 RQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQtLEIQRQQSDHDAE-RLRE 2415
Cdd:PRK03918 531 KEKLIKLKGEIKSLKKELEKLEELKKKLAELEKKLDELEEELAELLKELEELGFESVEELE-ERLKELEPFYNEYlELKD 609
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2416 AIAELEREKEKLKQEAKLLQLKSEEMQTVQQ--EQILQETQALQKSFlSEKDSLLQRERFIEQEKakleqlfqdEVAKAK 2493
Cdd:PRK03918 610 AEKELEREEKELKKLEEELDKAFEELAETEKrlEELRKELEELEKKY-SEEEYEELREEYLELSR---------ELAGLR 679
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2494 qlreeqqrqqqqmeqekqelmASMEEARRRQREAEEGVR--RKQEELQHLEQQRQQQEKLLAEENQRLRERLQRL--EEE 2569
Cdd:PRK03918 680 ---------------------AELEELEKRREEIKKTLEklKEELEEREKAKKELEKLEKALERVEELREKVKKYkaLLK 738
|
490
....*....|.
gi 254675251 2570 HRAALAHSEIA 2580
Cdd:PRK03918 739 ERALSKVGEIA 749
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2123-2447 |
3.23e-05 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 50.15 E-value: 3.23e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2123 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQm 2202
Cdd:COG4717 164 ELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2203 EELGKLKARIEAENRALILRDKDNTQRFLEEE---------------AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLa 2267
Cdd:COG4717 243 ERLKEARLLLLIAAALLALLGLGGSLLSLILTiagvlflvlgllallFLLLAREKASLGKEAEELQALPALEELEEEEL- 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2268 qQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGfqrTLEAERQRQLEMSAEA 2347
Cdd:COG4717 322 -EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEELEQEIAALLAEAGV---EDEEELRAALEQAEEY 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2348 ERLKLRMAEMSR--AQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTL---------EIQRQQSDHDAERLREA 2416
Cdd:COG4717 398 QELKEELEELEEqlEELLGELEELLEALDEEELEEELEELEEELEELEEELEELreelaeleaELEQLEEDGELAELLQE 477
|
330 340 350
....*....|....*....|....*....|.
gi 254675251 2417 IAELEREKEKLKQEAKLLQLKSEEMQTVQQE 2447
Cdd:COG4717 478 LEELKAELRELAEEWAALKLALELLEEAREE 508
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1444-1630 |
3.26e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.95 E-value: 3.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1444 RARAEEAEAQ------KRQAQEEAerlRRQVQDESQRKRQAEAELALRVKAEAEAAREKQralQALDELRLQAEEAER-- 1515
Cdd:pfam15709 337 RLRAERAEMRrleverKRREQEEQ---RRLQQEQLERAEKMREELELEQQRRFEEIRLRK---QRLEEERQRQEEEERkq 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1516 -RLRQAEAERARQVQVA----LETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLreeaerraqqqaeaerare 1590
Cdd:pfam15709 411 rLQLQAAQERARQQQEEfrrkLQELQRKKQQEEAERAEAEKQRQKELEMQLAEEQKRLMEM------------------- 471
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 254675251 1591 EAERELERWQLKANEALRLRLQAEEVAQQKS----LAQADAEKQ 1630
Cdd:pfam15709 472 AEEERLEYQRQKQEAEEKARLEAEERRQKEEeaarLALEEAMKQ 515
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
2123-2332 |
3.28e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.83 E-value: 3.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2123 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAAR--QRSQVEEELFSVRV 2200
Cdd:COG3883 30 AELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARalYRSGGSVSYLDVLL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2201 QMEELGKLKARIEAENRaLILRDKDNTQRFLEEEAE---KMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKML 2277
Cdd:COG3883 110 GSESFSDFLDRLSALSK-IADADADLLEELKADKAEleaKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLS 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 2278 KEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRT 2332
Cdd:COG3883 189 AEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 243
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3314-3352 |
3.72e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 43.47 E-value: 3.72e-05
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3314 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTATLL 3352
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1681-1986 |
3.89e-05 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 49.95 E-value: 3.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1681 IRLRA-ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAK-----VRAEMEVLLASKARAEEE-SRSTSEKSKQR 1753
Cdd:PRK05035 438 IRAIEqEKKKAEEAKARFEARQARLEREKAAREARHKKAAEARAAkdkdaVAAALARVKAKKAAATQPiVIKAGARPDNS 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1754 LEAEAGRFRELAEEAARLRALAEEAKRQRQlAEEDAARQRAEAERvlteklaaiseatrlkteAEIALKEKEAENERLRR 1833
Cdd:PRK05035 518 AVIAAREARKAQARARQAEKQAAAAADPKK-AAVAAAIARAKAKK------------------AAQQAANAEAEEEVDPK 578
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1834 LAEDEAFQRRrleeqaalhkadieerlAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAlkvsfeKAAAGKAELELEL 1913
Cdd:PRK05035 579 KAAVAAAIAR-----------------AKAKKAAQQAASAEPEEQVAEVDPKKAAVAAAIA------RAKAKKAEQQANA 635
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1914 grIRSNAEDTMRSKEQAELEAARQRQLaaeeeqrrreaeeRVQRSLAAEEEAARQRKVALE-EVERLKAKVEEA 1986
Cdd:PRK05035 636 --EPEEPVDPRKAAVAAAIARAKARKA-------------AQQQANAEPEEAEDPKKAAVAaAIARAKAKKAAQ 694
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1283-1563 |
3.95e-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: 49.89 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1283 DLRTRYSELTTLTSQYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLaEAHAQAKAQAELEAQELQRRM 1362
Cdd:pfam07888 77 ELESRVAELKEELRQSREKHEELEEKYKELSASSEELSEEKDALLAQRAAHEARIREL-EEDIKTLTQRVLERETELERM 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1363 QEEVARREEAAVDAQQQKRSIQEELQHLRQ---SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGE 1439
Cdd:pfam07888 156 KERAKKAGAQRKEEEAERKQLQAKLQQTEEelrSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAENEAL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1440 LQALRARAEEAEAQKRQAQ------EEAERLRRQVQDESQRKRQAEAELALRVKAEAEAARE-KQRALQALDELRLQAE- 1511
Cdd:pfam07888 236 LEELRSLQERLNASERKVEglgeelSSMAAQRDRTQAELHQARLQAAQLTLQLADASLALREgRARWAQERETLQQSAEa 315
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 254675251 1512 EAERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQE 1563
Cdd:pfam07888 316 DKDRIEKLSAELQRLEERLQEERMEReKLEVELGREKDCNRVQLSESRRELQE 368
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4349-4386 |
3.98e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 3.98e-05
10 20 30
....*....|....*....|....*....|....*...
gi 254675251 4349 QRFLEVQYLTGGLIEPDTPGRVSLDEALQRGTVDARTA 4386
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3314-3349 |
4.09e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.09e-05
10 20 30
....*....|....*....|....*....|....*.
gi 254675251 3314 LLQGSGCLAGIYLEDSKEKVTIYEAMRRGLLRPSTA 3349
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1163-1521 |
4.18e-05 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 49.48 E-value: 4.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1163 RQRELEQLGRQlryyRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEKALLEEI----ERHGEKVEECQKFAK 1238
Cdd:pfam02029 12 RRRAREERRRQ----KEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTakreERRQKRLQEALERQK 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1239 QYINAIKDYElqlitykaqlEPVASPAKKPKVQSGSESVIQEYVDLR-TRYSELTTLTSQyikfiSETLRRMEEEERLAE 1317
Cdd:pfam02029 88 EFDPTIADEK----------ESVAERKENNEEEENSSWEKEEKRDSRlGRYKEEETEIRE-----KEYQENKWSTEVRQA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1318 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELE-AQELQRRMQEEVARREEAAVDAQqqkrsiqEELQHLRQSSEA 1396
Cdd:pfam02029 153 EEEGEEEEDKSEEAEEVPTENFAKEEVKDEKIKKEKKvKYESKVFLDQKRGHPEVKSQNGE-------EEVTKLKVTTKR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1397 EIQAKAQQVEAAERSRMRIEEEIRvvrlqLETTERQRGGAEG-ELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1475
Cdd:pfam02029 226 RQGGLSQSQEREEEAEVFLEAEQK-----LEELRRRRQEKESeEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRR 300
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 254675251 1476 RQAEAElalRVKAEAEaarEKQRALQALDelRLQAEEAERRLRQAE 1521
Cdd:pfam02029 301 KQEEAE---RKLREEE---EKRRMKEEIE--RRRAEAAEKRQKLPE 338
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1234-1565 |
4.25e-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: 50.01 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1234 QKFAKQYINAIKDYelqlitYKAQLEPVASPAKKPKvQSGSESVIQEYVDLRTRY-SELTTLTSQyikfiSETLRRMEEE 1312
Cdd:NF033838 53 NESQKEHAKEVESH------LEKILSEIQKSLDKRK-HTQNVALNKKLSDIKTEYlYELNVLKEK-----SEAELTSKTK 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1313 ERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ----------ELQRRMQE-EVARREEAAVDAQQQKR 1381
Cdd:NF033838 121 KELDAAFEQFKKDTLEPGKKVAEATKKVEEAEKKAKDQKEEDRRnyptntyktlELEIAESDvEVKKAELELVKEEAKEP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1382 SIQEELQHLRQSSEAEiQAKAQQVEAAERSRMRIEEEIR---------VVRLQLETTE------RQRGGAEGELQALRAR 1446
Cdd:NF033838 201 RDEEKIKQAKAKVESK-KAEATRLEKIKTDREKAEEEAKrradaklkeAVEKNVATSEqdkpkrRAKRGVLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1447 AEEAEAQKRQAQEEAerlrrqVQDESQR--KRQAEAElalRVKAEAEAAREKQR-------ALQALDELRLQAEEAERRL 1517
Cdd:NF033838 280 ENDAKSSDSSVGEET------LPSPSLKpeKKVAEAE---KKVEEAKKKAKDQKeedrrnyPTNTYKTLELEIAESDVKV 350
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1518 RQAEA----ERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEH 1565
Cdd:NF033838 351 KEAELelvkEEAKEPRNEEKIKQAKAKVESKKAEATRLEKIKTDRKKAEEEA 402
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1302-1507 |
4.28e-05 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 47.90 E-value: 4.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1302 ISETLRRMEEEERLAEQQRAEERERLAEVEAALekqrqlaeahAQAKAQAELEAQELqRRMQEEVARREEAAVDAQQQKR 1381
Cdd:COG1842 14 INALLDKAEDPEKMLDQAIRDMEEDLVEARQAL----------AQVIANQKRLERQL-EELEAEAEKWEEKARLALEKGR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1382 siqeelQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKR------ 1455
Cdd:COG1842 83 ------EDLAREALERKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKDTLKARAKAAKAQEKvneals 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1456 -----QAQEEAERLRRQVQDESQRKrQAEAELALR--VKAEAEAAREKQRALQALDELR 1507
Cdd:COG1842 157 gidsdDATSALERMEEKIEEMEARA-EAAAELAAGdsLDDELAELEADSEVEDELAALK 214
|
|
| CCDC154 |
pfam15450 |
Coiled-coil domain-containing protein 154; CCDC154 is an osteopetrosis-related protein that ... |
1283-1562 |
4.29e-05 |
|
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: 49.83 E-value: 4.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1283 DLRTRYSELTTLTSQYIKFISEtlRRMEEEERLAEQQRAEERERLAEVEAALEKQRQL-----AEAHAQ-AKAQAELE-A 1355
Cdd:pfam15450 226 ELEGRWQKLQELTEERLRALQG--QREQEEGHLLEQCRGLDAAVVQLTKFVRQNQVSLnrvllAEQKARdAKGQLEESqA 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1356 QELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVE------AAERSRMRIEEEirVVRLQLETT 1429
Cdd:pfam15450 304 GELASYVQENLEAVQLAGELAQQETQGALELLQEKSQVLEGSVAELVRQVKdlsdhfLALSWRLDLQEQ--TLGLKLSEA 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1430 ERQRGGAEGE-LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqaldelrl 1508
Cdd:pfam15450 382 KKEWEGAERKsLEDLAQWQKEVAAHLREVQEKVDSLPRQIEAVSDKCVLHKSDSDLKISAEGKAREFEVEA--------- 452
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1509 qaeeaerrLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQ 1562
Cdd:pfam15450 453 --------MRQELAALLSSVQLLKEGNPGRKIAEIQGKLATFQNQIIKLENSIQ 498
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1332-1512 |
4.36e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 48.00 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1332 AALEKQRQLAEAHAQAKAQAELEAQelQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqssEAEIQAKAQQVEAAERS 1411
Cdd:COG1579 1 AMPEDLRALLDLQELDSELDRLEHR--LKELPAELAELEDELAALEARLEAAKTELEDL----EKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1412 RMRIEEEIRVVRlqletTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1491
Cdd:COG1579 75 IKKYEEQLGNVR-----NNKEYEALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
|
170 180
....*....|....*....|.
gi 254675251 1492 AAREKQRALQALDELRLQAEE 1512
Cdd:COG1579 150 ELAELEAELEELEAEREELAA 170
|
|
| CH_PARVA_B_rpt2 |
cd21306 |
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta ... |
5-112 |
4.36e-05 |
|
second calponin homology (CH) domain found in the alpha/beta parvin subfamily; The alpha/beta parvin subfamily includes alpha-parvin and beta-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Members of this subfamily contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409155 Cd Length: 121 Bit Score: 45.87 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 5 PDERDRVqKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMRF----HKLQNVQIALDYLRH 80
Cdd:cd21306 11 PDKLNVV-KKSLITFVNKHLNKLNLEVTDLDTQFHDGVYLVLLMGLLEGYFVPLHSFHLTPtsfeQKVHNVQFAFELMQD 89
|
90 100 110
....*....|....*....|....*....|..
gi 254675251 81 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHF 112
Cdd:cd21306 90 AGLPKPKARPEDIVNLDLKSTLRVLYNLFTKY 121
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
2234-2393 |
4.37e-05 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 49.49 E-value: 4.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2234 EAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEAtrlKAEAELLQQQKELAQEQARRLQE 2313
Cdd:COG2268 196 EIIRDARIAEAEAERETEIAIAQANREAEEAELEQEREIETARIAEAEAELAKK---KAEERREAETARAEAEAAYEIAE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2314 DKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAqrfrkQAEEIGEKLHRTELATQEKV 2393
Cdd:COG2268 273 ANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAEAEA-----EAEAIRAKGLAEAEGKRALA 347
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1368-1721 |
4.41e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 49.13 E-value: 4.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1368 RREEAAVDAQQQKRSIQEELQHLRQsseaEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARA 1447
Cdd:COG4372 21 KTGILIAALSEQLRKALFELDKLQE----ELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1448 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1527
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1528 VQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEAL 1607
Cdd:COG4372 177 SEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1608 RLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAET 1687
Cdd:COG4372 257 LKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLELALAILL 336
|
330 340 350
....*....|....*....|....*....|....
gi 254675251 1688 EQGEQQRQLLEEELARLQHEATAATQKRQELEAE 1721
Cdd:COG4372 337 AELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4100-4128 |
4.52e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 43.24 E-value: 4.52e-05
10 20
....*....|....*....|....*....
gi 254675251 4100 VRKRRVVIVDPETGKEMSVYEAYRKGLID 4128
Cdd:smart00250 6 AQSAIGGIIDPETGQKLSVEEALRRGLID 34
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2216-2578 |
4.74e-05 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 49.95 E-value: 4.74e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2216 NRALILRDKDNTQRflEEEAEKMKQVAEEAARLSVAAQEAARLrQLAEEDLAQQRALAEKMLKEKMQAVQEATRL----- 2290
Cdd:COG3096 278 NERRELSERALELR--RELFGARRQLAEEQYRLVEMARELEEL-SARESDLEQDYQAASDHLNLVQTALRQQEKIeryqe 354
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2291 -------KAEA-----ELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLkLRMAE 2356
Cdd:COG3096 355 dleelteRLEEqeevvEEAAEQLAEAEARLEAAEEEVDSLKSQLADYQQALdvQQTRAIQYQQAVQALEKARAL-CGLPD 433
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2357 MSraQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVqtlEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQL 2436
Cdd:COG3096 434 LT--PENAEDYLAAFRAKEQQATEEV----LELEQKLSVA---DAARRQFEKAYELVCKIAGEVERSQAWQTARELLRRY 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2437 KSEEMQTVQQEQILQEtqalqksfLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEqqrqqqqmeqekqelmas 2516
Cdd:COG3096 505 RSQQALAQRLQQLRAQ--------LAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELEEL------------------ 558
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 2517 MEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQR------LRERLQRLEEEHRAALAHSE 2578
Cdd:COG3096 559 LAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARapawlaAQDALERLREQSGEALADSQ 626
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1598-1784 |
4.79e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1598 RWQLKANEALRLRLQAE----EVAQQKSLAQADAEKQKEEaerearrrgKAEEQAVRQRELAEQELEKQRQLAEGTAQQR 1673
Cdd:pfam15709 335 RDRLRAERAEMRRLEVErkrrEQEEQRRLQQEQLERAEKM---------REELELEQQRRFEEIRLRKQRLEEERQRQEE 405
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1674 LAAEQELiRLRAETEQGEQQRQLLEEELARLQHE--------ATAATQKRQELEAELA---KVRAEMevllASKARAEEE 1742
Cdd:pfam15709 406 EERKQRL-QLQAAQERARQQQEEFRRKLQELQRKkqqeeaerAEAEKQRQKELEMQLAeeqKRLMEM----AEEERLEYQ 480
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 254675251 1743 SRSTSEKSKQRLEAEAGRFRElaEEAARLraLAEEAKRQRQL 1784
Cdd:pfam15709 481 RQKQEAEEKARLEAEERRQKE--EEAARL--ALEEAMKQAQE 518
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
1307-1480 |
4.79e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.56 E-value: 4.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1307 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQaeleaQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1386
Cdd:pfam15709 353 KRREQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRL-----EEERQRQEEEERKQRLQLQAAQERARQQQEE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1387 LQHLRQsseaEIQAKAQQVE---AAERSRMRIEEEIRVVrlqlETTERQRGGAEGELQALRARAEEAEAQKRQAQEEaer 1463
Cdd:pfam15709 428 FRRKLQ----ELQRKKQQEEaerAEAEKQRQKELEMQLA----EEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEE--- 496
|
170
....*....|....*..
gi 254675251 1464 lRRQVQDESQRKRQAEA 1480
Cdd:pfam15709 497 -RRQKEEEAARLALEEA 512
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1335-1555 |
5.06e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1335 EKQRQLAEAHAQ-AKAQAELEAqeLQR---RMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAER 1410
Cdd:COG3883 20 AKQKELSELQAElEAAQAELDA--LQAeleELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1411 SRMR------------IEEEIRvvrlQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQA 1478
Cdd:COG3883 98 SGGSvsyldvllgsesFSDFLD----RLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAEL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1479 EAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTA 1555
Cdd:COG3883 174 EAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAG 250
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1441-1679 |
5.24e-05 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 49.63 E-value: 5.24e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1441 QALRARAEEAEAQKRQAQEEAERLRRQVqDESQRKRQA--EAELALRVKAEAEAAREKQRALQA-LDELRLQAEEAERRL 1517
Cdd:COG3206 164 QNLELRREEARKALEFLEEQLPELRKEL-EEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESqLAEARAELAEAEARL 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1518 RQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREeaerraqqqaeaerareeaerele 1597
Cdd:COG3206 243 AALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRA------------------------ 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1598 rwQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELA--EQELEKQRQLAEGTAQQRLA 1675
Cdd:COG3206 299 --QIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRrlEREVEVARELYESLLQRLEE 376
|
....
gi 254675251 1676 AEQE 1679
Cdd:COG3206 377 ARLA 380
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
2131-2541 |
5.27e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.68 E-value: 5.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2131 EMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKA------EVTEAARQRSQVEEELFSVRVQMEE 2204
Cdd:PRK03918 232 ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvkelkELKEKAEEYIKLSEFYEEYLDELRE 311
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2205 LGKLKARIEAENRALI--LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEdlaqqralAEKMLKEKmq 2282
Cdd:PRK03918 312 IEKRLSRLEEEINGIEerIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEE--------LERLKKRL-- 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2283 AVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQ-----RQLEMSAEAERLKLRMAEM 2357
Cdd:PRK03918 382 TGLTPEKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcpvcgRELTEEHRKELLEEYTAEL 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2358 SRAQ---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKL-KQEAKL 2433
Cdd:PRK03918 462 KRIEkelKEIEEKERKLRKELRELEKVLKKESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLiKLKGEI 541
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2434 LQLKSE----------------EMQTVQQE--------------------QILQETQALQKSFLSEKDS---LLQRERFI 2474
Cdd:PRK03918 542 KSLKKElekleelkkklaelekKLDELEEElaellkeleelgfesveeleERLKELEPFYNEYLELKDAekeLEREEKEL 621
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 2475 EQEKAKLEQLFqDEVAKAKQLREEQQRQQQQMEQEKQELmaSMEEARRRQREAEEGVRRKQEELQHL 2541
Cdd:PRK03918 622 KKLEEELDKAF-EELAETEKRLEELRKELEELEKKYSEE--EYEELREEYLELSRELAGLRAELEEL 685
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
1393-1628 |
5.76e-05 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 49.06 E-value: 5.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1393 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQD-- 1470
Cdd:COG3883 13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGEra 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1471 -ESQRKRQAEAELAL------------RVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAErARQVQVALETAQR 1537
Cdd:COG3883 93 rALYRSGGSVSYLDVllgsesfsdfldRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAE-LEALKAELEAAKA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1538 saevELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVA 1617
Cdd:COG3883 172 ----ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAA 247
|
250
....*....|.
gi 254675251 1618 QQKSLAQADAE 1628
Cdd:COG3883 248 GAGAAGAAGAA 258
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1427-1678 |
6.00e-05 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 48.69 E-value: 6.00e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1427 ETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDEL 1506
Cdd:TIGR02794 25 HSVKPEPGGGAEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1507 RlQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEhvtvaqlreEAERRAQQQAEAE 1586
Cdd:TIGR02794 105 K-QAEQAAKQAEEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAA---------AEAKKKAEEAKKK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1587 RAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKeeaEREARRRGKAEEQAVRQRELAEQELEKQRQla 1666
Cdd:TIGR02794 175 AEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAA---AAAAEAERKADEAELGDIFGLASGSNAEKQ-- 249
|
250
....*....|..
gi 254675251 1667 EGTAQQRLAAEQ 1678
Cdd:TIGR02794 250 GGARGAAAGSEV 261
|
|
| DUF4670 |
pfam15709 |
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ... |
2222-2377 |
6.03e-05 |
|
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.
Pssm-ID: 464815 [Multi-domain] Cd Length: 522 Bit Score: 49.18 E-value: 6.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2222 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEA---ELLQ 2298
Cdd:pfam15709 355 REQEEQRRLQQEQLERAEKMREELELEQQRRFEEIRLRKQRLEEERQRQEEEERKQRLQLQAAQERARQQQEEfrrKLQE 434
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2299 QQKELAQEQARRLQEDKE---QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRaqaRAEEDAQRF---- 2371
Cdd:pfam15709 435 LQRKKQQEEAERAEAEKQrqkELEMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERR---QKEEEAARLalee 511
|
....*..
gi 254675251 2372 -RKQAEE 2377
Cdd:pfam15709 512 aMKQAQE 518
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
1899-2458 |
6.19e-05 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 49.29 E-value: 6.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1899 FEKAAAGKAELELELGRIRSNAEDTMRSKEQAElEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKvalEEVER 1978
Cdd:PRK03918 160 YENAYKNLGEVIKEIKRRIERLEKFIKRTENIE-ELIKEKEKELEEVLREINEISSELPELREELEKLEKEV---KELEE 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1979 LKAKVEEARRLRERAEQEsARQLQLAQEAAQKRLqAEEKAHAFVVQQREEELQQTLQQEQNMLdRLRSEAEAARRAAEEA 2058
Cdd:PRK03918 236 LKEEIEELEKELESLEGS-KRKLEEKIRELEERI-EELKKEIEELEEKVKELKELKEKAEEYI-KLSEFYEEYLDELREI 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2059 EEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKF 2138
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTPEKLEKE 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2139 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLK----------AEVTEAARQR--SQVEEELFSVRVQMEELG 2206
Cdd:PRK03918 393 LEELEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKkakgkcpvcgRELTEEHRKEllEEYTAELKRIEKELKEIE 472
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2207 KLKARIEAENRAL-ILRDKDNTQRFLEEEAEKMKQVAEE-----AARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2280
Cdd:PRK03918 473 EKERKLRKELRELeKVLKKESELIKLKELAEQLKELEEKlkkynLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLE 552
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2281 MQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQlEMSAEAERLKLRMAEMSRA 2360
Cdd:PRK03918 553 ELKKKLAELEKKLDELEEELAELLKELEELGFESVEELEERLKELEPFYNEYLELKDAEK-ELEREEKELKKLEEELDKA 631
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2361 Q---ARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTL------------VQTLEIQRQQSDHDAERLREAIAELEREKE 2425
Cdd:PRK03918 632 FeelAETEKRLEELRKELEELEKKYSEEEYEELREEYLelsrelaglraeLEELEKRREEIKKTLEKLKEELEEREKAKK 711
|
570 580 590
....*....|....*....|....*....|...
gi 254675251 2426 KLKQEAKLLQLKSEEMQTVQQEQILQETQALQK 2458
Cdd:PRK03918 712 ELEKLEKALERVEELREKVKKYKALLKERALSK 744
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1628-1985 |
6.30e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 48.75 E-value: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1628 EKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1707
Cdd:COG4372 9 GKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1708 ATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEE-AKRQRQLAE 1786
Cdd:COG4372 89 LQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQlESLQEELAA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1787 EDAARQR---AEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQL 1863
Cdd:COG4372 169 LEQELQAlseAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1864 RKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAE 1943
Cdd:COG4372 249 EELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKL 328
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 254675251 1944 EEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEE 1985
Cdd:COG4372 329 ELALAILLAELADLLQLLLVGLLDNDVLELLSKGAEAGVADG 370
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1746-2025 |
6.47e-05 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 48.38 E-value: 6.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1746 TSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEA-EIALKEK 1824
Cdd:pfam13868 21 NKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEyEEKLQER 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1825 EAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKvsfEKAAA 1904
Cdd:pfam13868 101 EQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEERE---AEREE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1905 GKAELELELGRIRSNAEDTMRSKEQAElEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK-V 1983
Cdd:pfam13868 178 IEEEKEREIARLRAQQEKAQDEKAERD-ELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEeA 256
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 254675251 1984 EEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQ 2025
Cdd:pfam13868 257 EREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQ 298
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1408-1527 |
6.66e-05 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 46.19 E-value: 6.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1408 AERSRMRIEEEIRVVRLQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvK 1487
Cdd:pfam05672 9 AEEAARILAEKRRQAREQREREEQER-----LEKEEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQR---K 80
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 254675251 1488 AEAEAAREKQRALQALDELRLQAEEAERRLRQaEAERARQ 1527
Cdd:pfam05672 81 AEEEAEEREQREQEEQERLQKQKEEAEAKARE-EAERQRQ 119
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1331-1831 |
7.07e-05 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 49.28 E-value: 7.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1331 EAALEKQRQLAEAhAQAKAQAELeAQELQRRMQEeVARREEAAVDAQQQKRSIQE---ELQHLRQSSEAEiqakaqqvea 1407
Cdd:PRK10929 25 EKQITQELEQAKA-AKTPAQAEI-VEALQSALNW-LEERKGSLERAKQYQQVIDNfpkLSAELRQQLNNE---------- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1408 aersrmriEEEIRVVRLQLETterqrggAEGELQALRARAEEAEaQKRQAQEEAERLRRQVQDESQ-RKRQAEAELALrv 1486
Cdd:PRK10929 92 --------RDEPRSVPPNMST-------DALEQEILQVSSQLLE-KSRQAQQEQDRAREISDSLSQlPQQQTEARRQL-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1487 kAEAEaarekqRALQALDELRLQAEEAERRLRQAEAerarqvqvaletAQRSAEVElqskrasfaektaqlertlqeehv 1566
Cdd:PRK10929 154 -NEIE------RRLQTLGTPNTPLAQAQLTALQAES------------AALKALVD------------------------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1567 tvaqlreeaerraqqqaeaerareeaerELERWQLKAN---EALRLRLqaeEVAQQKSlAQADAEKQKEeaerearrrgK 1643
Cdd:PRK10929 191 ----------------------------ELELAQLSANnrqELARLRS---ELAKKRS-QQLDAYLQAL----------R 228
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1644 AEEQAVRQRElAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLeEELARLQHEATAATQK-RQELEA-- 1720
Cdd:PRK10929 229 NQLNSQRQRE-AERALESTELLAEQSGDLPKSIVAQFKINRELSQALNQQAQRM-DLIASQQRQAASQTLQvRQALNTlr 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1721 ----ELAKVRAEMEVLLASKARAEEESRStsekskQRLEAEAGRFRelaeeAARLR--ALAEEAKRQRQLAEEDAARQRA 1794
Cdd:PRK10929 307 eqsqWLGVSNALGEALRAQVARLPEMPKP------QQLDTEMAQLR-----VQRLRyeDLLNKQPQLRQIRQADGQPLTA 375
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1795 EAERVLTEKLAA---------------ISEATRLK---TEAEIALKE-KEAENERL 1831
Cdd:PRK10929 376 EQNRILDAQLRTqrellnsllsggdtlILELTKLKvanSQLEDALKEvNEATHRYL 431
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1503-1969 |
7.34e-05 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 49.25 E-value: 7.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1503 LDELRLQAEEAERRLRQAEAERARQVQVALETAQR-SAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQ 1581
Cdd:COG3903 470 LETVREYAAERLAEAGERAAARRRHADYYLALAERaAAELRGPDQLAWLARLDAEHDNLRAALRWALAHGDAELALRLAA 549
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1582 QAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEkqkeeaeREARRRGKAEEQAVRQRELAEQELEK 1661
Cdd:COG3903 550 ALAPFWFLRGLLREGRRWLERALAAAGEAAAALAAAAALAAAAAAAR-------AAAAAAAAAAAAAAAAAAAAAAAAAA 622
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1662 QRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEE 1741
Cdd:COG3903 623 LLLLAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAA 702
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1742 ESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIAL 1821
Cdd:COG3903 703 LAAAAAAALAAAAAAAAAAAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAA 782
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1822 KEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEK 1901
Cdd:COG3903 783 AAALAAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAA 862
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1902 AAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQR 1969
Cdd:COG3903 863 AAAAAAALAAAAAAAAAAAAALLAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALAAAAAAAAAAAAA 930
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
1429-2031 |
7.73e-05 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 49.03 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1429 TERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQ--VQDESQRKRQA--EAELALRVKAEAEAARE--------- 1495
Cdd:PRK10246 214 TPEQVQSLTASLQVLTDEEKQLLTAQQQQQQSLNWLTRLdeLQQEASRRQQAlqQALAAEEKAQPQLAALSlaqparqlr 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1496 -----KQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQrsaevELQSKRASFAEKTAQLERTL---QEEHVT 1567
Cdd:PRK10246 294 phwerIQEQSAALAHTRQQIEEVNTRLQSTMALRARIRHHAAKQSA-----ELQAQQQSLNTWLAEHDRFRqwnNELAGW 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1568 VAQLREEAERRAQQQAEAERAREEaereleRWQLKANEALRLRLQAEEVAQqkslAQADAEKQKEEAEREARRRGKAEEQ 1647
Cdd:PRK10246 369 RAQFSQQTSDREQLRQWQQQLTHA------EQKLNALPAITLTLTADEVAA----ALAQHAEQRPLRQRLVALHGQIVPQ 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1648 AVRQRELAE------QELEKQRQLAEGTAQQRLAAEQELIRLRAETEQgEQQRQLLEEELARLQ------------HEAT 1709
Cdd:PRK10246 439 QKRLAQLQVaiqnvtQEQTQRNAALNEMRQRYKEKTQQLADVKTICEQ-EARIKDLEAQRAQLQagqpcplcgstsHPAV 517
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1710 AATQ---------KRQELEAELAK-------VRAEMEVLLASKARAEEESRSTSEKSK------QRLEAEAGRFRELAEE 1767
Cdd:PRK10246 518 EAYQalepgvnqsRLDALEKEVKKlgeegaaLRGQLDALTKQLQRDESEAQSLRQEEQaltqqwQAVCASLNITLQPQDD 597
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1768 AARLRALAEEAKRQ-RQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIA-----LKEKEAENERLRRLAEDEAFQ 1841
Cdd:PRK10246 598 IQPWLDAQEEHERQlRLLSQRHELQGQIAAHNQQIIQYQQQIEQRQQQLLTALAgyaltLPQEDEEASWLATRQQEAQSW 677
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1842 RRRLEEQAALhkadiEERLAQLRKASESELERQKGLVED---TLRQRRQVEEEIMALKvsfEKAAAGKAELELELGRIrs 1918
Cdd:PRK10246 678 QQRQNELTAL-----QNRIQQLTPLLETLPQSDDLPHSEetvALDNWRQVHEQCLSLH---SQLQTLQQQDVLEAQRL-- 747
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1919 naedtmrSKEQAELEAARQrqlaaeeeqrrREAEERVQRSLAA-EEEAARQRKVALEEveRLKAKVEEARRLRERAEQES 1997
Cdd:PRK10246 748 -------QKAQAQFDTALQ-----------ASVFDDQQAFLAAlLDEETLTQLEQLKQ--NLENQRQQAQTLVTQTAQAL 807
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 254675251 1998 ARQLQLAQEAAQKRLQAE--EKAHAFVVQQ------REEELQ 2031
Cdd:PRK10246 808 AQHQQHRPDGLDLTVTVEqiQQELAQLAQQlrenttRQGEIR 849
|
|
| MARTX_Nterm |
NF012221 |
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ... |
2122-2340 |
8.10e-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: 49.45 E-value: 8.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2122 LKQKQAA-DAEMEKHKKFAE-QTLRQ-KAQVEQELTTLRLQLEETDHQksildeelqrlkAEVTEAARQRSQVEEELFSV 2198
Cdd:NF012221 1551 AKQDDAAqNALADKERAEADrQRLEQeKQQQLAAISGSQSQLESTDQN------------ALETNGQAQRDAILEESRAV 1618
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2199 RVQMEELGKlkaRIEA----------------ENRALILRDK-----DNTQRFLEEEAEKMKQ--------VAEEAARLS 2249
Cdd:NF012221 1619 TKELTTLAQ---GLDAldsqatyagesgdqwrNPFAGGLLDRvqeqlDDAKKISGKQLADAKQrhvdnqqkVKDAVAKSE 1695
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2250 VAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKEQMAQQlveETQGF 2329
Cdd:NF012221 1696 AGVAQGEQNQANAEQDIDDAKADAEKRKDDALAKQNEAQQAESDANAAANDAQSRGEQDASAAENKANQAQA---DAKGA 1772
|
250
....*....|.
gi 254675251 2330 QRTLEAERQRQ 2340
Cdd:NF012221 1773 KQDESDKPNRQ 1783
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3761-3797 |
8.22e-05 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.47 E-value: 8.22e-05
10 20 30
....*....|....*....|....*....|....*..
gi 254675251 3761 LRLLDAQLATGGIVDPRLGFHLPLEVAYQRGYLNKDT 3797
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1311-2029 |
8.89e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 49.19 E-value: 8.89e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1311 EEERLAEQQR----AEERERLAEVEAALEKQRQLAEAHaQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1386
Cdd:PRK04863 299 RRQLAAEQYRlvemARELAELNEAESDLEQDYQAASDH-LNLVQTALRQQEKIERYQADLEELEERLEEQNEVVEEADEQ 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1387 LQHLR-QSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQ-----LETTERQRGGAEGELQALRARAEEAEAQKRQAQEE 1460
Cdd:PRK04863 378 QEENEaRAEAAEEEVDELKSQLADYQQALDVQQTRAIQYQqavqaLERAKQLCGLPDLTADNAEDWLEEFQAKEQEATEE 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1461 AERLRRQVQDESQRKRQAE--AELALRVKAEAEAAREKQRALQALDELRLQAEEAER----RLRQAEAERARQVQVALET 1534
Cdd:PRK04863 458 LLSLEQKLSVAQAAHSQFEqaYQLVRKIAGEVSRSEAWDVARELLRRLREQRHLAEQlqqlRMRLSELEQRLRQQQRAER 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1535 AQRSAEVELQSK--RASFAEK-TAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWqLKANEALRlRL 1611
Cdd:PRK04863 538 LLAEFCKRLGKNldDEDELEQlQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARAPAW-LAAQDALA-RL 615
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1612 QAEEVAQQKSLAQADAEKQKEEAERearrrgKAEEQAVRQRELAEQELEKQ-RQLaegtaQQRLAAEQELIRLRAETEQG 1690
Cdd:PRK04863 616 REQSGEEFEDSQDVTEYMQQLLERE------RELTVERDELAARKQALDEEiERL-----SQPGGSEDPRLNALAERFGG 684
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1691 EQQRQL-----LEEE------LARLQH--------EATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSK 1751
Cdd:PRK04863 685 VLLSEIyddvsLEDApyfsalYGPARHaivvpdlsDAAEQLAGLEDCPEDLYLIEGDPDSFDDSVFSVEELEKAVVVKIA 764
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1752 QRlEAEAGRFRE--LAEEAARlRALAEEAKRQRQLAEEDAARQRAEAERVLT-----EKLAAISEATRLKTEAEIALKEK 1824
Cdd:PRK04863 765 DR-QWRYSRFPEvpLFGRAAR-EKRIEQLRAEREELAERYATLSFDVQKLQRlhqafSRFIGSHLAVAFEADPEAELRQL 842
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1825 EAE-NERLRRLAEDEAfqrrrLEEQAALHKADIEERLAQLRK-ASESELerqkgLVEDTLRQR-RQVEEEIMALkvsfEK 1901
Cdd:PRK04863 843 NRRrVELERALADHES-----QEQQQRSQLEQAKEGLSALNRlLPRLNL-----LADETLADRvEEIREQLDEA----EE 908
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1902 AAA-----GKA--ELELELGRIRSNAEDTMRSKEQaeLEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAlE 1974
Cdd:PRK04863 909 AKRfvqqhGNAlaQLEPIVSVLQSDPEQFEQLKQD--YQQAQQTQRDAKQQAFALTEVVQRRAHFSYEDAAEMLAKNS-D 985
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1975 EVERLKAKVEEARRLRERA-EQESARQLQLAQ-------------------EAAQKRLQ---------AEEKA------- 2018
Cdd:PRK04863 986 LNEKLRQRLEQAEQERTRArEQLRQAQAQLAQynqvlaslkssydakrqmlQELKQELQdlgvpadsgAEERArarrdel 1065
|
810
....*....|...
gi 254675251 2019 HAFVV--QQREEE 2029
Cdd:PRK04863 1066 HARLSanRSRRNQ 1078
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2655-2693 |
9.00e-05 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 42.31 E-value: 9.00e-05
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 2655 YLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTALIL 2693
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| CH_jitterbug-like_rpt3 |
cd21185 |
third calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ... |
149-226 |
1.08e-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: 44.22 E-value: 1.08e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 149 DNFTTSWRDGRLFNAIIHRHKPMLIDMNKVYRQTNLENLDQAFSVAERdLGVTRLLDPEDVDVPQPDEKSIITYVSSL 226
Cdd:cd21185 20 NNFTTDWNDGRLLCGLVNALGGSVPGWPNLDPEESENNIQRGLEAGKS-LGVEPVLTAEEMADPEVEHLGIMAYAAQL 96
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3648-3684 |
1.08e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 42.08 E-value: 1.08e-04
10 20 30
....*....|....*....|....*....|....*..
gi 254675251 3648 RYLYGTGAVAGVYLPGSRQTLTIYQALKKGLLSAEVA 3684
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| HCR |
pfam07111 |
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ... |
2144-2575 |
1.15e-04 |
|
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.
Pssm-ID: 284517 [Multi-domain] Cd Length: 749 Bit Score: 48.59 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2144 RQKAQVEQELTTLRLQLEETDHQ---KSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALI 2220
Cdd:pfam07111 190 KQLAEAQKEAELLRKQLSKTQEEleaQVTLVESLRKYVGEQVPPEVHSQTWELERQELLDTMQHLQEDRADLQATVELLQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2221 LRDKDNTQRFLEEEAEKMKQVAEEAarlSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAE-AELLQQ 2299
Cdd:pfam07111 270 VRVQSLTHMLALQEEELTRKIQPSD---SLEPEFPKKCRSLLNRWREKVFALMVQLKAQDLEHRDSVKQLRGQvAELQEQ 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2300 QKELAQEQARRLQEDKEQMAQQLVEE--TQGFQ----RTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRK 2373
Cdd:pfam07111 347 VTSQSQEQAILQRALQDKAAEVEVERmsAKGLQmelsRAQEARRRQQQQTASAEEQLKFVVNAMSSTQIWLETTMTRVEQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2374 QAEEIG----------EKLHRTELATQEKVTLVQTleiqRQQSDHDAERLREAIAELEREKEKLKQEAKLL--------- 2434
Cdd:pfam07111 427 AVARIPslsnrlsyavRKVHTIKGLMARKVALAQL----RQESCPPPPPAPPVDADLSLELEQLREERNRLdaelqlsah 502
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2435 -----------QLKSEEMQTV----QQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQ-LFQDEVAKAKQLREE 2498
Cdd:pfam07111 503 liqqevgrareQGEAERQQLSevaqQLEQELQRAQESLASVGQQLEVARQGQQESTEEAASLRQeLTQQQEIYGQALQEK 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2499 QQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQ----EELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAAL 2574
Cdd:pfam07111 583 VAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQhratQEKERNQELRRLQDEARKEEGQRLARRVQELERDKNLML 662
|
.
gi 254675251 2575 A 2575
Cdd:pfam07111 663 A 663
|
|
| CH_PLS_rpt1 |
cd21292 |
first calponin homology (CH) domain found in the plastin family; The plastin family includes ... |
12-109 |
1.19e-04 |
|
first calponin homology (CH) domain found in the plastin family; The plastin family includes plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409141 Cd Length: 145 Bit Score: 45.35 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 12 QKKTFTKWVN---------KHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPR----EKGRMRFHKLQNVQIALDYL 78
Cdd:cd21292 25 EKVAFVNWINknlgddpdcKHLLPMDPNTDDLFEKVKDGILLCKMINLSVPDTIDErainKKKLTVFTIHENLTLALNSA 104
|
90 100 110
....*....|....*....|....*....|.
gi 254675251 79 RHRQVKLVNIRNDDIADGNPKLTLGLIWTII 109
Cdd:cd21292 105 SAIGCNVVNIGAEDLKEGKPHLVLGLLWQII 135
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1759-2005 |
1.23e-04 |
|
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.
Pssm-ID: 462303 [Multi-domain] Cd Length: 488 Bit Score: 47.97 E-value: 1.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1759 GRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDE 1838
Cdd:pfam07888 34 NRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEELRQSREKHEELEEKYKELSASSEEL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1839 AFQRRRLEEQAALHKADIEE------RLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELE 1912
Cdd:pfam07888 114 SEEKDALLAQRAAHEARIREleedikTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELRSLSKE 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1913 LGRIRSNAEDTMRSKEQAELEAARQRQLaaeeeQRRREAEERVQRSLAAEEEAARQRKVALEE-VERLKAKVEEARRLRE 1991
Cdd:pfam07888 194 FQELRNSLAQRDTQVLQLQDTITTLTQK-----LTTAHRKEAENEALLEELRSLQERLNASERkVEGLGEELSSMAAQRD 268
|
250
....*....|....*
gi 254675251 1992 RAEQESAR-QLQLAQ 2005
Cdd:pfam07888 269 RTQAELHQaRLQAAQ 283
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1642-2020 |
1.39e-04 |
|
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A. The other form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site.
Pssm-ID: 468201 [Multi-domain] Cd Length: 684 Bit Score: 48.09 E-value: 1.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1642 GKAEEQAVRQRELAEQELEK-----QRQLAEGTAQQRLAAEQELIRLRAE--TEQGEQQRQLLEEELARLQHEATAATQK 1714
Cdd:NF033838 50 SSGNESQKEHAKEVESHLEKilseiQKSLDKRKHTQNVALNKKLSDIKTEylYELNVLKEKSEAELTSKTKKELDAAFEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1715 RQELEAELAKVRAEMEVLLA-----SKARAEEESRSTSEKSKQRLEAEAGRFrELAEEAARLRALAEEAKRQRQLAEEDA 1789
Cdd:NF033838 130 FKKDTLEPGKKVAEATKKVEeaekkAKDQKEEDRRNYPTNTYKTLELEIAES-DVEVKKAELELVKEEAKEPRDEEKIKQ 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1790 ARQRAEAERvlteklaaiSEATRL---KTEAEIALKE-KEAENERLRRLAED-----EAFQRRRLEEQAALHKADIEERL 1860
Cdd:NF033838 209 AKAKVESKK---------AEATRLekiKTDREKAEEEaKRRADAKLKEAVEKnvatsEQDKPKRRAKRGVLGEPATPDKK 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1861 AQLRKASESELERQKgLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAE------------LELELgrirsnAEDTMRSKE 1928
Cdd:NF033838 280 ENDAKSSDSSVGEET-LPSPSLKPEKKVAEAEKKVEEAKKKAKDQKEEdrrnyptntyktLELEI------AESDVKVKE 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1929 qAELEAARQRqlaaeeeqrrreaeervqrslAAEEEAARQRKVALEEVERLKA---KVEEARRLRERAEQESARQLQLAQ 2005
Cdd:NF033838 353 -AELELVKEE---------------------AKEPRNEEKIKQAKAKVESKKAeatRLEKIKTDRKKAEEEAKRKAAEED 410
|
410
....*....|....*
gi 254675251 2006 EAAQKRLQAEEKAHA 2020
Cdd:NF033838 411 KVKEKPAEQPQPAPA 425
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3930-3964 |
1.40e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.40e-04
10 20 30
....*....|....*....|....*....|....*
gi 254675251 3930 LLEAQAATGYVIDPIKGLKLTVEEAVRMGIVGPEF 3964
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPET 37
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1323-1544 |
1.40e-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: 47.45 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1323 ERERLAEVEAALEKQRQLAEAHAQAKAQAE---LEAQELQRRMQEEVarreeaavdaqqqkRSIQEELQHLRQSSEAEIQ 1399
Cdd:pfam09787 42 STALTLELEELRQERDLLREEIQKLRGQIQqlrTELQELEAQQQEEA--------------ESSREQLQELEEQLATERS 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1400 AKaqqvEAAERSRMRIEEEIRVVRLQLETTERQRggaegelqalraraeeaEAQKRQAQEEAERLRRQVQDESQRKRQaE 1479
Cdd:pfam09787 108 AR----REAEAELERLQEELRYLEEELRRSKATL-----------------QSRIKDREAEIEKLRNQLTSKSQSSSS-Q 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1480 AELALRVKAEAEAAREKQRALQAL----DELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQ 1544
Cdd:pfam09787 166 SELENRLHQLTETLIQKQTMLEALstekNSLVLQLERMEQQIKELQGEGSNGTSINMEGISDGEGTRLR 234
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2144-2348 |
1.41e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 48.09 E-value: 1.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2144 RQKAQVEQELTTLRLQLEE--TDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIl 2221
Cdd:COG3206 182 EQLPELRKELEEAEAALEEfrQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPELL- 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2222 rDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEkmqAVQEATRLKAEAELLQQQK 2301
Cdd:COG3206 261 -QSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS---LEAELEALQAREASLQAQL 336
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 254675251 2302 ELAQEQARRLQEdKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAE 2348
Cdd:COG3206 337 AQLEARLAELPE-LEAELRRLEREVEVARELYESLLQRLEEARLAEA 382
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
2146-2573 |
1.44e-04 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.11 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2146 KAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEaENRALILRDK 2224
Cdd:PRK02224 193 KAQIEEkEEKDLHERLNGLESELAELDEEIERYEEQREQARETRDEADEVLEEHEERREELETLEAEIE-DLRETIAETE 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2225 DNTQRFLEEEAEKMKQVAEEAARLSVAAQEAArLRQLAEEDLAQQRALAEKMLKEKMQAVQE----ATRLKAEAELLQQQ 2300
Cdd:PRK02224 272 REREELAEEVRDLRERLEELEEERDDLLAEAG-LDDADAEAVEARREELEDRDEELRDRLEEcrvaAQAHNEEAESLRED 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2301 KELAQEQARRLQEDkeqmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2380
Cdd:PRK02224 351 ADDLEERAEELREE----AAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREERDELRE 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2381 KLH--RTELAT-QEKVTLVQTL-----------EIQRQQSDHDAERLREAIAELEREKEKLKQ-----EAKLLQLKSEEM 2441
Cdd:PRK02224 427 REAelEATLRTaRERVEEAEALleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEeveevEERLERAEDLVE 506
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2442 QTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQ---EKAKLEQLFQD--EVAKAKQLREEQQRQQQQMEQEKQELMAS 2516
Cdd:PRK02224 507 AEDRIERLEERREDLEELIAERRETIEEKRERAEElreRAAELEAEAEEkrEAAAEAEEEAEEAREEVAELNSKLAELKE 586
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2517 MEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQR---LEEEHRAA 2573
Cdd:PRK02224 587 RIESLERIRTLLAAIADAEDEIERLREKREALAELNDERRERLAEKRERkreLEAEFDEA 646
|
|
| EmrA |
COG1566 |
Multidrug resistance efflux pump EmrA [Defense mechanisms]; |
1316-1430 |
1.44e-04 |
|
Multidrug resistance efflux pump EmrA [Defense mechanisms];
Pssm-ID: 441174 [Multi-domain] Cd Length: 331 Bit Score: 47.35 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1316 AEQQRAEERERLAEVEAALEKQRQLAEAHAQ---AKAQAELEAQELQRRM---------QEEVARREEAAVDAQQQKRSI 1383
Cdd:COG1566 88 AEAQLAAAEAQLARLEAELGAEAEIAAAEAQlaaAQAQLDLAQRELERYQalykkgavsQQELDEARAALDAAQAQLEAA 167
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 254675251 1384 QEELQHLRQSSEAEiqakaQQVEAAERSRMRIEEEIRVVRLQLETTE 1430
Cdd:COG1566 168 QAQLAQAQAGLREE-----EELAAAQAQVAQAEAALAQAELNLARTT 209
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1444-1714 |
1.44e-04 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 47.95 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1444 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRqaeaELALRVKAEAEAAREKQRAlqaldELRLQAE----EAERRLRQ 1519
Cdd:COG2268 200 DARIAEAEAERETEIAIAQANREAEEAELEQER----EIETARIAEAEAELAKKKA-----EERREAEtaraEAEAAYEI 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1520 AEAERARQVQVALETAQRSAEVELQSKRAsfaektaqlertlqeehvtvaqlreeaerraqqqaeaerareeaerelerw 1599
Cdd:COG2268 271 AEANAEREVQRQLEIAEREREIELQEKEA--------------------------------------------------- 299
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1600 qlkanealrLRLQAEEVAQQKSLAQADAEKQKeeaerearrrgkaeeqavrQRELAEQELEKQRQLAEGTAQQRLAAeqe 1679
Cdd:COG2268 300 ---------EREEAELEADVRKPAEAEKQAAE-------------------AEAEAEAEAIRAKGLAEAEGKRALAE--- 348
|
250 260 270
....*....|....*....|....*....|....*.
gi 254675251 1680 lirlrAETEQGEQQRQL-LEEELARLQHEATAATQK 1714
Cdd:COG2268 349 -----AWNKLGDAAILLmLIEKLPEIAEAAAKPLEK 379
|
|
| Crescentin |
pfam19220 |
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ... |
2122-2424 |
1.52e-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: 1.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2122 LKQKQAADAEMEKHkkfAEQTLRQKAQVEQELTTLRLQLEETDHQksildeeLQRLKAEVTEAARQRSQVEEELFSVRVQ 2201
Cdd:pfam19220 113 LRDKTAQAEALERQ---LAAETEQNRALEEENKALREEAQAAEKA-------LQRAEGELATARERLALLEQENRRLQAL 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2202 MEELGKLKARIEAENRALILRDKDNTQRFLEEEAEkmkqvaeeaarlsVAAQEAARLRQLAEEDLAQQRALAEKM-LKEK 2280
Cdd:pfam19220 183 SEEQAAELAELTRRLAELETQLDATRARLRALEGQ-------------LAAEQAERERAEAQLEEAVEAHRAERAsLRMK 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2281 MQAVQeaTRLKAEAELLQQQKELAQEQARRLQEdKEQMAQQLVEETQGFQRT---LEAERQRQLEMSAEAERLKLRMAEM 2357
Cdd:pfam19220 250 LEALT--ARAAATEQLLAEARNQLRDRDEAIRA-AERRLKEASIERDTLERRlagLEADLERRTQQFQEMQRARAELEER 326
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 2358 SRAQARAEEDAQRFRKQAEEIGEKLhrtelatQEKV-TLVQTLEIQRQQSDHDAERLREaiaELEREK 2424
Cdd:pfam19220 327 AEMLTKALAAKDAALERAEERIASL-------SDRIaELTKRFEVERAALEQANRRLKE---ELQRER 384
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2293-2578 |
1.61e-04 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 47.81 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2293 EAELLQQQKELAQEQA----RRLQEDKEQMAQQLVEETQGfQRTLEAERQRQLEMS-----AEAERLKLRMAEMSRAQAR 2363
Cdd:pfam17380 267 ENEFLNQLLHIVQHQKavseRQQQEKFEKMEQERLRQEKE-EKAREVERRRKLEEAekarqAEMDRQAAIYAEQERMAME 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2364 AEEDAQRFRKQAEEI-GEKLHRTELATQ-EKVTLVQTLEIQRQQSDhdaERLREAIAELEREKEKLKQEAKLLQLKSEEM 2441
Cdd:pfam17380 346 RERELERIRQEERKReLERIRQEEIAMEiSRMRELERLQMERQQKN---ERVRQELEAARKVKILEEERQRKIQQQKVEM 422
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2442 QTVQQEQILQETQALQKsflsekdslLQRERFIEQEKAKLEQLfqdevakakqlreeqqRqqqqmEQEKQELMASMEEAR 2521
Cdd:pfam17380 423 EQIRAEQEEARQREVRR---------LEEERAREMERVRLEEQ----------------E-----RQQQVERLRQQEEER 472
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 2522 RRQREAEEGVRRKQ----EELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSE 2578
Cdd:pfam17380 473 KRKKLELEKEKRDRkraeEQRRKILEKELEERKQAMIEEERKRKLLEKEMEERQKAIYEEE 533
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3724-3760 |
1.67e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.70 E-value: 1.67e-04
10 20 30
....*....|....*....|....*....|....*..
gi 254675251 3724 RLLSAERAVTGYRDPYTEQTISLFQAMKKELIPAEEA 3760
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
2123-2570 |
1.71e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 47.99 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2123 KQKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETdhqKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2202
Cdd:COG4913 338 DRLEQLEREIERLERELEERERRRARLEALLAALGLPLPAS---AEEFAALRAEAAALLEALEEELEALEEALAEAEAAL 414
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2203 EELGKLKARIEAENRALILRDKDntqrfLEEEAEKMKQVAEEAARLS-VAAQEAARLRQLAEEDLAQQRAlAEKML---- 2277
Cdd:COG4913 415 RDLRRELRELEAEIASLERRKSN-----IPARLLALRDALAEALGLDeAELPFVGELIEVRPEEERWRGA-IERVLggfa 488
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2278 ------KEKMQAVQEA---TRLKAEAELLQQQKELAQEQARRLQED-----------------KEQMAQQL----VEETQ 2327
Cdd:COG4913 489 ltllvpPEHYAAALRWvnrLHLRGRLVYERVRTGLPDPERPRLDPDslagkldfkphpfrawlEAELGRRFdyvcVDSPE 568
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2328 GFQRT--------------------------------LEAERQRQ-LEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2374
Cdd:COG4913 569 ELRRHpraitragqvkgngtrhekddrrrirsryvlgFDNRAKLAaLEAELAELEEELAEAEERLEALEAELDALQERRE 648
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2375 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQ---SDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTvQQEQILQ 2451
Cdd:COG4913 649 ALQRLAEYSWDEIDVASAEREIAELEAELERldaSSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEK-ELEQAEE 727
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2452 ETQALQK--SFLSEKDSLLQRERFIEQekakLEQLFQDEVAKAKQLREEqqrqqqqmeqekqelmASMEEARRRQREAEE 2529
Cdd:COG4913 728 ELDELQDrlEAAEDLARLELRALLEER----FAAALGDAVERELRENLE----------------ERIDALRARLNRAEE 787
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 254675251 2530 GVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEH 2570
Cdd:COG4913 788 ELERAMRAFNREWPAETADLDADLESLPEYLALLDRLEEDG 828
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2150-2379 |
1.76e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 1.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2150 EQELTTLRLQLEE----TDHQKSILDEELQRLKAEVTEAARQRS-----QVEEELFSVRVQMEELGKLKARI-EAENRal 2219
Cdd:COG3096 450 EQQATEEVLELEQklsvADAARRQFEKAYELVCKIAGEVERSQAwqtarELLRRYRSQQALAQRLQQLRAQLaELEQR-- 527
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2220 iLRDKDNTQRFLEEEAEKMKQVAEEAARLsvaaqeaarlrqlaEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQ 2299
Cdd:COG3096 528 -LRQQQNAERLLEEFCQRIGQQLDAAEEL--------------EELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRA 592
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2300 Q-KEL---------AQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQ 2369
Cdd:COG3096 593 RiKELaarapawlaAQDALERLREQSGEALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPGGAEDP 672
|
250
....*....|
gi 254675251 2370 RFRKQAEEIG 2379
Cdd:COG3096 673 RLLALAERLG 682
|
|
| MukB |
COG3096 |
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ... |
2123-2435 |
1.77e-04 |
|
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 442330 [Multi-domain] Cd Length: 1470 Bit Score: 48.02 E-value: 1.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2123 KQKQAADAE---MEKHKKFAEQTLRQKAqVEQEL-----------TTLRLQlEETDHQKSILDEELQRLKAE---VTEAA 2185
Cdd:COG3096 297 ARRQLAEEQyrlVEMARELEELSARESD-LEQDYqaasdhlnlvqTALRQQ-EKIERYQEDLEELTERLEEQeevVEEAA 374
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2186 RQRSQVEEELFSVRVQMEELGKLKARI-----EAENRAL----ILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAA 2256
Cdd:COG3096 375 EQLAEAEARLEAAEEEVDSLKSQLADYqqaldVQQTRAIqyqqAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQAT 454
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2257 RLR-----QLAEEDLAQQR-----ALAEKMLKE--KMQAVQEATRL-------KAEAELLQQ---------QKELAQEQA 2308
Cdd:COG3096 455 EEVleleqKLSVADAARRQfekayELVCKIAGEveRSQAWQTARELlrryrsqQALAQRLQQlraqlaeleQRLRQQQNA 534
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2309 RRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE---EIGEKLHRT 2385
Cdd:COG3096 535 ERLLEEFCQRIGQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSELRQQLEQLRARIKELAARAPawlAAQDALERL 614
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 254675251 2386 ELATQEKVTLVQTLEIQRQQSdhdAERLREAIAE---LEREKEKLKQEAKLLQ 2435
Cdd:COG3096 615 REQSGEALADSQEVTAAMQQL---LEREREATVErdeLAARKQALESQIERLS 664
|
|
| PLEC |
smart00250 |
Plectin repeat; |
4239-4272 |
1.89e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 41.31 E-value: 1.89e-04
10 20 30
....*....|....*....|....*....|....
gi 254675251 4239 EETGPVAGILDTETLEKVSITEAMHRNLVDNITG 4272
Cdd:smart00250 5 EAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1345-1826 |
1.98e-04 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 47.34 E-value: 1.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1345 AQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRvvrl 1424
Cdd:COG3064 2 QEALEEKAAEAAAQERLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAK---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1425 QLETTERQRGGAEgelqalRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALD 1504
Cdd:COG3064 78 KLAEAEKAAAEAE------KKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1505 ELRLQAEEAERRlrqAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAE 1584
Cdd:COG3064 152 AEAEAARAAAAA---AAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1585 AERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1664
Cdd:COG3064 229 SREAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1665 LAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESR 1744
Cdd:COG3064 309 GAVAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1745 STSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEK 1824
Cdd:COG3064 389 AGILAAAGGGGLLGLRLDLGAALLEAASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKA 468
|
..
gi 254675251 1825 EA 1826
Cdd:COG3064 469 VA 470
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
2126-2286 |
2.19e-04 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 2.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2126 QAADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQmEEL 2205
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNN-KEY 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2206 GKLKARIEAENRALILRDKDnTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2285
Cdd:COG1579 92 EALQKEIESLKRRISDLEDE-ILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAA 170
|
.
gi 254675251 2286 E 2286
Cdd:COG1579 171 K 171
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
1355-1527 |
2.21e-04 |
|
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442746 [Multi-domain] Cd Length: 370 Bit Score: 47.15 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1355 AQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLrqSSEAEIQAKAQQVeaaersrmrieeeirvvrlqlETTERQRG 1434
Cdd:COG3524 175 REDAVRFAEEEVERAEERLRDAREALLAFRNRNGIL--DPEATAEALLQLI---------------------ATLEGQLA 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1435 GAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALrvkaeaeaarekQRALQALDELRLQAEEAE 1514
Cdd:COG3524 232 ELEAELAALRSYLSPNSPQVRQLRRRIAALEKQIAAERARLTGASGGDSL------------ASLLAEYERLELEREFAE 299
|
170
....*....|....*
gi 254675251 1515 RRLRQAEA--ERARQ 1527
Cdd:COG3524 300 KAYTSALAalEQARI 314
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
2126-2582 |
2.33e-04 |
|
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: 47.66 E-value: 2.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2126 QAADAEMEKHKKFAEQTLRQKAQVEQElTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEEL 2205
Cdd:TIGR00618 348 QTLHSQEIHIRDAHEVATSIREISCQQ-HTLTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQL 426
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2206 GKLKARIEAEnralilrdkdntQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQ 2285
Cdd:TIGR00618 427 AHAKKQQELQ------------QRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLQTKEQIHLQETRKKAVVLA 494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2286 EATRLKAEAELLQQQkELAQEQAR----------RLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMA 2355
Cdd:TIGR00618 495 RLLELQEEPCPLCGS-CIHPNPARqdidnpgpltRRMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFS 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2356 EMSRAQARAEEDAQRFRKQAEEIgekLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ 2435
Cdd:TIGR00618 574 ILTQCDNRSKEDIPNLQNITVRL---QDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALKLTALHA 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2436 LKSEEMQ----------TVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQ 2505
Cdd:TIGR00618 651 LQLTLTQervrehalsiRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENASSSL 730
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2506 MEQEKQELMA---SMEEARRRQRE-----AEEGVRRKQE---------ELQHLEQQRQQQEKLLAEENQRLRErlqrLEE 2568
Cdd:TIGR00618 731 GSDLAAREDAlnqSLKELMHQARTvlkarTEAHFNNNEEvtaalqtgaELSHLAAEIQFFNRLREEDTHLLKT----LEA 806
|
490
....*....|....
gi 254675251 2569 EHRAALAHSEIATT 2582
Cdd:TIGR00618 807 EIGQEIPSDEDILN 820
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1437-1571 |
2.42e-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: 46.67 E-value: 2.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1437 EGELQALRARAEEAEAQkrqAQEEAERLRRQVQDesqRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERR 1516
Cdd:pfam09787 67 RGQIQQLRTELQELEAQ---QQEEAESSREQLQE---LEEQLATERSARREAEAELERLQEELRYLEEELRRSKATLQSR 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1517 LRQAEAERARQ-VQVALETAQRSAEVELQSK----RASFAEKTAQLERTLQEEHVTVAQL 1571
Cdd:pfam09787 141 IKDREAEIEKLrNQLTSKSQSSSSQSELENRlhqlTETLIQKQTMLEALSTEKNSLVLQL 200
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
2137-2585 |
2.51e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 47.21 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2137 KFAEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAEN 2216
Cdd:COG5278 76 SFLEPYEEARAEIDELLAELRSLTADNPEQQARLDELEALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2217 RALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAEL 2296
Cdd:COG5278 156 ARLLLLALALAALLLAAAALLLLLLALAALLALAELLLLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2297 LQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAE 2376
Cdd:COG5278 236 AALALALALLLAALLLALLAALALAALLAAALLALAALLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAA 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2377 EIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQAL 2456
Cdd:COG5278 316 AAAAAAAAALAALLALALATALAAAAAALALLAALLAEAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAI 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2457 QKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQE 2536
Cdd:COG5278 396 AAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEALALAEEEALALAAASSELAEAGAALALAAAEALAEELAAVAALA 475
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 254675251 2537 ELQHLEQQRQQQEKLLAEENQRLRERLQRLEEEHRAALAHSEIATTQAA 2585
Cdd:COG5278 476 ALAAAAAALAEAEAAAALAAAAALSLALALAALLLAAAEAALAAALAAA 524
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1338-1707 |
2.69e-04 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 46.45 E-value: 2.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1338 RQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQ---QQKRSIQEELQHLRQSSEAEIQAKAQQVEA-AERSRM 1413
Cdd:pfam13868 9 RELNSKLLAAKCNKERDAQIAEKKRIKAEEKEEERRLDEMmeeERERALEEEEEKEEERKEERKRYRQELEEQiEEREQK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1414 RIEEEirvvrlqlettERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1493
Cdd:pfam13868 89 RQEEY-----------EEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEIDEFNEEQAEWKELEKEEEREEDERI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1494 REKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQrsaevelqskrasfAEKTAQLERTLQEEHvtvaqlre 1573
Cdd:pfam13868 158 LEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEK--------------AERDELRAKLYQEEQ-------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1574 eaerraqqQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRE 1653
Cdd:pfam13868 216 --------ERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMK 287
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1654 LAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHE 1707
Cdd:pfam13868 288 RLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLKE 341
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1744-1892 |
2.83e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 47.08 E-value: 2.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1744 RSTSEKSKQRLEAEAGRFRELAEEAArlralaEEAKRQRQL-AEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1822
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKEA------EAIKKEALLeAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLD 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 254675251 1823 EKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKasesELERQKGLVEDTLRQR--RQVEEEI 1892
Cdd:PRK12704 100 RKLELLEKREEELEKKEKELEQKQQELEKKEEELEELIEEQLQ----ELERISGLTAEEAKEIllEKVEEEA 167
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2142-2374 |
2.91e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 46.38 E-value: 2.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2142 TLRQKAQVEQELTTLRLQleetdhQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIEAENRALIL 2221
Cdd:TIGR02794 41 VLVDPGAVAQQANRIQQQ------KKPAAKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2222 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARlrQLAEEDLAQQRALAEKMLKE-KMQAVQEA-----TRLKAEAE 2295
Cdd:TIGR02794 115 EEKQKQAEEAKAKQAAEAKAKAEAEAERKAKEEAAK--QAEEEAKAKAAAEAKKKAEEaKKKAEAEAkakaeAEAKAKAE 192
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 2296 LLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQ 2374
Cdd:TIGR02794 193 EAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSEVDKYAAIIQQA 271
|
|
| CEP63 |
pfam17045 |
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole ... |
1618-1764 |
2.94e-04 |
|
Centrosomal protein of 63 kDa; CEP63 is a family of eukaryotic proteins involved in centriole activity.
Pssm-ID: 465338 [Multi-domain] Cd Length: 264 Bit Score: 45.97 E-value: 2.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1618 QQKSLAQA--DAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQ-ELIRLRAETEQGEQQR 1694
Cdd:pfam17045 101 QRKQLKEAreEAKSREEDRSELSRLNGKLEEFRQKSLEWEQQRLQYQQQVASLEAQRKALAEQsSLIQSAAYQVQLEGRK 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1695 QLLEEELARLQH-----EATAATQKRQELEAELAKVRAE-----MEVLLASKARAEEESRStSEKSKQRLEAEAGRFREL 1764
Cdd:pfam17045 181 QCLEASQSEIQRlrsklERAQDSLCAQELELERLRMRVSelgdsNRKLLEEQQRLLEELRM-SQRQLQVLQNELMELKAT 259
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1643-1866 |
3.13e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 46.86 E-value: 3.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1643 KAEE--------QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQK 1714
Cdd:PRK05035 447 KAEEakarfearQARLEREKAAREARHKKAAEARAAKDKDAVAAALARVKAKKAAATQPIVIKAGARPDNSAVIAAREAR 526
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1715 RQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE-EAKRQRQLAEEDAARQR 1793
Cdd:PRK05035 527 KAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARaKAKKAAQQAASAEPEEQ 606
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1794 AEAERVLTEKL-AAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAAlhKADIEERLAQLRKA 1866
Cdd:PRK05035 607 VAEVDPKKAAVaAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQ--ANAEPEEAEDPKKA 678
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1734-1933 |
3.15e-04 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 46.72 E-value: 3.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1734 ASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQrqlaEEDAARQRAEAERVLTEKLAAISEATRL 1813
Cdd:PRK09510 72 KSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQ----AEEAAKQAALKQKQAEEAAAKAAAAAKA 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1814 KTEAEIALKEKEAENerlrrlAEDEAfQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIM 1893
Cdd:PRK09510 148 KAEAEAKRAAAAAKK------AAAEA-KKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAA 220
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 254675251 1894 ALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE 1933
Cdd:PRK09510 221 AEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEVD 260
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1763-1998 |
3.67e-04 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 46.30 E-value: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1763 ELAEEAARLRALAEEAKRQRQLAEEdAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAeneRLRRLAEDEAFQR 1842
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAA-LKKEEKALLKQLAALERRIAALARRIRALEQELAALEA---ELAELEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1843 RRLEEQaalhKADIEERLAQLRKASE-------------SELERQKGLVEDTLRQRRqveEEIMALKVSFEKAAAGKAEL 1909
Cdd:COG4942 97 AELEAQ----KEELAELLRALYRLGRqpplalllspedfLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAEL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1910 ELELGRIRSNAEDtmRSKEQAELEAARQRQlaaeeeqrrreaeERVQRSLAAEEEAARQRKVAL-EEVERLKAKVEEARR 1988
Cdd:COG4942 170 EAERAELEALLAE--LEEERAALEALKAER-------------QKLLARLEKELAELAAELAELqQEAEELEALIARLEA 234
|
250
....*....|
gi 254675251 1989 LRERAEQESA 1998
Cdd:COG4942 235 EAAAAAERTP 244
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
2123-2327 |
3.77e-04 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 46.83 E-value: 3.77e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2123 KQKQAaDAEMEKHKKFAEQTLR---QKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQR----------S 2189
Cdd:PRK11281 50 KQKLL-EAEDKLVQQDLEQTLAlldKIDRQKEETEQLKQQLAQAPAKLRQAQAELEALKDDNDEETRETlstlslrqleS 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2190 QVEE-------------------------------ELFSVRVQMEELGKLKARIEAENRALI--LRDKDNT-QRFLEEEA 2235
Cdd:PRK11281 129 RLAQtldqlqnaqndlaeynsqlvslqtqperaqaALYANSQRLQQIRNLLKGGKVGGKALRpsQRVLLQAeQALLNAQN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2236 EKMKQVAEEAARLSVAAQE-----AARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAElLQQQKELAQEQARR 2310
Cdd:PRK11281 209 DLQRKSLEGNTQLQDLLQKqrdylTARIQRLEHQLQLLQEAINSKRLTLSEKTVQEAQSQDEAAR-IQANPLVAQELEIN 287
|
250
....*....|....*..
gi 254675251 2311 LqedkeQMAQQLVEETQ 2327
Cdd:PRK11281 288 L-----QLSQRLLKATE 299
|
|
| DUF4175 |
pfam13779 |
Domain of unknown function (DUF4175); |
1290-1529 |
3.95e-04 |
|
Domain of unknown function (DUF4175);
Pssm-ID: 463981 [Multi-domain] Cd Length: 833 Bit Score: 46.90 E-value: 3.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1290 ELTTLTSQYIKFISETLRRMEEEERLAEQQRAEEReRLAEVEAALEKQRQLAEAHAQAKAQAELeaQELQRRMQE-EVAR 1368
Cdd:pfam13779 517 ELREALDDYMQALAEQAQQNPQDLQQPDDPNAQEM-TQQDLQRMLDRIEELARSGRRAEAQQML--SQLQQMLENlQAGQ 593
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1369 REEAAVDAQQQKRSIQEELQHLRQ-----SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQAL 1443
Cdd:pfam13779 594 PQQQQQQGQSEMQQAMDELGDLLReqqqlLDETFRQLQQQGGQQQGQPGQQGQQGQGQQPGQGGQQPGAQMPPQGGAEAL 673
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1444 RARAEEAEAQKRQAQEEAERLRRQVQ-DESQRKRQA-----EAELALRVKAEAEAAREKQRALQALdelrlqaEEAERRL 1517
Cdd:pfam13779 674 GDLAERQQALRRRLEELQDELKELGGkEPGQALGDAgramrDAEEALGQGDLAGAVDAQGRALEAL-------RKGAQQL 746
|
250
....*....|..
gi 254675251 1518 RQAEAERARQVQ 1529
Cdd:pfam13779 747 AEAMQQQQGQGQ 758
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
1376-1577 |
4.16e-04 |
|
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]
Pssm-ID: 274303 [Multi-domain] Cd Length: 346 Bit Score: 45.99 E-value: 4.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1376 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrmRIEEEIRVVRLqletteRQRGGAEGELQALRARAEEAEAQKR 1455
Cdd:TIGR02794 49 AQQANRIQQQKKPAAKKEQERQKKLEQQAEEAEKQ---RAAEQARQKEL------EQRAAAEKAAKQAEQAAKQAEEKQK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1456 QAQEEAErlrrqvQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERrlrQAEAERArqvqvALETA 1535
Cdd:TIGR02794 120 QAEEAKA------KQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKK---KAEAEAK-----AKAEA 185
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 254675251 1536 QRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAER 1577
Cdd:TIGR02794 186 EAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAER 227
|
|
| CHASE3 |
COG5278 |
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms]; |
1667-2016 |
4.19e-04 |
|
Extracytoplasmic sensor domain CHASE3 (specificity unknown) [Signal transduction mechanisms];
Pssm-ID: 444089 [Multi-domain] Cd Length: 530 Bit Score: 46.44 E-value: 4.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1667 EGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRST 1746
Cdd:COG5278 113 EALIDQWLAELEQVIALRRAGGLEAALALVRSGEGKALMDEIRARLLLLALALAALLLAAAALLLLLLALAALLALAELL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1747 SEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEA 1826
Cdd:COG5278 193 LLALARALAALLLLLLLEAELAAAAALLAAAAALAALAALELLAALALALALLLAALLLALLAALALAALLAAALLALAA 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1827 ENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGK 1906
Cdd:COG5278 273 LLLALAAAAALAAAAALELAAAEALALAELELELLLAAAAAAAAAAAAAAAALAALLALALATALAAAAAALALLAALLA 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1907 AELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAKVEEA 1986
Cdd:COG5278 353 EAAAAAAEEAEAAAEAAAAALAGLAEVEAEGAAEAVELEVLAIAAAAAAAAAEAAAAAAAAAAASAAEALELAEALAEAL 432
|
330 340 350
....*....|....*....|....*....|
gi 254675251 1987 RRLRERAEQESARQLQLAQEAAQKRLQAEE 2016
Cdd:COG5278 433 ALAEEEALALAAASSELAEAGAALALAAAE 462
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
979-1472 |
4.36e-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: 46.64 E-value: 4.36e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 979 DPARECAQRIAEQQKAQAE-VEGLGKGVARLSAEAEKV-LALPEPSPAAPTLRSELELTLGKLEQVRSLSAIYLEKLK-- 1054
Cdd:pfam05483 264 EESRDKANQLEEKTKLQDEnLKELIEKKDHLTKELEDIkMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNka 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1055 --TISLVIR----STQGAEEVLKTHEEQLKEAQavpatlQELEATKASLKKLRAQAEAQQPVFNTLRDELrgaqevgERL 1128
Cdd:pfam05483 344 kaAHSFVVTefeaTTCSLEELLRTEQQRLEKNE------DQLKIITMELQKKSSELEEMTKFKNNKEVEL-------EEL 410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1129 QQRHGERDV---EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQL-------RYYRESADPLSAWLQDAKRRQEQI 1198
Cdd:pfam05483 411 KKILAEDEKlldEKKQFEKIAEELKGKEQELIFLLQAREKEIHDLEIQLtaiktseEHYLKEVEDLKTELEKEKLKNIEL 490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1199 QAVPIANCQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK------KPKVQS 1272
Cdd:pfam05483 491 TAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIqkgdevKCKLDK 570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1273 GSESVIQEYVDLRTRYSELTTLTS------QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQLAEAHA 1345
Cdd:pfam05483 571 SEENARSIEYEVLKKEKQMKILENkcnnlkKQIENKNKNIEELHQENKALKKKGSAENKQLNAYEIKVNKlELELASAKQ 650
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1346 QAKA-----QAELEAQEL-QRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRmriEEEI 1419
Cdd:pfam05483 651 KFEEiidnyQKEIEDKKIsEEKLLEEVEKAKAIADEAVKLQKEIDKRCQHKIAEMVALMEKHKHQYDKIIEER---DSEL 727
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 254675251 1420 RVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES 1472
Cdd:pfam05483 728 GLYKNKEQEQSSAKAALEIELSNIKAELLSLKKQLEIEKEEKEKLKMEAKENT 780
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1386-1534 |
4.57e-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: 44.92 E-value: 4.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1386 ELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIrvvrlqlETTERQRGGAEGELQALRARAEEAEAQKRQA-------- 1457
Cdd:COG1579 21 RLEHRLKELPAELAELEDELAALEARLEAAKTEL-------EDLEKEIKRLELEIEEVEARIKKYEEQLGNVrnnkeyea 93
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1458 -QEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALET 1534
Cdd:COG1579 94 lQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171
|
|
| RecN |
COG0497 |
DNA repair ATPase RecN [Replication, recombination and repair]; |
1650-1940 |
4.69e-04 |
|
DNA repair ATPase RecN [Replication, recombination and repair];
Pssm-ID: 440263 [Multi-domain] Cd Length: 555 Bit Score: 46.22 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1650 RQREL------AEQELEKQRQLAegtaQQRLAAEQELIRLRAETEQGEQQRQLLEEELarlqheataatqkrQELEAelA 1723
Cdd:COG0497 142 AQRELldafagLEELLEEYREAY----RAWRALKKELEELRADEAERARELDLLRFQL--------------EELEA--A 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1724 KVRAEMEVLLaskaraEEEsrstseksKQRLEAeAGRFRELAEEAarLRALAEEakrqrqlaEEDAARQRAEAERVLtEK 1803
Cdd:COG0497 202 ALQPGEEEEL------EEE--------RRRLSN-AEKLREALQEA--LEALSGG--------EGGALDLLGQALRAL-ER 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1804 LAAISE-----ATRLkTEAEIALKEKEAEnerLRRLAEDEAFQRRRLEEqaalhkadIEERLAQLRKaseseLERQKGL- 1877
Cdd:COG0497 256 LAEYDPslaelAERL-ESALIELEEAASE---LRRYLDSLEFDPERLEE--------VEERLALLRR-----LARKYGVt 318
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 1878 VEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAED--TMRSKEQAELEAARQRQL 1940
Cdd:COG0497 319 VEELLAYAEELRAELAELENSDERLEELEAELAEAEAELLEAAEKlsAARKKAAKKLEKAVTAEL 383
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1305-1481 |
4.82e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.44 E-value: 4.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1305 TLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQ---------LAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVD 1375
Cdd:PRK12678 45 GMRKGELIAAIKEARGGGAAAAAATPAAPAAAARRaaraaaaarQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEA 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1376 AQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEirvvrlqlETTERQRGGAEGELQALRARAEEAEAQKR 1455
Cdd:PRK12678 125 AQARERRERGEAARRGAARKAGEGGEQPATEARADAAERTEEE--------ERDERRRRGDREDRQAEAERGERGRREER 196
|
170 180
....*....|....*....|....*.
gi 254675251 1456 QAQEEAERLRRQVQDESQRKRQAEAE 1481
Cdd:PRK12678 197 GRDGDDRDRRDRREQGDRREERGRRD 222
|
|
| PRK10246 |
PRK10246 |
exonuclease subunit SbcC; Provisional |
981-1673 |
4.85e-04 |
|
exonuclease subunit SbcC; Provisional
Pssm-ID: 182330 [Multi-domain] Cd Length: 1047 Bit Score: 46.72 E-value: 4.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 981 ARECAQRIAEQQKAQAEVEGLGKGVARLSaeaekvLALPepspaAPTLRSELEltlGKLEQVRSLSAIyleKLKTISLVI 1060
Cdd:PRK10246 256 QQEASRRQQALQQALAAEEKAQPQLAALS------LAQP-----ARQLRPHWE---RIQEQSAALAHT---RQQIEEVNT 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1061 RSTQGAEEVLKTHEEQLKEAQAVPATLQELeatkaslkklrAQAEAQQPVFNTLRDELRG-----AQEVGERLQQRhger 1135
Cdd:PRK10246 319 RLQSTMALRARIRHHAAKQSAELQAQQQSL-----------NTWLAEHDRFRQWNNELAGwraqfSQQTSDREQLR---- 383
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1136 dveveRWRERVTQLLERWQAVLAQT-----DVRQRELEQLGRQlRYYRESADPLSAWLQDAKRRQEQIQAvpiANCQAAR 1210
Cdd:PRK10246 384 -----QWQQQLTHAEQKLNALPAITltltaDEVAAALAQHAEQ-RPLRQRLVALHGQIVPQQKRLAQLQV---AIQNVTQ 454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1211 EQLRQEKALLEEIERHGEKVEE-------CQKFAKqyinaIKDYElqliTYKAQLEPvASPAkkPKVQSGSESVIQEYVD 1283
Cdd:PRK10246 455 EQTQRNAALNEMRQRYKEKTQQladvktiCEQEAR-----IKDLE----AQRAQLQA-GQPC--PLCGSTSHPAVEAYQA 522
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1284 LRtryselttltsqyikfISETLRRMEEEERLAEQQRAEERERLAEVEaALEKQRQLAEAHAQAKAQaelEAQELQRRMQ 1363
Cdd:PRK10246 523 LE----------------PGVNQSRLDALEKEVKKLGEEGAALRGQLD-ALTKQLQRDESEAQSLRQ---EEQALTQQWQ 582
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1364 EEVARREEAAVDAQQQKRSIQEELQHLRQ----SSEAEIQAkaqQVEAAERSRMRIEEEIRVVRLQLETTERQrggaege 1439
Cdd:PRK10246 583 AVCASLNITLQPQDDIQPWLDAQEEHERQlrllSQRHELQG---QIAAHNQQIIQYQQQIEQRQQQLLTALAG------- 652
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1440 lQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELA-LRVKAEAEAAREKQRALQALDELR--------LQA 1510
Cdd:PRK10246 653 -YALTLPQEDEEASWLATRQQEAQSWQQRQNELTALQNRIQQLTpLLETLPQSDDLPHSEETVALDNWRqvheqclsLHS 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1511 E-EAERRLRQAEAERARQVQVALETAqrsaeveLQSKRasFAEKTAQLERTLQEEhvTVAQLREEAERRAQQQAEAERAR 1589
Cdd:PRK10246 732 QlQTLQQQDVLEAQRLQKAQAQFDTA-------LQASV--FDDQQAFLAALLDEE--TLTQLEQLKQNLENQRQQAQTLV 800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1590 EEAERELERWQLKANEALRLRLQAEEVAQQksLAQadaekqkeeaerearRRGKAEEQAVRQRELAEQelekQRQLAEGT 1669
Cdd:PRK10246 801 TQTAQALAQHQQHRPDGLDLTVTVEQIQQE--LAQ---------------LAQQLRENTTRQGEIRQQ----LKQDADNR 859
|
....
gi 254675251 1670 AQQR 1673
Cdd:PRK10246 860 QQQQ 863
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3350-3385 |
4.87e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.87e-04
10 20 30
....*....|....*....|....*....|....*.
gi 254675251 3350 TLLLEAQAATGFLVDPVRNQRLYVHEAVKAGVVGPE 3385
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2693-2726 |
4.96e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 4.96e-04
10 20 30
....*....|....*....|....*....|....
gi 254675251 2693 LLEAQAASGFLLDPVRNRRLTVNEAVKEGVVGPE 2726
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| COG3899 |
COG3899 |
Predicted ATPase [General function prediction only]; |
1666-2162 |
5.21e-04 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443106 [Multi-domain] Cd Length: 1244 Bit Score: 46.39 E-value: 5.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1666 AEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV----------RAEMEVLLAS 1735
Cdd:COG3899 737 PDPEEEYRLALLLELAEALYLAGRFEEAEALLERALAARALAALAALRHGNPPASARAYAnlgllllgdyEEAYEFGELA 816
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1736 KARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKT 1815
Cdd:COG3899 817 LALAERLGDRRLEARALFNLGFILHWLGPLREALELLREALEAGLETGDAALALLALAAAAAAAAAAAALAAAAAAAARL 896
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1816 EAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMAL 1895
Cdd:COG3899 897 LAAAAAALAAAAAAAALAAAELARLAAAAAAAAALALAAAAAAAAAAALAAAAAAAALAAALALAAAAAAAAAAALAAAA 976
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1896 KVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE 1975
Cdd:COG3899 977 AAAAAAAAAAAAAALEAAAAALLALLAAAAAAAAAAAALAAALLAAALAALAAAAAAAALLAAAAALALLAALAAAAAAA 1056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1976 VERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVVQQREEELQQTLQQEQNMLDRLRSEAEAARRAA 2055
Cdd:COG3899 1057 AAAAALAAAAALLAAAAAAAAAAAAAAAAAALAAALAAAALAAAAAAALALAAALAALALAAALAALALAAAARAAAALL 1136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2056 EEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKH 2135
Cdd:COG3899 1137 LLAAALALALAALLLLAALLLALALLLLALAALALAAALAALAAALLAAAAAAAAAAALLAALLALAARLAALLALALLA 1216
|
490 500
....*....|....*....|....*..
gi 254675251 2136 KKFAEQTLRQKAQVEQELTTLRLQLEE 2162
Cdd:COG3899 1217 LEAAALLLLLLLAALALAAALLALRLL 1243
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
2213-2330 |
5.24e-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: 5.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2213 EAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEaarlRQLAEEDLAQQRALAE--KMLKEKMQavQEATRL 2290
Cdd:cd16269 180 EAEAEAILQADQALTEKEKEIEAERAKAEAAEQERKLLEEQQ----RELEQKLEDQERSYEEhlRQLKEKME--EERENL 253
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 254675251 2291 KAEAELLQQQKElaQEQARRLQEDKEQMAQQLVEETQGFQ 2330
Cdd:cd16269 254 LKEQERALESKL--KEQEALLEEGFKEQAELLQEEIRSLK 291
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1643-1786 |
5.32e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 46.55 E-value: 5.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1643 KAEEQAVRQR-ELAEQElekqrqlaegtAQQRLaaEQELIRLRAETEqgEQQRQLLEEELARLQHEATAATQKRQELEAE 1721
Cdd:PTZ00491 662 KSQEAAARHQaELLEQE-----------ARGRL--ERQKMHDKAKAE--EQRTKLLELQAESAAVESSGQSRAEALAEAE 726
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1722 LAKVRAEMEVLLAS-KARAEE-ESRSTSEKSKQRLEAEAGRFRELAE-EAARLRALAE-EAKRQRQLAE 1786
Cdd:PTZ00491 727 ARLIEAEAEVEQAElRAKALRiEAEAELEKLRKRQELELEYEQAQNElEIAKAKELADiEATKFERIVE 795
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
1031-1247 |
5.33e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 5.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1031 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQAVPATLQELEATKASLkklraqaEAQQPV 1110
Cdd:COG4913 614 ALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREIAELEAELERL-------DASSDD 686
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1111 FNTLRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLlerwqavlaqtdvrQRELEQLGRQLRYYRESADPLSAWLQD 1190
Cdd:COG4913 687 LAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQA--------------EEELDELQDRLEAAEDLARLELRALLE 752
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1191 AKRRQEQIQAVPiancQAAREQLRQE-KALLEEIERHGEKVEEC-QKFAKQYINAIKDY 1247
Cdd:COG4913 753 ERFAAALGDAVE----RELRENLEERiDALRARLNRAEEELERAmRAFNREWPAETADL 807
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2981-3018 |
5.37e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.37e-04
10 20 30
....*....|....*....|....*....|....*...
gi 254675251 2981 RQALRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVA 3018
Cdd:smart00250 1 QRLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2654-2690 |
5.53e-04 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 40.16 E-value: 5.53e-04
10 20 30
....*....|....*....|....*....|....*..
gi 254675251 2654 RYLKGRSSIAGLLLKPTNEKLSVYTALQRQLLSPGTA 2690
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1515-1836 |
5.65e-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: 45.68 E-value: 5.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1515 RRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAER 1594
Cdd:pfam13868 32 KRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERIQ 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1595 ELERWQLKANEALRLRLQAEevaQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegtaqqRL 1674
Cdd:pfam13868 112 EEDQAEAEEKLEKQRQLREE---IDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEI--------EE 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1675 AAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRsTSEKSKQRL 1754
Cdd:pfam13868 181 EKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKER-RLAEEAERE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1755 EAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRL 1834
Cdd:pfam13868 260 EEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKL 339
|
..
gi 254675251 1835 AE 1836
Cdd:pfam13868 340 KE 341
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
2210-2578 |
5.84e-04 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 46.49 E-value: 5.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2210 ARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLS-------VAAQEAARLRQLAEEDLAQQRAL--AEKMLKEK 2280
Cdd:PRK04863 281 RRVHLEEALELRRELYTSRRQLAAEQYRLVEMARELAELNeaesdleQDYQAASDHLNLVQTALRQQEKIerYQADLEEL 360
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2281 MQAVQEATRLKAEAellQQQKELAQEQARRLQEDKEQMAQQLVEETQGF--QRTLEAERQRQLEMSAEAERLklrMAEMS 2358
Cdd:PRK04863 361 EERLEEQNEVVEEA---DEQQEENEARAEAAEEEVDELKSQLADYQQALdvQQTRAIQYQQAVQALERAKQL---CGLPD 434
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2359 RAQARAEEDAQRFRKQAEEIGEKLhrteLATQEKVTLVQTLeiqRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKS 2438
Cdd:PRK04863 435 LTADNAEDWLEEFQAKEQEATEEL----LSLEQKLSVAQAA---HSQFEQAYQLVRKIAGEVSRSEAWDVARELLRRLRE 507
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2439 EEMQTVQQEQILQETQALQKSFLSEKDSllqrERFIEQEKAKLEQLFQDEvakakqlreeqqRQQQQMEQEKQELMASME 2518
Cdd:PRK04863 508 QRHLAEQLQQLRMRLSELEQRLRQQQRA----ERLLAEFCKRLGKNLDDE------------DELEQLQEELEARLESLS 571
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 2519 EARRRQREAEEGVRRKQEelqhleqqrqQQEKLLAEENQR------LRERLQRLEEEHRAALAHSE 2578
Cdd:PRK04863 572 ESVSEARERRMALRQQLE----------QLQARIQRLAARapawlaAQDALARLREQSGEEFEDSQ 627
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1396-1529 |
5.96e-04 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 46.05 E-value: 5.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1396 AEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRK 1475
Cdd:PRK12678 53 AAIKEARGGGAAAAAATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRE 132
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1476 RQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQ 1529
Cdd:PRK12678 133 RGEAARRGAARKAGEGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAE 186
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
928-1356 |
6.09e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 45.91 E-value: 6.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 928 RHYQQLLQSLEQGEQEESRCQRCISELKDIRLQLEAcetrtvhrlrlpldkdpARECAQRIAEQQKAQAEVEGLGKGVAR 1007
Cdd:COG4717 88 EEYAELQEELEELEEELEELEAELEELREELEKLEK-----------------LLQLLPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1008 LSAEAEKVLALPEpspAAPTLRSELELTLGKLEQVRSLSAiyLEKLKTISLVIRSTQGAEEVLKTHEEQLKEAQavpatl 1087
Cdd:COG4717 151 LEERLEELRELEE---ELEELEAELAELQEELEELLEQLS--LATEEELQDLAEELEELQQRLAELEEELEEAQ------ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1088 QELEATKASLKKLRAQAEAQQPvFNTLRDELRGAQEVGERL-----QQRHGERDVEV------------------ERWRE 1144
Cdd:COG4717 220 EELEELEEELEQLENELEAAAL-EERLKEARLLLLIAAALLallglGGSLLSLILTIagvlflvlgllallflllAREKA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1145 RVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRE-SADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQE-KALLEE 1222
Cdd:COG4717 299 SLGKEAEELQALPALEELEEEELEELLAALGLPPDlSPEELLELLDRIEELQELLREAEELEEELQLEELEQEiAALLAE 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1223 IerHGEKVEECQKFAKQYiNAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQYIKFI 1302
Cdd:COG4717 379 A--GVEDEEELRAALEQA-EEYQELKEELEELEEQLEELLGELEELLEALDEEELEEELEELEEELEELEEELEELREEL 455
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1303 SET---LRRMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQ 1356
Cdd:COG4717 456 AELeaeLEQLEEDGELAEllQELEELKAELRELAEEWAALKLALELLEEAREEYREERL 514
|
|
| CCDC22 |
pfam05667 |
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ... |
1300-1559 |
6.15e-04 |
|
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.
Pssm-ID: 461708 [Multi-domain] Cd Length: 600 Bit Score: 46.17 E-value: 6.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1300 KFISETLR----RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQR-RMQEEVARREEAAV 1374
Cdd:pfam05667 250 KRIAEQLRsaalAGTEATSGASRSAQDLAELLSSFSGSSTTDTGLTKGSRFTHTEKLQFTNEAPAaTSSPPTKVETEEEL 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1375 DAQQQK--RSIQEELQHLrqssEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQrggaegelQALRARA-EEAE 1451
Cdd:pfam05667 330 QQQREEelEELQEQLEDL----ESSIQELEKEIKKLESSIKQVEEELEELKEQNEELEKQ--------YKVKKKTlDLLP 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1452 aqkrQAQEEAERLRRQVQDESQRKrqaeAELAlrvkAEAEAAR----EKQRALQalDELRLQAEEAERRLRQAEAERaRQ 1527
Cdd:pfam05667 398 ----DAEENIAKLQALVDASAQRL----VELA----GQWEKHRvpliEEYRALK--EAKSNKEDESQRKLEEIKELR-EK 462
|
250 260 270
....*....|....*....|....*....|..
gi 254675251 1528 VQVALEtaqrsaevELQSKRASFAEKTAQLER 1559
Cdd:pfam05667 463 IKEVAE--------EAKQKEELYKQLVAEYER 486
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
2409-2537 |
6.18e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.97 E-value: 6.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2409 DAERLREAIAELEREKEKLKQEAKLLqlkseemqtvqqEQILQETQALQKSFLSEKDSLLQRErfiEQEKAKLEQLFQDE 2488
Cdd:PRK00409 514 DKEKLNELIASLEELERELEQKAEEA------------EALLKEAEKLKEELEEKKEKLQEEE---DKLLEEAEKEAQQA 578
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 254675251 2489 VAKAKQLREEQQRQQQQMEQEKQELMAS--MEEARRRQREAEEGVRRKQEE 2537
Cdd:PRK00409 579 IKEAKKEADEIIKELRQLQKGGYASVKAheLIEARKRLNKANEKKEKKKKK 629
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
3649-3687 |
6.29e-04 |
|
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous pemphigoid antigen.
Pssm-ID: 459901 Cd Length: 39 Bit Score: 40.00 E-value: 6.29e-04
10 20 30
....*....|....*....|....*....|....*....
gi 254675251 3649 YLYGTGAVAGVYLPGSRQTLTIYQALKKGLLSAEVARLL 3687
Cdd:pfam00681 1 LLEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1414-1559 |
6.76e-04 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 44.43 E-value: 6.76e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1414 RIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA 1493
Cdd:COG1842 20 KAEDPEKMLDQAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEEKARLALEKGREDLAREALERKAELEAQ 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1494 REKQRAL-----QALDELRLQAEEAERRLRQAEAERaRQVQVALETAQRSAEVELQSKRASFAEKTAQLER 1559
Cdd:COG1842 100 AEALEAQlaqleEQVEKLKEALRQLESKLEELKAKK-DTLKARAKAAKAQEKVNEALSGIDSDDATSALER 169
|
|
| SMC_N |
pfam02463 |
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ... |
1031-1565 |
6.93e-04 |
|
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: 46.12 E-value: 6.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1031 ELELTLGKLEQVRSLSAIYLEKLKTISLVIRSTQGAEEVLKthEEQLKEAQAVPATLQELEATKASLKKLRAQAEAQQPV 1110
Cdd:pfam02463 394 EEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEE--EEESIELKQGKLTEEKEELEKQELKLLKDELELKKSE 471
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1111 FNTLRDELRgaQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQ-LGRQLRYYRESADPLSAWLQ 1189
Cdd:pfam02463 472 DLLKETQLV--KLQEQLELLLSRQKLEERSQKESKARSGLKVLLALIKDGVGGRIISAHgRLGDLGVAVENYKVAISTAV 549
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1190 DAKRRQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKVEecQKFAKQYINAIKDYE-LQLITYKAQLEPVASPAK-- 1266
Cdd:pfam02463 550 IVEVSATADEVEERQKLVRALTELPLGARKLRLLIPKLKLPL--KSIAVLEIDPILNLAqLDKATLEADEDDKRAKVVeg 627
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1267 ------------KPKVQSGSESVIQEYVDLRTRYSELTTLTS---QYIKFISETLRRMEEEERLAE-----------QQR 1320
Cdd:pfam02463 628 ilkdteltklkeSAKAKESGLRKGVSLEEGLAEKSEVKASLSeltKELLEIQELQEKAESELAKEEilrrqleikkkEQR 707
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1321 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQA 1400
Cdd:pfam02463 708 EKEELKKLKLEAEELLADRVQEAQDKINEELKLLKQKIDEEEEEEEKSRLKKEEKEEEKSELSLKEKELAEEREKTEKLK 787
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1401 KAQQVEAAERS------RMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ--AQEEAERLRRQVQDES 1472
Cdd:pfam02463 788 VEEEKEEKLKAqeeelrALEEELKEEAELLEEEQLLIEQEEKIKEEELEELALELKEEQKLEklAEEELERLEEEITKEE 867
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1473 QRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAE 1552
Cdd:pfam02463 868 LLQELLLKEEELEEQKLKDELESKEEKEKEEKKELEEESQKLNLLEEKENEIEERIKEEAEILLKYEEEPEELLLEEADE 947
|
570
....*....|...
gi 254675251 1553 KTAQLERTLQEEH 1565
Cdd:pfam02463 948 KEKEENNKEEEEE 960
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1643-2023 |
7.03e-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: 7.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1643 KAEEQAVRQRELAEQElekQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEElarlqheataATQKRQELEAEL 1722
Cdd:COG3064 9 AAEAAAQERLEQAEAE---KRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAE----------AEQRAAELAAEA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1723 AKVRAEmevllASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTE 1802
Cdd:COG3064 76 AKKLAE-----AEKAAAEAEKKAAAEKAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1803 KLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTL 1882
Cdd:COG3064 151 KAEAEAARAAAAAAAAAAAAAARAAAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1883 RQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAE 1962
Cdd:COG3064 231 EAALAAVEATEEAALGGAEEAADLAAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGA 310
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1963 EEAARQRKVALEEVERLKAKVEEARRLRERAEQESARQLQLAQEAAQKRLQAEEKAHAFVV 2023
Cdd:COG3064 311 VAAEEAVLAAAAAAGALVVRGGGAASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEA 371
|
|
| KpsE |
COG3524 |
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis]; |
2137-2304 |
7.39e-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: 7.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2137 KFAEQTLrqkAQVEQELTTLRLQLEETDHQKSILDEElqrlkAEVTEAARQRSQVEEELFSVRVQMEEL----------- 2205
Cdd:COG3524 180 RFAEEEV---ERAEERLRDAREALLAFRNRNGILDPE-----ATAEALLQLIATLEGQLAELEAELAALrsylspnspqv 251
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2206 GKLKARIEAenralilrdkdntqrfLEeeaekmKQVAEEAARLSVAAQEAARLRQLAE-EDLAQQRALAEKMLKEKMQAV 2284
Cdd:COG3524 252 RQLRRRIAA----------------LE------KQIAAERARLTGASGGDSLASLLAEyERLELEREFAEKAYTSALAAL 309
|
170 180
....*....|....*....|
gi 254675251 2285 QEAtrlKAEAEllQQQKELA 2304
Cdd:COG3524 310 EQA---RIEAA--RQQRYLA 324
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
1228-1511 |
7.41e-04 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.82 E-value: 7.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1228 EKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSELTTLTSQyikfisETLR 1307
Cdd:PRK10929 58 EERKGSLERAKQYQQVIDNFPKLSAELRQQLNNERDEPRSVPPNMSTDALEQEILQVSSQLLEKSRQAQQ------EQDR 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1308 RMEEEERLAE--QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAeleaqelqrrMQEEVARReEAAVDaqqqkrsiQE 1385
Cdd:PRK10929 132 AREISDSLSQlpQQQTEARRQLNEIERRLQTLGTPNTPLAQAQLTA----------LQAESAAL-KALVD--------EL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1386 ELQHLRQSSEAEIqakaqqveaaerSRMRIeeeirvvrlqlETTERQRGGAEGELQALRAR--------AEEAEAQKRQA 1457
Cdd:PRK10929 193 ELAQLSANNRQEL------------ARLRS-----------ELAKKRSQQLDAYLQALRNQlnsqrqreAERALESTELL 249
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1458 QEEAERLRRQVQDESQRKRQAEAEL---ALRVKAEA----EAAREKQRALQALDELRLQAE 1511
Cdd:PRK10929 250 AEQSGDLPKSIVAQFKINRELSQALnqqAQRMDLIAsqqrQAASQTLQVRQALNTLREQSQ 310
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1448-1527 |
7.84e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 7.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1448 EEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELAL----RVKAE--AEAAREKQRALQA-LDELRLQAEEAERRLRQA 1520
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEAqqqeLVALEglAAELEEKQQELEAqLEQLQEKAAETSQERKQK 217
|
....*..
gi 254675251 1521 EAERARQ 1527
Cdd:PRK11448 218 RKEITDQ 224
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1646-1841 |
8.17e-04 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 45.78 E-value: 8.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1646 EQAVRQRELAEQELEKQRQLAEgTAQQRLAA---EQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAEL 1722
Cdd:COG3206 171 EEARKALEFLEEQLPELRKELE-EAEAALEEfrqKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAEARLAALRAQL 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1723 AKVRAEMEVLLASKA--------------RAEEESRSTSEKSK-QRLEAE-AGRFRELAEEAARLRALAEEAKRQRQLAE 1786
Cdd:COG3206 250 GSGPDALPELLQSPViqqlraqlaeleaeLAELSARYTPNHPDvIALRAQiAALRAQLQQEAQRILASLEAELEALQARE 329
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 1787 EDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQ 1841
Cdd:COG3206 330 ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQRLEEARLAEALT 384
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1757-1866 |
8.32e-04 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 45.71 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1757 EAGRFRELAEEAARLRALAEEAKRQRQLAEE--------DAARQRAEAERVLTEKLAAISEATRLKTEAEIA-LKEKEAE 1827
Cdd:PRK11448 130 KPGPFVPPEDPENLLHALQQEVLTLKQQLELqarekaqsQALAEAQQQELVALEGLAAELEEKQQELEAQLEqLQEKAAE 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 254675251 1828 NERLRRLaedeafQRRRLEEQAAlHKADIEERL------AQLRKA 1866
Cdd:PRK11448 210 TSQERKQ------KRKEITDQAA-KRLELSEEEtrilidQQLRKA 247
|
|
| PRK06991 |
PRK06991 |
electron transport complex subunit RsxB; |
1317-1420 |
8.32e-04 |
|
electron transport complex subunit RsxB;
Pssm-ID: 235903 [Multi-domain] Cd Length: 270 Bit Score: 44.79 E-value: 8.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1317 EQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAqelqrRMQEEVARREEAAVDAQQQKRS-IQEELQHLRQSSE 1395
Cdd:PRK06991 149 QAQADAARARHDARQARLRREREAAEARAAARAAASAAA-----AAAEASAAAAPAADDAEAKKRAiIAAALERARKKKE 223
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254675251 1396 ----------------AEIQAkaqQVEAAERSRMRIEEEIR 1420
Cdd:PRK06991 224 elaaqgagpkntegvsAAVQA---QIDAAEARRKRLAEQRD 261
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1476-1818 |
8.35e-04 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 45.71 E-value: 8.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1476 RQAEAELALRVKAEAEAAREKQR--ALQAldelRLQAEEAERRLRQAEAERARQVQValETAQRSAEVELQSKRASFAEK 1553
Cdd:PRK05035 432 RQAKAEIRAIEQEKKKAEEAKARfeARQA----RLEREKAAREARHKKAAEARAAKD--KDAVAAALARVKAKKAAATQP 505
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1554 TAQLERTLQEEHVTVAQLREEaerraqqqaeaerareeaerelerwqlkanealrlRLQAEEVAQQKSLAQADAEKQKEE 1633
Cdd:PRK05035 506 IVIKAGARPDNSAVIAAREAR-----------------------------------KAQARARQAEKQAAAAADPKKAAV 550
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1634 AEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAqqrlaaeqelirlRAETEQGEQQrqlleeelarlqHEATAATQ 1713
Cdd:PRK05035 551 AAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIA-------------RAKAKKAAQQ------------AASAEPEE 605
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1714 KRQELEAELAKVRAEMEVLLASKARAEEESRSTSEkskqrleaeagrfrelaeEAARLRALAEE---AKRQRQLAEEDAA 1790
Cdd:PRK05035 606 QVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEP------------------VDPRKAAVAAAiarAKARKAAQQQANA 667
|
330 340
....*....|....*....|....*...
gi 254675251 1791 RQRAEAERVLTEKLAAISEATRLKTEAE 1818
Cdd:PRK05035 668 EPEEAEDPKKAAVAAAIARAKAKKAAQQ 695
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1672-1827 |
8.53e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.59 E-value: 8.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1672 QRLAAEQELIRlRAETEQGEQQRQLlEEELARLQHEATAATQKRQELEAELAkvraEMEVLLASKARAEEESRSTSEKSK 1751
Cdd:PRK00409 495 KRLGLPENIIE-EAKKLIGEDKEKL-NELIASLEELERELEQKAEEAEALLK----EAEKLKEELEEKKEKLQEEEDKLL 568
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1752 QRLEAEAgrfrelaeEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAE 1827
Cdd:PRK00409 569 EEAEKEA--------QQAIKEAKKEADEIIKELRQLQKGGYASVKAHELIEARKRLNKANEKKEKKKKKQKEKQEE 636
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
1358-1991 |
8.65e-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: 45.48 E-value: 8.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1358 LQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAE 1437
Cdd:pfam05483 79 LYSKLYKEAEKIKKWKVSIEAELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKENNATRHLCN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1438 gELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAElaLRVKAEaeaarekqralQALDELRLQAEEAERRL 1517
Cdd:pfam05483 159 -LLKETCARSAEKTKKYEYEREETRQVYMDLNNNIEKMILAFEE--LRVQAE-----------NARLEMHFKLKEDHEKI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1518 RQAEAERARQV-----QVALETAQrSAEVELQSKRASFaektaqlerTLQEEHVTVAQLREEAERRAQQQAEAERAREEA 1592
Cdd:pfam05483 225 QHLEEEYKKEIndkekQVSLLLIQ-ITEKENKMKDLTF---------LLEESRDKANQLEEKTKLQDENLKELIEKKDHL 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1593 ERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQlaegTAQQ 1672
Cdd:pfam05483 295 TKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLR----TEQQ 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1673 RLaaeqelirlraetEQGEQQRQLLEEELARLQHEATAATQ----KRQELEaELAKVRAEMEVLLASKARAEEESRSTSE 1748
Cdd:pfam05483 371 RL-------------EKNEDQLKIITMELQKKSSELEEMTKfknnKEVELE-ELKKILAEDEKLLDEKKQFEKIAEELKG 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1749 KSKQRLEAEAGRFRELAEEAARLRALaeEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLkteaeialkekeaEN 1828
Cdd:pfam05483 437 KEQELIFLLQAREKEIHDLEIQLTAI--KTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL-------------EN 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1829 ERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGL--VEDTLRQRR--------QVEEEIMALKVS 1898
Cdd:pfam05483 502 KELTQEASDMTLELKKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELesVREEFIQKGdevkckldKSEENARSIEYE 581
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1899 FEKAAAGKAELELELGRIRSNAEDTMRSKEQAELE--------AARQRQLAAEEEQRRREAEERVQRSLAAEE------E 1964
Cdd:pfam05483 582 VLKKEKQMKILENKCNNLKKQIENKNKNIEELHQEnkalkkkgSAENKQLNAYEIKVNKLELELASAKQKFEEiidnyqK 661
|
650 660 670
....*....|....*....|....*....|.
gi 254675251 1965 AARQRKVA----LEEVERLKAKVEEARRLRE 1991
Cdd:pfam05483 662 EIEDKKISeeklLEEVEKAKAIADEAVKLQK 692
|
|
| COG4487 |
COG4487 |
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown]; |
2260-2490 |
8.66e-04 |
|
Uncharacterized conserved protein, contains DUF2130 domain [Function unknown];
Pssm-ID: 443580 [Multi-domain] Cd Length: 425 Bit Score: 45.32 E-value: 8.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2260 QLAEEDLAQQRALAEKMLKEKmqavqeatrlkaEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQR 2339
Cdd:COG4487 18 SLYADIVKQRRAEFEKELAER------------LADAAKREAALELAEAKAKAQLQEQVAEKDAEIAELRARLEAEERKK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2340 QLEMSAEAERlklRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEkvtLVQTLEIQRQQsdhdaerlreaiaE 2419
Cdd:COG4487 86 ALAVAEEKEK---ELAALQEALAEKDAKLAELQAKELELLKKERELEDAKRE---AELTVEKERDE-------------E 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 2420 LEREKEKLKQEAKLLQLKSEEMQTVQQEQILQetqalqksflsekdsllQRERFIEQEKAKLEQLFQDEVA 2490
Cdd:COG4487 147 LDELKEKLKKEEEEKQLAEKSLKVAEYEKQLK-----------------DMQEQIEELKRKKEQGSTQLQG 200
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1458-1782 |
9.30e-04 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 45.24 E-value: 9.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1458 QEEAERLRRQVQDESQRKRQAEAELALRV---------KAEAEAAREKQRALQALDEL-----RLQAEEAERRLRQAEAE 1523
Cdd:pfam02029 4 EEEAARERRRRAREERRRQKEEEEPSGQVtesvepnehNSYEEDSELKPSGQGGLDEEeafldRTAKREERRQKRLQEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1524 RaRQVQVALETAQRSAEVELQSKRASFAE-KTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLK 1602
Cdd:pfam02029 84 E-RQKEFDPTIADEKESVAERKENNEEEEnSSWEKEEKRDSRLGRYKEEETEIREKEYQENKWSTEVRQAEEEGEEEEDK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1603 ANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQEL-I 1681
Cdd:pfam02029 163 SEEAEEVPTENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAeV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1682 RLRAETEQGEQQRQLLEEElarlQHEATAATQKRQELEAELAKVRAEMEVllASKARAEEESRSTSEKSKQRLEAEAGRf 1761
Cdd:pfam02029 243 FLEAEQKLEELRRRRQEKE----SEEFEKLRQKQQEAELELEELKKKREE--RRKLLEEEEQRRKQEEAERKLREEEEK- 315
|
330 340
....*....|....*....|.
gi 254675251 1762 RELAEEAARLRALAEEaKRQR 1782
Cdd:pfam02029 316 RRMKEEIERRRAEAAE-KRQK 335
|
|
| GBP_C |
cd16269 |
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ... |
1317-1418 |
9.32e-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: 44.49 E-value: 9.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1317 EQQRAEERERLAEVEAALEKQRQLAEAHAQAkaqaelEAQELQRRMQEEVARREEaaVDAQQQKRSIQEELQHLRQSSEA 1396
Cdd:cd16269 177 QSKEAEAEAILQADQALTEKEKEIEAERAKA------EAAEQERKLLEEQQRELE--QKLEDQERSYEEHLRQLKEKMEE 248
|
90 100
....*....|....*....|..
gi 254675251 1397 EIQAKAQQVEAAERSRMRIEEE 1418
Cdd:cd16269 249 ERENLLKEQERALESKLKEQEA 270
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
1377-1546 |
9.37e-04 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 45.39 E-value: 9.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1377 QQQKRSIQEELQHLRQSSEAEIQAKAQQVE-----AAERSRM--RIE-EEIRVVRLQLETTerqrgGAEGELQAlRARAE 1448
Cdd:PTZ00491 647 DSLQKSVQLAIEITTKSQEAAARHQAELLEqeargRLERQKMhdKAKaEEQRTKLLELQAE-----SAAVESSG-QSRAE 720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1449 -EAEAQKRQAQEEAErlrrqVQDESQRKRqaeaelALRVKAEAEAAREKQRALQALDELRLQAE---EAERRLRQAEAER 1524
Cdd:PTZ00491 721 aLAEAEARLIEAEAE-----VEQAELRAK------ALRIEAEAELEKLRKRQELELEYEQAQNEleiAKAKELADIEATK 789
|
170 180
....*....|....*....|....*.
gi 254675251 1525 ARQVQVAL--ET--AQRSAEVELQSK 1546
Cdd:PTZ00491 790 FERIVEALgrETliAIARAGPELQAK 815
|
|
| PRK10929 |
PRK10929 |
putative mechanosensitive channel protein; Provisional |
2244-2469 |
1.00e-03 |
|
putative mechanosensitive channel protein; Provisional
Pssm-ID: 236798 [Multi-domain] Cd Length: 1109 Bit Score: 45.43 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2244 EAARLsvAAQEAARLRQLAEE--DLAQQRALAEKMLKE---KMQAVQEATRLKAEAELLQQQKELA-------------- 2304
Cdd:PRK10929 120 EKSRQ--AQQEQDRAREISDSlsQLPQQQTEARRQLNEierRLQTLGTPNTPLAQAQLTALQAESAalkalvdelelaql 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2305 -----QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAE-AERLKLRMAEMSRAQARA----EEDAQRFRKQ 2374
Cdd:PRK10929 198 sannrQELARLRSELAKKRSQQLDAYLQALRNQLNSQRQREAERALEsTELLAEQSGDLPKSIVAQfkinRELSQALNQQ 277
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2375 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQ------SDHDAERLREAIA---------ELERE-----------KEKLK 2428
Cdd:PRK10929 278 AQRMDLIASQQRQAASQTLQVRQALNTLREQsqwlgvSNALGEALRAQVArlpempkpqQLDTEmaqlrvqrlryEDLLN 357
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 254675251 2429 QEAKLLQLKSEEMQ--TVQQEQILQETQALQKSFLSekdSLLQ 2469
Cdd:PRK10929 358 KQPQLRQIRQADGQplTAEQNRILDAQLRTQRELLN---SLLS 397
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
2310-2589 |
1.00e-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: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2310 RLQEDKEQMAQQLVEETQGFQRT--LEAERQRQLE-MSAEAERlklrmAEMSRAQARAEEDAQR--FRKQAEEIGEKLHR 2384
Cdd:TIGR02168 169 KYKERRKETERKLERTRENLDRLedILNELERQLKsLERQAEK-----AERYKELKAELRELELalLVLRLEELREELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2385 TELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQ-----LKSEEMQTVQQEQILQETQALQKS 2459
Cdd:TIGR02168 244 LQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALAneisrLEQQKQILRERLANLERQLEELEA 323
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2460 FLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQ 2539
Cdd:TIGR02168 324 QLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIE 403
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 254675251 2540 HLEQQRQQQEKLLAEENQRLRERLQRLeEEHRAALAHSEIATTQAASTKA 2589
Cdd:TIGR02168 404 RLEARLERLEDRRERLQQEIEELLKKL-EEAELKELQAELEELEEELEEL 452
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3021-3054 |
1.03e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 39.39 E-value: 1.03e-03
10 20 30
....*....|....*....|....*....|....
gi 254675251 3021 LLEAQAGTGHIIDPATSARLTVDEAVRAGLVGPE 3054
Cdd:smart00250 3 LLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPE 36
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
1307-1563 |
1.09e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 44.53 E-value: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1307 RRMEEEERLAEQQRAEERERLAEV-EAALEKQRQLAEAHAQAKAQAELEaqelqrrmqeevarREEAAVDAQQQKRSIQE 1385
Cdd:pfam00038 28 KLLETKISELRQKKGAEPSRLYSLyEKEIEDLRRQLDTLTVERARLQLE--------------LDNLRLAAEDFRQKYED 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1386 ELQhLRQSSEAEIQAKAQQVEAAERSR----MRI--------------EEEIRVVRLQLETTERQ---RGGAEGEL-QAL 1443
Cdd:pfam00038 94 ELN-LRTSAENDLVGLRKDLDEATLARvdleAKIeslkeelaflkknhEEEVRELQAQVSDTQVNvemDAARKLDLtSAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1444 RARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQA-LDELRLQAEEAERRLRQAEA 1522
Cdd:pfam00038 173 AEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIeLQSLKKQKASLERQLAETEE 252
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 254675251 1523 ERARQvqvaLETAQRSaeveLQSKRASFAEKTAQLERTLQE 1563
Cdd:pfam00038 253 RYELQ----LADYQEL----ISELEAELQETRQEMARQLRE 285
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
1060-1745 |
1.12e-03 |
|
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.
Pssm-ID: 432349 [Multi-domain] Cd Length: 1191 Bit Score: 45.60 E-value: 1.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1060 IRSTQGAEEVLKTHEEQLKEAQAVPATLQE-LEATKASLKKLRAQAEAQqpvFNTLRDELRGAQEVG-ERLQQRHGERDV 1137
Cdd:pfam12128 250 FNTLESAELRLSHLHFGYKSDETLIASRQEeRQETSAELNQLLRTLDDQ---WKEKRDELNGELSAAdAAVAKDRSELEA 326
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1138 EVERWRERVTQLLERWQAVLAQTDVRQRELEQLGRQLRYYRESADPLSAWLQDAKRRQEQIQAVPIANCQAAREQLRQEK 1217
Cdd:pfam12128 327 LEDQHGAFLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDIAGIKDKLAKIREAR 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1218 AL-LEEIERHGEKVE-ECQKFAKQYINAIKDYELQLITYKAQL-----EPVASPAKKPKVQSGSESVIQEYVDLRTRYSE 1290
Cdd:pfam12128 407 DRqLAVAEDDLQALEsELREQLEAGKLEFNEEEYRLKSRLGELklrlnQATATPELLLQLENFDERIERAREEQEAANAE 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1291 LTTLTSQYIKFIS---ETLRRMEEEERLAEQQRaeerERLAEVEAALEKQRqlAEAHAQAKAQAELEAQELQRRMQEEVA 1367
Cdd:pfam12128 487 VERLQSELRQARKrrdQASEALRQASRRLEERQ----SALDELELQLFPQA--GTLLHFLRKEAPDWEQSIGKVISPELL 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1368 RREEaaVDAQQQKRSIQEELQ------HLRQ-------SSEAEIQAKAQQVE----AAERSRMRIEEEIRVVRLQLETTE 1430
Cdd:pfam12128 561 HRTD--LDPEVWDGSVGGELNlygvklDLKRidvpewaASEEELRERLDKAEealqSAREKQAAAEEQLVQANGELEKAS 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1431 RQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRalQALDELRLQA 1510
Cdd:pfam12128 639 REETFARTALKNARLDLRRLFDEKQSEKDKKNKALAERKDSANERLNSLEAQLKQLDKKHQAWLEEQK--EQKREARTEK 716
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1511 EEAERRLRQAEAERARQVQVALETAQRSAEVELQS----------KRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQ 1580
Cdd:pfam12128 717 QAYWQVVEGALDAQLALLKAAIAARRSGAKAELKAletwykrdlaSLGVDPDVIAKLKREIRTLERKIERIAVRRQEVLR 796
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1581 QQAEAErareeaerelERWQLkanEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELE 1660
Cdd:pfam12128 797 YFDWYQ----------ETWLQ---RRPRLATQLSNIERAISELQQQLARLIADTKLRRAKLEMERKASEKQQVRLSENLR 863
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1661 KQRQLAEGTAQQRLAAEQElirlRAETEQGEQQRQlLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAE 1740
Cdd:pfam12128 864 GLRCEMSKLATLKEDANSE----QAQGSIGERLAQ-LEDLKLKRDYLSESVKKYVEHFKNVIADHSGSGLAETWESLREE 938
|
....*
gi 254675251 1741 EESRS 1745
Cdd:pfam12128 939 DHYQN 943
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
1310-1493 |
1.19e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 44.94 E-value: 1.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1310 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQH 1389
Cdd:PRK05035 522 AREARKAQARARQAEKQAAAAADPKKAAVAAAIARAKAKKAAQQAANAEAEEEVDPKKAAVAAAIARAKAKKAAQQAASA 601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1390 LRQSSEAEIQAKAQQVEAA-ERSRMRIEEEIRVVRLQLETTERQRggaegELQALRARAEEAEAQKRQAQEEAErlrrqv 1468
Cdd:PRK05035 602 EPEEQVAEVDPKKAAVAAAiARAKAKKAEQQANAEPEEPVDPRKA-----AVAAAIARAKARKAAQQQANAEPE------ 670
|
170 180
....*....|....*....|....*
gi 254675251 1469 QDESQRKRQAEAELAlRVKAEAEAA 1493
Cdd:PRK05035 671 EAEDPKKAAVAAAIA-RAKAKKAAQ 694
|
|
| COG3903 |
COG3903 |
Predicted ATPase [General function prediction only]; |
1585-2014 |
1.28e-03 |
|
Predicted ATPase [General function prediction only];
Pssm-ID: 443109 [Multi-domain] Cd Length: 933 Bit Score: 45.01 E-value: 1.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1585 AERAREEAERELERWQLKANEALRLRLQAEevaqqkSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ 1664
Cdd:COG3903 487 RAAARRRHADYYLALAERAAAELRGPDQLA------WLARLDAEHDNLRAALRWALAHGDAELALRLAAALAPFWFLRGL 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1665 LAEGT--AQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1742
Cdd:COG3903 561 LREGRrwLERALAAAGEAAAALAAAAALAAAAAAARAAAAAAAAAAAAAAAAAAAAAAAAAALLLLAALAAAAAAAAAAA 640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1743 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1822
Cdd:COG3903 641 AAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAALAAAAAALAAAAAAAALAAAAAAALAAAAAAAAA 720
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1823 EKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKA 1902
Cdd:COG3903 721 AAAAAALLAAAAAAALAAAAAAAALALAAAAAAAAAAAAAAALAAAAAAAALAALLLALAAAAAALAAAAAAAAAAAAAA 800
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1903 AAGKAELELELGRIRSNAEDTMRSKEQAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEEVERLKAK 1982
Cdd:COG3903 801 AAAAAAAAAAAAAAALAAAAAAAAAAAAALAAALAAAAAAAAAAAAAAAAAAALAAALAAAAAAAAAAALAAAAAAAAAA 880
|
410 420 430
....*....|....*....|....*....|..
gi 254675251 1983 VEEARRLRERAEQESARQLQLAQEAAQKRLQA 2014
Cdd:COG3903 881 AAALLAAAAAAAAAAAAAAAAAAALAAAAAAA 912
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1308-1495 |
1.32e-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: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1308 RMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAqakaqaELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEEL 1387
Cdd:pfam05262 206 RESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNA------DKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQ 279
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1388 QHLRQSSEAEIQAKAQQVEAAERsrmrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQKRqaQEEAERLRRQ 1467
Cdd:pfam05262 280 KREIEKAQIEIKKNDEEALKAKD-------------------------HKAFDLKQESKASEKEAEDK--ELEAQKKREP 332
|
170 180
....*....|....*....|....*....
gi 254675251 1468 VQDESQR-KRQAEAElalrVKAEAEAARE 1495
Cdd:pfam05262 333 VAEDLQKtKPQVEAQ----PTSLNEDAID 357
|
|
| HMMR_N |
pfam15905 |
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ... |
2123-2430 |
1.34e-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: 44.42 E-value: 1.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2123 KQKQAADAEMEKHKkfaeqtlrqkaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQM 2202
Cdd:pfam15905 63 KKSQKNLKESKDQK-----------ELEKEIRALVQERGEQDKRLQALEEELEKVEAKLNAAVREKTSLSASVASLEKQL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2203 EELGKLKArieaenralILRDKdntqrFLEEEAEKmkqvaeeaaRLSVAAQEAARLRQLAEEDLAQQRALAEKMLKeKMQ 2282
Cdd:pfam15905 132 LELTRVNE---------LLKAK-----FSEDGTQK---------KMSSLSMELMKLRNKLEAKMKEVMAKQEGMEG-KLQ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2283 AVQeaTRLKAEAELLQQQKELAQEQARRLQEDKEQmAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQA 2362
Cdd:pfam15905 188 VTQ--KNLEHSKGKVAQLEEKLVSTEKEKIEEKSE-TEKLLEYITELSCVSEQVEKYKLDIAQLEELLKEKNDEIESLKQ 264
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 2363 RAEEDAQRFRKQAEEIGEKLhrtELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQE 2430
Cdd:pfam15905 265 SLEEKEQELSKQIKDLNEKC---KLLESEKEELLREYEEKEQTLNAELEELKEKLTLEEQEHQKLQQK 329
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
2077-2398 |
1.40e-03 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 44.95 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2077 EEAERLKQSAEEQAQAQAQAQAAAEKLRKEAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQ-TLRQKAQVEQELTT 2155
Cdd:COG5185 272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQLAAAEAEQELEESKRETETgIQNLTAEIEQGQES 351
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2156 LRLQLEETDHQKSILDEElqrlkaevteaaRQRSQVEEELFSVRVQMEElgkLKARIEAENRALilrdKDNTQRFLEEEA 2235
Cdd:COG5185 352 LTENLEAIKEEIENIVGE------------VELSKSSEELDSFKDTIES---TKESLDEIPQNQ----RGYAQEILATLE 412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2236 EKMKQVAEEAARLSVAaqeaarLRQLAEEDLAQQRAL--AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEqARRLQE 2313
Cdd:COG5185 413 DTLKAADRQIEELQRQ------IEQATSSNEEVSKLLneLISELNKVMREADEESQSRLEEAYDEINRSVRSK-KEDLNE 485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2314 DKEQMAQQLVEETQGFQrTLEAERQRQLE-----MSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELA 2388
Cdd:COG5185 486 ELTQIESRVSTLKATLE-KLRAKLERQLEgvrskLDQVAESLKDFMRARGYAHILALENLIPASELIQASNAKTDGQAAN 564
|
330
....*....|
gi 254675251 2389 TQEKVTLVQT 2398
Cdd:COG5185 565 LRTAVIDELT 574
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1686-1818 |
1.44e-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: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1686 ETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELA 1765
Cdd:pfam05262 207 ESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKA 286
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1766 EEAARLRA-------------LAEEAKRQRQLAEEDAARQRAEAERVlTEKLAAISEATRLKTEAE 1818
Cdd:pfam05262 287 QIEIKKNDeealkakdhkafdLKQESKASEKEAEDKELEAQKKREPV-AEDLQKTKPQVEAQPTSL 351
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
1647-2558 |
1.49e-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: 45.04 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1647 QAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVR 1726
Cdd:TIGR00606 200 QKVQEHQMELKYLKQYKEKACEIRDQITSKEAQLESSREIVKSYENELDPLKNRLKEIEHNLSKIMKLDNEIKA-LKSRK 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1727 AEMEVLLASKARAEEESRSTSEKSKQRLEAEAGR-FRELAEEAARLRALAEEAKRQRQLAEEDAA-------RQRAEAER 1798
Cdd:TIGR00606 279 KQMEKDNSELELKMEKVFQGTDEQLNDLYHNHQRtVREKERELVDCQRELEKLNKERRLLNQEKTellveqgRLQLQADR 358
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1799 VLTEKLAAISEATRLKTEAEIALKEKEAENERlrRLAEDEAFQRRRLEEQA---ALHKADIEERLAQLRKASESELERQK 1875
Cdd:TIGR00606 359 HQEHIRARDSLIQSLATRLELDGFERGPFSER--QIKNFHTLVIERQEDEAktaAQLCADLQSKERLKQEQADEIRDEKK 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1876 GLVEDTLRQRRQVEEEIMALKVSFEK----AAAGKAELELELGRIRSNAeDTMRSKEQAELEAARQRQLAAEEEQRRREA 1951
Cdd:TIGR00606 437 GLGRTIELKKEILEKKQEELKFVIKElqqlEGSSDRILELDQELRKAER-ELSKAEKNSLTETLKKEVKSLQNEKADLDR 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1952 EERvqrSLAAEEEAARQRKVALEEVERL-KAKVEEARRLRERAEQESARQLQLAQEAAQKRlQAEEKAHAF-----VVQQ 2025
Cdd:TIGR00606 516 KLR---KLDQEMEQLNHHTTTRTQMEMLtKDKMDKDEQIRKIKSRHSDELTSLLGYFPNKK-QLEDWLHSKskeinQTRD 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2026 REEELQQTLQQEQNMLDRLRSEAEAARRAAEEAEEAREQAEREAAQSRKQVEEAERLKQSAEEQAQAQAQAQAAAEKLRK 2105
Cdd:TIGR00606 592 RLAKLNKELASLEQNKNHINNELESKEEQLSSYEDKLFDVCGSQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQ 671
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2106 EAEQEAARRAQAEQAALKQKQAADAEMEKHKKFAEQTLRQKaQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAA 2185
Cdd:TIGR00606 672 LTDENQSCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLK-STESELKKKEKRRDEMLGLAPGRQSIIDLKEKEIPELR 750
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2186 RQRSQVEEELFSVRVQMEELGKLKARIEAENRA--LILRDKDNTQRFLEEEAEKMKQVAEEAARL-----SVAAQEAARL 2258
Cdd:TIGR00606 751 NKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESakVCLTDVTIMERFQMELKDVERKIAQQAAKLqgsdlDRTVQQVNQE 830
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2259 RQLAEEDL---AQQRALAEKMLKEKMQAVQEatrLKAEAELLQQQKELAQEQARRLQedkeQMAQQLVEETQGFQRTLEA 2335
Cdd:TIGR00606 831 KQEKQHELdtvVSKIELNRKLIQDQQEQIQH---LKSKTNELKSEKLQIGTNLQRRQ----QFEEQLVELSTEVQSLIRE 903
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2336 ERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQT-LEIQRQQSDHDAERLR 2414
Cdd:TIGR00606 904 IKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHGYMKDIENKIQDgKDDYLKQKETELNTVN 983
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2415 EAIAELEREKEKLKQEAKLLQLKSEEMQtvQQEQILQETQALQKsfLSEKDSLLQRERfieqeKAKLEQLFQDEVAKAKQ 2494
Cdd:TIGR00606 984 AQLEECEKHQEKINEDMRLMRQDIDTQK--IQERWLQDNLTLRK--RENELKEVEEEL-----KQHLKEMGQMQVLQMKQ 1054
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 2495 LReeqqrqqqqmeqekQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQR 2558
Cdd:TIGR00606 1055 EH--------------QKLEENIDLIKRNHVLALGRQKGYEKEIKHFKKELREPQFRDAEEKYR 1104
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1297-1475 |
1.51e-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: 44.14 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1297 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVAR---REEAA 1373
Cdd:pfam13868 159 EYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKarqRQELQ 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1374 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLeTTERQRGGAEGELQALRARAEEAEAQ 1453
Cdd:pfam13868 239 QAREEQIELKERRLAEEAEREEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEH-RRELEKQIEEREEQRAAEREEELEEG 317
|
170 180
....*....|....*....|..
gi 254675251 1454 KRQAQEEAERLRRqVQDESQRK 1475
Cdd:pfam13868 318 ERLREEEAERRER-IEEERQKK 338
|
|
| CH_FIMB_rpt1 |
cd21294 |
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar ... |
6-109 |
1.53e-03 |
|
first calponin homology (CH) domain found in Saccharomyces cerevisiae fimbrin and similar proteins; Fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409143 Cd Length: 125 Bit Score: 41.66 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 6 DERDRVQkktFTKWVNK---------HLIKAQRHISDLYEDLRDGHNLISLLEvlsgDSLP-------------REKGRM 63
Cdd:cd21294 4 NEDERRE---FTKHINAvlagdpdvgSRLPFPTDTFQLFDECKDGLVLSKLIN----DSVPdtidervlnkpprKNKPLN 76
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 254675251 64 RFHKLQNVQIALDYLRHRQVKLVNIRNDDIADGNPKLTLGLIWTII 109
Cdd:cd21294 77 NFQMIENNNIVINSAKAIGCSVVNIGAGDIIEGREHLILGLIWQII 122
|
|
| Tektin |
pfam03148 |
Tektin family; Tektins are cytoskeletal proteins. They have been demonstrated in such cellular ... |
1660-1935 |
1.61e-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: 44.08 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1660 EKQRQLAEgtaQQRLAAE---QELIRLRAETEQGEQQRQllEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASK 1736
Cdd:pfam03148 6 QELYREAE---AQRNDAErlrQESRRLRNETDAKTKWDQ--YDSNRRLGERIQDITFWKSELEKELEELDEEIELLLEEK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1737 ARAEEESRSTSEK---SKQRLEAEAGRF----------RELAEEA-------ARLRALAEEAkrQRQLAEEDAARQRAEA 1796
Cdd:pfam03148 81 RRLEKALEALEEPlhiAQECLTLREKRQgidlvhdeveKELLKEVeliegiqELLQRTLEQA--WEQLRLLRAARHKLEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1797 ErvLTEKLAAI---SEATRLK-TEAEIALKEKEAENERLRRLAED-EAFQRRRLEE-QAALHK-ADIEERLAQLRKASES 1869
Cdd:pfam03148 159 D--LSDKKEALeidEKCLSLNnTSPNISYKPGPTRIPPNSSTPEEwEKFTQDNIERaEKERAAsAQLRELIDSILEQTAN 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1870 ELERQKGLVEDTLRQRrqVEEEIMAlkvsfekaaagKAELELELGRIRSNAEDTmrSKEQAELEAA 1935
Cdd:pfam03148 237 DLRAQADAVNFALRKR--IEETEDA-----------KNKLEWQLKKTLQEIAEL--EKNIEALEKA 287
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1440-1529 |
1.62e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.82 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1440 LQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELalrvKAEAEaarekQRALQALDELRLQAEEAERRLRQ 1519
Cdd:PRK00409 525 LEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKL----LEEAE-----KEAQQAIKEAKKEADEIIKELRQ 595
|
90
....*....|
gi 254675251 1520 AEAERARQVQ 1529
Cdd:PRK00409 596 LQKGGYASVK 605
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1685-1812 |
1.66e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 44.69 E-value: 1.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1685 AETEQGEQQRQLLEEELARLQHEATAATQKR-QELEAELAKVRAEMEVLLAsKARAEEESRSTSEKSKQRLEAEAGRFRE 1763
Cdd:COG0542 411 EELDELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKA-RWEAEKELIEEIQELKEELEQRYGKIPE 489
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1764 LAEEAARLRALAEEAKRQRQLA--EEDAAR-------------QRAEAERVLT-------------EKLAAISEATR 1812
Cdd:COG0542 490 LEKELAELEEELAELAPLLREEvtEEDIAEvvsrwtgipvgklLEGEREKLLNleeelhervigqdEAVEAVADAIR 566
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
1642-1823 |
1.69e-03 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 44.46 E-value: 1.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1642 GKAEEQAVRQRELAEQELEKQRQLAEGTAQQR-LAAEQELIRLRAEteqgeqQRQLLEEELARLQHEATAATQKRQELEA 1720
Cdd:COG2433 375 GLSIEEALEELIEKELPEEEPEAEREKEHEEReLTEEEEEIRRLEE------QVERLEAEVEELEAELEEKDERIERLER 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1721 ELAKVRAEMEvllaSKARAEEESRstsekskqRLEAEAGRF-RELAEEAARLRALAEEAKRQRQLAEEDaarqrAEAERV 1799
Cdd:COG2433 449 ELSEARSEER----REIRKDREIS--------RLDREIERLeRELEEERERIEELKRKLERLKELWKLE-----HSGELV 511
|
170 180
....*....|....*....|....
gi 254675251 1800 LTEKLAAISEATRLKTEAEIALKE 1823
Cdd:COG2433 512 PVKVVEKFTKEAIRRLEEEYGLKE 535
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1755-1879 |
1.73e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 44.48 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1755 EAEAGRFRELA-EEAARLRALAEEAKRQ----RQLAEEDAA--------RQRAEAERVLTEKLAAISEAtrlKTEAEIAL 1821
Cdd:COG2268 205 EAEAERETEIAiAQANREAEEAELEQEReietARIAEAEAElakkkaeeRREAETARAEAEAAYEIAEA---NAEREVQR 281
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1822 KEKEAENERLRRLAEDEAfQRRRLEEQAALHK-ADIEERLAQLRKASESELERQKGLVE 1879
Cdd:COG2268 282 QLEIAEREREIELQEKEA-EREEAELEADVRKpAEAEKQAAEAEAEAEAEAIRAKGLAE 339
|
|
| COG5283 |
COG5283 |
Phage-related tail protein [Mobilome: prophages, transposons]; |
1604-1826 |
1.73e-03 |
|
Phage-related tail protein [Mobilome: prophages, transposons];
Pssm-ID: 444094 [Multi-domain] Cd Length: 747 Bit Score: 44.46 E-value: 1.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1604 NEALRLRLQ-AEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQ--LAEGTAQQRLAAEQEl 1680
Cdd:COG5283 9 DKPFKSALEsAKQRVAALAQALKALEAPTRALARALERAKQAAARLQTKYNKLRQSLQRLRQalDQAGIDTRQLSAAQR- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1681 iRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAeLAKVRAEME-----VLLASKARAEEESRSTSEKSKQRLE 1755
Cdd:COG5283 88 -RLRSSLEQTNRQLERQQQRLARLGARQDRLKAARARLQR-LAGAGAAAAaigaaLAASVKPAIDFEDAMADVAATVDLD 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1756 AEAGRFRELAEEA----ARLRALAEE-AKRQRQLAEEDAARQRAEAervLTEKLAAISEATRLKTE--AEIALKEKEA 1826
Cdd:COG5283 166 KSSEQFKALGKQArelsAQTPQSADDiAAGQAALAQAGVSAEDILA---FTPTAAKLATAFDTDAEeaAEIAAKILNA 240
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
2146-2523 |
1.75e-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: 1.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2146 KAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVteaarqrSQVEEELFSVRVQMEELGKLKARIEAENRALILRDKD 2225
Cdd:pfam07888 54 NRQREKEKERYKRDREQWERQRRELESRVAELKEEL-------RQSREKHEELEEKYKELSASSEELSEEKDALLAQRAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2226 NTQRFLEEE---AEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLkekmQAVQEATRLKAEAELLQQQKE 2302
Cdd:pfam07888 127 HEARIRELEediKTLTQRVLERETELERMKERAKKAGAQRKEEEAERKQLQAKLQ----QTEEELRSLSKEFQELRNSLA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2303 LAQEQARRLQEDKEQMAQQLveeTQGFQRTLEAER--------QRQLEMSAE-AERLKLRMAEMSRAQARAEEDAQRFRK 2373
Cdd:pfam07888 203 QRDTQVLQLQDTITTLTQKL---TTAHRKEAENEAlleelrslQERLNASERkVEGLGEELSSMAAQRDRTQAELHQARL 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2374 QAEEIGEKLHRTELATQE-KVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAkllqlkseemqtvqqeqilQE 2452
Cdd:pfam07888 280 QAAQLTLQLADASLALREgRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEER-------------------ME 340
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 2453 TQALQKSFLSEKDS----LLQRERFIEQEKAKLeQLFQDEvakakqlreeqqrqQQQMEQEKQELMASMEEARRR 2523
Cdd:pfam07888 341 REKLEVELGREKDCnrvqLSESRRELQELKASL-RVAQKE--------------KEQLQAEKQELLEYIRQLEQR 400
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
2290-2583 |
1.76e-03 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 1.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2290 LKAEAELLQQQKELAQEQARRLQEdKEQMAQQLVEETQGFQRTLEAERqrqlEMSAEAERLKLRMAEmsraqaraeedaq 2369
Cdd:pfam01576 7 MQAKEEELQKVKERQQKAESELKE-LEKKHQQLCEEKNALQEQLQAET----ELCAEAEEMRARLAA------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2370 rfRKQaeEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvqqEQI 2449
Cdd:pfam01576 69 --RKQ--ELEEILHELESRLEEEEERSQQLQNEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAKIKKLE----EDI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2450 LqetqalqksFLSEKDSLLQRER-FIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQmeqekqelMASMEEARRRQ---R 2525
Cdd:pfam01576 141 L---------LLEDQNSKLSKERkLLEERISEFTSNLAEEEEKAKSLSKLKNKHEAM--------ISDLEERLKKEekgR 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 2526 EAEEGVRRKQEELQHLEQQRQQQEKLLAEEnqrLRERLQRLEEEHRAALAHSEIATTQ 2583
Cdd:pfam01576 204 QELEKAKRKLEGESTDLQEQIAELQAQIAE---LRAQLAKKEEELQAALARLEEETAQ 258
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1297-1491 |
1.80e-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: 44.14 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1297 QYIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEevarreeaavda 1376
Cdd:pfam13868 156 RILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKE------------ 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1377 QQQKRSIQEELQHLRQSSEAEIQAKAQQvEAAERSRMRIEEEiRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQ 1456
Cdd:pfam13868 224 REEAEKKARQRQELQQAREEQIELKERR-LAEEAEREEEEFE-RMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEE 301
|
170 180 190
....*....|....*....|....*....|....*
gi 254675251 1457 AQEEAERLRRQVQDESQRKRQAEAELALRVKAEAE 1491
Cdd:pfam13868 302 REEQRAAEREEELEEGERLREEEAERRERIEEERQ 336
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
1610-1780 |
1.83e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 44.30 E-value: 1.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1610 RLQAEEVAQQKSLA-QADAE-KQKEEAEREARRRGkaEEQAVRQRELA---------EQELEKQRQLAEGTAQQRLAAEQ 1678
Cdd:PRK11637 114 KLEQQQAAQERLLAaQLDAAfRQGEHTGLQLILSG--EESQRGERILAyfgylnqarQETIAELKQTREELAAQKAELEE 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1679 ELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEESRSTSEkskqrleaea 1758
Cdd:PRK11637 192 KQSQQKTLLYEQQAQQQKLEQARNERKKTLTGLESSLQKDQQQLSELRANESRLRDSIARAEREAKARAE---------- 261
|
170 180
....*....|....*....|..
gi 254675251 1759 grfRElAEEAARLRALAEEAKR 1780
Cdd:PRK11637 262 ---RE-AREAARVRDKQKQAKR 279
|
|
| tolA_full |
TIGR02794 |
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ... |
2172-2380 |
1.84e-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: 44.07 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2172 EELQRLKAEVTEAARQRSQVEEELfsvRVQMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKM-----KQVAEEAA 2246
Cdd:TIGR02794 50 QQANRIQQQKKPAAKKEQERQKKL---EQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQaeekqKQAEEAKA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2247 RLS---VAAQEAARLRQLAEEdlAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLV 2323
Cdd:TIGR02794 127 KQAaeaKAKAEAEAERKAKEE--AAKQAEEEAKAKAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKA-EEAKAKAEAAKA 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 2324 EETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGE 2380
Cdd:TIGR02794 204 KAAAEAAAKAEAEAAAAAAAEAERKADEAELGDIFGLASGSNAEKQGGARGAAAGSE 260
|
|
| PspC_subgroup_1 |
NF033838 |
pneumococcal surface protein PspC, choline-binding form; The pneumococcal surface protein PspC, ... |
1364-1848 |
1.86e-03 |
|
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: 44.62 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1364 EEVARREEAAVDAQQQK--RSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEG-EL 1440
Cdd:NF033838 53 NESQKEHAKEVESHLEKilSEIQKSLDKRKHTQNVALNKKLSDIKTEYLYELNVLKEKSEAELTSKTKKELDAAFEQfKK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1441 QALRARAEEAEAQK------RQAQEEAERLRRQVQDESQRKRQAE-AELALRVKaEAEAAREKQRALQALDELRLQAEEA 1513
Cdd:NF033838 133 DTLEPGKKVAEATKkveeaeKKAKDQKEEDRRNYPTNTYKTLELEiAESDVEVK-KAELELVKEEAKEPRDEEKIKQAKA 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1514 ERRLRQAEAERARQVQVALETAQRSAEvelqskrasfaektaqlertlqeehvtvaqlreeaerraqqqaeaerareeae 1593
Cdd:NF033838 212 KVESKKAEATRLEKIKTDREKAEEEAK----------------------------------------------------- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1594 relERWQLKANEALRLRLQAEEVAQQKSLAQADAeKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEgtAQQR 1673
Cdd:NF033838 239 ---RRADAKLKEAVEKNVATSEQDKPKRRAKRGV-LGEPATPDKKENDAKSSDSSVGEETLPSPSLKPEKKVAE--AEKK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1674 LAAEQElirlRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEmevllasKARAEEESRSTSEKSKQR 1753
Cdd:NF033838 313 VEEAKK----KAKDQKEEDRRNYPTNTYKTLELEIAESDVKVKEAELELVKEEAK-------EPRNEEKIKQAKAKVESK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1754 LeAEAGRFrelaeeaarlralaEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRR 1833
Cdd:NF033838 382 K-AEATRL--------------EKIKTDRKKAEEEAKRKAAEEDKVKEKPAEQPQPAPAPQPEKPAPKPEKPAEQPKAEK 446
|
490
....*....|....*..
gi 254675251 1834 LAEDEAFQ--RRRLEEQ 1848
Cdd:NF033838 447 PADQQAEEdyARRSEEE 463
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1317-1424 |
1.89e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 44.43 E-value: 1.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1317 EQQRAEERERLAEVEAAL-----------EKQRQLAEAHAQAKAQAELEAQELQRRMQEEVA------RREEAAVDAQQQ 1379
Cdd:PRK00409 526 EELERELEQKAEEAEALLkeaeklkeeleEKKEKLQEEEDKLLEEAEKEAQQAIKEAKKEADeiikelRQLQKGGYASVK 605
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 254675251 1380 KRSIQEELQHLRQSSeaEIQAKAQQVEAAERSRMRIEEEIRVVRL 1424
Cdd:PRK00409 606 AHELIEARKRLNKAN--EKKEKKKKKQKEKQEELKVGDEVKYLSL 648
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2174-2387 |
1.96e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 44.03 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2174 LQRLKAEVTEAARQRSQVEEElfsvrvQMEELGKLKARIEAENRALilrdkdNTQRFLEEEAEKMkqvAEEAARLSVAAQ 2253
Cdd:PRK09510 67 QQQQQKSAKRAEEQRKKKEQQ------QAEELQQKQAAEQERLKQL------EKERLAAQEQKKQ---AEEAAKQAALKQ 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2254 eaarlrQLAEEDLAQQRALAEKMLKEKMQAVQEATRlKAEAELLQQQKELAQEQAR-RLQEDKEQMAQQLVEETQGFQRT 2332
Cdd:PRK09510 132 ------KQAEEAAAKAAAAAKAKAEAEAKRAAAAAK-KAAAEAKKKAEAEAAKKAAaEAKKKAEAEAAAKAAAEAKKKAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 2333 LEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTEL 2387
Cdd:PRK09510 205 AEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKAAAEV 259
|
|
| PLN02939 |
PLN02939 |
transferase, transferring glycosyl groups |
2139-2387 |
1.96e-03 |
|
transferase, transferring glycosyl groups
Pssm-ID: 215507 [Multi-domain] Cd Length: 977 Bit Score: 44.51 E-value: 1.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2139 AEQTLRQKAQVEQELTTLRLQLEETDHQK----------SILDEELQRLKAEVT-EAARQRSQVEEELFSVRVQMEELGK 2207
Cdd:PLN02939 158 LEKILTEKEALQGKINILEMRLSETDARIklaaqekihvEILEEQLEKLRNELLiRGATEGLCVHSLSKELDVLKEENML 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2208 LKARIEAENRALI-LRDKDNTQRFLEEEAEKMK-QVAEEAARLSVAAQEAARLRQLaeedlaQQRALAEKMlkEKMQAVQ 2285
Cdd:PLN02939 238 LKDDIQFLKAELIeVAETEERVFKLEKERSLLDaSLRELESKFIVAQEDVSKLSPL------QYDCWWEKV--ENLQDLL 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2286 EATRLKAE--AELLQQQKELaqeqarrlqEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQAR 2363
Cdd:PLN02939 310 DRATNQVEkaALVLDQNQDL---------RDKVDKLEASLKEANVSKFSSYKVELLQQKLKLLEERLQASDHEIHSYIQL 380
|
250 260
....*....|....*....|....
gi 254675251 2364 AEEDAQRFRKQAEEIGEKLHRTEL 2387
Cdd:PLN02939 381 YQESIKEFQDTLSKLKEESKKRSL 404
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
2139-2317 |
1.97e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 44.24 E-value: 1.97e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2139 AEQTLRQKAQVEQELTTLRLQLEETDHQKSILDEELQRLKAEVTEAarQRSQVEEELFSVRVQME-ELGKLKARIEAENR 2217
Cdd:COG3206 214 AKLLLQQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEL--LQSPVIQQLRAQLAELEaELAELSARYTPNHP 291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2218 ALilrdkdntQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELL 2297
Cdd:COG3206 292 DV--------IALRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVA 363
|
170 180
....*....|....*....|
gi 254675251 2298 QQQKELAQEQARRLQEDKEQ 2317
Cdd:COG3206 364 RELYESLLQRLEEARLAEAL 383
|
|
| PRK07353 |
PRK07353 |
F0F1 ATP synthase subunit B'; Validated |
1307-1388 |
2.04e-03 |
|
F0F1 ATP synthase subunit B'; Validated
Pssm-ID: 235999 [Multi-domain] Cd Length: 140 Bit Score: 41.53 E-value: 2.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1307 RRMEEEERLAEQQRAEERERLAEVEA-ALEKQRQLAEAHAQAK---AQAELEAQELQRR-----MQEEVARREEAAVDAQ 1377
Cdd:PRK07353 32 KVVEEREDYIRTNRAEAKERLAEAEKlEAQYEQQLASARKQAQaviAEAEAEADKLAAEalaeaQAEAQASKEKARREIE 111
|
90
....*....|.
gi 254675251 1378 QQKRSIQEELQ 1388
Cdd:PRK07353 112 QQKQAALAQLE 122
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2201-2499 |
2.09e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 43.75 E-value: 2.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2201 QMEELGKLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEK 2280
Cdd:pfam13868 27 QIAEKKRIKAEEKEEERRLDEMMEEERERALEEEEEKEEERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2281 MQAVQEATRLKAEAELLQQQKELA--QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMS 2358
Cdd:pfam13868 107 VERIQEEDQAEAEEKLEKQRQLREeiDEFNEEQAEWKELEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREI 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2359 RAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQlks 2438
Cdd:pfam13868 187 ARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKERRLAEEAEREEEEF--- 263
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 2439 EEMQTVQQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQ 2499
Cdd:pfam13868 264 ERMLRKQAEDEEIEQEEAEKRRMKRLEHRRELEKQIEEREEQRAAEREEELEEGERLREEE 324
|
|
| ATAD3_N |
pfam12037 |
ATPase family AAA domain-containing protein 3, N-terminal; This is the conserved N-terminal ... |
1643-1783 |
2.15e-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: 43.43 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1643 KAEEQaVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEA-- 1720
Cdd:pfam12037 52 KKQEQ-TRQAELQAKIKEYEAAQEQLKIERQRVEYEERRKTLQEETKQKQQRAQYQDELARKRYQDQLEAQRRRNEELlr 130
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 1721 ---ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEA-GRFRELAE-EAARLRALAEEAKRQRQ 1783
Cdd:pfam12037 131 kqeESVAKQEAMRIQAQRRQTEEHEAELRRETERAKAEAEAeARAKEEREnEDLNLEQLREKANEERE 198
|
|
| PLEC |
smart00250 |
Plectin repeat; |
2730-2766 |
2.15e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 38.62 E-value: 2.15e-03
10 20 30
....*....|....*....|....*....|....*..
gi 254675251 2730 KLLSAERAVTGYKDPYTGEQISLFQAMKKDLIVRDHG 2766
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLIDPETG 38
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
2143-2440 |
2.17e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 44.51 E-value: 2.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2143 LRQKAQVEQ-ELTTLRLQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVRVQMEELGKLKARIeaenralil 2221
Cdd:PRK01156 188 LEEKLKSSNlELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRYESEI--------- 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2222 RDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQK 2301
Cdd:PRK01156 259 KTAESDLSMELEKNNYYKELEERHMKIINDPVYKNRNYINDYFKYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2302 ELAQEQARRLQEDKEQMAQQLVEET--QGFQRTLEAERQRQLEMSAEAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIG 2379
Cdd:PRK01156 339 NDYIKKKSRYDDLNNQILELEGYEMdyNSYLKSIESLKKKIEEYSKNIERMS---AFISEILKIQEIDPDAIKKELNEIN 415
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2380 EKLHR--TELAT--QEKVTLVQTL-EIQR--------------------QQSDH-------DAERLREAIAELEREKEKL 2427
Cdd:PRK01156 416 VKLQDisSKVSSlnQRIRALRENLdELSRnmemlngqsvcpvcgttlgeEKSNHiinhyneKKSRLEEKIREIEIEVKDI 495
|
330
....*....|...
gi 254675251 2428 KQEAKllQLKSEE 2440
Cdd:PRK01156 496 DEKIV--DLKKRK 506
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1307-1477 |
2.18e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 44.12 E-value: 2.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1307 RRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAElEAQELQRRMQEEVARREEAAVDAQQQKRSIQEE 1386
Cdd:PRK12678 78 RRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPE-AAQARERRERGEAARRGAARKAGEGGEQPATEA 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1387 LQHLRQSSEAEIQAKAQQVEAAERSRMRieeeiRVVRLQLETTERQRGGaEGELQALRARAEEAEAQKRQAQEEAERLRR 1466
Cdd:PRK12678 157 RADAAERTEEEERDERRRRGDREDRQAE-----AERGERGRREERGRDG-DDRDRRDRREQGDRREERGRRDGGDRRGRR 230
|
170
....*....|.
gi 254675251 1467 QVQDESQRKRQ 1477
Cdd:PRK12678 231 RRRDRRDARGD 241
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
2238-2437 |
2.27e-03 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.99 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2238 MKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLQEDKE- 2316
Cdd:COG4717 48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQl 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2317 ----QMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEK 2392
Cdd:COG4717 128 lplyQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQR 207
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 254675251 2393 vtlVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLK 2437
Cdd:COG4717 208 ---LAELEEELEEAQEELEELEEELEQLENELEAAALEERLKEAR 249
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1789-2011 |
2.27e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 43.60 E-value: 2.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1789 AARQRAEAERVLTEKLAAISEATRLKTEAEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEErLAQLRKASE 1868
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAE-LEKEIAELR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1869 SELERQKGLVEDTLRQR-RQVEEEIMALKVSFEKAAAGKAELEL--ELGRIRSNAEDTMRsKEQAELEAARQRQLAAEEE 1945
Cdd:COG4942 97 AELEAQKEELAELLRALyRLGRQPPLALLLSPEDFLDAVRRLQYlkYLAPARREQAEELR-ADLAELAALRAELEAERAE 175
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1946 QRRREAEERVQRSLAAEEEAARQRKVALEEvERLKAKVEEARRLRERAEQESARQLQLAQEAAQKR 2011
Cdd:COG4942 176 LEALLAELEEERAALEALKAERQKLLARLE-KELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
1646-1789 |
2.33e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.84 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1646 EQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKV 1725
Cdd:pfam05262 209 QEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQEAKNLPKPADTSSPKEDKQVAENQKREIEKAQI 288
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 254675251 1726 RAEM---EVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDA 1789
Cdd:pfam05262 289 EIKKndeEALKAKDHKAFDLKQESKASEKEAEDKELEAQKKREPVAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
1852-2269 |
2.38e-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: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1852 HKADIEERLAQlRKASESELERQKGLVEDTLRQ---RRQVEEEIMALKVSFEKAAAGKAELElelgrirsnaedTMRSKE 1928
Cdd:pfam17380 280 HQKAVSERQQQ-EKFEKMEQERLRQEKEEKAREverRRKLEEAEKARQAEMDRQAAIYAEQE------------RMAMER 346
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1929 QAELEAARQRQLAAeeeqrrreaeervqrslaaEEEAARQRKVALE-----EVERLKAKvEEARRLRERAEQESARQLQL 2003
Cdd:pfam17380 347 ERELERIRQEERKR-------------------ELERIRQEEIAMEisrmrELERLQME-RQQKNERVRQELEAARKVKI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2004 AQEAAQKRLQAEEKAHAFVvqqreeelqqtlqqeqnmldrlrseaeaarraaeeaeeareqaereaaqsRKQVEEAERlk 2083
Cdd:pfam17380 407 LEEERQRKIQQQKVEMEQI--------------------------------------------------RAEQEEARQ-- 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2084 qsaeeqaqaqaqaqaaaEKLRKEAEQEAARRAQAEQAALKQKQaadaEMEKHKKFAEQTLRQKAQVEQElttLRLQLEET 2163
Cdd:pfam17380 435 -----------------REVRRLEEERAREMERVRLEEQERQQ----QVERLRQQEEERKRKKLELEKE---KRDRKRAE 490
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2164 DHQKSILDEELQRLKAEVTEAARQRSQVEEElfsvrvqMEELGKlkaRIEAENRALILRDKDNTQRFLEEE---AEKMKQ 2240
Cdd:pfam17380 491 EQRRKILEKELEERKQAMIEEERKRKLLEKE-------MEERQK---AIYEEERRREAEEERRKQQEMEERrriQEQMRK 560
|
410 420
....*....|....*....|....*....
gi 254675251 2241 VAEEAARLSVAAQEAARLRQLAEEDLAQQ 2269
Cdd:pfam17380 561 ATEERSRLEAMEREREMMRQIVESEKARA 589
|
|
| AtpF |
COG0711 |
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ... |
1440-1539 |
2.49e-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: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1440 LQALRARAEEAE---AQKRQAQEEAERLRRQVQDEsQRKRQAEAElALRVKAEAEAAREKQRALQALDelrlqaEEAERR 1516
Cdd:COG0711 26 LKALDERQEKIAdglAEAERAKEEAEAALAEYEEK-LAEARAEAA-EIIAEARKEAEAIAEEAKAEAE------AEAERI 97
|
90 100
....*....|....*....|...
gi 254675251 1517 LRQAEAERARQVQVALETAQRSA 1539
Cdd:COG0711 98 IAQAEAEIEQERAKALAELRAEV 120
|
|
| growth_prot_Scy |
NF041483 |
polarized growth protein Scy; |
2128-2585 |
2.49e-03 |
|
polarized growth protein Scy;
Pssm-ID: 469371 [Multi-domain] Cd Length: 1293 Bit Score: 44.43 E-value: 2.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2128 ADAEMEKHKKFAEQTLRQKAQVEQELTTLRLQLEETDHQKSildEELQRLKAEVTEAARQR-SQVEEELFSVRVQMEELg 2206
Cdd:NF041483 209 AEAILRRARKDAERLLNAASTQAQEATDHAEQLRSSTAAES---DQARRQAAELSRAAEQRmQEAEEALREARAEAEKV- 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2207 kLKARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEeaarlsvAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQE 2286
Cdd:NF041483 285 -VAEAKEAAAKQLASAESANEQRTRTAKEEIARLVGE-------ATKEAEALKAEAEQALADARAEAEKLVAEAAEKART 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2287 ATRLKAEAELLQQQKElAQEQARRLQEDKEQMAQQLVEEtqgfqrtleAERQRQlEMSAEAERLKLRMAEMS-RAQARAE 2365
Cdd:NF041483 357 VAAEDTAAQLAKAART-AEEVLTKASEDAKATTRAAAEE---------AERIRR-EAEAEADRLRGEAADQAeQLKGAAK 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2366 EDAQRFRKQAEEIGEKLHRTElatqekvtlvqtleiqrqqsdHDAERLR-EAIAELEREKEKLKQEAkllqLKSEEMQTV 2444
Cdd:NF041483 426 DDTKEYRAKTVELQEEARRLR---------------------GEAEQLRaEAVAEGERIRGEARREA----VQQIEEAAR 480
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2445 QQEQILQETQALQKSFLSEKDSLLQRERFIEQEKAKLEQLfQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQ 2524
Cdd:NF041483 481 TAEELLTKAKADADELRSTATAESERVRTEAIERATTLRR-QAEETLERTRAEAERLRAEAEEQAEEVRAAAERAARELR 559
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 2525 REAEEGVRRKQEELqhleqqrqqqekllAEENQRLR----ERLQRLEEEHRAALAHSEIATTQAA 2585
Cdd:NF041483 560 EETERAIAARQAEA--------------AEELTRLHteaeERLTAAEEALADARAEAERIRREAA 610
|
|
| PTZ00491 |
PTZ00491 |
major vault protein; Provisional |
2231-2369 |
2.52e-03 |
|
major vault protein; Provisional
Pssm-ID: 240439 [Multi-domain] Cd Length: 850 Bit Score: 44.24 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2231 LEEEA------EKMK-QVAEEAAR---LSVAAQEAARlrQLAEEDLAQQRALAEKMLKEkMQAVQEATRLKAEAELLQQQ 2300
Cdd:PTZ00491 675 LEQEArgrlerQKMHdKAKAEEQRtklLELQAESAAV--ESSGQSRAEALAEAEARLIE-AEAEVEQAELRAKALRIEAE 751
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 2301 KELAQEQARRLQEDKEQmaQQLVEetqgfqrtLEAERQRQLeMSAEAERLKLRMAEMSR----AQARAEEDAQ 2369
Cdd:PTZ00491 752 AELEKLRKRQELELEYE--QAQNE--------LEIAKAKEL-ADIEATKFERIVEALGRetliAIARAGPELQ 813
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
2131-2539 |
2.56e-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: 44.34 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2131 EMEKHKKFAEQTLRQKAQVEQELttlRLQLEETDHQ----KSILDEELQRLKAEVTEAAR---QRSQVEEELFSVRVQME 2203
Cdd:pfam15921 121 EMQMERDAMADIRRRESQSQEDL---RNQLQNTVHEleaaKCLKEDMLEDSNTQIEQLRKmmlSHEGVLQEIRSILVDFE 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2204 E-----------LGKLKARIEAENRALILRDKDNTQRFL-------EEEAEKMKQVAEEAARLsVAAQEAARLRQLAEED 2265
Cdd:pfam15921 198 EasgkkiyehdsMSTMHFRSLGSAISKILRELDTEISYLkgrifpvEDQLEALKSESQNKIEL-LLQQHQDRIEQLISEH 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2266 LAQQRALAEKmlkekmqavqeATRLKAEAELLQQQKELAQEQAR-------RLQEDKEQMAQQLVEETQGFQRTLEaERQ 2338
Cdd:pfam15921 277 EVEITGLTEK-----------ASSARSQANSIQSQLEIIQEQARnqnsmymRQLSDLESTVSQLRSELREAKRMYE-DKI 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2339 RQLEMsaeaerlKLRMAEMSRAQARAEEDaqRFRKQAEEIGEKLHR--TELATQEKvtlvqTLEIQRQQSDHDAERLRE- 2415
Cdd:pfam15921 345 EELEK-------QLVLANSELTEARTERD--QFSQESGNLDDQLQKllADLHKREK-----ELSLEKEQNKRLWDRDTGn 410
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2416 --AIAELEREKEKLKQEAKLLQLKSEEMQTVQQEQILQETQALQ-KSFLSEKDSLLQRErfIEQEKAKLEQLFQDEVAKa 2492
Cdd:pfam15921 411 siTIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQgKNESLEKVSSLTAQ--LESTKEMLRKVVEELTAK- 487
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 254675251 2493 KQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQ 2539
Cdd:pfam15921 488 KMTLESSERTVSDLTASLQEKERAIEATNAEITKLRSRVDLKLQELQ 534
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
1383-1718 |
2.59e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 43.74 E-value: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1383 IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAE 1462
Cdd:COG4372 4 LGEKVGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1463 RLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVE 1542
Cdd:COG4372 84 ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1543 LQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSL 1622
Cdd:COG4372 164 EELAALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1623 AQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELA 1702
Cdd:COG4372 244 LEEDKEELLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLE 323
|
330
....*....|....*.
gi 254675251 1703 RLQHEATAATQKRQEL 1718
Cdd:COG4372 324 LAKKLELALAILLAEL 339
|
|
| CH_PLS_FIM_rpt2 |
cd21218 |
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes ... |
18-108 |
2.71e-03 |
|
second calponin homology (CH) domain found in the plastin/fimbrin family; This family includes plastin and fimbrin. Plastin has three isoforms, plastin-1, -2, and -3, which are all actin-bundling proteins. Plastin-1, also called intestine-specific plastin, or I-plastin, is an actin-bundling protein in the absence of calcium. Plastin-2, also called L-plastin, LC64P, or lymphocyte cytosolic protein 1 (LCP-1), plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-3, also called T-plastin, is found in intestinal microvilli, hair cell stereocilia, and fibroblast filopodia. It may play a role in the regulation of bone development. Fimbrin has been found in plants and fungi. Arabidopsis thaliana fimbrin (AtFIM) includes fimbrin-1, -2, -3, -4, and -5; they cross-link actin filaments (F-actin) in a calcium independent manner. They stabilize and prevent F-actin depolymerization mediated by profilin. They act as key regulators of actin cytoarchitecture, probably involved in cell cycle, cell division, cell elongation and cytoplasmic tractus. AtFIM5 is an actin bundling factor that is required for pollen germination and pollen tube growth. Fungal fimbrin binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Members of this family contain four copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409067 Cd Length: 114 Bit Score: 40.36 E-value: 2.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 18 KWVNKHLIKAQR---HISDLYEDLRDGHNLISLLEVLSGDSLPREKGRM---RFHKLQNVQIALDYLRhrQVKLVN-IRN 90
Cdd:cd21218 17 RWVNYHLKKAGPtkkRVTNFSSDLKDGEVYALLLHSLAPELCDKELVLEvlsEEDLEKRAEKVLQAAE--KLGCKYfLTP 94
|
90
....*....|....*...
gi 254675251 91 DDIADGNPKLTLGLIWTI 108
Cdd:cd21218 95 EDIVSGNPRLNLAFVATL 112
|
|
| CH_PLS2_rpt3 |
cd21330 |
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or ... |
7-115 |
2.76e-03 |
|
third calponin homology (CH) domain found in plastin-2; Plastin-2, also called L-plastin, or LC64P, or lymphocyte cytosolic protein 1 (LCP-1), is an actin-binding protein that plays a role in the activation of T-cells in response to costimulation through TCR/CD3 and CD2 or CD28. It modulates the cell surface expression of IL2RA/CD25 and CD69. Plastin-2 contains four copies of the CH domain. This model corresponds to the third CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409179 Cd Length: 125 Bit Score: 40.74 E-value: 2.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 7 ERDRVQKKTFTKWVNKhlIKAQRHISDLYEDLRDGHNLISLLEVL---------SGDSLPREKGRMRfhKLQNVQIALDY 77
Cdd:cd21330 9 EGETREERTFRNWMNS--LGVNPRVNHLYSDLSDALVIFQLYEKIkvpvdwnrvNKPPYPKLGENMK--KLENCNYAVEL 84
|
90 100 110
....*....|....*....|....*....|....*....
gi 254675251 78 LRHR-QVKLVNIRNDDIADGNPKLTLGLIWTIILHFQIS 115
Cdd:cd21330 85 GKNKaKFSLVGIAGQDLNEGNRTLTLALIWQLMRRYTLN 123
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2364-2488 |
2.86e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.61 E-value: 2.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2364 AEEDAQRFRKQAEEigeklhRTELATQEKVTLVQTlEIQRQQSDHDAErLREAIAELEREKEKLKQEAKLLQLKSEEMQt 2443
Cdd:PRK12704 36 AEEEAKRILEEAKK------EAEAIKKEALLEAKE-EIHKLRNEFEKE-LRERRNELQKLEKRLLQKEENLDRKLELLE- 106
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 254675251 2444 vQQEQILQEtqalqksflsEKDSLLQRERFIEQEKAKLEQLFQDE 2488
Cdd:PRK12704 107 -KREEELEK----------KEKELEQKQQELEKKEEELEELIEEQ 140
|
|
| SPEC |
smart00150 |
Spectrin repeats; |
487-581 |
3.01e-03 |
|
Spectrin repeats;
Pssm-ID: 197544 [Multi-domain] Cd Length: 101 Bit Score: 40.01 E-value: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 487 LRYLQDLLAWVEENQRRIDSAEWGVDLPSVEAQLGSHRGMHQSIEEFRAKIERARNDESQL---SPATRGAYRDCLGRLD 563
Cdd:smart00150 4 LRDADELEAWLEEKEQLLASEDLGKDLESVEALLKKHEAFEAELEAHEERVEALNELGEQLieeGHPDAEEIEERLEELN 83
|
90
....*....|....*...
gi 254675251 564 LQYAKLLNSSKARLRSLE 581
Cdd:smart00150 84 ERWEELKELAEERRQKLE 101
|
|
| Golgin_A5 |
pfam09787 |
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ... |
1653-1849 |
3.18e-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: 42.82 E-value: 3.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1653 ELAEQELEKQRQLAEGTAQqrlAAEQELIRLR-AETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEV 1731
Cdd:pfam09787 3 ESAKQELADYKQKAARILQ---SKEKLIASLKeGSGVEGLDSSTALTLELEELRQERDLLREEIQKLRGQIQQLRTELQE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1732 LLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARL----RALAEEAKRQRQLAEEDAARQRAEAER----VLTEK 1803
Cdd:pfam09787 80 LEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLqeelRYLEEELRRSKATLQSRIKDREAEIEKlrnqLTSKS 159
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 254675251 1804 LAAISEA---TRLKTEAEiALKEKEAENERLRRLAEDEAFQRRRLEEQA 1849
Cdd:pfam09787 160 QSSSSQSeleNRLHQLTE-TLIQKQTMLEALSTEKNSLVLQLERMEQQI 207
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
1596-1863 |
3.39e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.98 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1596 LERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARR-----RGKAEEQAVRQRELAEQELEKQRQLAEGTA 1670
Cdd:pfam13868 65 EERKEERKRYRQELEEQIEEREQKRQEEYEEKLQEREQMDEIVERiqeedQAEAEEKLEKQRQLREEIDEFNEEQAEWKE 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1671 QQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEEsrstsEKS 1750
Cdd:pfam13868 145 LEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAERDELRAKLYQEEQE-----RKE 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1751 KQRLEAEAGRFRELAEEAARLRALAEEAKRQRQlaEEDAARQRAEAERVLT------EKLAAISEATRLKTEAEIALKEK 1824
Cdd:pfam13868 220 RQKEREEAEKKARQRQELQQAREEQIELKERRL--AEEAEREEEEFERMLRkqaedeEIEQEEAEKRRMKRLEHRRELEK 297
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 254675251 1825 EAENERLRRLAEDEAF--QRRRLEEQAALHKADIEERLAQL 1863
Cdd:pfam13868 298 QIEEREEQRAAEREEEleEGERLREEEAERRERIEEERQKK 338
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1335-1466 |
3.47e-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: 3.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1335 EKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHL--RQSSEAEIQAKAQQVEAAERSR 1412
Cdd:pfam05672 11 EAARILAEKRRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeeERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1413 MRIEEEIRVVRLQLETTERQRGGAEGELQalraraeeaEAQKRQAQEEAERLRR 1466
Cdd:pfam05672 91 REQEEQERLQKQKEEAEAKAREEAERQRQ---------EREKIMQQEEQERLER 135
|
|
| TolA |
COG3064 |
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis]; |
1425-1888 |
3.75e-03 |
|
Membrane protein TolA involved in colicin uptake [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442298 [Multi-domain] Cd Length: 485 Bit Score: 43.49 E-value: 3.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1425 QLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALR--VKAEAEAAREKQRALQA 1502
Cdd:COG3064 17 RLEQAEAEKRAAAEAEQKAKEEAEEERLAELEAKRQAEEEAREAKAEAEQRAAELAAEAAKklAEAEKAAAEAEKKAAAE 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1503 LDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSKRASFAEKTAQLERTLQEehVTVAQLREEAERRAQQQ 1582
Cdd:COG3064 97 KAKAAKEAEAAAAAEKAAAAAEKEKAEEAKRKAEEEAKRKAEEERKAAEAEAAAKAEAEAA--RAAAAAAAAAAAAAARA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1583 AEAERAREEAERELERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQELEKQ 1662
Cdd:COG3064 175 AAGAAAALVAAAAAAVEAADTAAAAAAALAAAAAAAAADAALLALAVAARAAAASREAALAAVEATEEAALGGAEEAADL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1663 RQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELAKVRAEMEVLLASKARAEEE 1742
Cdd:COG3064 255 AAVGVLGAALAAAAAGAAALSSGLVVVAAALAGLAAAAAGLVLDDSAALAAELLGAVAAEEAVLAAAAAAGALVVRGGGA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1743 SRSTSEKSKQRLEAEAGRFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAEAERVLTEKLAAISEATRLKTEAEIALK 1822
Cdd:COG3064 335 ASLEAALSLLAAGAAAAAAGAGALATGALGDALAAEAAGALLLGKLADVEEAAGAGILAAAGGGGLLGLRLDLGAALLEA 414
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1823 EKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQV 1888
Cdd:COG3064 415 ASAVELRVLLALAGAAGAVVALLVKLVADLAGGLVGIGKALTGDADALLGILKAVALDGGAVLADL 480
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
2203-2320 |
3.90e-03 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.03 E-value: 3.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2203 EELGKLKARIEAENRALILRDKDNTQrfLEEeaekmkQVAEEAARLSVAAQEAARLRQLAEEdLAQQRALAEKMLKEKMQ 2282
Cdd:PRK09039 53 SALDRLNSQIAELADLLSLERQGNQD--LQD------SVANLRASLSAAEAERSRLQALLAE-LAGAGAAAEGRAGELAQ 123
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 254675251 2283 AVQEATRLKAEA----ELLQQQKELAQEQARRLQ--------EDKEQMAQ 2320
Cdd:PRK09039 124 ELDSEKQVSARAlaqvELLNQQIAALRRQLAALEaaldasekRDRESQAK 173
|
|
| SPFH_like_u3 |
cd03406 |
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This ... |
1302-1403 |
3.96e-03 |
|
Uncharacterized family; SPFH (stomatin, prohibitin, flotillin, and HflK/C) superfamily; This model summarizes an uncharacterized family of proteins similar to stomatin, prohibitin, flotillin, HflK/C (SPFH) and podocin. The conserved domain common to the SPFH superfamily has also been referred to as the Band 7 domain. Many superfamily members are associated with lipid rafts. Individual proteins of the SPFH superfamily may cluster to form membrane microdomains which may in turn recruit multiprotein complexes. Microdomains formed from flotillin proteins may in addition be dynamic units with their own regulatory functions. Flotillins have been implicated in signal transduction, vesicle trafficking, cytoskeleton rearrangement and are known to interact with a variety of proteins. Stomatin interacts with and regulates members of the degenerin/epithelia Na+ channel family in mechanosensory cells of Caenorhabditis elegans and vertebrate neurons and participates in trafficking of Glut1 glucose transporters. Prohibitin may act as a chaperone for the stabilization of mitochondrial proteins. Prokaryotic HflK/C plays a role in the decision between lysogenic and lytic cycle growth during lambda phage infection. Flotillins have been implicated in the progression of prion disease, in the pathogenesis of neurodegenerative diseases such as Parkinson's and Alzheimer's disease and, in cancer invasion and metastasis. Mutations in the podocin gene give rise to autosomal recessive steroid resistant nephritic syndrome.
Pssm-ID: 259804 [Multi-domain] Cd Length: 293 Bit Score: 42.67 E-value: 3.96e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1302 ISETLRR----MEEEE-RLAeqqRAEERERLAEVEAALEKQRQLAEAHAQAKA-----QAELEAQELQRRMQE-----EV 1366
Cdd:cd03406 160 IPEAIRRnyeaMEAEKtKLL---IAEQHQKVVEKEAETERKRAVIEAEKDAEVakiqmQQKIMEKEAEKKISEiedemHL 236
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254675251 1367 ArREEAAVDAQQQKRSIQEELQHLRQSSE----AEIQAKAQ 1403
Cdd:cd03406 237 A-REKARADAEYYRALREAEANKLKLTPEylelKKYQAIAN 276
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2221-2394 |
3.98e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 43.07 E-value: 3.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2221 LRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEEDLAQQRALAEKMLKEKMQAVQEATRLKAEAELLQQQ 2300
Cdd:pfam05262 177 ISDKKVVEALREDNEKGVNFRRDMTDLKERESQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADKQRDEVRQKQQE 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2301 KELAQEQAR--------RLQEDKEQMAQQLVEETQgfQRTLEAERQRQlemsAEAERLKLRMAEMSRAQARAEEDAQRFR 2372
Cdd:pfam05262 257 AKNLPKPADtsspkedkQVAENQKREIEKAQIEIK--KNDEEALKAKD----HKAFDLKQESKASEKEAEDKELEAQKKR 330
|
170 180
....*....|....*....|..
gi 254675251 2373 kqaEEIGEKLHRTELATQEKVT 2394
Cdd:pfam05262 331 ---EPVAEDLQKTKPQVEAQPT 349
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
2258-2432 |
4.02e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 4.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2258 LRQLAEEDLAQQRALAEKMLKEkmqavqeatrlkAEAELLQQQKELAQEQARRLQEDKEQMAQQLVEETQGFQRTLEAER 2337
Cdd:PRK12704 25 RKKIAEAKIKEAEEEAKRILEE------------AKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2338 QRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEIgEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAI 2417
Cdd:PRK12704 93 QKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEEL-EELIEEQLQELERISGLTAEEAKEILLEKVEEEARHEA 171
|
170
....*....|....*.
gi 254675251 2418 AELEREKEKL-KQEAK 2432
Cdd:PRK12704 172 AVLIKEIEEEaKEEAD 187
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1393-1527 |
4.12e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1393 SSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQVQDES 1472
Cdd:PRK12678 69 TPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARR-GAARKAGE 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 1473 QRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1527
Cdd:PRK12678 148 GGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERGRREERGRDGDD 202
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
2984-3021 |
4.12e-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: 4.12e-03
10 20 30
....*....|....*....|....*....|....*...
gi 254675251 2984 LRGTNVIAGVWLEEAGQKLSIYEALKKDLLQPEVAVAL 3021
Cdd:pfam00681 2 LEAQAATGGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1354-1492 |
4.39e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 43.53 E-value: 4.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1354 EAQELQRRMqEEVARREEAAVDAQQQkrSIQEELQHLRQSsEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQR 1433
Cdd:COG0542 412 ELDELERRL-EQLEIEKEALKKEQDE--ASFERLAELRDE-LAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKI 487
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 1434 GGAEGELQALRARAEEAEAQKRQ---AQEEAE-----------RLrrqVQDESQRKRQAEAELALRVKAEAEA 1492
Cdd:COG0542 488 PELEKELAELEEELAELAPLLREevtEEDIAEvvsrwtgipvgKL---LEGEREKLLNLEEELHERVIGQDEA 557
|
|
| PRK12678 |
PRK12678 |
transcription termination factor Rho; Provisional |
1341-1529 |
4.48e-03 |
|
transcription termination factor Rho; Provisional
Pssm-ID: 237171 [Multi-domain] Cd Length: 672 Bit Score: 43.35 E-value: 4.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1341 AEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIR 1420
Cdd:PRK12678 67 AATPAAPAAAARRAARAAAAARQAEQPAAEAAAAKAEAAPAARAAAAAAAEAASAPEAAQARERRERGEAARRGAARKAG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1421 vvRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQvqDESQRKRQAE-AELALRVKAEAEAAREKQRA 1499
Cdd:PRK12678 147 --EGGEQPATEARADAAERTEEEERDERRRRGDREDRQAEAERGERG--RREERGRDGDdRDRRDRREQGDRREERGRRD 222
|
170 180 190
....*....|....*....|....*....|
gi 254675251 1500 LQALDELRLQAEEAERRLRQAEAERARQVQ 1529
Cdd:PRK12678 223 GGDRRGRRRRRDRRDARGDDNREDRGDRDG 252
|
|
| PLN03188 |
PLN03188 |
kinesin-12 family protein; Provisional |
1304-1488 |
4.70e-03 |
|
kinesin-12 family protein; Provisional
Pssm-ID: 215621 [Multi-domain] Cd Length: 1320 Bit Score: 43.38 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1304 ETLRRMEEEER---LAEQQRAEererLAEVEAALEKQRQlaEAHAQAKAQAELE-----AQELQRRMQEEVARREEAAVD 1375
Cdd:PLN03188 1052 ERLRWTEAESKwisLAEELRTE----LDASRALAEKQKH--ELDTEKRCAEELKeamqmAMEGHARMLEQYADLEEKHIQ 1125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1376 AQQQKRSIQEELQHLRQSSE------AE---IQAKAQQVEA----AERSRMRIEEEIRVVRLQLETTER--QRGG----- 1435
Cdd:PLN03188 1126 LLARHRRIQEGIDDVKKAAAragvrgAEskfINALAAEISAlkveREKERRYLRDENKSLQAQLRDTAEavQAAGellvr 1205
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1436 ---AEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKA 1488
Cdd:PLN03188 1206 lkeAEEALTVAQKRAMDAEQEAAEAYKQIDKLKRKHENEISTLNQLVAESRLPKEA 1261
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1349-1686 |
4.71e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.93 E-value: 4.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1349 AQAELEAQELQRRMQEEVAR--REEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEIRVVRLQl 1426
Cdd:pfam02029 2 EDEEEAARERRRRAREERRRqkEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEEEAFLDRTAKREERRQKRLQ- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1427 ETTERQRggaEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAA--REKQRALQALD 1504
Cdd:pfam02029 81 EALERQK---EFDPTIADEKESVAERKENNEEEENSSWEKEEKRDSRLGRYKEEETEIREKEYQENKwsTEVRQAEEEGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1505 ELRLQAEEAERRLRQAEAERarqvQVALETAQRSAEVELQSKrASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAE 1584
Cdd:pfam02029 158 EEEDKSEEAEEVPTENFAKE----EVKDEKIKKEKKVKYESK-VFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1585 AERAREEAERELERWQlkANEALRLRLQA--EEVAQQKSLAQADAEKQKEEAEREARRRGKAEEQAVRQRELAEQElekq 1662
Cdd:pfam02029 233 SQEREEEAEVFLEAEQ--KLEELRRRRQEkeSEEFEKLRQKQQEAELELEELKKKREERRKLLEEEEQRRKQEEAE---- 306
|
330 340
....*....|....*....|....
gi 254675251 1663 RQLAEGTAQQRLaaEQELIRLRAE 1686
Cdd:pfam02029 307 RKLREEEEKRRM--KEEIERRRAE 328
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
1114-1482 |
4.83e-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: 4.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1114 LRDELRGAQEVGERLQQRHGERDVEVERWRERVTQLLERWQAVLAQTDVRQRELEQLgrqLRYYRESADPLSAWLQDAKR 1193
Cdd:pfam07888 32 LQNRLEECLQERAELLQAQEAANRQREKEKERYKRDREQWERQRRELESRVAELKEE---LRQSREKHEELEEKYKELSA 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1194 RQEQIQAVPIANCQAAREQLRQEKALLEEIERHGEKV-------EECQKFAKQYINAIKDYELQLITYKAQLEPVASPAK 1266
Cdd:pfam07888 109 SSEELSEEKDALLAQRAAHEARIRELEEDIKTLTQRVleretelERMKERAKKAGAQRKEEEAERKQLQAKLQQTEEELR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1267 K--PKVQSGSESVIQEYVDLRTRYSELTTLTSqyiKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQRQLAEAH 1344
Cdd:pfam07888 189 SlsKEFQELRNSLAQRDTQVLQLQDTITTLTQ---KLTTAHRKEAENEALLEELRSLQERLNASERKVEGLGEELSSMAA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1345 AQAKAQAELEAQELQrrMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEiRVVRL 1424
Cdd:pfam07888 266 QRDRTQAELHQARLQ--AAQLTLQLADASLALREGRARWAQERETLQQSAEADKDRIEKLSAELQRLEERLQEE-RMERE 342
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1425 QLETT-ERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAEL 1482
Cdd:pfam07888 343 KLEVElGREKDCNRVQLSESRRELQELKASLRVAQKEKEQLQAEKQELLEYIRQLEQRL 401
|
|
| MAP7 |
pfam05672 |
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ... |
1304-1431 |
4.93e-03 |
|
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.
Pssm-ID: 461709 [Multi-domain] Cd Length: 153 Bit Score: 40.79 E-value: 4.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1304 ETLRRMEEEERLAEQQRA-EERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQEL-QRRMQEEVARREEAAVDAQQQKR 1381
Cdd:pfam05672 11 EAARILAEKRRQAREQRErEEQERLEKEEEERLRKEELRRRAEEERARREEEARRLeEERRREEEERQRKAEEEAEEREQ 90
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 254675251 1382 SIQEELQHLRQSSEAeiqAKAQQVEAAErsRMRIEEEIRVVRLQLETTER 1431
Cdd:pfam05672 91 REQEEQERLQKQKEE---AEAKAREEAE--RQRQEREKIMQQEEQERLER 135
|
|
| TPH |
pfam13868 |
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ... |
2124-2397 |
5.02e-03 |
|
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.
Pssm-ID: 464007 [Multi-domain] Cd Length: 341 Bit Score: 42.60 E-value: 5.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2124 QKQAADAEMEKHKKFAEQTLRQKAQVEQELTTLR----LQLEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVR 2199
Cdd:pfam13868 53 RERALEEEEEKEEERKEERKRYRQELEEQIEEREqkrqEEYEEKLQEREQMDEIVERIQEEDQAEAEEKLEKQRQLREEI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2200 VQMEELGKL-----KARIEAENRALILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLAEE--DLAQQRAL 2272
Cdd:pfam13868 133 DEFNEEQAEwkeleKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKEREIARLRAQQEKAQDEKAErdELRAKLYQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2273 AEKMLKEKMQAVQEA-TRLKAEAELLQQQKELAQEQARRLQEDK--EQMAQQLVEETQGFQRTLEAERQRQLEMSAEAER 2349
Cdd:pfam13868 213 EEQERKERQKEREEAeKKARQRQELQQAREEQIELKERRLAEEAerEEEEFERMLRKQAEDEEIEQEEAEKRRMKRLEHR 292
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 254675251 2350 LKLRMAEMSRAQARAEEDAQRFRKQAEEIGEKLHRTELATQEKVTLVQ 2397
Cdd:pfam13868 293 RELEKQIEEREEQRAAEREEELEEGERLREEEAERRERIEEERQKKLK 340
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
1648-2005 |
5.10e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 43.41 E-value: 5.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1648 AVRQRELAEQELEKQRQLAEgtAQQRLAAEQE-LIRLRAETEQGEQQRQLLEEEL----ARLQ--HEATAATQKRQELEA 1720
Cdd:PRK04863 278 ANERRVHLEEALELRRELYT--SRRQLAAEQYrLVEMARELAELNEAESDLEQDYqaasDHLNlvQTALRQQEKIERYQA 355
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1721 ELAKVraemevllasKARAEEESRSTSEKSKQRLEAEAgRFRELAEEAARLR--------ALAEEAKRQRQLAEEDAARQ 1792
Cdd:PRK04863 356 DLEEL----------EERLEEQNEVVEEADEQQEENEA-RAEAAEEEVDELKsqladyqqALDVQQTRAIQYQQAVQALE 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1793 RAE------------AERVLTEKLAAISEATRLKTEAEIALKEKEAENER-------LRRLAED----EAFQR-----RR 1844
Cdd:PRK04863 425 RAKqlcglpdltadnAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHSQfeqayqlVRKIAGEvsrsEAWDVarellRR 504
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1845 LEEQAALhkadiEERLAQLRkASESELERQkglvedtLRQRRQVEEeimaLKVSFEKAAAGKAELELELGRIRSNAEDTM 1924
Cdd:PRK04863 505 LREQRHL-----AEQLQQLR-MRLSELEQR-------LRQQQRAER----LLAEFCKRLGKNLDDEDELEQLQEELEARL 567
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1925 RSKEQaELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVALEE-------------------VERLKAKVEE 1985
Cdd:PRK04863 568 ESLSE-SVSEARERRMALRQQLEQLQARIQRLAARAPAWLAAQDALARLREqsgeefedsqdvteymqqlLERERELTVE 646
|
410 420
....*....|....*....|
gi 254675251 1986 ARRLRERAEQESARQLQLAQ 2005
Cdd:PRK04863 647 RDELAARKQALDEEIERLSQ 666
|
|
| PLEC |
smart00250 |
Plectin repeat; |
3389-3420 |
5.16e-03 |
|
Plectin repeat;
Pssm-ID: 197605 Cd Length: 38 Bit Score: 37.46 E-value: 5.16e-03
10 20 30
....*....|....*....|....*....|..
gi 254675251 3389 KLLSAEKAVTGYKDPYSGNTISLFQAMKKGLV 3420
Cdd:smart00250 2 RLLEAQSAIGGIIDPETGQKLSVEEALRRGLI 33
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
2197-2377 |
5.20e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 42.76 E-value: 5.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2197 SVRVQMEE----LGKLKARIEAENRA-LILRDKDNTQRFLEEEAEKMK------QVAEEAARLSVAAQEAARLRQLAEED 2265
Cdd:PRK11637 62 SVRQQQQQraslLAQLKKQEEAISQAsRKLRETQNTLNQLNKQIDELNasiaklEQQQAAQERLLAAQLDAAFRQGEHTG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2266 LAQQRALAEKMLKEKMQA----VQEAtRLKAEAELLQQQKELAQEqaRRLQEDKEQMAQQLVEETQGFQRTLE---AERQ 2338
Cdd:PRK11637 142 LQLILSGEESQRGERILAyfgyLNQA-RQETIAELKQTREELAAQ--KAELEEKQSQQKTLLYEQQAQQQKLEqarNERK 218
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 254675251 2339 RQL---------------EMSAEAERLKLRMAEMSR-AQARAEE---DAQRFRKQAEE 2377
Cdd:PRK11637 219 KTLtglesslqkdqqqlsELRANESRLRDSIARAEReAKARAERearEAARVRDKQKQ 276
|
|
| Borrelia_P83 |
pfam05262 |
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins. |
2256-2431 |
5.32e-03 |
|
Borrelia P83/100 protein; This family consists of several Borrelia P83/P100 antigen proteins.
Pssm-ID: 114011 [Multi-domain] Cd Length: 489 Bit Score: 42.68 E-value: 5.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2256 ARLRQLAEEDLAQQRAL-------AEKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRlQEDKEQMAQQLVEETQG 2328
Cdd:pfam05262 184 EALREDNEKGVNFRRDMtdlkereSQEDAKRAQQLKEELDKKQIDADKAQQKADFAQDNADK-QRDEVRQKQQEAKNLPK 262
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2329 FQRTLEAERQRQLemsaeAERLKlrmAEMSRAQARAEEDAQRFRKQAEEIGEKLHRtELATQEKVTLVQTLEIQRQQSDh 2408
Cdd:pfam05262 263 PADTSSPKEDKQV-----AENQK---REIEKAQIEIKKNDEEALKAKDHKAFDLKQ-ESKASEKEAEDKELEAQKKREP- 332
|
170 180
....*....|....*....|...
gi 254675251 2409 DAERLREAIAELEREKEKLKQEA 2431
Cdd:pfam05262 333 VAEDLQKTKPQVEAQPTSLNEDA 355
|
|
| PspA |
COG1842 |
Phage shock protein A [Transcription, Signal transduction mechanisms]; |
1643-1800 |
5.33e-03 |
|
Phage shock protein A [Transcription, Signal transduction mechanisms];
Pssm-ID: 441447 [Multi-domain] Cd Length: 217 Bit Score: 41.73 E-value: 5.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1643 KAEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAE--QELIRLraeteqgEQQRQLLEEELARLQHEATAATQKRQELEA 1720
Cdd:COG1842 54 KRLERQLEELEAEAEKWEEKARLALEKGREDLAREalERKAEL-------EAQAEALEAQLAQLEEQVEKLKEALRQLES 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1721 ELAKVRAEMEVLLASKARAEEESRSTSEKSKQRLEAEAGRFRELAEEAARLRALAE---EAKRQRQLAEE-DAARQRAEA 1796
Cdd:COG1842 127 KLEELKAKKDTLKARAKAAKAQEKVNEALSGIDSDDATSALERMEEKIEEMEARAEaaaELAAGDSLDDElAELEADSEV 206
|
....
gi 254675251 1797 ERVL 1800
Cdd:COG1842 207 EDEL 210
|
|
| PRK05035 |
PRK05035 |
electron transport complex protein RnfC; Provisional |
2228-2440 |
5.38e-03 |
|
electron transport complex protein RnfC; Provisional
Pssm-ID: 235334 [Multi-domain] Cd Length: 695 Bit Score: 43.01 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2228 QRFleeEAEKMKQVAEEAARLSVAAQEAARLRqlAEEDLAQQRALAEkmLKEKmQAVQEATRLKAEAELLQQQKELAQEQ 2307
Cdd:PRK05035 453 ARF---EARQARLEREKAAREARHKKAAEARA--AKDKDAVAAALAR--VKAK-KAAATQPIVIKAGARPDNSAVIAARE 524
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2308 ARRLQEDKEQMAQQLVEETQGFQRTLEAERQR-------QLEMSAEAE-----RLKLRMAEMSRAQAR-AEEDAQRFRKQ 2374
Cdd:PRK05035 525 ARKAQARARQAEKQAAAAADPKKAAVAAAIARakakkaaQQAANAEAEeevdpKKAAVAAAIARAKAKkAAQQAASAEPE 604
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 2375 AEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKLLQLKSEE 2440
Cdd:PRK05035 605 EQVAEVDPKKAAVAAAIARAKAKKAEQQANAEPEEPVDPRKAAVAAAIARAKARKAAQQQANAEPE 670
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
1191-1519 |
5.61e-03 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 42.92 E-value: 5.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1191 AKRRQEQIQAVpIANCQAAREQLRQE-KALLEEIERHGEKVEECQKfakQYINAIKdyelQLITYKAQLEPVASPAkkpk 1269
Cdd:pfam06160 84 AKKALDEIEEL-LDDIEEDIKQILEElDELLESEEKNREEVEELKD---KYRELRK----TLLANRFSYGPAIDEL---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1270 vqsgsESVIQEYVDLRTRYSELTTlTSQYIKfISETLRRMEEEERLAEQQRAEERERLAEVEAALEKQ-RQLAEAHAQAK 1348
Cdd:pfam06160 152 -----EKQLAEIEEEFSQFEELTE-SGDYLE-AREVLEKLEEETDALEELMEDIPPLYEELKTELPDQlEELKEGYREME 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1349 AQ--------AELEAQELQRRMQEEVARREEAAVD-AQQQKRSIQEELQHLRQSSEAEIQAKA----------QQVEAAE 1409
Cdd:pfam06160 225 EEgyalehlnVDKEIQQLEEQLEENLALLENLELDeAEEALEEIEERIDQLYDLLEKEVDAKKyveknlpeieDYLEHAE 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1410 RSRMRIEEEIRVV----RLQLETTERQRgGAEGELQALRARAEEAE---AQKRQA----QEEAERLRRQVQD-ESQRKRQ 1477
Cdd:pfam06160 305 EQNKELKEELERVqqsyTLNENELERVR-GLEKQLEELEKRYDEIVerlEEKEVAyselQEELEEILEQLEEiEEEQEEF 383
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 254675251 1478 AEAELALRvkaeaeaaREKQRALQALDELRLQAEEAERRLRQ 1519
Cdd:pfam06160 384 KESLQSLR--------KDELEAREKLDEFKLELREIKRLVEK 417
|
|
| CCDC34 |
pfam13904 |
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ... |
1304-1408 |
5.87e-03 |
|
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.
Pssm-ID: 464032 [Multi-domain] Cd Length: 221 Bit Score: 41.61 E-value: 5.87e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1304 ETLRRMEEEERLAEQQRAEERERLAE--VEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDA----- 1376
Cdd:pfam13904 69 QKELQAQKEEREKEEQEAELRKRLAKekYQEWLQRKARQQTKKREESHKQKAAESASKSLAKPERKVSQEEAKEVlqewe 148
|
90 100 110
....*....|....*....|....*....|....*
gi 254675251 1377 ---QQQKRSIQEELQHLRQSSEAEIQAKAQQVEAA 1408
Cdd:pfam13904 149 rkkLEQQQRKREEEQREQLKKEEEEQERKQLAEKA 183
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
1437-1630 |
6.03e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.49 E-value: 6.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1437 EGELQALRARAEEAEAQKRQAQEEAERLRRQvqdESQRKRQAEAELALRVKAEAEAAREKQRAlqaldELRLQAEEAERR 1516
Cdd:PRK09510 84 KEQQQAEELQQKQAAEQERLKQLEKERLAAQ---EQKKQAEEAAKQAALKQKQAEEAAAKAAA-----AAKAKAEAEAKR 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1517 LrqaeAERARQvqvALETAQRSAEVELQSKRASFAEKTAQLERTLQEEHVTVAQLREEAERRAQQQAEAERAReeaerel 1596
Cdd:PRK09510 156 A----AAAAKK---AAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAA------- 221
|
170 180 190
....*....|....*....|....*....|....
gi 254675251 1597 ERWQLKANEALRLRLQAEEVAQQKSLAQADAEKQ 1630
Cdd:PRK09510 222 EAKAAAAKAAAEAKAAAEKAAAAKAAEKAAAAKA 255
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
1067-1518 |
6.09e-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: 42.81 E-value: 6.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1067 EEVLKTHEEQLKE-AQAVPATLQELEATKASLKKLRAQAEAQQPVFNTLRDELRGAQEVGERLQQRHGERDVEVERWRER 1145
Cdd:pfam05557 61 EKREAEAEEALREqAELNRLKKKYLEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQER 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1146 VTQLLERWQAV---LAQTDVRQREL---EQLGRQLRYYRESADPLSAWLQDAKRRQEQiqavpIANCQAAREQLRQEKAL 1219
Cdd:pfam05557 141 LDLLKAKASEAeqlRQNLEKQQSSLaeaEQRIKELEFEIQSQEQDSEIVKNSKSELAR-----IPELEKELERLREHNKH 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1220 LEEIERHGEKVEECQKFAKQYINAIKDYELQLITYKAQLEPVASPAKK-PKVQSGSESVIQEYVDLRTRYSEL------- 1291
Cdd:pfam05557 216 LNENIENKLLLKEEVEDLKRKLEREEKYREEAATLELEKEKLEQELQSwVKLAQDTGLNLRSPEDLSRRIEQLqqreivl 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1292 ----TTLTSQyIKFISETLRRMEEEERLAEQQRAEERERLAEVEAALEK-QRQL----------------------AEAH 1344
Cdd:pfam05557 296 keenSSLTSS-ARQLEKARRELEQELAQYLKKIEDLNKKLKRHKALVRRlQRRVllltkerdgyrailesydkeltMSNY 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1345 AQAKAQAELEAQELQRRMQ---EEVARR----EEAAVDAQQQKRSIQEELQHLRQ--------SSEAEIQAKAQQVEAAE 1409
Cdd:pfam05557 375 SPQLLERIEEAEDMTQKMQahnEEMEAQlsvaEEELGGYKQQAQTLERELQALRQqesladpsYSKEEVDSLRRKLETLE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1410 RSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQ--DESQRKRQAEAELALRVK 1487
Cdd:pfam05557 455 LERQRLREQKNELEMELERRCLQGDYDPKKTKVLHLSMNPAAEAYQQRKNQLEKLQAEIErlKRLLKKLEDDLEQVLRLP 534
|
490 500 510
....*....|....*....|....*....|.
gi 254675251 1488 AEAEAAREKQralqaLDELRLQAEEAERRLR 1518
Cdd:pfam05557 535 ETTSTMNFKE-----VLDLRKELESAELKNQ 560
|
|
| CH_PARVA_rpt2 |
cd21337 |
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called ... |
5-113 |
6.73e-03 |
|
second calponin homology (CH) domain found in alpha-parvin; Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. It is also involved in the reorganization of the actin cytoskeleton, the formation of lamellipodia and ciliogenesis, as well as in the establishement of cell polarity, cell adhesion, cell spreading, and directed cell migration. Alpha-parvin contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409186 Cd Length: 129 Bit Score: 39.98 E-value: 6.73e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 5 PDERDrVQKKTFTKWVNKHLIKAQRHISDLYEDLRDGHNLISLLEVLSGDSLPREKGRMR----FHKLQNVQIALDYLRH 80
Cdd:cd21337 15 PDKLN-VVKKTLITFVNKHLNKLNLEVTELETQFADGVYLVLLMGLLEGYFVPLHSFFLTpdsfEQKVLNVSFAFELMQD 93
|
90 100 110
....*....|....*....|....*....|...
gi 254675251 81 RQVKLVNIRNDDIADGNPKLTLGLIWTIILHFQ 113
Cdd:cd21337 94 GGLEKPKPRPEDIVNCDLKSTLRVLYNLFTKYR 126
|
|
| tolA |
PRK09510 |
cell envelope integrity inner membrane protein TolA; Provisional |
2298-2432 |
6.80e-03 |
|
cell envelope integrity inner membrane protein TolA; Provisional
Pssm-ID: 236545 [Multi-domain] Cd Length: 387 Bit Score: 42.10 E-value: 6.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2298 QQQKELAQEQARRLQEDKEQMAQQLVEETQgfQRTLEAERQRQLEMSAEAERLKLRMAEMSR------AQARAEEDAQRF 2371
Cdd:PRK09510 79 EQRKKKEQQQAEELQQKQAAEQERLKQLEK--ERLAAQEQKKQAEEAAKQAALKQKQAEEAAakaaaaAKAKAEAEAKRA 156
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 254675251 2372 R---KQAEEIGEKLHRTELATQEKVTLVQTLEIQ-RQQSDHDAERLREAIAelereKEKLKQEAK 2432
Cdd:PRK09510 157 AaaaKKAAAEAKKKAEAEAAKKAAAEAKKKAEAEaAAKAAAEAKKKAEAEA-----KKKAAAEAK 216
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
2402-2624 |
6.91e-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: 42.80 E-value: 6.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2402 QRQQSDH----DAERLREAIAELEREKEKLKQEAKLLQLKSEEMQtvQQEQILQEtqalQKSFLSEKDSLLQRERfIEQE 2477
Cdd:pfam17380 286 ERQQQEKfekmEQERLRQEKEEKAREVERRRKLEEAEKARQAEMD--RQAAIYAE----QERMAMERERELERIR-QEER 358
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2478 KAKLEQLFQDEVAKAKQLREEQQRQQQQMEQEKQELMASMEEARRRQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQ 2557
Cdd:pfam17380 359 KRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKILEEERQRKIQQQKVEMEQIRAEQEEARQREVR 438
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 2558 RLRE----RLQRLEEEHRAALAHSEIATTQAASTKALPNGRDApdgpsvEAEPEYTFEGLRQKVPAQQLQE 2624
Cdd:pfam17380 439 RLEEerarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEK------EKRDRKRAEEQRRKILEKELEE 503
|
|
| PRK07735 |
PRK07735 |
NADH-quinone oxidoreductase subunit C; |
1318-1512 |
7.04e-03 |
|
NADH-quinone oxidoreductase subunit C;
Pssm-ID: 236081 [Multi-domain] Cd Length: 430 Bit Score: 42.27 E-value: 7.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1318 QQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEEVARREEAAVDAQQQKRSIQEELQHLRQSSEAE 1397
Cdd:PRK07735 76 KQKREGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKREGTEEVTEEEKAAAKAKAAAAAKAKAAALAKQKREGTEEVTE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1398 IQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERLRRQVQDES-QRKR 1476
Cdd:PRK07735 156 EEEETDKEKAKAKAAAAAKAKAAALAKQKAAEAGEGTEEVTEEEKAKAKAKAAAAAKAKAAALAKQKASQGNGDSgDEDA 235
|
170 180 190
....*....|....*....|....*....|....*.
gi 254675251 1477 QAEAELALRVKAEAeAAREKQRALQALDELRLQAEE 1512
Cdd:PRK07735 236 KAKAIAAAKAKAAA-AARAKTKGAEGKKEEEPKQEE 270
|
|
| ClpA |
COG0542 |
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ... |
1406-1523 |
7.16e-03 |
|
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440308 [Multi-domain] Cd Length: 836 Bit Score: 42.76 E-value: 7.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1406 EAAERSRMRIE---EEIRVVRLQLETTERqrggaegELQALRaraeeaEAQKRQAQEEAERLRRQVQDESQRKRQAEAel 1482
Cdd:COG0542 397 EAAARVRMEIDskpEELDELERRLEQLEI-------EKEALK------KEQDEASFERLAELRDELAELEEELEALKA-- 461
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 254675251 1483 alRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAE 1523
Cdd:COG0542 462 --RWEAEKELIEEIQELKEELEQRYGKIPELEKELAELEEE 500
|
|
| Caldesmon |
pfam02029 |
Caldesmon; |
1310-1571 |
7.22e-03 |
|
Caldesmon;
Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.55 E-value: 7.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1310 EEEERLAEQQRAEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEE-------VARREEAAVDAQQQKRS 1382
Cdd:pfam02029 5 EEAARERRRRAREERRRQKEEEEPSGQVTESVEPNEHNSYEEDSELKPSGQGGLDEeeafldrTAKREERRQKRLQEALE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1383 IQEELQHLRQSSEAEIQAKAQQVEAAERSRMRIEEEI--RVVRLQLETTE-RQRGGAEGELQALRARAEEAEAQKRQAQE 1459
Cdd:pfam02029 85 RQKEFDPTIADEKESVAERKENNEEEENSSWEKEEKRdsRLGRYKEEETEiREKEYQENKWSTEVRQAEEEGEEEEDKSE 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1460 EAERLRRQV-QDESQRKRQAEAELALRVKAEAEAAREK-------QRALQALDELRLQAEEAERRLRQAEAERARQVQVa 1531
Cdd:pfam02029 165 EAEEVPTENfAKEEVKDEKIKKEKKVKYESKVFLDQKRghpevksQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAEVF- 243
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 254675251 1532 LETAQRSAEVElQSKRASFAEKTAQLERTLQEEHVTVAQL 1571
Cdd:pfam02029 244 LEAEQKLEELR-RRRQEKESEEFEKLRQKQQEAELELEEL 282
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
1321-1496 |
7.30e-03 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 42.46 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1321 AEERERLAEVEAalekQRQLAEAHAQAKA---QAELEAQELQRRMQEEvarreeaavdAQQQKRSIQEELQHLrqssEAE 1397
Cdd:PRK12704 29 AEAKIKEAEEEA----KRILEEAKKEAEAikkEALLEAKEEIHKLRNE----------FEKELRERRNELQKL----EKR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1398 IQAKAQQVEAAERSRMRIEEEIRVVRLQLETTERqrggaegELQALRARAEEAEAQKRQA--------QEEA-ERLRRQV 1468
Cdd:PRK12704 91 LLQKEENLDRKLELLEKREEELEKKEKELEQKQQ-------ELEKKEEELEELIEEQLQElerisgltAEEAkEILLEKV 163
|
170 180
....*....|....*....|....*...
gi 254675251 1469 QDEsqrkrqAEAELALRVKAEAEAAREK 1496
Cdd:PRK12704 164 EEE------ARHEAAVLIKEIEEEAKEE 185
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
1448-1565 |
7.30e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 42.51 E-value: 7.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1448 EEAeaqKRQAQEEAERLRRQVQDESQRKRQAEAELAlrvkaeaEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQ 1527
Cdd:PRK00409 505 EEA---KKLIGEDKEKLNELIASLEELERELEQKAE-------EAEALLKEAEKLKEELEEKKEKLQEEEDKLLEEAEKE 574
|
90 100 110
....*....|....*....|....*....|....*....
gi 254675251 1528 VQVALETAQRSAEVELQSKRASFAEKTAQL-ERTLQEEH 1565
Cdd:PRK00409 575 AQQAIKEAKKEADEIIKELRQLQKGGYASVkAHELIEAR 613
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
1849-2025 |
7.42e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.06 E-value: 7.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1849 AALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELELGRIRSNAEDTMRSKE 1928
Cdd:COG4942 14 AAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1929 QAELEAARQRQLAAEEEQRRREAEERVQRSLAAEEEAARQRKVAL-----------EEVERLKAKVEEARRLRERAEQES 1997
Cdd:COG4942 94 ELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylkylaparrEQAEELRADLAELAALRAELEAER 173
|
170 180 190
....*....|....*....|....*....|
gi 254675251 1998 ARQLQL--AQEAAQKRLQAEEKAHAFVVQQ 2025
Cdd:COG4942 174 AELEALlaELEEERAALEALKAERQKLLAR 203
|
|
| YqiK |
COG2268 |
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown]; |
1777-1938 |
7.55e-03 |
|
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
Pssm-ID: 441869 [Multi-domain] Cd Length: 439 Bit Score: 42.17 E-value: 7.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1777 EAKRQRQLAEEDAARQRAEAERvLTEKlaAISEATRLKTEAEIA-------LKEKEAENERLRRLAEdeafQRRRLEEQA 1849
Cdd:COG2268 189 LGRRKIAEIIRDARIAEAEAER-ETEI--AIAQANREAEEAELEqereietARIAEAEAELAKKKAE----ERREAETAR 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1850 ALHKADIEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALKVSFEKAAAGKAELELElgrirsnaedtmrskEQ 1929
Cdd:COG2268 262 AEAEAAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRKPAEAEKQAAEAE---------------AE 326
|
....*....
gi 254675251 1930 AELEAARQR 1938
Cdd:COG2268 327 AEAEAIRAK 335
|
|
| SAC6 |
COG5069 |
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton]; |
5-140 |
7.63e-03 |
|
Ca2+-binding actin-bundling protein fimbrin/plastin (EF-Hand superfamily) [Cytoskeleton];
Pssm-ID: 227401 [Multi-domain] Cd Length: 612 Bit Score: 42.62 E-value: 7.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 5 PDERDRVQKKTFTKWVNKHLIKAQrhISDLYEDLRDGHNLISLLEVLSGD---SLPREKGR-------MRFHKLQNVQIA 74
Cdd:COG5069 373 FDAEGEFEARVFTFWLNSLDVSPE--ITNLFGDLRDQLILLQALSKKLMPmtvTHKLVKKQpasgieeNRFKAFENENYA 450
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 75 LDYLRHRQVKLVNIRNDDIADGNpKLTLGLIW-------TIILHFQISDiqvsgqsEDMTAKEKLLLWSQRMV 140
Cdd:COG5069 451 VDLGITEGFSLVGIKGLEILDGI-RLKLTLVWqvlrsntALFNHVLKKD-------GCGLSDSDLCAWLGSLG 515
|
|
| FAM184 |
pfam15665 |
Family with sequence similarity 184, A and B; The function of FAM184 is not known. |
2305-2493 |
7.77e-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: 41.18 E-value: 7.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2305 QEQARRLQEDKEQMAQQLVEETQGFQRTLEAERQRQLEMSAEAERLKLRMAEMSRAQARAEEDAQRFRKQAEEigEKLHR 2384
Cdd:pfam15665 13 EAEIQALKEAHEEEIQQILAETREKILQYKSKIGEELDLKRRIQTLEESLEQHERMKRQALTEFEQYKRRVEE--RELKA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2385 TELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAKL-LQLKSEEMQTVQQEQ---ILQETQALQKSF 2460
Cdd:pfam15665 91 EAEHRQRVVELSREVEEAKRAFEEKLESFEQLQAQFEQEKRKALEELRAkHRQEIQELLTTQRAQsasSLAEQEKLEELH 170
|
170 180 190
....*....|....*....|....*....|...
gi 254675251 2461 LSEKDSLLQRERFIEQEKAKLEQLFQDEVAKAK 2493
Cdd:pfam15665 171 KAELESLRKEVEDLRKEKKKLAEEYEQKLSKAQ 203
|
|
| PLN02316 |
PLN02316 |
synthase/transferase |
1493-1547 |
8.23e-03 |
|
synthase/transferase
Pssm-ID: 215180 [Multi-domain] Cd Length: 1036 Bit Score: 42.55 E-value: 8.23e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 254675251 1493 AREKQRALQaldelRLQAEEAERRlRQAEAERARQVQVALETAQRS-AEVELQSKR 1547
Cdd:PLN02316 251 LEEKRRELE-----KLAKEEAERE-RQAEEQRRREEEKAAMEADRAqAKAEVEKRR 300
|
|
| CusB_dom_1 |
pfam00529 |
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ... |
1391-1570 |
8.69e-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: 41.64 E-value: 8.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1391 RQSSEAEIQAKAQQVEA-AERSRMRIE-EEIRVVRLQLETTERQRGGAEGELQALRARAEEAEAQKRQAQEEAERlRRQV 1468
Cdd:pfam00529 54 TDYQAALDSAEAQLAKAqAQVARLQAElDRLQALESELAISRQDYDGATAQLRAAQAAVKAAQAQLAQAQIDLAR-RRVL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1469 QDESQRKRQAEAELALRVKAEAEAAREKQRALQALDELRLQAEEAERRLRQAEAERARQVQVALETAQRSAEVELQSK-- 1546
Cdd:pfam00529 133 APIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRSELSGAQLQIAEAEAELKLAKLDLERTei 212
|
170 180
....*....|....*....|....
gi 254675251 1547 RASFAEKTAQLERTLQEEHVTVAQ 1570
Cdd:pfam00529 213 RAPVDGTVAFLSVTVDGGTVSAGL 236
|
|
| CCCAP |
pfam15964 |
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ... |
2144-2470 |
8.90e-03 |
|
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.
Pssm-ID: 435040 [Multi-domain] Cd Length: 703 Bit Score: 42.20 E-value: 8.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2144 RQKAQVEQELTTLRLQ-LEETDHQKSILDEELQRLKAEVTEAARQRSQVEEELFSVrVQMEE---LGKLKARIEAEN-RA 2218
Cdd:pfam15964 285 QHEAVLAQTHTNVHMQtIERLTKERDDLMSALVSVRSSLAEAQQRESSAYEQVKQA-VQMTEeanFEKTKALIQCEQlKS 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2219 LILRDKDNTQRFLEEEAEKMKQVAEEAARLSVAAQEAARLRQLA-EEDLAQQRALAEKMLKEKMQAVQEATrlKAEAELL 2297
Cdd:pfam15964 364 ELERQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLAlSQNVAQLEAQVEKVTREKNSLVSQLE--EAQKQLA 441
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2298 QQQKELAQEQAR-RLQEDKEQMAQqlvEETQGFQRTLEAERQRQLEMS-AEAERLKL-------RMAEMSRAQARAEEDA 2368
Cdd:pfam15964 442 SQEMDVTKVCGEmRYQLNQTKMKK---DEAEKEHREYRTKTGRQLEIKdQEIEKLGLelseskqRLEQAQQDAARAREEC 518
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2369 QRFrkqAEEIGEKLHRTELATQEKVTLVQ--------------------TLEIQRQQSDHDaERLREAIAELEREK---E 2425
Cdd:pfam15964 519 LKL---TELLGESEHQLHLTRLEKESIQQsfsneakaqalqaqqreqelTQKMQQMEAQHD-KTVNEQYSLLTSQNtfiA 594
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 254675251 2426 KLKQEAKLLQLKSEEMQTVQQEQILQETQalQKSFLSEKDSLLQR 2470
Cdd:pfam15964 595 KLKEECCTLAKKLEEITQKSRSEVEQLSQ--EKEYLQDRLEKLQK 637
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
1172-1384 |
9.06e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 9.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1172 RQLRYYRESADPLSAWLQD-AKRRQEQIQAVpiancQAAREQLRQEKALLEEIERHGEKVEECQKFAKQYINA---IKDY 1247
Cdd:COG3206 164 QNLELRREEARKALEFLEEqLPELRKELEEA-----EAALEEFRQKNGLVDLSEEAKLLLQQLSELESQLAEAraeLAEA 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1248 ELQLITYKAQLEPVASPAKKPKVQSGSESVIQEYVDLRTRYSEL-TTLTSQYIKF------ISETLRRMEEEERLAEQQR 1320
Cdd:COG3206 239 EARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELsARYTPNHPDVialraqIAALRAQLQQEAQRILASL 318
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 254675251 1321 AEERERLAEVEAALEKQRQLAEAHAQAKAQAELEAQELQRRMQEE-------VARREEAAVDAQQQKRSIQ 1384
Cdd:COG3206 319 EAELEALQAREASLQAQLAQLEARLAELPELEAELRRLEREVEVArelyeslLQRLEEARLAEALTVGNVR 389
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
1716-1901 |
9.11e-03 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.06 E-value: 9.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1716 QELEAELAKVRAEMEVLLASKARAEEEsrstsekskqrleaeagrFRELAEEAARLRALAEEAKRQRQLAEEDAARQRAE 1795
Cdd:COG1579 13 QELDSELDRLEHRLKELPAELAELEDE------------------LAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1796 AERvLTEKLAAISEATRLKteaeiALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKADIEERLAQLRKASESELERQK 1875
Cdd:COG1579 75 IKK-YEEQLGNVRNNKEYE-----ALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELD 148
|
170 180
....*....|....*....|....*.
gi 254675251 1876 GLVEDTLRQRRQVEEEIMALKVSFEK 1901
Cdd:COG1579 149 EELAELEAELEELEAEREELAAKIPP 174
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
2122-2586 |
9.26e-03 |
|
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.
Pssm-ID: 431111 [Multi-domain] Cd Length: 766 Bit Score: 42.12 E-value: 9.26e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2122 LKQKQAADAEMEKHKKFAEQTLRQKAQVEQELTtlrlQLEETDHQKSILDEELQRLKAEVTEAARQRSQVE-----EELF 2196
Cdd:pfam10174 58 LKEQYRVTQEENQHLQLTIQALQDELRAQRDLN----QLLQQDFTTSPVDGEDKFSTPELTEENFRRLQSEherqaKELF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2197 SVRVQMEELgklKARIEAENRALILRDkDNTQRFLE---EEAEKMKQVAEEAARLSVAAQEAARLRQLaeEDLAQQRALA 2273
Cdd:pfam10174 134 LLRKTLEEM---ELRIETQKQTLGARD-ESIKKLLEmlqSKGLPKKSGEEDWERTRRIAEAEMQLGHL--EVLLDQKEKE 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2274 EKMLKEKMQAVQEATRLKAEAELLQQQKELAQEQARRLqedkEQMAQQLVEETQGFQRTLEaerqrqLEMSAEAERLKlr 2353
Cdd:pfam10174 208 NIHLREELHRRNQLQPDPAKTKALQTVIEMKDTKISSL----ERNIRDLEDEVQMLKTNGL------LHTEDREEEIK-- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2354 maemsraQARAEEDAQRFRK-QAEEIGEKLHRTELATQEKVTLVQTLEIQRQQSDHDAERLREAIAELEREKEKLKQEAK 2432
Cdd:pfam10174 276 -------QMEVYKSHSKFMKnKIDQLKQELSKKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVD 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2433 LLQLKSEEMQTV-----QQEQILQETQALQKSFLSE-KDSLLQRERFIEQEKAKLEQLFQDEVAKAKQLREEQQRQQQQM 2506
Cdd:pfam10174 349 ALRLRLEEKESFlnkktKQLQDLTEEKSTLAGEIRDlKDMLDVKERKINVLQKKIENLQEQLRDKDKQLAGLKERVKSLQ 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 2507 EQEKQE--LMASMEEArrrQREAEEGVRRKQEELQHLEQQRQQQEKLLAEENQRLRERLQRLE----EEHRAALAHSEIA 2580
Cdd:pfam10174 429 TDSSNTdtALTTLEEA---LSEKERIIERLKEQREREDRERLEELESLKKENKDLKEKVSALQpeltEKESSLIDLKEHA 505
|
....*.
gi 254675251 2581 TTQAAS 2586
Cdd:pfam10174 506 SSLASS 511
|
|
| Plectin |
pfam00681 |
Plectin repeat; This family includes repeats from plectin, desmoplakin, envoplakin and bullous ... |
4245-4275 |
9.52e-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: 9.52e-03
10 20 30
....*....|....*....|....*....|.
gi 254675251 4245 AGILDTETLEKVSITEAMHRNLVDNITGQRL 4275
Cdd:pfam00681 9 GGIIDPVTGERLSVEEAVKRGLIDPETAQKL 39
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1644-1744 |
9.56e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 9.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1644 AEEQAVRQRELAEQELEKQRQLAEGTAQQRLAAEQELIRLRAETEQGEQQRQLLEEELARLQHEATAATQKRQELEAELA 1723
Cdd:PRK11448 143 LLHALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKRKEIT 222
|
90 100
....*....|....*....|.
gi 254675251 1724 KvRAEMEVLLaskarAEEESR 1744
Cdd:PRK11448 223 D-QAAKRLEL-----SEEETR 237
|
|
| hsdR |
PRK11448 |
type I restriction enzyme EcoKI subunit R; Provisional |
1374-1520 |
9.64e-03 |
|
type I restriction enzyme EcoKI subunit R; Provisional
Pssm-ID: 236912 [Multi-domain] Cd Length: 1123 Bit Score: 42.25 E-value: 9.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1374 VDAQQQKRSIQEELQHLRQSSEAEIQAKAQQVEAAERsrmrieeeirvvrlqletterqrggAEGELQALRARAEEAEAQ 1453
Cdd:PRK11448 138 EDPENLLHALQQEVLTLKQQLELQAREKAQSQALAEA-------------------------QQQELVALEGLAAELEEK 192
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 254675251 1454 KRQAQEEAERLRRQVQdesqrkrQAEAElalrvkaeaEAAREKQRALQALDELRLqaEEAERR------LRQA 1520
Cdd:PRK11448 193 QQELEAQLEQLQEKAA-------ETSQE---------RKQKRKEITDQAAKRLEL--SEEETRilidqqLRKA 247
|
|
| PRK11281 |
PRK11281 |
mechanosensitive channel MscK; |
1146-1423 |
9.65e-03 |
|
mechanosensitive channel MscK;
Pssm-ID: 236892 [Multi-domain] Cd Length: 1113 Bit Score: 42.21 E-value: 9.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1146 VTQLLERWQAVLAQTDVRQRELEQLGRQLryyrESADplsAWLQDAkrrQEQIQAVPIANCQAAREQLrqEKALLEEIER 1225
Cdd:PRK11281 61 VQQDLEQTLALLDKIDRQKEETEQLKQQL----AQAP---AKLRQA---QAELEALKDDNDEETRETL--STLSLRQLES 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1226 hgeKVEECQKFAKQYINAIKDYELQLITYKAQLEpvaspakkpKVQSGSESVIQEYVDLRTRYSelTTLTSQyiKFISET 1305
Cdd:PRK11281 129 ---RLAQTLDQLQNAQNDLAEYNSQLVSLQTQPE---------RAQAALYANSQRLQQIRNLLK--GGKVGG--KALRPS 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1306 LR-RMEEEERLAEQQRAEERERLA---EVEAALEKQRQLAEAHAQakaQAELEAQELQ------RRMQ-EEVARREEAAV 1374
Cdd:PRK11281 193 QRvLLQAEQALLNAQNDLQRKSLEgntQLQDLLQKQRDYLTARIQ---RLEHQLQLLQeainskRLTLsEKTVQEAQSQD 269
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 254675251 1375 DAQQQKRS--IQEELQHLRQSSEAEIQAKA-------------QQVEAAERSRMRIEEEIRVVR 1423
Cdd:PRK11281 270 EAARIQANplVAQELEINLQLSQRLLKATEklntltqqnlrvkNWLDRLTQSERNIKEQISVLK 333
|
|
| PRK12705 |
PRK12705 |
hypothetical protein; Provisional |
1749-1897 |
9.92e-03 |
|
hypothetical protein; Provisional
Pssm-ID: 237178 [Multi-domain] Cd Length: 508 Bit Score: 42.00 E-value: 9.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1749 KSKQRLEAEAGRFRELA-EEAARLRALAEEAKRQRQLAEEDAARQRAEAERV-----------LTEKLAAisEATRLKTE 1816
Cdd:PRK12705 26 KKRQRLAKEAERILQEAqKEAEEKLEAALLEAKELLLRERNQQRQEARREREelqreeerlvqKEEQLDA--RAEKLDNL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1817 AEIALKEKEAENERLRRLAEDEAFQRRRLEEQAALHKadiEERLAQLRKASESELERQKGLVEDTLRQRRQVEEEIMALK 1896
Cdd:PRK12705 104 ENQLEEREKALSARELELEELEKQLDNELYRVAGLTP---EQARKLLLKLLDAELEEEKAQRVKKIEEEADLEAERKAQN 180
|
.
gi 254675251 1897 V 1897
Cdd:PRK12705 181 I 181
|
|
| PRK12472 |
PRK12472 |
hypothetical protein; Provisional |
1432-1570 |
1.00e-02 |
|
hypothetical protein; Provisional
Pssm-ID: 237110 [Multi-domain] Cd Length: 508 Bit Score: 41.78 E-value: 1.00e-02
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 254675251 1432 QRGGAEGElQALRArAEEAEAQKRQAQEEAERLRRQVQDESQRKRQAEAELALRVKAEAEAAREKQRAlqaldelrlQAE 1511
Cdd:PRK12472 193 ETLAREAE-DAARA-ADEAKTAAAAAAREAAPLKASLRKLERAKARADAELKRADKALAAAKTDEAKA---------RAE 261
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 254675251 1512 EAERRLRQAEAERARQvqvaLETAQrsAEVELQSKRASFAEKTAQLERTLQEEHVTVAQ 1570
Cdd:PRK12472 262 ERQQKAAQQAAEAATQ----LDTAK--ADAEAKRAAAAATKEAAKAAAAKKAETAKAAT 314
|
|
| |
